NCBI Conserved Domain Search

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

893-1240

1.66e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 1.66e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   893 RLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVE---ERLSKLQKHNAELE 969
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   970 LQRERAEQMLQEKSEELKEkmdkltrqlfDDVQKEEQQRLVlekgfelktQAYEKQIESLREEIKALKDERSQLHhqlEE 1049
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAE----------AEAEIEELEAQI---------EQLKEELKALREALDELRAELTLLN---EE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEkHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1130 HLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN--------HLQKLFREETDINESIRHEV 1201
Cdd:TIGR02168  898 ELSEELR---ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleEAEALENKIEDDEEEARRRL 974

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961013  1202 TRLTSE-------NMM-IPDFKQQ---ISELERQKQDLESRLKEQAEKIE 1240
Cdd:TIGR02168  975 KRLENKikelgpvNLAaIEEYEELkerYDFLTAQKEDLTEAKETLEEAIE 1024

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

849-1239

1.29e-12

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: 72.84 E-value: 1.29e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   849 RYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQR--LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV 926
Cdd:pfam15921  268 RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   927 QK----LEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLfDDVQ 1002
Cdd:pfam15921  348 EKqlvlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRREL-DDRN 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1003 KEEQQRLVLEKGFELKTQA-YEKQIESLREEIKALkDERSQLHHQLEEgqvTSDRLKGEVARLSKQAKTISEFEKEIEll 1081
Cdd:pfam15921  426 MEVQRLEALLKAMKSECQGqMERQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSERTVS-- 499

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1082 qaqkiDVEKHVQSQKREMRERMSEVTKqllesydiedVRSR--LSVEDLEHLNEDGELWfayeglkkatrvleSHFQSQK 1159
Cdd:pfam15921  500 -----DLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGDHL--------------RNVQTEC 550

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1160 DCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRLKEQAEKI 1239
Cdd:pfam15921  551 EALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE---INDRRLELQEFKILKDKKDAKIRELEARV 627

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

848-1150

1.14e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.14e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  848 RRYRKLLQEHKavilQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRV---GDLE 924
Cdd:COG1196   213 ERYRELKEELK----ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeleEAQA 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  925 KVQKLEAELEKAATHRHSYEEKGRRYRDTVEE----------RLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLT 994
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEEleeelaeleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  995 RQLFDDVQKEEQQRLVLEKGFELKTQAYE--KQIESLREEIKALKDERSQLHHQLEEGQvtsDRLKGEVARLSKQAKTIS 1072
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAElaAQLEELEEAEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE 445

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961013 1073 EFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTkQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRV 1150
Cdd:COG1196   446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

961-1030

4.03e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.72 E-value: 4.03e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961013  961 LQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDD-----VQKEEQQRLVLEKGFELKTQAYEKQIESLR 1030
Cdd:cd16269   217 LEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEqeralESKLKEQEALLEEGFKEQAELLQEEIRSLK 291

Spc7

smart00787

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

960-1131

4.77e-04

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

Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 4.77e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    960 KLQKHNAELELQRERAEQMLQEkSEELKEKMDKLtrqlfDDVQKEEQQRLVlekgfelktqAYEKQIESLREEIKALKDE 1039
Cdd:smart00787  120 QLVKTFARLEAKKMWYEWRMKL-LEGLKEGLDEN-----LEGLKEDYKLLM----------KELELLNSIKPKLRDRKDA 183

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   1040 RSQLHHQLEEG-----QVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQLL 1111
Cdd:smart00787  184 LEEELRQLKQLedeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEAEKKLE 263

                           170       180
                    ....*....|....*....|...
gi 568961013   1112 ES--YDIEDVRS-RLSVEDLEHL 1131
Cdd:smart00787  264 QCrgFTFKEIEKlKEQLKLLQSL 286

pfam00612

IQ calmodulin-binding motif; Calmodulin-binding motif.

831-851

4.06e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.

Pssm-ID: 459869 Cd Length: 21 Bit Score: 35.76 E-value: 4.06e-03

                           10        20
                   ....*....|....*....|.
gi 568961013   831 RVATITIQAHTRGFLARRRYR 851
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21

smart00015

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...

830-851

4.95e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.

Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.38 E-value: 4.95e-03

                            10        20
                    ....*....|....*....|..
gi 568961013    830 IRVATITIQAHTRGFLARRRYR 851
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23

Name

Accession

Description

Interval

E-value

MYSc_Myo5

cd01380

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

81-741

0e+00

Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 1201.21 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380     1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01380    81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01380   161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01380   241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  400 ALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK-NSLFEKPRMSNSSFIIQHFADKVE 556
Cdd:cd01380   401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  557 YQCEGFLEKNRDTVYDMLVEILRASKFHlcaaffqespvpsspfgamitvksakqviKPntkhfrtTVGNKFRSSLYLLM 636
Cdd:cd01380   481 YQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KK-------TVGSQFRDSLILLM 524

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  637 ETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEV 716
Cdd:cd01380   525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKT 604

                         650       660
                  ....*....|....*....|....*
gi 568961013  717 CKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01380   605 CENILENLILDPDKYQFGKTKIFFR 629

MYSc

smart00242

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

62-752

0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.

Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 956.23 E-value: 0e+00

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013     62 NPDILVGENDLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVA 141
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    142 EEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVgSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDR 300
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    301 ADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE-RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIV 379
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    380 TSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEK 538
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSK 478

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    539 P-RMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitVKSAKQVIKPnt 617
Cdd:smart00242  479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------VSNAGSKKRF-- 544

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    618 khfrTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:smart00242  545 ----QTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620

                           650       660       670       680       690
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568961013    698 RYGILMTQQELSLS-DKKEVCKVVLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLR 752
Cdd:smart00242  621 RYRVLLPDTWPPWGgDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676

Myosin_head

pfam00063

Myosin head (motor domain);

70-741

0e+00

Myosin head (motor domain);

Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 909.35 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    70 NDLTALSYLHEPAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYK-SDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSN---AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF 226
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   227 DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVET 306
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   307 QKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   387 KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF-SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPR-MSN 543
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRTT 623
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKKRFIT 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:pfam00063  556 VGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILA 635

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 568961013   704 TQ-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:pfam00063  636 PKtWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674

COG5022

Myosin heavy chain [General function prediction only];

12-1240

0e+00

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 891.74 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   12 RVWIPDPEEVWKSAEIAK-DYRAGDRVLRLLLEDGmELEyPVDPGSLPPLR-NPDILVGENDLTALSYLHEPAVLHNLRI 89
Cdd:COG5022    11 GCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDG-ESV-SVKKKVLGNDRiKLPKFDGVDDLTELSYLNEPAVLHNLEK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   90 RFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTV 169
Cdd:COG5022    89 RY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  170 SARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRV 247
Cdd:COG5022   168 NAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  248 VFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKIL 327
Cdd:COG5022   248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  328 AAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYA 407
Cdd:COG5022   328 AAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  408 HLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDF 487
Cdd:COG5022   407 NLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  488 YDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLE 564
Cdd:COG5022   487 FDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLD 566

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  565 KNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamiTVKSAKQVIKPntkhfrtTVGNKFRSSLYLLMETLNATTP 644
Cdd:COG5022   567 KNKDPLNDDLLELLKASTNEFVSTLFDD------------EENIESKGRFP-------TLGSRFKESLNSLMSTLNSTQP 627

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  645 HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM-----TQQELSLSDKKEVCKV 719
Cdd:COG5022   628 HYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKS 707

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  720 VLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVR-- 797
Cdd:COG5022   708 ILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRlv 787

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  798 ----KAITATALKEAWAAIILQKYCRGYLvrnlyQLIRVATITIqahTRGFLARRRYRKLLQEHKAVILQKYARAWLARR 873
Cdd:COG5022   788 dyelKWRLFIKLQPLLSLLGSRKEYRSYL-----ACIIKLQKTI---KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  874 RFQNIRRFVLNIQLTYRVQRLQKKLEDQNREnhglVEKLTSLAALRVGDLEKVQKLEAELE-------KAATHRHSYEEK 946
Cdd:COG5022   860 RFSLLKKETIYLQSAQRVELAERQLQELKID----VKSISSLKLVNLELESEIIELKKSLSsdlienlEFKTELIARLKK 935

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  947 GRRYRDTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKLTrQLFDDVQKEEQQRlvleKGFELKTQAYEKQI 1026
Cdd:COG5022   936 LLNNIDLEEGPSIEYVKLPELNKLHEVESK--LKETSEEYEDLLKKST-ILVREGNKANSEL----KNFKKELAELSKQY 1008

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1027 ESLREEIKALKDERSQL-HHQLEEGQVTSDRlkGEVARLSKQAKTISEFEKEIELLQAQKIDVekhvqSQKREMRERMSe 1105
Cdd:COG5022  1009 GALQESTKQLKELPVEVaELQSASKIISSES--TELSILKPLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLDD- 1080

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1106 vtkqlLESYDIEDVRSRLSVedlehLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:COG5022  1081 -----KQLYQLESTENLLKT-----INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLS 1150

                        1210      1220      1230      1240      1250
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568961013 1186 LFREETDIN--ESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:COG5022  1151 VLQLELDGLfwEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELI 1207

MYSc

cd00124

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

81-741

0e+00

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

Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 818.76 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMG-DMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd00124     1 AAILHNLRERYARDL-IYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  160 SGESGAGKTVSARYAMRYFATVSKSSSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd00124    80 SGESGAGKTETTKLVLKYLAALSGSGSSKSsssassIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  234 GANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEE----FNYTRMGGNTVIEGVNDRADMVETQKT 309
Cdd:cd00124   160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE--RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVK 387
Cdd:cd00124   240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  388 PMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:cd00124   320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNS 544
Cdd:cd00124   400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqespvpsspfgamitvksakqvikpntkhfrttv 624
Cdd:cd00124   480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  625 gnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd00124   518 --QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961013  705 Q-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd00124   596 GaTEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633

MYSc_class_II

cd01377

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

81-741

0e+00

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

Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 738.89 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01377     1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSSNAH--------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd01377    80 GESGAGKTENTKKVIQYLASVAASSKKKKesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  233 IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTL 312
Cdd:cd01377   160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01377   240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd01377   320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMS--NSSFII 548
Cdd:cd01377   400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKksEAHFIL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  549 QHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAkqvikpntkhFRtTVGNKF 628
Cdd:cd01377   480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGS----------FR-TVSQLH 548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  629 RSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQEL 708
Cdd:cd01377   549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628

                         650       660       670
                  ....*....|....*....|....*....|....
gi 568961013  709 -SLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01377   629 kGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662

MYSc_Myo11

cd01384

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

81-741

0e+00

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.

Pssm-ID: 276835 Cd Length: 647 Bit Score: 697.89 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd01384     1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  160 SGESGAGKTVSARYAMRYFATVSK--SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANM 237
Cdd:cd01384    80 SGESGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  238 RTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKK 317
Cdd:cd01384   160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  318 DFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDS---HLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd01384   240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd01384   320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  475 YMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd01384   400 YTKEEIDWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPRSTHETFAQKLYQTLKD-HKRFSKPKLSRTDFTIDHYAG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSspfgamiTVKSAKqvikpntkhFrTTVGNKFRSSLY 633
Cdd:cd01384   479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREG-------TSSSSK---------F-SSIGSRFKQQLQ 541

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDK 713
Cdd:cd01384   542 ELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDE 621

                         650       660
                  ....*....|....*....|....*...
gi 568961013  714 KEVCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd01384   622 KAACKKILEKA--GLKGYQIGKTKVFLR 647

MYSc_Myo8

cd01383

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

81-741

0e+00

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

Pssm-ID: 276834 Cd Length: 647 Bit Score: 682.12 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDmdPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01383     1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd01383    78 GESGAGKTETAKIAMQYLAALGGGSSG--IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  241 LLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQ 320
Cdd:cd01383   156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  321 MDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDA 400
Cdd:cd01383   236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  401 LAKKIYAHLFDFIVEQINQALHFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKED 479
Cdd:cd01383   316 LAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  480 IPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNKNSLFEKPRmsNSSFIIQHFADKVEYQ 558
Cdd:cd01383   396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  559 CEGFLEKNRDTVYDMLVEILRASKFHLCAAF------FQESPVPSSPFGamitvKSAKQvikpntkhfRTTVGNKFRSSL 632
Cdd:cd01383   473 TSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFaskmldASRKALPLTKAS-----GSDSQ---------KQSVATKFKGQL 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSD 712
Cdd:cd01383   539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618

                         650       660
                  ....*....|....*....|....*....
gi 568961013  713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01383   619 PLSTSVAILQQFNILPEMYQVGYTKLFFR 647

MYSc_Myo7

cd01381

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

82-741

0e+00

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

Pssm-ID: 276832 Cd Length: 648 Bit Score: 673.58 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAEsKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01381     2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSSSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAISGQHS--WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQM 321
Cdd:cd01381   159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  322 DVFKILAAILHLGNVQ--VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01381   239 DIFKLLAAILHLGNIKfeATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  400 ALAKKIYAHLFDFIVEQINQALHF-SGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYM 476
Cdd:cd01381   319 AFVKGIYGRLFIWIVNKINSAIYKpRGTDSsrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  477 KEDIPWTLIDFYDNQPVIDLI-EAKMGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRM-SNSSFIIQHFADK 554
Cdd:cd01381   399 KEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGN-NKNYLKPKSdLNTSFGINHFAGV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  555 VEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAKQVIkpntkhfrtTVGNKFRSSLYL 634
Cdd:cd01381   478 VFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS--------ETRKKSP---------TLSSQFRKSLDQ 540

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  635 LMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL------MTQQEL 708
Cdd:cd01381   541 LMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLvpgippAHKTDC 620

                         650       660       670
                  ....*....|....*....|....*....|...
gi 568961013  709 SLSDKKEVCKVVLHrliqDSNqYQFGRTKIFFR 741
Cdd:cd01381   621 RAATRKICCAVLGG----DAD-YQLGKTKIFLK 648

MYSc_Myo1

cd01378

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

82-741

0e+00

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276829 Cd Length: 652 Bit Score: 671.56 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01378     2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01378    81 ESGAGKTEASKRIMQYIAAVSGGSESevERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01378   161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  320 QMDVFKILAAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSE---TVVKPMTRPQAIN 396
Cdd:cd01378   241 QDSIFRILAAILHLGNIQFAEDEEGNAAIS-DTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAY 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd01378   320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEY 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  476 MKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLyNNFVNKNSLFEKP----RMSNSSFIIQ 549
Cdd:cd01378   400 VREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLTAGdATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRIK 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamitvksakQVIKPNTKhfR-TTVGNKF 628
Cdd:cd01378   479 HYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE------------------GVDLDSKK--RpPTAGTKF 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  629 RSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGilmtqqel 708
Cdd:cd01378   539 KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK-------- 610

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 568961013  709 SLSDK---------KEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01378   611 LLSPKtwpawdgtwQGGVESILKDLNIPPEEYQMGKTKIFIR 652

MYSc_Myo22

cd14883

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

82-741

0e+00

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 655.55 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14883     2 GINTNLKVRYK-KDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSSSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd14883    81 ESGAGKTETTKLILQYLCAVTNNHS--WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  242 LEKSRVVFQSENERNYHIFYQLCASAQQS-EFKH-LKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd14883   159 LEQSRITFQAPGERNYHVFYQLLAGAKHSkELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINAR 398
Cdd:cd14883   239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  399 DALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKE 478
Cdd:cd14883   319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  479 DIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKP--RMSNSSFIIQHFADKV 555
Cdd:cd14883   399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  556 EYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFF----QESPVPSSPFGAMITVKSAkqvikpnTKHFRTTVGNKFRSS 631
Cdd:cd14883   478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdLLALTGLSISLGGDTTSRG-------TSKGKPTVGDTFKHQ 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  632 LYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ-QELSL 710
Cdd:cd14883   551 LQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRaRSADH 630

                         650       660       670
                  ....*....|....*....|....*....|.
gi 568961013  711 SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14883   631 KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661

MYSc_Myo4

cd14872

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

81-741

0e+00

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

Pssm-ID: 276839 Cd Length: 644 Bit Score: 607.93 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14872     1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd14872    80 GESGAGKTEATKQCLSFFAEVAGSTNG--VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  241 LLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQ 320
Cdd:cd14872   158 LLEKSRVVYQIKGERNFHIFYQLLASPDPA--SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  321 MDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCE---LLGLETSKVAQWLCNRKI-VTSSETVVKPMTRPQAIN 396
Cdd:cd14872   236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQATD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  397 ARDALAKKIYAHLFDFIVEQINQALH-FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14872   316 ACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  476 MKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14872   396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsspfgamitvksakQVIKPNTKHFRTTVGNKFRSSLY 633
Cdd:cd14872   476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------------PPSEGDQKTSKVTLGGQFRKQLS 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL-SD 712
Cdd:cd14872   536 ALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVgPD 615

                         650       660
                  ....*....|....*....|....*....
gi 568961013  713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14872   616 DRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644

MYSc_Myo42

cd14903

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

81-741

0e+00

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

Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 599.07 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14903     1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVEdKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14903    80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEfkHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd14903   159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  320 QMDVFKILAAILHLGNVQVTTVGN--ERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd14903   237 QEVLFEVLAGILHLGQLQIQSKPNddEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd14903   317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFADKVEY 557
Cdd:cd14903   397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  558 QCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKhfrTTVGNKFRSSLYLLME 637
Cdd:cd14903   477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT---TTVGTQFKDSLNELMT 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  638 TLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVC 717
Cdd:cd14903   554 TIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAERC 633

                         650       660
                  ....*....|....*....|....*
gi 568961013  718 KVVLHRL-IQDSNQYQFGRTKIFFR 741
Cdd:cd14903   634 EALMKKLkLESPEQYQMGLTRIYFQ 658

MYSc_Myo6

cd01382

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

84-741

0e+00

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

Pssm-ID: 276833 Cd Length: 649 Bit Score: 593.46 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01382     4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  163 SGAGKTVSARYAMRYFaTVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd01382    83 SGAGKTESTKYILRYL-TESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLklgsaeefnytrmggnTVIEGVNDRADMVETQKTFTLLGFKKDFQMD 322
Cdd:cd01382   162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEKLD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  323 VFKILAAILHLGNVQVTTVGNER---SSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSE----TVVK-PMTRPQ 393
Cdd:cd01382   226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHtFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd01382   306 ANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY-FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  474 EYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPRMSNSS------- 545
Cdd:cd01382   385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKH-KNHFRLSIPRKSKLKihrnlrd 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  546 ---FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAKQVIKPNTKhfrt 622
Cdd:cd01382   464 degFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK--------DSKQKAGKLSFI---- 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  623 TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd01382   532 SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKY 611

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568961013  703 MTqQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01382   612 LP-PKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649

MYSc_Myo9

cd01385

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

84-741

0e+00

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

Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 584.72 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGES 163
Cdd:cd01385     4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  164 GAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLE 243
Cdd:cd01385    83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  244 KSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDV 323
Cdd:cd01385   163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  324 FKILAAILHLGNVQV---TTVGNERSSVSEDDShLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDA 400
Cdd:cd01385   243 FSVLSAVLHLGNIEYkkkAYHRDESVTVGNPEV-LDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  401 LAKKIYAHLFDFIVEQINQAL----HFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYM 476
Cdd:cd01385   322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKlYNNFVNKNSLFEKPRMSNSSFIIQHFADKV 555
Cdd:cd01385   402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  556 EYQCEGFLEKNRDTVYDMLVEILRASK-----------------------FHLCAAFFQESPVPSS----PFGAMITVKS 608
Cdd:cd01385   481 KYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligidpvavfrwavlraFFRAMAAFREAGRRRAqrtaGHSLTLHDRT 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  609 AKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPS 688
Cdd:cd01385   561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961013  689 RWTYLEFYSRYGILMTQQELSlsdKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01385   641 RYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690

MYSc_Myo10

cd14873

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

82-741

0e+00

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

Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 567.50 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14873     2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSSNA-------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVISQQSLELslkektsCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  234 GANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLL 313
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  314 GFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSvseDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14873   241 QFSKEEVREVSRLLAGILHLGNIEFITAGGAQVS---FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  394 AINARDALAKKIYAHLFDFIVEQINQALHfsGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14873   318 AVDSRDSLAMALYARCFEWVIKKINSRIK--GKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  473 EEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14873   396 LEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHAN-NHFYVKPRVAVNNFGVKHYA 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamITVKSAKQVIKPNTKHFRTTVGNKFRSSL 632
Cdd:cd14873   475 GEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH-----------VSSRNNQDTLKCGSKHRRPTVSSQFKDSL 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLsD 712
Cdd:cd14873   544 HSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE-D 622

                         650       660
                  ....*....|....*....|....*....
gi 568961013  713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14873   623 VRGKCTSLLQLYDASNSEWQLGKTKVFLR 651

MYSc_Myo15

cd01387

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

82-741

0e+00

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

Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 566.69 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01387     2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMRTYL 241
Cdd:cd01387    81 ESGSGKTEATKLIMQYLAAVNQRRNNL-VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQM 321
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  322 DVFKILAAILHLGNV----QVTTVGNERSSVSEDdSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd01387   239 SIFRILASVLHLGNVyfhkRQLRHGQEGVSVGSD-AEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01387   318 RDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIR 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  478 EDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKL-YNNFVNKnsLFEKPRMSNSSFIIQHFADKV 555
Cdd:cd01387   398 EQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHYAGQV 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  556 EYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQ------ESPVPSSPFGAMITvksakqvIKPNTKhfrtTVGNKFR 629
Cdd:cd01387   476 WYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSshraqtDKAPPRLGKGRFVT-------MKPRTP----TVAARFQ 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQeLS 709
Cdd:cd01387   545 DSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK-LP 623

                         650       660       670
                  ....*....|....*....|....*....|....
gi 568961013  710 LSDKKEVCKVVLHRL--IQDSNQYQFGRTKIFFR 741
Cdd:cd01387   624 RPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657

MYSc_Myo29

cd14890

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

82-741

0e+00

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

Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 566.33 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMAR----NNRNQS 156
Cdd:cd14890     2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  157 IIVSGESGAGKTVSARYAMRYFATVSKSSSN-----------------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLARITSGFAQgasgegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  220 KYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVND 299
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLR-GECSSIPSCDD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  300 RADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVgnERSSVSEDDS---HLKVFCELLGLETSKVAQWLCNR 376
Cdd:cd14890   240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATtlqSLKLAAELLGVNEDALEKALLTR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  377 KIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYAN 456
Cdd:cd14890   318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  457 EKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM----GILELLDEECLLpHGTDEN--WLQKLYNNF- 529
Cdd:cd14890   398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRF-KGEEANkkFVSQLHASFg 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  530 -----------VNKNSLFEKPRMSNS-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvps 597
Cdd:cd14890   477 rksgsggtrrgSSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS---------------- 540

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  598 spfgamitvksakqvikpnTKHFR-TTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVL 676
Cdd:cd14890   541 -------------------RRSIReVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961013  677 ETIRISAQSYPSRWTYLEFYSRYGILMTQQElslsDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14890   602 EAIQIRQQGFALREEHDSFFYDFQVLLPTAE----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662

MYSc_Myo3

cd01379

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

81-741

0e+00

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

Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 558.82 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01379     1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSsNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd01379    80 GESGAGKTESANLLVQQLTVLGKAN-NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  241 LLEKSRVVFQSENERNYHIFYQLCAS-AQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMV---ETQKTFTLLGFK 316
Cdd:cd01379   159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREkfeEIEQCFKVIGFT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  317 KDFQMDVFKILAAILHLGNVQVTTVGNE----RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01379   239 KEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  393 QAINARDALAKKIYAHLFDFIVEQINQAL----HFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd01379   319 EATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvnKNSLFEKPRMSNSSFI 547
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSNALSFG 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLcaaffqespvpsspfgamitvksakqvikpntkhFRTTVGNK 627
Cdd:cd01379   476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPL----------------------------------VRQTVATY 521

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQE 707
Cdd:cd01379   522 FRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWN 601

                         650       660       670
                  ....*....|....*....|....*....|....
gi 568961013  708 LSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd01379   602 EEVVANRENCRLILERLKLDN--WALGKTKVFLK 633

MYSc_Myo43

cd14904

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

81-741

0e+00

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

Pssm-ID: 276869 Cd Length: 653 Bit Score: 556.86 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14904     1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVeDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14904    80 SGESGAGKTETTKIVMNHLASVAGGRKDKTI-AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGN---TVIEGVNDRADMVETQKTFTLLGFK 316
Cdd:cd14904   159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQY--LGDSlaqMQIPGLDDAKLFASTQKSLSLIGLD 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  317 KDFQMDVFKILAAILHLGNVQVTTVGnERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14904   237 NDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14904   316 NRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  476 MKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK--NSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14904   396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKkdNESIDFPKVKRTQFIINHYAG 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNtkhfrtTVGNKFRSSLY 633
Cdd:cd14904   476 PVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEG----KSGKGTKAPK------SLGSQFKTSLS 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIlMTQQELSLSDK 713
Cdd:cd14904   546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI-MFPPSMHSKDV 624

                         650       660
                  ....*....|....*....|....*....
gi 568961013  714 KEVCKVVLHRLIQDSN-QYQFGRTKIFFR 741
Cdd:cd14904   625 RRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653

MYSc_Myo40

cd14901

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

81-739

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: 548.24 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGD---MDPHIFAVAEEAYKQMARNNR- 153
Cdd:cd14901     1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  154 ---NQSIIVSGESGAGKTVSARYAMRYFATVS-KSSSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14901    80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsATTHGQNaterenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  224 ISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTV-IEGVNDRAD 302
Cdd:cd14901   160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  303 MVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ-VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTS 381
Cdd:cd14901   240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:cd14901   320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYseSTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSL-FE 537
Cdd:cd14901   400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFsVS 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  538 KPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLcaaffqespVPSspfgamitvksakqvikpnt 617
Cdd:cd14901   480 KLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF---------LSS-------------------- 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  618 khfrtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14901   531 -----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568961013  698 RYGILMTQQElslSDKKEVCKVVLHR---------LIQDSNQYQFGRTKIF 739
Cdd:cd14901   606 TYSCLAPDGA---SDTWKVNELAERLmsqlqhselNIEHLPPFQVGKTKVF 653

MYSc_Myo31

cd14892

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

87-741

2.68e-178

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: 540.89 E-value: 2.68e-178

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   87 LRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMD---PHIFAVAEEAYKQM----ARNNRNQSIIV 159
Cdd:cd14892     7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASsppPHVFSIAERAYRAMkgvgKGQGTPQSIVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  160 SGESGAGKTVSARYAMRYFATVSKSSS---------NAH--VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14892    86 SGESGAGKTEASKYIMKYLATASKLAKgastskgaaNAHesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  229 RNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQK 308
Cdd:cd14892   166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKV--FCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:cd14892   246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVakAAGLLGVDAAELMFKLVTQTTSTARGSVL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  387 K-PMTRPQAINARDALAKKIYAHLFDFIVEQINQA----------LHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYA 455
Cdd:cd14892   326 EiKLTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsgvtgGAASPTFSPFIGILDIFGFEIMPTNSFEQLCINFT 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  456 NEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLYNNFVNKN 533
Cdd:cd14892   406 NEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKRkTTDKQLLTIYHQTHLDKH 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  534 SLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqespvpsspfgamitvksakqvi 613
Cdd:cd14892   486 PHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------- 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  614 kpntkhfrttvgnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYL 693
Cdd:cd14892   535 -------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFE 601

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568961013  694 EFYSRYGIL--------MTQQELSLSD-KKEVCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd14892   602 EFYEKFWPLarnkagvaASPDACDATTaRKKCEEIVARAL--ERENFQLGRTKVFLR 656

MYSc_Myo27

cd14888

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

81-741

7.33e-177

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

Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 537.35 E-value: 7.33e-177

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14888     1 ASILHSLNLRFDIDE-IYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  160 SGESGAGKTVSARYAMRYFATVSKSS--SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN------- 230
Cdd:cd14888    79 SGESGAGKTESTKYVMKFLACAGSEDikKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKskrmsgd 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  231 --QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQS-------EFKHLKLG----------------SAEEFNY 285
Cdd:cd14888   159 rgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyEENDEKLAkgadakpisidmssfePHLKFRY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  286 TRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ-VTTVGNERSSV--SEDDSHLKVFCELL 362
Cdd:cd14888   239 LTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVvsASCTDDLEKVASLL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  363 GLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHT-FIGVLDIYGFET 441
Cdd:cd14888   319 GVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLlFCGVLDIFGFEC 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  442 FDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDEN 520
Cdd:cd14888   399 FQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  521 WLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpSSPF 600
Cdd:cd14888   479 LCNKLCQKHKG-HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLF------SAYL 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  601 GAMITVKSakqvikpnTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIR 680
Cdd:cd14888   552 RRGTDGNT--------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQ 623

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961013  681 ISAQSYPSRWTYLEFYSRYGILMTQQElslsdKKEVckvvlhrliqdsNQYQFGRTKIFFR 741
Cdd:cd14888   624 VSRAGYPVRLSHAEFYNDYRILLNGEG-----KKQL------------SIWAVGKTLCFFK 667

MYSc_Myh10

cd14920

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

82-741

1.61e-167

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: 513.40 E-value: 1.61e-167

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14920     2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14920    81 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14920   161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14920   240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14920   320 DFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPRM--SNSSFI 547
Cdd:cd14920   400 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQE-QGSHSKFQKPRQlkDKADFC 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE--SPVPSSPFGAMiTVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14920   479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdRIVGLDQVTGM-TETAFGSAYKTKKGMFR-TVG 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14920   557 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 636

                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 568961013  706 Q-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14920   637 AiPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673

MYSc_Myh7b

cd14927

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

82-741

4.17e-165

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: 507.18 E-value: 4.17e-165

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14927     2 SVLHNLRRRYS-RWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVS-------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14927    81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  229 RNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQ 307
Cdd:cd14927   161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNPYDYHFCSqGVTTVDNMDDGEELMATD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  308 KTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVK 387
Cdd:cd14927   240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  388 PMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd14927   320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN--- 543
Cdd:cd14927   400 FILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKkrk 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  544 --SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqESPVPSSpfgamiTVKSAKQVIKPNTKHFR 621
Cdd:cd14927   480 yeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY-ENYVGSD------STEDPKSGVKEKRKKAA 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  622 T--TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14927   553 SfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 568961013  700 GILMTQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14927   633 RILNPSAipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676

MYSc_Myh3

cd14913

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

81-741

5.71e-165

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: 506.51 E-value: 5.71e-165

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14913     1 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVS---------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14913    80 GESGAGKTVNTKRVIQYFATIAatgdlakkkDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14913   160 LASADIETYLLEKSRVTFQLKAERSYHIFYQIL-SNKKPELIELLLITTNPYDYPFISqGEILVASIDDAEELLATDSAI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14913   239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14913   319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SNSS 545
Cdd:cd14913   399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVvkgrAEAH 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsSPFGAMITVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14913   479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-------ATFATADADSGKKKVAKKKGSSFQ-TVS 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14913   551 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961013  706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14913   631 AipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668

MYSc_Myh1_insects_crustaceans

cd14909

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

81-741

7.05e-165

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: 506.30 E-value: 7.05e-165

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14909     1 ASVLHNLRQRY-YAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSS-------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd14909    80 GESGAGKTENTKKVIAYFATVGASKktdeaakSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  234 GANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTFTL 312
Cdd:cd14909   160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLLSDNIYDYYIVSqGKVTVPNVDDGEEFSLTDQAFDI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14909   239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14909   319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN-----SSF 546
Cdd:cd14909   399 EEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpgqqaAHF 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  547 IIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFrTTVGN 626
Cdd:cd14909   479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQ------AKGGRGKKGGGF-ATVSS 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ 706
Cdd:cd14909   552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631

                         650       660       670
                  ....*....|....*....|....*....|....*
gi 568961013  707 ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14909   632 IQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666

MYSc_Myh15_mammals

cd14929

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

81-741

1.02e-164

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 505.66 E-value: 1.02e-164

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14929     1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14929    80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQqsEFKHLKLGSA--EEFNYTRMGGNTViEGVNDRADMVETQKTFTLLG 314
Cdd:cd14929   160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSAnpSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14929   237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd14929   317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  475 YMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQ---- 549
Cdd:cd14929   397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE--SPVPSSPFGAMITVKSAKqvikpntkhFRtTVGNK 627
Cdd:cd14929   477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENyiSTDSAIQFGEKKRKKGAS---------FQ-TVASL 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL--MTQ 705
Cdd:cd14929   547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILnpRTF 626

                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 568961013  706 QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14929   627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662

MYSc_Myo46

cd14907

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

83-741

1.85e-160

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: 494.55 E-value: 1.85e-160

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP---------IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14907     3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  154 NQSIIVSGESGAGKTVSARYAMRYFATVS------------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNS 215
Cdd:cd14907    82 KQAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevltltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  216 SRFGKYTEISFDERNQ-IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL---GSAEEFNYTRMGGN 291
Cdd:cd14907   162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKKSNC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  292 TVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ---VTTVGNERSSVSeDDSHLKVFCELLGLETSK 368
Cdd:cd14907   242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQfddSTLDDNSPCCVK-NKETLQIIAKLLGIDEEE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  369 VAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSG--KQHTF------IGVLDIYGFE 440
Cdd:cd14907   321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDekDQQLFqnkylsIGLLDIFGFE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  441 TFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTL--IDFYDNQPVIDLIE-AKMGILELLDEECLLPHGT 517
Cdd:cd14907   401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLATGT 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  518 DENWLQKLYNNFvNKNSLFEKPRMSNS-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVP 596
Cdd:cd14907   481 DEKLLNKIKKQH-KNNSKLIFPNKINKdTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGS 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  597 SSPFGAMITVKSAKQvikpntkhfrTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVL 676
Cdd:cd14907   560 QQQNQSKQKKSQKKD----------KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961013  677 ETIRISAQSYPSRWTYLEFYSRYGILmtqqelslsdkkevckvvlhrliqdSNQYQFGRTKIFFR 741
Cdd:cd14907   630 ESIRVRKQGYPYRKSYEDFYKQYSLL-------------------------KKNVLFGKTKIFMK 669

MYSc_Myo36

cd14897

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

83-741

1.02e-157

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 486.12 E-value: 1.02e-157

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDM-DPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14897     3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSkSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd14897    82 ESGAGKTESTKYMIKHLMKLS-PSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVETQKTFT-------LLG 314
Cdd:cd14897   161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILR-DDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  315 F-KKDFQMdVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14897   240 FsEEDISV-IFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  394 AINARDALAKKIYAHLFDFIVEQINQALH----FSGK-QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14897   319 ANDSRDALAKDLYSRLFGWIVGQINRNLWpdkdFQIMtRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNKNSLFEKPRMSNSSFI 547
Cdd:cd14897   399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsspfgamitvksakqvikpnTKHfrttvgnk 627
Cdd:cd14897   478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------------TSY-------- 523

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQE 707
Cdd:cd14897   524 FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSN 603

                         650       660       670
                  ....*....|....*....|....*....|....
gi 568961013  708 LSLSDKKEVCKVVLHrlIQDSNQYQFGRTKIFFR 741
Cdd:cd14897   604 KVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635

MYSc_Myh2_insects_mollusks

cd14911

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

82-741

4.68e-156

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: 483.33 E-value: 4.68e-156

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14911     2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVS----KSSSNAH------------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEIS 225
Cdd:cd14911    81 ESGAGKTENTKKVIQFLAYVAaskpKGSGAVPhpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  226 FDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVE 305
Cdd:cd14911   161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  306 TQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETV 385
Cdd:cd14911   240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  386 VKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFN 464
Cdd:cd14911   320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  465 LHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd14911   400 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGV 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKpntKHFRtT 623
Cdd:cd14911   480 ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRK---GMFR-T 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14911   556 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 635

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568961013  704 TQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14911   636 PNViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674

MYSc_Myh7

cd14917

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

81-741

1.71e-154

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: 479.21 E-value: 1.71e-154

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14917     1 PAVLYNLKERYA-SWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVS---------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14917    80 GESGAGKTVNTKRVIQYFAVIAaigdrskkdQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14917   160 LASADIETYLLEKSRVIFQLKAERDYHIFYQIL-SNKKPELLDMLLITNNPYDYAFISqGETTVASIDDAEELMATDNAF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14917   239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14917   319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNSS 545
Cdd:cd14917   399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnikgKPEAH 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPfgamitVKSAKQVIKPNTKHfrTTVG 625
Cdd:cd14917   479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP------IEKGKGKAKKGSSF--QTVS 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14917   551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961013  706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14917   631 AipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668

MYSc_Myo47

cd14908

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

81-741

4.27e-152

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: 473.24 E-value: 4.27e-152

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY------SGQNM---GDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14908     1 PAILHSLSRRFFRGI-IYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVE----------DKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:cd14908    80 IRaSQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGS--------AEEFNYTRMGGNT 292
Cdd:cd14908   160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  293 VIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVS---EDDSHLKVFCELLGLETSKV 369
Cdd:cd14908   240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVDVDKL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  370 AQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ--HTFIGVLDIYGFETFDVNSF 447
Cdd:cd14908   320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  448 EQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLP-HGTDENWLQKL 525
Cdd:cd14908   400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  526 YNNF-------VNKNSLFEKPRM--SNSSFIIQHFADKVEYQCE-GFLEKNRDTVydmlveilraskfhlcaaffqespv 595
Cdd:cd14908   480 YETYlpeknqtHSENTRFEATSIqkTKLIFAVRHFAGQVQYTVEtTFCEKNKDEI------------------------- 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  596 psspfgamitvksakqvikPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGV 675
Cdd:cd14908   535 -------------------PLTADSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGV 595

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  676 LETIRISAQSYPSRWTYLEFYSRYGILM-TQQELSLSDK-----------KEVCKV-VLHRLIQD--------SNQYQFG 734
Cdd:cd14908   596 LEAVRVARSGYPVRLPHKDFFKRYRMLLpLIPEVVLSWSmerldpqklcvKKMCKDlVKGVLSPAmvsmknipEDTMQLG 675


                  ....*..
gi 568961013  735 RTKIFFR 741
Cdd:cd14908   676 KSKVFMR 682

MYSc_Myo28

cd14889

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

83-741

6.99e-152

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276854 Cd Length: 659 Bit Score: 471.70 E-value: 6.99e-152

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQM----ARNNRNQSII 158
Cdd:cd14889     3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  159 VSGESGAGKTVSARYAMRYFATVSKSssNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR 238
Cdd:cd14889    82 ISGESGAGKTESTKLLLRQIMELCRG--NSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  239 TYLLEKSRVVFQSENERNYHIFYQLCA--SAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADmvETQKTFTLLGFK 316
Cdd:cd14889   159 EYLLEKSRVVHQDGGEENFHIFYYMFAgiSAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYD--EVCNAMDMVGFT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  317 KDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAI 395
Cdd:cd14889   237 EQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  396 NARDALAKKIYAHLFDFIVEQINQAL---HFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14889   317 DARDSIAKVAYGRVFGWIVSKINQLLapkDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQ 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  473 EEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPRMSNSSFIIQHF 551
Cdd:cd14889   397 KEYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPKFTVNHY 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  552 ADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpSSPFGAMITVKSAKQVIKPNTKHFR-TTVGNKFRS 630
Cdd:cd14889   476 AGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTAT---RSRTGTLMPRAKLPQAGSDNFNSTRkQSVGAQFKH 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  631 SLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL 710
Cdd:cd14889   553 SLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPALPG 632

                         650       660       670
                  ....*....|....*....|....*....|.
gi 568961013  711 SdkKEVCKVVLHRliQDSNQYQFGRTKIFFR 741
Cdd:cd14889   633 T--KQSCLRILKA--TKLVGWKCGKTRLFFK 659

MYSc_Myh16

cd14934

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

82-741

5.87e-151

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: 469.51 E-value: 5.87e-151

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14934     2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSSSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14934    81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL-GSAEEFNYTRMGgNTVIEGVNDRADMVETQKTFTLLGF 315
Cdd:cd14934   161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  316 KKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAI 395
Cdd:cd14934   240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  396 NARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14934   320 NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  476 MKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKP-----RMSNSSFIIQ 549
Cdd:cd14934   400 KREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFELV 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvkSAKQviKPNTKHFrtTVGNKFR 629
Cdd:cd14934   480 HYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG---------SKKQ--KRGSSFM--TVSNFYR 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ-EL 708
Cdd:cd14934   547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNViPQ 626

                         650       660       670
                  ....*....|....*....|....*....|...
gi 568961013  709 SLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14934   627 GFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659

MYSc_Myh6

cd14916

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

81-741

4.03e-150

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: 467.61 E-value: 4.03e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14916     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSK----------SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14916    80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKT 309
Cdd:cd14916   160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQIL-SNKKPELLDMLLVTNNPYDYAFVSqGEVSVASIDDSEELLATDSA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14916   239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  390 TRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14916   319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNS 544
Cdd:cd14916   399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpSSPFGAMITVKSAKQVIKPNTKHFRtTV 624
Cdd:cd14916   479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF------STYASADTGDSGKGKGGKKKGSSFQ-TV 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL-- 702
Cdd:cd14916   552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnp 631

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568961013  703 MTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14916   632 AAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670

MYSc_Myh8

cd14918

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

81-741

4.73e-150

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 467.29 E-value: 4.73e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14918     1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14918    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14918   160 LASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDSAI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14918   239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14918   319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SNSS 545
Cdd:cd14918   399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsSPFGAMITVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14918   479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-------STYASAEADSGAKKGAKKKGSSFQ-TVS 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14918   551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961013  706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14918   631 AipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668

MYSc_Myh18

cd14932

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

82-741

1.21e-149

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 466.43 E-value: 1.21e-149

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14932     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSS-----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14932    81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRADMVETQK 308
Cdd:cd14932   161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL---EDYSKYRFlsNGNVTIPGQQDKELFAETME 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14932   238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd14932   318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPR--M 541
Cdd:cd14932   398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGN-NPKFQKPKklK 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  542 SNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESP--VPSSPFGAMitVKSAKQVIKPNTKH 619
Cdd:cd14932   477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDriVGLDKVAGM--GESLHGAFKTRKGM 554

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  620 FRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14932   555 FR-TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 568961013  700 GILM-TQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14932   634 EILTpNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676

MYSc_Myh2_mammals

cd14912

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

81-741

5.83e-149

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 464.59 E-value: 5.83e-149

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14912     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14912    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14912   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLITTNPYDYPFVSqGEISVASIDDQEELMATDS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14912   239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14912   319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SN 543
Cdd:cd14912   399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRtT 623
Cdd:cd14912   479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAG----GGAKKGGKKKGSSFQ-T 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14912   554 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568961013  704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14912   634 ASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673

MYSc_Myo30

cd14891

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

81-741

1.16e-148

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276856 Cd Length: 645 Bit Score: 462.98 E-value: 1.16e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFA-ESKLIYTYSGIILVAMNPYKQLPiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNN---RNQS 156
Cdd:cd14891     1 AGILHNLEERSKlDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  157 IIVSGESGAGKTVSARYAMRY------------FATVSKSSSNAH-----VEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFlttravggkkasGQDIEQSSKKRKlsvtsLDERLMDTNPILESFGNAKTLRNHNSSRFG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  220 KYTEISF-DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVN 298
Cdd:cd14891   158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  299 DRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQV----TTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLC 374
Cdd:cd14891   238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALEKVIT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  375 NRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFD-VNSFEQFCIN 453
Cdd:cd14891   318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLIN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  454 YANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNK 532
Cdd:cd14891   398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTH-KR 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  533 NSLF--EKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvpsspfgamitvksak 610
Cdd:cd14891   477 HPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------------------- 527

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  611 qvikpntkhfrttvgNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRW 690
Cdd:cd14891   528 ---------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961013  691 TYLEFYSRYGILMTQQELSL--SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14891   593 TYAELVDVYKPVLPPSVTRLfaENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645

MYSc_Myh1_mammals

cd14910

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

81-741

4.13e-148

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 462.28 E-value: 4.13e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14910     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14910    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14910   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14910   239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14910   319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN---- 543
Cdd:cd14910   399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkve 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFRtT 623
Cdd:cd14910   479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGG------GKKGGKKKGSSFQ-T 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14910   552 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568961013  704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14910   632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671

MYSc_Myh13

cd14923

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

81-741

1.18e-146

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: 458.38 E-value: 1.18e-146

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14923     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVS----------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14923    80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKT 309
Cdd:cd14923   160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQI-MSNKKPELIDLLLISTNPFDFPFVSqGEVTVASIDDSEELLATDNA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14923   239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  390 TRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14923   319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNS 544
Cdd:cd14923   399 LEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpakgKAEA 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvkSAKQVIKPNTKHFRtTV 624
Cdd:cd14923   479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSG-----GSKKGGKKKGSSFQ-TV 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14923   553 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA 632

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568961013  705 QQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14923   633 SAipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671

MYSc_Myh4

cd14915

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

81-741

2.62e-146

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: 457.65 E-value: 2.62e-146

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14915     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14915    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14915   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPELIEMLLITTNPYDFAFVSqGEITVPSIDDQEELMATDS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14915   239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14915   319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSN 543
Cdd:cd14915   399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKpakgKAE 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFRtT 623
Cdd:cd14915   479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGG------GKKGGKKKGSSFQ-T 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14915   552 VSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568961013  704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14915   632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671

MYSc_Myh11

cd14921

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

82-741

1.20e-145

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: 456.02 E-value: 1.20e-145

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14921     2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKS-------SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14921    81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEF-NYTRMGGNTVIEGVNDRADMV-ETQKTFTL 312
Cdd:cd14921   161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL---EGFnNYTFLSNGFVPIPAAQDDEMFqETLEAMSI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14921   238 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14921   318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  472 QEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRM--SNSS 545
Cdd:cd14921   398 QEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGN-HPKFQKPKQlkDKTE 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE-SPVPSSPFGAMITVKSAKQVIKPNTKHFRtTV 624
Cdd:cd14921   477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGLDQMAKMTESSLPSASKTKKGMFR-TV 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14921   556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961013  705 QQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14921   636 NAiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673

PTZ00014

myosin-A; Provisional

71-791

2.70e-145

myosin-A; Provisional

Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 459.88 E-value: 2.70e-145

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   71 DLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:PTZ00014  100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:PTZ00014  179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQK 308
Cdd:PTZ00014  259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLdVPGIDDVKDFEEVME 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTtvGNERSSVSE----DDSHLKVF---CELLGLETSKVAQWLCNRKIVTS 381
Cdd:PTZ00014  337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDYESLKKELTVKVTYAG 414

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:PTZ00014  415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:PTZ00014  495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  541 MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGamitvksAKQVIkpntkhf 620
Cdd:PTZ00014  575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLA-------KGQLI------- 640

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  621 rttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:PTZ00014  641 ----GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFK 716

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  701 ILmtqqELSLS-----DKKEVCKVVLHRLIQDSNQYQFGRTKIFFR---AGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQ 772
Cdd:PTZ00014  717 YL----DLAVSndsslDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKK 792

                         730
                  ....*....|....*....
gi 568961013  773 RRKFLRERQAALTIQRYFR 791
Cdd:PTZ00014  793 KRKVRKNIKSLVRIQAHLR 811

MYSc_Myh14_mammals

cd14930

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

82-741

3.80e-142

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.

Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 446.46 E-value: 3.80e-142

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14930     2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14930    81 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTviEGVNDRADMVETQKTFTLLG 314
Cdd:cd14930   161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14930   239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14930   319 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPR--MSNSSFI 547
Cdd:cd14930   399 EYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE-QGGHPKFQRPRhlRDQADFS 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFF----------QESPVPSSPFGAmitvksakqviKPNT 617
Cdd:cd14930   478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivgleQVSSLGDGPPGG-----------RPRR 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  618 KHFRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14930   547 GMFR-TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 568961013  698 RYGILMTQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14930   626 RYEILTPNAiPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670

MYSc_Myo19

cd14880

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

83-739

2.11e-141

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 444.29 E-value: 2.11e-141

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYK--QMARNNRNQSII 158
Cdd:cd14880     3 VLRCLQARYTAD-TFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  159 VSGESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14880    82 VSGESGAGKTWTSRCLMKFYAVVAASPTSweshkiaERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEgvndraDMVE-TQKTF 310
Cdd:cd14880   162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE------DCFEvTREAM 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSS---VSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV- 386
Cdd:cd14880   236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVf 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  387 -KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHT-FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFN 464
Cdd:cd14880   316 kKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTtFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  465 LHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd14880   396 AHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSR 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  544 S-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvPSSPfgamitVKSAKQVIKPNTKHFRT 622
Cdd:cd14880   476 EpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF-----PANP------EEKTQEEPSGQSRAPVL 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  623 TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14880   545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624

                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 568961013  703 MTQQELSLSDKKEVCKVVLHrliqdSNQYQFGRTKIF 739
Cdd:cd14880   625 RRLRPHTSSGPHSPYPAKGL-----SEPVHCGRTKVF 656

MYSc_Myo34

cd14895

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

81-741

1.51e-140

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: 443.63 E-value: 1.51e-140

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDaiIHAYSGQNMGDMD--PHIFAVAEEAYKQMARNN------ 152
Cdd:cd14895     1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPGLYD--LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRRLhepgas 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  153 -RNQSIIVSGESGAGKTVSARYAMRYFATVSK--------SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14895    78 kKNQTILVSGESGAGKTETTKFIMNYLAESSKhttatsssKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  224 ISF-----DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFK--HLKLGSAEEFNYTRMGGNTVI-E 295
Cdd:cd14895   158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelQLELLSAQEFQYISGGQCYQRnD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  296 GVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVqvtTVGNERSSVSEDDS---------------------H 354
Cdd:cd14895   238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNV---LFVASSEDEGEEDNgaasapcrlasaspssltvqqH 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  355 LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALhfSGKQHT----- 429
Cdd:cd14895   315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS--PQRQFAlnpnk 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  430 --------FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK- 500
Cdd:cd14895   393 aankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRp 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  501 MGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNS--SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEIL 578
Cdd:cd14895   473 SGIFSLLDEECVVPKGSDAGFARKLYQRLQE-HSNFSASRTDQAdvAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  579 -RASKFHLCAAFfqespvpsSPFGAmiTVKSAKQVIKPNTKHFRTT-----VGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14895   552 gKTSDAHLRELF--------EFFKA--SESAELSLGQPKLRRRSSVlssvgIGSQFKQQLASLLDVVQQTQTHYIRCIKP 621

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ---ELSLSDKKEVCKVvlhrliqdsN 729
Cdd:cd14895   622 NDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKnasDATASALIETLKV---------D 692

                         730
                  ....*....|..
gi 568961013  730 QYQFGRTKIFFR 741
Cdd:cd14895   693 HAELGKTRVFLR 704

MYSc_Myh9

cd14919

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

82-741

4.37e-140

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: 441.07 E-value: 4.37e-140

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14919     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKS----SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANM 237
Cdd:cd14919    81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  238 RTYLLEKSRVVFQSENERNYHIFYQLCASAQQsefkHLKLG-SAEEFNYTRM--GGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14919   161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE----HLKTDlLLEPYNKYRFlsNGHVTIPGQQDKDMFQETMEAMRIMG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14919   237 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14919   317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPRM--SNSSFI 547
Cdd:cd14919   397 EYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQKPKQlkDKADFC 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE-SPVPSSPFGAMITVKSAKQVIKPNTKHFRtTVGN 626
Cdd:cd14919   476 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvDRIIGLDQVAGMSETALPGAFKTRKGMFR-TVGQ 554

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ 706
Cdd:cd14919   555 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 634

                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 568961013  707 -ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14919   635 iPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670

MYSc_Myo14

cd14876

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

81-739

1.40e-138

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276843 Cd Length: 649 Bit Score: 436.34 E-value: 1.40e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSG-QNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14876     1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14876    80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQKTFTLLGFKKD 318
Cdd:cd14876   160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKF--LNPKCLdVPGIDDVADFEEVLESLKSMGLTEE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  319 FQMDVFKILAAILHLGNVQVTT-----VGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14876   238 QIDTVFSIVSGVLLLGNVKITGkteqgVDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14876   318 AEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  474 EYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14876   398 LYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTI 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAK-QVIkpntkhfrttvGNKFRSS 631
Cdd:cd14876   478 GDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG--------KIAKgSLI-----------GSQFLKQ 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  632 LYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILmtqqELSLS 711
Cdd:cd14876   539 LESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL----DLGIA 614

                         650       660       670
                  ....*....|....*....|....*....|...
gi 568961013  712 -DKKEVCKVVLHRLIQDSN----QYQFGRTKIF 739
Cdd:cd14876   615 nDKSLDPKVAALKLLESSGlsedEYAIGKTMVF 647

MYSc_Myo41

cd14902

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

81-741

1.69e-138

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: 438.56 E-value: 1.69e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY--------SGQNMGDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14902     1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  152 NR-NQSIIVSGESGAGKTVSARYAMRYFATV--------SKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14902    80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  223 EISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEF----NYTRMGGNTVIEGVN 298
Cdd:cd14902   160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellnSYGPSFARKRAVADK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  299 DRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVS---EDDSHLKVFCELLGLETSKVAQWLCN 375
Cdd:cd14902   240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvtaASRFHLAKCAELMGVDVDKLETLLSS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  376 RKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAL-HFSGKQH--------TFIGVLDIYGFETFDVNS 446
Cdd:cd14902   320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInYFDSAVSisdedeelATIGILDIFGFESLNRNG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  447 FEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKL 525
Cdd:cd14902   400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  526 YNNFVNKNslfekprmsnsSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamiT 605
Cdd:cd14902   480 YRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSP------G 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  606 VKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQS 685
Cdd:cd14902   543 ADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  686 YPSRWTYLEFYSRYGILMTQQELSLSDKK-------------EVCKVVLHRLIQDSNQ---------------------- 730
Cdd:cd14902   623 YSVRLAHASFIELFSGFKCFLSTRDRAAKmnnhdlaqalvtvLMDRVLLEDGVEREEKnpgaltavtgdgsgtafendcr 702

                         730
                  ....*....|....
gi 568961013  731 ---YQFGRTKIFFR 741
Cdd:cd14902   703 rkdVQVGRTLVFCK 716

MYSc_Myh19

cd15896

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

82-741

1.99e-138

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 436.80 E-value: 1.99e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd15896     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKS-----------SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd15896    81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRADMVETQK 308
Cdd:cd15896   161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL---ENYNNYRFlsNGNVTIPGQQDKDLFTETME 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd15896   238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd15896   318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIE---AKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd15896   398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKD 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  544 SS-FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQ--ESPVPSSPFGAMITVKSAkqvIKPNTKHF 620
Cdd:cd15896   478 EAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvDRIVGLDKVSGMSEMPGA---FKTRKGMF 554

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  621 RtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:cd15896   555 R-TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 633

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 568961013  701 ILMTQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd15896   634 ILTPNAiPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675

MYSc_Myo25

cd14886

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

83-741

3.33e-134

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: 424.68 E-value: 3.33e-134

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMG-----DMDPHIFAVAEEAYKQMARNNRNQS 156
Cdd:cd14886     3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  157 IIVSGESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14886    82 CIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFK 316
Cdd:cd14886   161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKLFSK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  317 KDFQmDVFKILAAILHLGNVQ---VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14886   241 NEID-SFYKCISGILLAGNIEfseEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14886   320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  474 EYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLPHGTDENWLQKLYNNFvnKNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14886   400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI--KNNSFIPGKGSQCNFTIVHTA 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSspfgamitvksakqvikPNTKHfrTTVGNKFRSSL 632
Cdd:cd14886   478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED-----------------GNMKG--KFLGSTFQLSI 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL-- 710
Cdd:cd14886   539 DQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQna 618

                         650       660       670
                  ....*....|....*....|....*....|..
gi 568961013  711 -SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14886   619 gEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650

MYSc_Myo45

cd14906

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

83-734

1.31e-133

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

Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 425.55 E-value: 1.31e-133

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14906     3 ILNNLGKRY-KSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14906    82 GESGSGKTEASKTILQYLINTSSSNQqqnnnnnnnNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  232 II-GANMRTYLLEKSRVVFQSENER-NYHIFYQLCASAQQSEFKHLKLGS-AEEFNY-------------TRMGGNTVIE 295
Cdd:cd14906   162 KIdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdPSKYRYldarddvissfksQSSNKNSNHN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  296 GVNDRADMVETQKTFTL-LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVF---CELLGLETSKVAQ 371
Cdd:cd14906   242 NKTESIESFQLLKQSMEsMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIESVFKQ 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  372 WLCNRKIVTSSETVV--KPMTRPQAINARDALAKKIYAHLFDFIVEQINQ-----------ALHFSGKQHTFIGVLDIYG 438
Cdd:cd14906   322 ALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIFG 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  439 FETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGT 517
Cdd:cd14906   402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGS 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  518 DENWLQKLYNNFVNKNSLFEKPrMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvps 597
Cdd:cd14906   482 EQSLLEKYNKQYHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQ----- 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  598 spfgamitvksaKQVIKPNTKHFRT---TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACG 674
Cdd:cd14906   556 ------------QITSTTNTTKKQTqsnTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVG 623

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  675 VLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSlSDKKEVCKVVLHRLIQDSNQYQFG 734
Cdd:cd14906   624 VLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRK-NNNNPKLASQLILQNIQSKLKTMG 682

MYSc_Myo39

cd14900

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

83-702

1.31e-130

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

Pssm-ID: 276865 Cd Length: 627 Bit Score: 414.32 E-value: 1.31e-130

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 150
Cdd:cd14900     3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  151 --NNR--NQSIIVSGESGAGKTVSARYAMRYFA---------TVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSR 217
Cdd:cd14900    82 glNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  218 FGKYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKhlklgsaeEFNYTRMggntviegv 297
Cdd:cd14900   162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK--------RDMYRRV--------- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  298 NDRADMVetqktftllGFKKDFQMDVFKILAAILHLGNV--QVTTVGNERSSvseDDSHLKVFCE--------LLGLETS 367
Cdd:cd14900   225 MDAMDII---------GFTPHERAGIFDLLAALLHIGNLtfEHDENSDRLGQ---LKSDLAPSSIwsrdaaatLLSVDAT 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  368 KVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF--SGKQHT---FIGVLDIYGFETF 442
Cdd:cd14900   293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVF 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  443 DVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENW 521
Cdd:cd14900   373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTL 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  522 LQKLYNNFVNkNSLFEKPRMSNSS--FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfhlcaaffqespvpssp 599
Cdd:cd14900   453 ASKLYRACGS-HPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY------------------- 512

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  600 fgamitvksakqvikpntkhfrttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETI 679
Cdd:cd14900   513 -------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567

                         650       660
                  ....*....|....*....|...
gi 568961013  680 RISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14900   568 RVARAGFPIRLLHDEFVARYFSL 590

MYSc_Myo35

cd14896

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

81-741

1.14e-129

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: 412.64 E-value: 1.14e-129

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14896     1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSSSNAHVE--DKVLasnPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR 238
Cdd:cd14896    80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKD 318
Cdd:cd14896   156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  319 FQMDVFKILAAILHLGNVQVTTVGNERSSVSE--DDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14896   236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAvsSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQHTF--IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd14896   316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  475 YMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14896   396 CQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQKCHYHHGD-HPSYAKPQLPLPVFTVRHYAG 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitvkSAKQVIKPNtkhfRTTVGNKFRSSLY 633
Cdd:cd14896   475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEA--------------EPQYGLGQG----KPTLASRFQQSLG 536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDK 713
Cdd:cd14896   537 DLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDR 616

                         650       660
                  ....*....|....*....|....*...
gi 568961013  714 KEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14896   617 ERCGAILSQVLGAESPLYHLGATKVLLK 644

MYSc_Myo38

cd14899

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

82-699

3.85e-116

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

Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 378.67 E-value: 3.85e-116

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 150
Cdd:cd14899     2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  151 NNRNQSIIVSGESGAGKTVSARYAMRYFATVS----------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDN 214
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCgtgnnnltnsesisppASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  215 SSRFGKYTEISF-DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQL------CASAQQSEFKHLKLGSAEEFNYTR 287
Cdd:cd14899   161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGGPQSFRLLNQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  288 MGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNER------------SSVSEDDSHL 355
Cdd:cd14899   241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfadearvmSSTTGAFDHF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  356 KVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGK--------- 426
Cdd:cd14899   321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  427 ------QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK 500
Cdd:cd14899   401 vddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  501 -MGILELLDEECLLPHGTDENWLQKLYNNFVNKNslfEKPRMSNSS-------FIIQHFADKVEYQCEGFLEKNRDTVYD 572
Cdd:cd14899   481 pIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKN---SHPHFRSAPliqrttqFVVAHYAGCVTYTIDGFLAKNKDSFCE 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  573 MLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14899   558 SAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP 637

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 568961013  653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14899   638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684

MYSc_Myo13

cd14875

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

83-741

1.73e-112

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: 367.21 E-value: 1.73e-112

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQM-ARNNRNQSIIVS 160
Cdd:cd14875     3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVS----KSSSNAHVEDKVLA----SNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14875    83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  233 -IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHL-KLGSAEEFNYTRmGGNTVI------EGVNDRADMV 304
Cdd:cd14875   163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLN-GGNTFVrrgvdgKTLDDAHEFQ 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  305 ETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVsEDDSHLKVFCELLGLETSKVAQWLcnrkIVTSSET 384
Cdd:cd14875   242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQI-ADETPFLTACRLLQLDPAKLRECF----LVKSKTS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  385 VVKPMTRPQ-AINARDALAKKIYAHLFDFIVEQINQALHFSG--KQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:cd14875   317 LVTILANKTeAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:cd14875   397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  541 MS-NSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcAAFFQESPVPSSPFGAmitvksakqvikpntkH 619
Cdd:cd14875   477 STiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNS-----TDEFIRTLLSTEKGLA----------------R 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  620 FRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14875   536 RKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568961013  700 GILMTQQELSL---SDKKEVCKVVL---HRLIQ-DSNQYQFGRTKIFFR 741
Cdd:cd14875   616 YLIMPRSTASLfkqEKYSEAAKDFLayyQRLYGwAKPNYAVGKTKVFLR 664

MYSc_Myo17

cd14879

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

82-740

6.75e-112

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: 364.95 E-value: 6.75e-112

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAESkLIYTY-SGIILVAMNPYKQLPIYGDAIIHAY-------SGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14879     5 AITSHLASRFRSD-LPYTRlGSSALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAH-VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14879    84 DQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  233 IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYT-RMGGNTVIEGV--NDRADMVETQKT 309
Cdd:cd14879   164 IGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLPLGPgsDDAEGFQELKTA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTT--VGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNR-KIVtSSEtVV 386
Cdd:cd14879   244 LKTLGFKRKHVAQICQLLAAILHLGNLEFTYdhEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKtKLV-RKE-LC 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  387 KPMTRP-QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFD---VNSFEQFCINYANEKLQQ 461
Cdd:cd14879   322 TVFLDPeGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHN 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMG--ILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKP 539
Cdd:cd14879   402 YVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGglLGILDDQTRRMPKKTDEQMLEALRKRFGNHSSFIAVG 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  540 RMS----NSSFIIQHFADKVEYQCEGFLEKNRDtvydmlveilraskfHLCAAFfqespvpsspfgaMITVKSAKQvikp 615
Cdd:cd14879   482 NFAtrsgSASFTVNHYAGEVTYSVEGFLERNGD---------------VLSPDF-------------VNLLRGATQ---- 529

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  616 ntkhfrttvgnkFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEF 695
Cdd:cd14879   530 ------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEF 597

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 568961013  696 YSRYGILMTQQELSLSDKKevckvVLHRLIQDSNQYQFGRTKIFF 740
Cdd:cd14879   598 CERYKSTLRGSAAERIRQC-----ARANGWWEGRDYVLGNTKVFL 637

MYSc_Myo37

cd14898

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

82-702

7.54e-108

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: 351.51 E-value: 7.54e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQlpIYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNrNQSIIVSG 161
Cdd:cd14898     2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFatVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDerNQIIGANMRTYL 241
Cdd:cd14898    77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  242 LEKSRVVFQSENERNYHIFYQLCASAqqsefkhlKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKdFQm 321
Cdd:cd14898   153 LEKSRVTHHEKGERNFHIFYQFCASK--------RLNIKNDFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIAN-FK- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  322 DVFKILAAILHLGNVQVTtvgNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDAL 401
Cdd:cd14898   223 SIEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSM 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  402 AKKIYAHLFDFIVEQINQALHFSGKQHtfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIP 481
Cdd:cd14898   300 ARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIE 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  482 WTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL--YNN-FVNKNslfekprmSNSSFIIQHFADKVEYQ 558
Cdd:cd14898   378 WPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNgFINTK--------ARDKIKVSHYAGDVEYD 449

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  559 CEGFLEKNRDtvydmlveilrasKFHLcaaffqespvpsSPFGAMITvksakqvikpNTKHFRTTVGNKFRSSLYLLMET 638
Cdd:cd14898   450 LRDFLDKNRE-------------KGQL------------LIFKNLLI----------NDEGSKEDLVKYFKDSMNKLLNS 494

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961013  639 LNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14898   495 INETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558

MYSc_Myo26

cd14887

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

81-741

1.23e-101

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276852 Cd Length: 725 Bit Score: 339.32 E-value: 1.23e-101

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAES-------KLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14887     1 PNLLENLYQRYNKAyinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  154 NQSIIVSGESGAGKTVSARYAMRYFATVS---KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14887    81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTrmggntviegvndrADMVETQKTF 310
Cdd:cd14887   161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA--ATQKSSAGEGDPES--------------TDLRRITAAM 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLC---NRKIVTSSETVVK 387
Cdd:cd14887   225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKClssGLKVTEASRKHLK 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  388 PMTRP--------------------------------QAINARDALAKKIYAHLFDFIVEQINQALHFSGK--------- 426
Cdd:cd14887   305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  427 -----QHTFIGVLDIYGFETF---DVNSFEQFCINYANEKlqqqfnLHVFKLEQ----EE--YMKEDIPWTLIDFYDNQP 492
Cdd:cd14887   385 tpsttGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANER------LHCFLLEQlilnEHmlYTQEGVFQNQDCSAFPFS 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  493 -------------VIDLI-EAKMGILELLDEECLLPH----------GTDENW------------LQKLYNNFVNKNSLF 536
Cdd:cd14887   459 fplastltsspssTSPFSpTPSFRSSSAFATSPSLPSslsslssslsSSPPVWegrdnsdlfyekLNKNIINSAKYKNIT 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  537 EKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfhlCAAFFQESPVPSSPFGAMITVKsakqvikpn 616
Cdd:cd14887   539 PALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-----CSTYTRLVGSKKNSGVRAISSR--------- 604

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  617 tkhfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFY 696
Cdd:cd14887   605 ----RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELW 680

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*
gi 568961013  697 SRYGILMTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14887   681 RRYETKLPMALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725

MYSc_Myo24A

cd14937

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

83-741

2.41e-96

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

Pssm-ID: 276897 Cd Length: 637 Bit Score: 321.96 E-value: 2.41e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLpiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14937     3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  163 SGAGKTVSARYAMRYFatVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd14937    78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTrMGGNTVIEGVNDRADMVETQKTFTLLGFKkDFQMD 322
Cdd:cd14937   156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYI-VNKNVVIPEIDDAKDFGNLMISFDKMNMH-DMKDD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  323 VFKILAAILHLGNVQVTTV-GNERSSVSE-DDSHLKVFCE---LLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd14937   234 LFLTLSGLLLLGNVEYQEIeKGGKTNCSElDKNNLELVNEisnLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd14937   314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFADKVEY 557
Cdd:cd14937   394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNFVIKHTVSDVTY 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  558 QCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvksakqVIKPNTKHFrttvgnKFRSSLYLLME 637
Cdd:cd14937   474 TITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES-------------LGRKNLITF------KYLKNLNNIIS 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  638 TLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAqSYPSRWTYLEFYSRYGIL--MTQQELSLSDKKE 715
Cdd:cd14937   535 YLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-FFQYKYTFDVFLSYFEYLdySTSKDSSLTDKEK 613

                         650       660
                  ....*....|....*....|....*.
gi 568961013  716 VCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd14937   614 VSMILQNTV--DPDLYKVGKTMVFLK 637

MYSc_Myo16

cd14878

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

82-741

2.18e-94

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 317.14 E-value: 2.18e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGDMDPHIFAVAEEAYKQMARNNRNQSII 158
Cdd:cd14878     2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  159 VSGESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF-DERNQIIGANM 237
Cdd:cd14878    81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  238 RTYLLEKSRVVFQSENERNYHIFYQLC--ASAQQSEFKHLKLGSAEEF-NYTRMGGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14878   160 YTYMLEKSRLVSQPPGQSNFLIFYLLMdgLSAEEKYGLHLNNLCAHRYlNQTMREDVSTAERSLNREKLAVLKQALNVVG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14878   240 FSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  395 INARDALAKKIYAHLFDFIVEQINQALH----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14878   320 EFYRDLLAKSLYSRLFSFLVNTVNCCLQsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  471 EQEEYMKEDIPWTLIDFYDNQP-VIDLIEAK-MGILELLDEECLLPHGTDENWLQKL--YNNFVNKNSLFEK-------- 538
Cdd:cd14878   400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLqsLLESSNTNAVYSPmkdgngnv 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  539 -PRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitvksakqvikpnt 617
Cdd:cd14878   480 aLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSK------------------------ 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  618 khfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14878   536 ---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLS 612

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568961013  698 RYGILMtqqELSLSDKK-----EVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14878   613 RYKPLA---DTLLGEKKkqsaeERCRLVLQQCKLQG--WQMGVRKVFLK 656

MYSc_Myo20

cd14881

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

82-740

6.44e-92

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 309.74 E-value: 6.44e-92

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFAESKLiYTYSGIILVAMNPYKQLPiygdAIIHAYSGQNMGDMdPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14881     2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYRDVG----NPLTLTSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAIILSG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  162 ESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDErnqiiGANMRT-- 239
Cdd:cd14881    76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYRTki 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  240 --YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKT-FTLLGFK 316
Cdd:cd14881   151 hcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAcLGILGIP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  317 kdFqMDVFKILAAILHLGNVQVTTvGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14881   231 --F-LDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNM 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  397 ARDALAKKIYAHLFDFIVEQIN--QALHFSGKQHT---FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14881   307 TRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  472 QEEYMKEDIPWTL-IDFYDNQPVIDLIEA-KMGILELLDEECLlPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQ 549
Cdd:cd14881   387 IESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIR 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfHLCAaffqespvpsspFGamitvksakqvIKPNTKHFRTTVGNkfr 629
Cdd:cd14881   466 HFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCN------------FG-----------FATHTQDFHTRLDN--- 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  630 sslylLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELS 709
Cdd:cd14881   517 -----LLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLR 591

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 568961013  710 LSDKKEV--CKVVL-----HRLIQDSN---QYQFGRTKIFF 740
Cdd:cd14881   592 RVEEKALedCALILqfleaQPPSKLSSvstSWALGKRHIFL 632

MYSc_Myo23

cd14884

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

81-732

3.87e-88

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: 300.67 E-value: 3.87e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS-------GQNMGDMDPHIFAVAEEAYKQMARNN 152
Cdd:cd14884     1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  153 RNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14884    80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  233 I---------GANMRTYLLEKSRVVFQSENERNYHIFYQL---CASAQQSE------FKHLKLGSAEEFNYTR-MGGNTV 293
Cdd:cd14884   160 QknmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARrnlvrnCGVYGLLNPDESHQKRsVKGTLR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  294 IEGVNDRADMVETQK---TFTLL-------GFKKDFQMDVFKILAAILHLGNvqvttvgnerssvseddSHLKVFCELLG 363
Cdd:cd14884   240 LGSDSLDPSEEEKAKdekNFVALlhglhyiKYDERQINEFFDIIAGILHLGN-----------------RAYKAAAECLQ 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  364 LETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAlHFSGKQ-------------HTF 430
Cdd:cd14884   303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRN-VLKCKEkdesdnediysinEAI 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  431 IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEE 510
Cdd:cd14884   382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKL 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  511 CLLPHG-TDENWLQKLYNNfVNKNSLFEK-------PRMSNSS----------FIIQHFADKVEYQCEGFLEKNRDTVYD 572
Cdd:cd14884   462 KNQGQKkTDDHFFRYLLNN-ERQQQLEGKvsygfvlNHDADGTakkqnikkniFFIRHYAGLVTYRINNWIDKNSDKIET 540

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  573 MLVEILRASKfhlcaaffqespvpsspfgaMITVKSAkqVIKPNTKHFrTTVGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14884   541 SIETLISCSS--------------------NRFLREA--NNGGNKGNF-LSVSKKYIKELDNLFTQLQSTDMYYIRCFLP 597

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRwtylefysrygilMTQQELSLSDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14884   598 NAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK-------------IPKKETAAALKEQIAKELEKCNSNTDIEYQ 664

MYSc_Myo18

cd01386

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

83-741

5.30e-87

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: 297.68 E-value: 5.30e-87

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01386     3 VLHTLRQRYG-ANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  163 SGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd01386    82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRA-DMVETQKTFTLLGFKKDFQM 321
Cdd:cd01386   162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAaAFSKLQAAMKTLGISEEEQR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  322 DVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRK---IVTSSETVVKPMTRPQ----- 393
Cdd:cd01386   242 AIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHlsgGPQQSTTSSGQESPARsssgg 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  394 ----AINARDALAKKIYAHLFDFIVEQINQALhfSGKQHTF--IGVLDIYGFETFDVN------SFEQFCINYANEKLQQ 461
Cdd:cd01386   322 pkltGVEALEGFAAGLYSELFAAVVSLINRSL--SSSHHSTssITIVDTPGFQNPAHSgsqrgaTFEDLCHNYAQERLQL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDN-QPVIDLI---------------EAKMGILELLDEECLLPHGTDENWLQKL 525
Cdd:cd01386   400 LFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSDDTFLERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  526 YNNF----VNKNSLFEKPRMSNSSFIIQHF--ADKVEYQCEGFLeknrdtvydmlveilRASKFHLCA----AFFQESpv 595
Cdd:cd01386   480 FSHYgdkeGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGWL---------------KAAKENPSAqnatQLLQES-- 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  596 pSSPFGAmitVKsakqvikpntkhfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPN------DEKMPFEFDSKRIVQ- 668
Cdd:cd01386   543 -QKETAA---VK-------------RKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPAAGDELLDv 605

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  669 -----QLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVC--KVVLHRLIQ----DSNQYQFGRTK 737
Cdd:cd01386   606 pllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVAdeRKAVEELLEeldlEKSSYRIGLSQ 685


                  ....
gi 568961013  738 IFFR 741
Cdd:cd01386   686 VFFR 689

MYSc_Myo44

cd14905

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

93-741

2.58e-81

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

Pssm-ID: 276870 Cd Length: 673 Bit Score: 281.21 E-value: 2.58e-81

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   93 ESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGdMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSA 171
Cdd:cd14905    12 KKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  172 RYAMRYFATVSKSSSNaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRVVFQS 251
Cdd:cd14905    90 KIIIQYLLTTDLSRSK-YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQN 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  252 ENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAIL 331
Cdd:cd14905   169 KGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFII 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  332 HLGNVQVTTvGNERSSVsEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSEtvvkpmtrpqAINARDALAKKIYAHLFD 411
Cdd:cd14905   249 ILGNVTFFQ-KNGKTEV-KDRTLIESLSHNITFDSTKLENILISDRSMPVNE----------AVENRDSLARSLYSALFH 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  412 FIVEQINQALHFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPW-TLIDFYDN 490
Cdd:cd14905   317 WIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDN 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  491 QPVIDLIEAKMGILELLDEECllpHGTDENWLQKLyNNFVNKNSLF-EKPrmsnSSFIIQHFADKVEYQCEGFLEKNRDT 569
Cdd:cd14905   396 EESVEMMEKIINLLDQESKNI---NSSDQIFLEKL-QNFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDE 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  570 VYDML-----------------VEILRASKFHLCAAFFQESPVPSSPFGAMITVKSA-----KQVIKPNTKH------FR 621
Cdd:cd14905   468 ILQRTnvlhknsitkylfsrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLSCgsnnpNNVNNPNNNSggggggGN 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  622 TTVGNKFRSSLYLLMETLNATTP------HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEF 695
Cdd:cd14905   548 SGGGSGSGGSTYTTYSSTNKAINnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIF 627

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 568961013  696 YSRYGILMTQQE--LSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14905   628 FDRFSFFFQNQRnfQNLFEKLKENDINIDSILPPP--IQVGNTKIFLR 673

MYSc_Myo12

cd14874

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

82-741

7.68e-78

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

Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 270.20 E-value: 7.68e-78

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYsgqnmgdmdpHIFAVAEEAYKQMARNNRN-QSIIVS 160
Cdd:cd14874     2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  161 GESGAGKTVSARYAMRYFATVSKSS-SNAHVEdkvlASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR- 238
Cdd:cd14874    71 GESGSGKSYNAFQVFKYLTSQPKSKvTTKHSS----AIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKy 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNT--VIEGVNDRADMVETQKTftlLGFK 316
Cdd:cd14874   146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTenIQSDVNHFKHLEDALHV---LGFS 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  317 KDFQMDVFKILAAILHLGNVQVTTVGNerSSVSED------DSHLKVFCELLGLEtskVAQWLcnrKIVTSSETVVKPMT 390
Cdd:cd14874   223 DDHCISIYKIISTILHIGNIYFRTKRN--PNVEQDvveignMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDGTTID 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  391 RPQAINARDALAKKIYAHLFDFIVEQInqALHFSGKQHT-FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14874   295 LNAALDNRDSFAMLIYEELFKWVLNRI--GLHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  470 LEQEEYMKEDIPwtlIDF-----YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKnSLFEKPRMSN 543
Cdd:cd14874   373 DQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDR-SSYGKARNKE 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  544 S-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQespvpSSPFGAMITVKSAKQVIKPNTKHfrt 622
Cdd:cd14874   449 RlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE-----SYSSNTSDMIVSQAQFILRGAQE--- 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  623 tvgnkfrsslylLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14874   521 ------------IADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568961013  703 MTQQELSLSDKKEVCKVVLH-RLIQDSNQYQFGRTKIFFR 741
Cdd:cd14874   589 LPGDIAMCQNEKEIIQDILQgQGVKYENDFKIGTEYVFLR 628

MYSc_Myo21

cd14882

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

83-741

6.46e-77

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276848 Cd Length: 642 Bit Score: 267.76 E-value: 6.46e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14882     3 ILEELRHRY-LMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  163 SGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd14882    82 SYSGKTTNARLLIKHLCYLGDGNRG--ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  243 EKSRVVFQSENERNYHIFYQLCASAQQSE-FKHLKLGSAEEFNYTRMGGNTVIEGV----NDRADMVETQKTFTLLGFKK 317
Cdd:cd14882   160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYLRIPPEVPPSKLkyrrDDPEGNVERYKEFEEILKDL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  318 DFQMD----VFKILAAILHLGNVQVttVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14882   240 DFNEEqletVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  394 AINARDALAKKIYAHLFDFIVEQINQALHFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14882   318 ARDARDVLASTLYSRLVDWIINRINMKMSFPravfGDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFI 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  470 LEQEEYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTdenwlQKLYNNFVNKNSLFEKPrMSNSSFII 548
Cdd:cd14882   397 SEMLEMEEEDIPTINLRFYDNKTAVDqLMTKPDGLFYIIDDASRSCQDQ-----NYIMDRIKEKHSQFVKK-HSAHEFSV 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  549 QHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvpsspfgamiTVKSAKQVIKPNTKHFRTTVGNKF 628
Cdd:cd14882   471 AHYTGRIIYDAREFADKNRDFVPPEMIETMRSS-----------------------LDESVKLMFTNSQVRNMRTLAATF 527

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  629 RSSLYLLMETL----NATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14882   528 RATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAF 607

                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 568961013  705 QQELSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14882   608 DFDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642

MYSc_Myo32

cd14893

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

84-699

1.54e-65

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

Pssm-ID: 276858 Cd Length: 741 Bit Score: 237.18 E-value: 1.54e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN----------MGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14893     4 LYTLRARYRMEQ-VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAH-----------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14893    83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  223 EISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQ--SEFKHLKLG-SAEEFNYTRMGGNTVIEGVND 299
Cdd:cd14893   163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNkCVNEFVMLKQADPLATNFALD 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  300 RADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQV---------------TTVGNERSSVSEDDSHLKVFCELLGL 364
Cdd:cd14893   243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLAAKLLEV 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  365 ETSKVAQWLCNRKIVT--SSETV--VKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAL-----HFSGK----QHTFI 431
Cdd:cd14893   323 EPVVLDNYFRTRQFFSkdGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSniviNSQGV 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  432 GVLDIYGFETFD--VNSFEQFCINYANEK-----LQQQFNLHVFKLEQEEYMKED--IPWTLIDF-YDNQPVIDLIEAK- 500
Cdd:cd14893   403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKvhhfyVQNTLAINFSFLEDESQQVENrlTVNSNVDItSEQEKCLQLFEDKp 482

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  501 MGILELLDEECLLPHGTDENWLQKLY--NNFV------NKNSLFEKPRMSNSS-----FIIQHFADKVEYQCEGFLEKNR 567
Cdd:cd14893   483 FGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVgglsrpNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSKNM 562

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  568 DTVYDMLVEILRASKFHLCAAffqespVPSSPFGAMITVKSAKQVIKpntkhfRTTVGNKFRSSLY-------------- 633
Cdd:cd14893   563 LSISSTCAAIMQSSKNAVLHA------VGAAQMAAASSEKAAKQTEE------RGSTSSKFRKSASsaresknitdsaat 630

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961013  634 -------LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14893   631 dvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703

Motor_domain

cd01363

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

104-227

2.04e-44

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.

Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 158.66 E-value: 2.04e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  104 ILVAMNPYKQLPIYGDA-IIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVS 182
Cdd:cd01363     1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013  183 KSSSNA--------------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFD 227
Cdd:cd01363    81 FNGINKgetegwvylteitvTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139

MYSc_Myo24B

cd14938

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

81-739

6.25e-42

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

Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 165.39 E-value: 6.25e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14938     1 PSVLYHLKERF-KNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  160 SGESGAGKTVSARYAMRYFATVSKSS------SNAHVEDKVLAS----------------NPITEAVGNAKTTRNDNSSR 217
Cdd:cd14938    80 SGESGSGKSEIAKNIINFIAYQVKGSrrlptnLNDQEEDNIHNEentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  218 FGKYTEISFDERnQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEefNYTRMGGNTVIEGV 297
Cdd:cd14938   160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIE--NYSMLNNEKGFEKF 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  298 NDRAD-MVETQKTFTLLgFKKDFQMD-VFKILAAILHLGNVQVTTV---------------------------GNERSSV 348
Cdd:cd14938   237 SDYSGkILELLKSLNYI-FDDDKEIDfIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilseleNSEDIGL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  349 SEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSeTVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQH 428
Cdd:cd14938   316 DENVKNLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNIN 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  429 TF---IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTL-IDFYDNQPVID-LIEAKMGI 503
Cdd:cd14938   395 INtnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGS 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  504 LELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR---MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRA 580
Cdd:cd14938   475 LFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  581 SKFHLCAAFFQESPVPSSpfgAMITVKSAKQVIKPNTKHFRTTVGNK-------FRSSLYLLMETLNATTPHYVRCIKPN 653
Cdd:cd14938   555 SENEYMRQFCMFYNYDNS---GNIVEEKRRYSIQSALKLFKRRYDTKnqmavslLRNNLTELEKLQETTFCHFIVCMKPN 631

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  654 DEK-MPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMtqqelslSDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14938   632 ESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN-------EDLKEKVEALIKSYQISNYEWM 704


                  ....*..
gi 568961013  733 FGRTKIF 739
Cdd:cd14938   705 IGNNMIF 711

MYSc_Myo33

cd14894

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

187-705

8.15e-35

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

Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 144.12 E-value: 8.15e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  187 NAHVEDK---VLASNPITEAVGNAKTTRNDNSSRFGKYT--EISFDERN---QIIGANMRTYLLEKSRVVFQ------SE 252
Cdd:cd14894   239 NPHAAKKlsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTtlQVAFGLHPwefQICGCHISPFLLEKSRVTSErgresgDQ 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  253 NERNYHIFYQLCASAQQSEF-----KHLKLGSAEEFNYTRMG-GNTVIEGVNDRADM----VETQKT----FTLLGFKKD 318
Cdd:cd14894   319 NELNFHILYAMVAGVNAFPFmrllaKELHLDGIDCSALTYLGrSDHKLAGFVSKEDTwkkdVERWQQvidgLDELNVSPD 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  319 FQMDVFKILAAILHLGNVQVT--TVGNE--RSSVSEDDSHLKVfCELLGL-ETSKVAQWLCNRKIV--TSSETVVKPMTR 391
Cdd:cd14894   399 EQKTIFKVLSAVLWLGNIELDyrEVSGKlvMSSTGALNAPQKV-VELLELgSVEKLERMLMTKSVSlqSTSETFEVTLEK 477

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  392 PQAINARDALAKKIYAHLFDFIVEQINQALHFS-----GKQH------------TFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14894   478 GQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINY 557

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  455 ANEKLQQqfnlhvfKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQ-----KLY-NN 528
Cdd:cd14894   558 LSEKLYA-------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFvRN 630

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  529 FVNKNS--LFEKPR-MSNSS-----------FIIQHFADKVEYQCEGFLEKNRDTVY-DMLVEILRASKFHLCAAFFQES 593
Cdd:cd14894   631 IYDRNSsrLPEPPRvLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYaNLLVGLKTSNSSHFCRMLNESS 710

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  594 PVPSSPFGAMITVKSAKQVIKpNTKHFrttVGnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRAC 673
Cdd:cd14894   711 QLGWSPNTNRSMLGSAESRLS-GTKSF---VG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQ 785

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 568961013  674 GV---LETIRISAQSYP----SRWTYLefySRYGILMTQ 705
Cdd:cd14894   786 RLirqMEICRNSSSSYSaidiSKSTLL---TRYGSLLRE 821

PRK03918

DNA double-strand break repair ATPase Rad50;

890-1240

8.88e-14

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 8.88e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  890 RVQRLQKKLEDQNRENHGLVEKLTSLAALR--VGDLEK---------VQKLEAELEKAATHRHSYEEKgrryRDTVEERL 958
Cdd:PRK03918  339 RLEELKKKLKELEKRLEELEERHELYEEAKakKEELERlkkrltgltPEKLEKELEELEKAKEEIEEE----ISKITARI 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  959 SKLQKHNAEL-------------------ELQRERAEQMLQEKSEELK------EKMDKLTRQLFDDVQKEEQQRLVLEK 1013
Cdd:PRK03918  415 GELKKEIKELkkaieelkkakgkcpvcgrELTEEHRKELLEEYTAELKriekelKEIEEKERKLRKELRELEKVLKKESE 494

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1014 GFELKTQAyeKQIESLREEIKALKDErsqlhhQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhvq 1093
Cdd:PRK03918  495 LIKLKELA--EQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK--- 563

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1094 sQKREMRERMSEVTKQLLES--YDIEDVRSRLsvEDLEhlnedgELWFAYEGLKKATRVLESHFQSQKDCYE------KE 1165
Cdd:PRK03918  564 -KLDELEEELAELLKELEELgfESVEELEERL--KELE------PFYNEYLELKDAEKELEREEKELKKLEEeldkafEE 634

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961013 1166 IEGLNFKVVHLSQEINHLQKLFREETdiNESIRHEVTRLTSEnmmIPDFKQQISELERQKQDLES---RLKEQAEKIE 1240
Cdd:PRK03918  635 LAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRE---LAGLRAELEELEKRREEIKKtleKLKEELEERE 707

SMC_prok_B

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

893-1240

1.66e-13

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 1.66e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   893 RLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVE---ERLSKLQKHNAELE 969
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   970 LQRERAEQMLQEKSEELKEkmdkltrqlfDDVQKEEQQRLVlekgfelktQAYEKQIESLREEIKALKDERSQLHhqlEE 1049
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAE----------AEAEIEELEAQI---------EQLKEELKALREALDELRAELTLLN---EE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEkHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1130 HLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN--------HLQKLFREETDINESIRHEV 1201
Cdd:TIGR02168  898 ELSEELR---ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleEAEALENKIEDDEEEARRRL 974

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961013  1202 TRLTSE-------NMM-IPDFKQQ---ISELERQKQDLESRLKEQAEKIE 1240
Cdd:TIGR02168  975 KRLENKikelgpvNLAaIEEYEELkerYDFLTAQKEDLTEAKETLEEAIE 1024

SMC_prok_B

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

874-1198

2.18e-13

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.18e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   874 RFQNIRRFVLNIQL---TYRVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdleKVQKLEAELEkaaTHRHSYEEkgrry 950
Cdd:TIGR02168  214 RYKELKAELRELELallVLRLEELREELEELQEELKEAEEELEELTA-------ELQELEEKLE---ELRLEVSE----- 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   951 rdtVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqLFDDVQKEEQQRLVLEKGFELKTQAYE---KQIE 1027
Cdd:TIGR02168  279 ---LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-LEAQLEELESKLDELAEELAELEEKLEelkEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1028 SLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISefeKEIELLQAQKIDVEKHVQSQKREMRERMSEvt 1107
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLKK-- 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1108 kqlLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKAtrvleshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLF 1187
Cdd:TIGR02168  430 ---LEEAELKELQAELEELEEELEELQEELERLEEALEEL--------REELEEAEQALDAAERELAQLQARLDSLERLQ 498

                          330
                   ....*....|.
gi 568961013  1188 REETDINESIR 1198
Cdd:TIGR02168  499 ENLEGFSEGVK 509

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

849-1239

1.29e-12

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: 72.84 E-value: 1.29e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   849 RYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQR--LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV 926
Cdd:pfam15921  268 RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   927 QK----LEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLfDDVQ 1002
Cdd:pfam15921  348 EKqlvlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRREL-DDRN 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1003 KEEQQRLVLEKGFELKTQA-YEKQIESLREEIKALkDERSQLHHQLEEgqvTSDRLKGEVARLSKQAKTISEFEKEIEll 1081
Cdd:pfam15921  426 MEVQRLEALLKAMKSECQGqMERQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSERTVS-- 499

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1082 qaqkiDVEKHVQSQKREMRERMSEVTKqllesydiedVRSR--LSVEDLEHLNEDGELWfayeglkkatrvleSHFQSQK 1159
Cdd:pfam15921  500 -----DLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGDHL--------------RNVQTEC 550

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1160 DCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRLKEQAEKI 1239
Cdd:pfam15921  551 EALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE---INDRRLELQEFKILKDKKDAKIRELEARV 627

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

945-1240

5.07e-12

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.87 E-value: 5.07e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   945 EKGRRYRDTVEERLSKLQKHNAELELQRERaeqmLQEKSEElKEKMDKLTRQLfddvQKEEQQRLVLEK-GFELKTQAYE 1023
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLER----LRREREK-AERYQALLKEK----REYEGYELLKEKeALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1024 KQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQA-----KTISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAEKERELEDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1099 MRERMSEVTKQLLESYDIEdvrsrlsvEDLEHLNEDGELWFA-YEGLKKATRVLESH-----------FQSQKDcYEKEI 1166
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELE--------REIEEERKRRDKLTEeYAELKEELEDLRAEleevdkefaetRDELKD-YREKL 394

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961013  1167 EGLNfkvvhlsQEINHLQKLFREETDINESIRHEVTRLtseNMMIPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:TIGR02169  395 EKLK-------REINELKRELDRLQEELQRLSEELADL---NAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458

SMC_prok_B

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

922-1238

9.45e-12

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 9.45e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   922 DLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEE-----------RLSKLQKHNAELELQRERAEQMLQEKSEELKEKM 990
Cdd:TIGR02168  187 NLDRLEDILNELERQLKSLERQAEKAERYKELKAElrelelallvlRLEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   991 DKLTRQLFDDVQKEEQQRLVLEKGFELKT--QAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQ- 1067
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKl 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1068 ---AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSvEDLEHLNEDgelwfayegL 1144
Cdd:TIGR02168  347 eelKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE-ARLERLEDR---------R 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1145 KKATRVLESHFQSQKdcyEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSEnmmIPDFKQQISELeRQ 1224
Cdd:TIGR02168  417 ERLQQEIEELLKKLE---EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA---LDAAERELAQL-QA 489

                          330
                   ....*....|....
gi 568961013  1225 KQDLESRLKEQAEK 1238
Cdd:TIGR02168  490 RLDSLERLQENLEG 503

SMC_prok_B

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

925-1240

2.77e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 2.77e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   925 KVQKLEAELEKAAThrhsyEEKGRRYRDTVEERLSKLQKhnaeLELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKE 1004
Cdd:TIGR02168  171 KERRKETERKLERT-----RENLDRLEDILNELERQLKS----LERQAEKAER-YKELKAELRELELALLVLRLEELREE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1005 EQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQ 1084
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1085 KIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRLSvedlehlnedgELWFAYEGLKKATRVLESHFQSQKDCY- 1162
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELE-----------ELEAELEELESRLEELEEQLETLRSKVa 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1163 --EKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE--NMMIPDFKQQISELERQKQDLESRLKEQAEK 1238
Cdd:TIGR02168  390 qlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelQAELEELEEELEELQEELERLEEALEELREE 469


                   ..
gi 568961013  1239 IE 1240
Cdd:TIGR02168  470 LE 471

PRK02224

DNA double-strand break repair Rad50 ATPase;

895-1238

3.01e-11

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 3.01e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  895 QKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYR------DTVEERLSKLQKHNAEL 968
Cdd:PRK02224  191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreelETLEAEIEDLRETIAET 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  969 ELQRERAEQMLQEKSEELKEKMDKLTRQL----FDDVQKE--EQQRLVLEKGFE----------LKTQAYEKQIESLREE 1032
Cdd:PRK02224  271 EREREELAEEVRDLRERLEELEEERDDLLaeagLDDADAEavEARREELEDRDEelrdrleecrVAAQAHNEEAESLRED 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1033 IKALKDERSQLHhqlEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVE---KHVQSQKREMRERMSEVTKQ 1109
Cdd:PRK02224  351 ADDLEERAEELR---EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPvdlGNAEDFLEELREERDELRER 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1110 LLE-SYDIEDVRSRlsVEDLEHLNEDG---ELWFAYEGLKKATRVLEShfQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:PRK02224  428 EAElEATLRTARER--VEEAEALLEAGkcpECGQPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERAED 503

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568961013 1186 LFREETDIN--ESIRHEVTRLTSENMMIPDFKQ-QISELERQKQDLESRLKEQAEK 1238
Cdd:PRK02224  504 LVEAEDRIErlEERREDLEELIAERRETIEEKReRAEELRERAAELEAEAEEKREA 559

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

896-1243

3.96e-11

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: 67.35 E-value: 3.96e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   896 KKLEDQNRENHGLVEKltslaalrvgDLEKVQKLEAELEKAAT-------HRHSYEEkgrrYRDTVEERLSKLQKHNAEL 968
Cdd:TIGR04523  127 NKLEKQKKENKKNIDK----------FLTEIKKKEKELEKLNNkyndlkkQKEELEN----ELNLLEKEKLNIQKNIDKI 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   969 ELQRERAEQMLQeKSEELKEKMDKLTRQLfddvQKEEQQRLVLEKGFELKTQAYEK---QIESLREEIKALKDERSQLHH 1045
Cdd:TIGR04523  193 KNKLLKLELLLS-NLKKKIQKNKSLESQI----SELKKQNNQLKDNIEKKQQEINEkttEISNTQTQLNQLKDEQNKIKK 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1046 QLEEGQVTSDRLKGEVARLSKQAKTIsefEKEIELLQAQKI-DVEKHVQSQKREMRERMSEVTKQLLESY--------DI 1116
Cdd:TIGR04523  268 QLSEKQKELEQNNKKIKELEKQLNQL---KSEISDLNNQKEqDWNKELKSELKNQEKKLEEIQNQISQNNkiisqlneQI 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1117 EDVRSRLSVEDLEHLNEDGELwfayeglKKATRVLEShFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE-ETDI-- 1193
Cdd:TIGR04523  345 SQLKKELTNSESENSEKQREL-------EEKQNEIEK-LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQkDEQIkk 416

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961013  1194 ----NESIRHEVTRL----TSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEGFS 1243
Cdd:TIGR04523  417 lqqeKELLEKEIERLketiIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474

SMC_prok_B

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

960-1241

1.01e-10

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 1.01e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   960 KLQKHNAELELQRERAE-QMLQEKSEELKEKMDKLTRQlfddVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKD 1038
Cdd:TIGR02168  171 KERRKETERKLERTRENlDRLEDILNELERQLKSLERQ----AEKAERYKELKAELRELELALLVLRLEELREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1039 ERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQ----AQKIDVEKhVQSQKREMRERMSEVTKQLLE-S 1113
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLE---VSELEEEIEELQkelyALANEISR-LEQQKQILRERLANLERQLEElE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1114 YDIEDVRSRLsVEDLEHLNEdgelwfayegLKKATRVLESHFQSQkdcyEKEIEGLNFKVVHLSQEINHLQKLFREETDI 1193
Cdd:TIGR02168  323 AQLEELESKL-DELAEELAE----------LEEKLEELKEELESL----EAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 568961013  1194 NESIRHEVTRLTSenmmipdfkqQISELERQKQDLESRLKEQAEKIEG 1241
Cdd:TIGR02168  388 VAQLELQIASLNN----------EIERLEARLERLEDRRERLQQEIEE 425

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

848-1150

1.14e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.14e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  848 RRYRKLLQEHKavilQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRV---GDLE 924
Cdd:COG1196   213 ERYRELKEELK----ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeleEAQA 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  925 KVQKLEAELEKAATHRHSYEEKGRRYRDTVEE----------RLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLT 994
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEEleeelaeleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  995 RQLFDDVQKEEQQRLVLEKGFELKTQAYE--KQIESLREEIKALKDERSQLHHQLEEGQvtsDRLKGEVARLSKQAKTIS 1072
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAElaAQLEELEEAEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE 445

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961013 1073 EFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTkQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRV 1150
Cdd:COG1196   446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522

SMC_prok_B

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

850-1079

2.36e-10

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 2.36e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   850 YRKLLQEHKAVILQKYARAWLARRRFQNIRRfvLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKL 929
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLER--QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   930 EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQ-------MLQEKSEELKEKMDKLTRQLFDDVQ 1002
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledrrerLQQEIEELLKKLEEAELKELQAELE 443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1003 KEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHH----------QLEEGQVTSD----------RLKGEVA 1062
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqarldslerLQENLEGFSEgvkallknqsGLSGILG 523

                          250
                   ....*....|....*..
gi 568961013  1063 RLSKQAKTISEFEKEIE 1079
Cdd:TIGR02168  524 VLSELISVDEGYEAAIE 540

PRK02224

DNA double-strand break repair Rad50 ATPase;

896-1240

3.40e-10

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 3.40e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  896 KKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERA 975
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  976 EQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktqAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSD 1055
Cdd:PRK02224  352 DD-LEERAEELREEAAELESELEEAREAVEDRREEIE--------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1056 RLKGEVARLSKQAKTISEFEKEIELLQA--------QKIDVEKHVQSQKrEMRERMSEVTKQLLesyDIEDVRSRLSvED 1127
Cdd:PRK02224  423 ELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIE-EDRERVEELEAELE---DLEEEVEEVE-ER 497

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1128 LEHLnedgelwfayEGLKKAtrvleshfqsqkdcyEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:PRK02224  498 LERA----------EDLVEA---------------EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 568961013 1208 -----------NMMIPDFKQQISELERQKQDLESRLkEQAEKIE 1240
Cdd:PRK02224  553 aeekreaaaeaEEEAEEAREEVAELNSKLAELKERI-ESLERIR 595

YhaN

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

923-1239

9.83e-10

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 9.83e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  923 LEKVQKLEAELEKAATHRHSYEEKgRRYRDTVEERLSKLQKHNAELELQRERAEQM------------LQEKSEELKEKM 990
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLlqllplyqeleaLEAELAELPERL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  991 DKLTRQLFDDVQKEEQQRLV----------LEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGE 1060
Cdd:COG4717   149 EELEERLEELRELEEELEELeaelaelqeeLEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1061 VARLSKQAKTISEFEK-------------------------------------EIELLQAQKIDVEKHVQSQKREMRERM 1103
Cdd:COG4717   229 LEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflVLGLLALLFLLLAREKASLGKEAEELQ 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1104 SEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHF-QSQKDCYEKEIEGL-NFKVVHLSQEIN 1181
Cdd:COG4717   309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEeELQLEELEQEIAALlAEAGVEDEEELR 388

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961013 1182 HLQKLFREETDINE---SIRHEVTRLTSENMMIPDF------KQQISELERQKQDLESRLKEQAEKI 1239
Cdd:COG4717   389 AALEQAEEYQELKEeleELEEQLEELLGELEELLEAldeeelEEELEELEEELEELEEELEELREEL 455

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

923-1115

2.20e-09

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: 59.17 E-value: 2.20e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  923 LEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELE-LQRERAEqmLQEKSEELKEKMDKLTRQLfDDV 1001
Cdd:COG1579     9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEdLEKEIKR--LELEIEEVEARIKKYEEQL-GNV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1002 QKEEQQrlvlekgfelktQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQ-AKTISEFEKEIEL 1080
Cdd:COG1579    86 RNNKEY------------EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAElEEKKAELDEELAE 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568961013 1081 LQAQkidvEKHVQSQKREMRERMSEvtkQLLESYD 1115
Cdd:COG1579   154 LEAE----LEELEAEREELAAKIPP---ELLALYE 181

PRK03918

DNA double-strand break repair ATPase Rad50;

988-1238

2.38e-09

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.38e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  988 EKMDKLTRQL--FDDVQKEEQQRLVLEKGFELKTQAYEKQI---ESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA 1062
Cdd:PRK03918  145 ESREKVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELE 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1063 RLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQllesydIEDVRSRlsVEDLEHLNEDGELWF 1139
Cdd:PRK03918  225 KLEKEVKELEELKEEIEELEKELESLEGSKRKleeKIRELEERIEELKKE------IEELEEK--VKELKELKEKAEEYI 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1140 AYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREEtdinESIRHEVTRLTSENMMIPDFKQQIS 1219
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL----KELEKRLEELEERHELYEEAKAKKE 372

                         250
                  ....*....|....*....
gi 568961013 1220 ELERQKQDLESRLKEQAEK 1238
Cdd:PRK03918  373 ELERLKKRLTGLTPEKLEK 391

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

890-1129

2.70e-09

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.70e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEK-GRRYRDTVEERLSKLQKHNAEL 968
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIPEIQAELSKL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   969 ELQRERAEQMLQEKSEELKEKmDKLTRQLFDDVQKEEQQRLVLE---KGFELKTQAYEKQIESLREEIKALKDERSQLHH 1045
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRL-TLEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLES 882

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1046 QLEEgqvtsdrLKGEVARLSKQaktISEFEKEIELLQAQkIDVEKHVQSQKREMRERMSEVTKQLLESY--DIEDVRSRL 1123
Cdd:TIGR02169  883 RLGD-------LKKERDELEAQ---LRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKgeDEEIPEEEL 951


                   ....*.
gi 568961013  1124 SVEDLE 1129
Cdd:TIGR02169  952 SLEDVQ 957

YhaN

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

879-1240

4.06e-09

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 4.06e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  879 RRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYrdtveERL 958
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE-------EELEELEAELEELREELEKLEKLLQLL-----PLY 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  959 SKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLtRQLFDDVQKEEQQrlvLEKGFELKTQAYEKQIESLREEIKALKD 1038
Cdd:COG4717   132 QELEALEAELAELPERLEE-LEERLEELRELEEEL-EELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQ 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1039 ERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEK-------------------------------------EIELL 1081
Cdd:COG4717   207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflVLGLL 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1082 QAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHF-QSQKD 1160
Cdd:COG4717   287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEeELQLE 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1161 CYEKEIEGL-NFKVVHLSQEINHLQKLFREETDINE---SIRHEVTRLTSENMMIPDF-------------KQQISELER 1223
Cdd:COG4717   367 ELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEeleELEEQLEELLGELEELLEAldeeeleeeleelEEELEELEE 446

                         410
                  ....*....|....*..
gi 568961013 1224 QKQDLESRLKEQAEKIE 1240
Cdd:COG4717   447 ELEELREELAELEAELE 463

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

849-1185

4.37e-09

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 4.37e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   849 RYRKLLQEhkaviLQKYaRAWLARRRFQNIRRfvlniqltyRVQRLQKKLEDQNREnhglVEKLTslaalrvgdlEKVQK 928
Cdd:TIGR02169  212 RYQALLKE-----KREY-EGYELLKEKEALER---------QKEAIERQLASLEEE----LEKLT----------EEISE 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   929 LEAELEKAATHRhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELkEKMDKLTRQLFDDVQKEEQQR 1008
Cdd:TIGR02169  263 LEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLEAEIDKLLAEI 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1009 LVLEKgfelKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVarlskqaktiSEFEKEIELLQaQKIDV 1088
Cdd:TIGR02169  339 EELER----EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----------KDYREKLEKLK-REINE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1089 EKHVQSQKREMRERMSEvtkqllesyDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShFQSQKDCYEKEIEG 1168
Cdd:TIGR02169  404 LKRELDRLQEELQRLSE---------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-LAADLSKYEQELYD 473

                          330
                   ....*....|....*..
gi 568961013  1169 LNFKVVHLSQEINHLQK 1185
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQR 490

PRK03918

DNA double-strand break repair ATPase Rad50;

862-1241

5.33e-09

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.33e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  862 LQKYARAW--------LARRRFQNIRRFvlnIQLTYRVQRL----QKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKL 929
Cdd:PRK03918  157 LDDYENAYknlgevikEIKRRIERLEKF---IKRTENIEELikekEKELEEVLREINEISSELPELR-------EELEKL 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  930 EAELEKAATHRHSYEEKgrryrdtvEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqlFDDVQKEEQQRL 1009
Cdd:PRK03918  227 EKEVKELEELKEEIEEL--------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--LKELKEKAEEYI 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1010 VLEK---GFELKTQAYEKQIESLREEIKALKDersqlhhQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKI 1086
Cdd:PRK03918  297 KLSEfyeEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1087 DVEKHVQSQKREMRERMSEVTKQLLE----SYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVL--------ESH 1154
Cdd:PRK03918  370 KKEELERLKKRLTGLTPEKLEKELEElekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEH 449

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1155 FQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREEtdinESIRHEVTRLTSENMMIPDFKQ--------QISELERQKQ 1226
Cdd:PRK03918  450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELREL----EKVLKKESELIKLKELAEQLKEleeklkkyNLEELEKKAE 525

                         410
                  ....*....|....*
gi 568961013 1227 DLEsRLKEQAEKIEG 1241
Cdd:PRK03918  526 EYE-KLKEKLIKLKG 539

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

872-1113

5.48e-09

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.52 E-value: 5.48e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   872 RRRFQNIRRFVLNIQLTyRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEE-KGRRY 950
Cdd:pfam17380  359 KRELERIRQEEIAMEIS-RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREV 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   951 RDTVEERLSKLQKHNAElELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYekqiesLR 1030
Cdd:pfam17380  438 RRLEEERAREMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM------IE 510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1031 EEIKalkdeRSQLHHQLEEGQVTsdrlkgeVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKR---EMRERMSEVT 1107
Cdd:pfam17380  511 EERK-----RKLLEKEMEERQKA-------IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMM 578


                   ....*.
gi 568961013  1108 KQLLES 1113
Cdd:pfam17380  579 RQIVES 584

PRK03918

DNA double-strand break repair ATPase Rad50;

851-1123

1.13e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.13e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  851 RKLLQEHKAVILQKYarawlaRRRFQNIRRFVLNI-----QLTYRVQRLQKKLEDQNR--ENHGLVEKLTSL-AALRVGD 922
Cdd:PRK03918  443 RELTEEHRKELLEEY------TAELKRIEKELKEIeekerKLRKELRELEKVLKKESEliKLKELAEQLKELeEKLKKYN 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  923 LEKVQKLEAELEKaaTHRHSYEEKGRryRDTVEERLSKLQkhnaELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQ 1002
Cdd:PRK03918  517 LEELEKKAEEYEK--LKEKLIKLKGE--IKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGFESVE 588

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1003 KEEQQRLVLEKGFE--LKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQ---------AKTI 1071
Cdd:PRK03918  589 ELEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelREEY 668

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568961013 1072 SEFEKEIELLQAQKIDVEKHVQSQKR---EMRERMSEVTKQLLESYDIEDVRSRL 1123
Cdd:PRK03918  669 LELSRELAGLRAELEELEKRREEIKKtleKLKEELEEREKAKKELEKLEKALERV 723

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

894-1239

2.25e-08

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 2.25e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   894 LQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELElQRE 973
Cdd:TIGR04523  216 LESQISELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK-ELE 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   974 RAEQMLQEKSEELK-EKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK---QIESLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR04523  288 KQLNQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQlneQISQLKKELTNSESENSEKQRELEE 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1050 GQVTSDRLKGEvarlskqaktISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVE--- 1126
Cdd:TIGR04523  368 KQNEIEKLKKE----------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiik 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1127 ------DLEhlNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRhe 1200
Cdd:TIGR04523  438 nnseikDLT--NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK-- 513

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 568961013  1201 vtrltsenmmipDFKQQISELERQKQDLESRLKEQAEKI 1239
Cdd:TIGR04523  514 ------------DLTKKISSLKEKIEKLESEKKEKESKI 540

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

892-1241

3.50e-08

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: 58.26 E-value: 3.50e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   892 QRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHrhsYEEKGRRyRDTVEERLSKLQKHNAEL--E 969
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQ-KNNALKKIRELEAQISELqeD 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   970 LQRERAEQMLQEKSE-ELKEKMDKLTRQLFDDV----------QKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKD 1038
Cdd:pfam01576  280 LESERAARNKAEKQRrDLGEELEALKTELEDTLdttaaqqelrSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALE 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1039 ErsqLHHQLEEgqvtSDRLKGEVARlSKQA--KTISEFEKEIELLQAQKIDVE---KHVQSQKREMRERMSEVTKQLLES 1113
Cdd:pfam01576  360 E---LTEQLEQ----AKRNKANLEK-AKQAleSENAELQAELRTLQQAKQDSEhkrKKLEGQLQELQARLSESERQRAEL 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1114 YDiEDVRSRLSVEDLEHLNEDGElwfayeglKKATRV------LESHFQSQKDCYEKEIE---GLNFKVVHLSQEINHLQ 1184
Cdd:pfam01576  432 AE-KLSKLQSELESVSSLLNEAE--------GKNIKLskdvssLESQLQDTQELLQEETRqklNLSTRLRQLEDERNSLQ 502

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568961013  1185 KLFREEtdinESIRHEVTRltsenmmipdfkqQISELERQKQDLESRLKEQAEKIEG 1241
Cdd:pfam01576  503 EQLEEE----EEAKRNVER-------------QLSTLQAQLSDMKKKLEEDAGTLEA 542

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

866-1240

3.90e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.90e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  866 ARAWLARRRFQniRRFVlniqlTYRVQRLQKKLEDQNRENHGLVEKLTS--------LAAL--RVGDLEKVQKLEaELE- 934
Cdd:COG4913   501 ALRWVNRLHLR--GRLV-----YERVRTGLPDPERPRLDPDSLAGKLDFkphpfrawLEAElgRRFDYVCVDSPE-ELRr 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  935 --KAAT------HRHSYEEKGRRYRdtVEERL-------SKLQkhnaelELQRERAEqmLQEKSEELKEKMDKLTRQLFD 999
Cdd:COG4913   573 hpRAITragqvkGNGTRHEKDDRRR--IRSRYvlgfdnrAKLA------ALEAELAE--LEEELAEAEERLEALEAELDA 642

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1000 DVQKEEQQRLVLEKGFElktqayEKQIESLREEIKALKDERSQLhhqleegqvtsDRLKGEVARLskqaktisefEKEIE 1079
Cdd:COG4913   643 LQERREALQRLAEYSWD------EIDVASAEREIAELEAELERL-----------DASSDDLAAL----------EEQLE 695

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1080 LLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQK 1159
Cdd:COG4913   696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1160 DCYEKEIEGLNFKVVHLSQEINHLQKLFREETDI----NESIRHEVTRLTSENmmIPDFKQQISEL-----ERQKQDLES 1230
Cdd:COG4913   776 DALRARLNRAEEELERAMRAFNREWPAETADLDAdlesLPEYLALLDRLEEDG--LPEYEERFKELlnensIEFVADLLS 853

                         410
                  ....*....|
gi 568961013 1231 RLKEQAEKIE 1240
Cdd:COG4913   854 KLRRAIREIK 863

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

1012-1240

5.36e-08

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 5.36e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1012 EKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQkidvEKH 1091
Cdd:TIGR02169  662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQLEQE----EEK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1092 VQSQKREMRERMSEvTKQLLESYDIEdvrsrlsvedLEHLNED-GELWFAYEGLKKATRVLESHF-QSQKDCYEKEIEGL 1169
Cdd:TIGR02169  735 LKERLEELEEDLSS-LEQEIENVKSE----------LKELEARiEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKL 803

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961013  1170 NFKVVHLSQEINH----LQKLFREETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:TIGR02169  804 EEEVSRIEARLREieqkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

864-1232

5.96e-08

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.06 E-value: 5.96e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   864 KYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLE--DQNRENHGLVEKLTSLAALRvgDLEKVQKL-EAELEKAAThr 940
Cdd:pfam17380  259 RYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEkmEQERLRQEKEEKAREVERRR--KLEEAEKArQAEMDRQAA-- 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   941 hSYEEKGRRYRDTvEERLSKLQKHNAELELQRERAEQMLQEKSeelkeKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQ 1020
Cdd:pfam17380  335 -IYAEQERMAMER-ERELERIRQEERKRELERIRQEEIAMEIS-----RMRELERLQMERQQKNERVRQELEAARKVKIL 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1021 AYEKQieslrEEIKALKDERSQLHHQLEEG-QVTSDRLKGEVAR-LSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam17380  408 EEERQ-----RKIQQQKVEMEQIRAEQEEArQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1099 MRER--MSEVTKQLLESyDIEDVRSRLSVED-----LEHLNEDGELWFAYEglkKATRVLESHFQSQKDCYEKeiEGLNF 1171
Cdd:pfam17380  483 KRDRkrAEEQRRKILEK-ELEERKQAMIEEErkrklLEKEMEERQKAIYEE---ERRREAEEERRKQQEMEER--RRIQE 556

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961013  1172 KVVHLSQEINHLQKLFREETDI-----NESIRHEVTRLTSENMMIPDFKQQISELerQKQDLESRL 1232
Cdd:pfam17380  557 QMRKATEERSRLEAMEREREMMrqiveSEKARAEYEATTPITTIKPIYRPRISEY--QPPDVESHM 620

PTZ00121

MAEBL; Provisional

890-1240

6.27e-08

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 6.27e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  890 RVQRLQKKLEDQNRenhglVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRryrdtvEERLSKLQKHNAELE 969
Cdd:PTZ00121 1379 KADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK------ADEAKKKAEEAKKAD 1447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  970 LQRERAEQmlQEKSEELKEKMDKLTRQlfDDVQKEEQQRlvlEKGFELKTQAYE--KQIESLR--EEIKALKDE--RSQL 1043
Cdd:PTZ00121 1448 EAKKKAEE--AKKAEEAKKKAEEAKKA--DEAKKKAEEA---KKADEAKKKAEEakKKADEAKkaAEAKKKADEakKAEE 1520

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1044 HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDV--EKHVQSQKREMRERMSEVTKQlLESYDIEDVRS 1121
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKK-AEEARIEEVMK 1599

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1122 RLSVEDL---EHLNEDGELWFAYEGLKKATRVleshfqsqkdcyEKEIEGLNFKVvhlSQEINHLQKLFREEtDINESIR 1198
Cdd:PTZ00121 1600 LYEEEKKmkaEEAKKAEEAKIKAEELKKAEEE------------KKKVEQLKKKE---AEEKKKAEELKKAE-EENKIKA 1663

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 568961013 1199 HEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705

YhaN

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

848-1239

6.54e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 6.54e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  848 RRYRKLLQEHKAV---ILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRvgdlE 924
Cdd:COG4717    88 EEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE----E 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  925 KVQKLEAELEKAATHRhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQML---QEKSEELKEKMDKLTRQLFDDV 1001
Cdd:COG4717   164 ELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELeeaQEELEELEEELEQLENELEAAA 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1002 QKE---EQQRLVLEKGFELKTQAYEKQIESLREEIKA---------------LKDERSQLHHQLEEGQVTSDRLKGEVAR 1063
Cdd:COG4717   241 LEErlkEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEE 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1064 LSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESyDIEDVRSRLSVEDLEHLNEDGELWFAYEG 1143
Cdd:COG4717   321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ-EIAALLAEAGVEDEEELRAALEQAEEYQE 399

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1144 LKKATRVLESHFQSQKDCYEKEIEGLNFKvvHLSQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDfKQQISELER 1223
Cdd:COG4717   400 LKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQ 476

                         410
                  ....*....|....*.
gi 568961013 1224 QKQDLESRLKEQAEKI 1239
Cdd:COG4717   477 ELEELKAELRELAEEW 492

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

893-1128

7.26e-08

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 7.26e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   893 RLQKKLEDQNRENHGLVEKLtSLAALRVGDLE-KVQKLEAELEKAATHRHSYEEKGRRY---RDTVEERLSKLQkhnAEL 968
Cdd:TIGR02169  291 RVKEKIGELEAEIASLERSI-AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELK---EEL 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   969 ELQRERAEQM------LQEKSEELKEKMDKLTRQLFDdvQKEEQQRLVLEKgfelktQAYEKQIESLREEIKALKDERSQ 1042
Cdd:TIGR02169  367 EDLRAELEEVdkefaeTRDELKDYREKLEKLKREINE--LKRELDRLQEEL------QRLSEELADLNAAIAGIEAKINE 438

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1043 LHHQLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRErmSEVTKQLLESYdiedVRSR 1122
Cdd:TIGR02169  439 LEEEKEDKA---LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE--AEAQARASEER----VRGG 509


                   ....*.
gi 568961013  1123 LSVEDL 1128
Cdd:TIGR02169  510 RAVEEV 515

SMC_prok_B

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

846-1115

7.41e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 7.41e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   846 ARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNI-----QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRV 920
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   921 GDLEKVQKLEAELEKA----ATHRHSYEEKGRRYRDT------VEERLSKLQKHNAELELQRERAEQMLQEKSE------ 984
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLkeelKALREALDELRAELTLLneeaanLRERLESLERRIAATERRLEDLEEQIEELSEdiesla 858

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   985 ----ELKEKMDKLTRQL---FDDVQKEEQQRLVLEKGFELKT---QAYEKQIESLREEIKALKDERSQLHHQLEEGQVTS 1054
Cdd:TIGR02168  859 aeieELEELIEELESELealLNERASLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1055 DRLKG-----------------------------EVARLSKQAK--------TISEFEKEIE---LLQAQKIDVEKHVQS 1094
Cdd:TIGR02168  939 DNLQErlseeysltleeaealenkieddeeearrRLKRLENKIKelgpvnlaAIEEYEELKErydFLTAQKEDLTEAKET 1018

                          330       340
                   ....*....|....*....|.
gi 568961013  1095 QKREMRERMSEVTKQLLESYD 1115
Cdd:TIGR02168 1019 LEEAIEEIDREARERFKDTFD 1039

PTZ00121

MAEBL; Provisional

890-1232

8.57e-08

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 8.57e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdlEKVQKLEAELEKAATHRHSYEEKGR--RYRDTVEERLSKLQKHNAE 967
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELKKAEEEKKKveQLKKKEAEEKKKAEELKKA 1655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  968 LELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRlvlekgfelKTQAYEKQIESLREEIKALKDERSQLHHQL 1047
Cdd:PTZ00121 1656 EEENKIKAAE-EAKKAEEDKKKAEEAKKAEEDEKKAAEALK---------KEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1048 EEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQsqkrEMRERMSEVTKqllESYDIEDVRSRLSVE- 1126
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE----EIRKEKEAVIE---EELDEEDEKRRMEVDk 1798

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1127 DLEHLNEDGELwfAYEGLKKATRVLeshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTS 1206
Cdd:PTZ00121 1799 KIKDIFDNFAN--IIEGGKEGNLVI----NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNK 1872

                         330       340       350
                  ....*....|....*....|....*....|
gi 568961013 1207 ENMMIPDFKQQISELERQKQ----DLESRL 1232
Cdd:PTZ00121 1873 EKDLKEDDEEEIEEADEIEKidkdDIEREI 1902

PRK03918

DNA double-strand break repair ATPase Rad50;

896-1112

9.41e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 9.41e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  896 KKLEDQNRENHGLVEKLTSLAALRVG---DLEKVQKLEAEL-----------EKAATHRHSYEEKGRRYRDTVEERLSKL 961
Cdd:PRK03918  518 EELEKKAEEYEKLKEKLIKLKGEIKSlkkELEKLEELKKKLaelekkldeleEELAELLKELEELGFESVEELEERLKEL 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  962 QK-HNAELELQRerAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRLVLEKGFELKTQAY--------EKQIESLREE 1032
Cdd:PRK03918  598 EPfYNEYLELKD--AEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKELEELEKKYseeeyeelREEYLELSRE 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1033 IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE 1112
Cdd:PRK03918  675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFE 754

PRK02224

DNA double-strand break repair Rad50 ATPase;

890-1137

1.31e-07

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 1.31e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  890 RVQRLQKKLEDqnrenhgLVEKLTSLAAlRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKL-------Q 962
Cdd:PRK02224  476 RVEELEAELED-------LEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAeelreraA 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  963 KHNAELELQRERAeQMLQEKSEELKEKMDKLTRQLfdDVQKEEQQRL-VLEKGFELKTqAYEKQIESLREEIKALKD--- 1038
Cdd:PRK02224  548 ELEAEAEEKREAA-AEAEEEAEEAREEVAELNSKL--AELKERIESLeRIRTLLAAIA-DAEDEIERLREKREALAElnd 623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1039 -------ERSQLHHQLEEgQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKRE------MRERMSE 1105
Cdd:PRK02224  624 errerlaEKRERKRELEA-EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEleeleeLRERREA 702

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568961013 1106 V--TKQLLESYDIE---------DVRSRL---SVEDLEH-LNEDGEL 1137
Cdd:PRK02224  703 LenRVEALEALYDEaeelesmygDLRAELrqrNVETLERmLNETFDL 749

CCDC22

pfam05667

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...

892-1115

2.39e-07

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.

Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.03 E-value: 2.39e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   892 QRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV-----QKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNA 966
Cdd:pfam05667  246 TKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELlssfsGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVET 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   967 ELELQRERAEQM--LQEKSEELKEKMDKLT----------RQLFDDVQKEEQQRLVLEKGFELKTQAY------EKQIES 1028
Cdd:pfam05667  326 EEELQQQREEELeeLQEQLEDLESSIQELEkeikklessiKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaEENIAK 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1029 LREEIKALKDERSQLHHQLEEGQVTsdrLKGEVARLsKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRErmsEVTK 1108
Cdd:pfam05667  406 LQALVDASAQRLVELAGQWEKHRVP---LIEEYRAL-KEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE---ELYK 478


                   ....*..
gi 568961013  1109 QLLESYD 1115
Cdd:pfam05667  479 QLVAEYE 485

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

886-1073

2.78e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.78e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSL------AALRVGDLEK-VQKLEAELEKAATHRHSYEEKGRRYRDTVEERL 958
Cdd:COG4942    31 QLQQEIAELEKELAALKKEEKALLKQLAALerriaaLARRIRALEQeLAALEAELAELEKEIAELRAELEAQKEELAELL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  959 SKLQKH----------NAELELQRERAEQMLQEKSEELKEKMDKLTRQLFD------DVQKEEQQRLVLEKGFELKTQAY 1022
Cdd:COG4942   111 RALYRLgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAElaalraELEAERAELEALLAELEEERAAL 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568961013 1023 EKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISE 1073
Cdd:COG4942   191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241

mukB

PRK04863

chromosome partition protein MukB;

866-1241

3.06e-07

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 3.06e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  866 ARAWLarrRFQNIRRFVLNIQLTYRvQRLQKKLEDQNRENHGLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRHS--- 942
Cdd:PRK04863  271 AADYM---RHANERRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAELN----EAESDLEQDYQAASDHLNLvqt 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  943 ---YEEKGRRYRDTVEERLSKLQKHNAELELQRERAEqMLQEKSEELKEKMDKLTRQLFDDVQK-EEQQRLVLEkgFELK 1018
Cdd:PRK04863  343 alrQQEKIERYQADLEELEERLEEQNEVVEEADEQQE-ENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQ--YQQA 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1019 TQAYEKQ-----------------IESLREEIKALKDERSQLHHQLEEGQVTSD----------RLKGEVARL--SKQAK 1069
Cdd:PRK04863  420 VQALERAkqlcglpdltadnaedwLEEFQAKEQEATEELLSLEQKLSVAQAAHSqfeqayqlvrKIAGEVSRSeaWDVAR 499

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1070 -TISEFEKEIEL------LQAQKIDVEKHVQSQKREMReRMSEVTKQLLESYDIEDvrsrlsveDLEHLNEDGElwfaye 1142
Cdd:PRK04863  500 eLLRRLREQRHLaeqlqqLRMRLSELEQRLRQQQRAER-LLAEFCKRLGKNLDDED--------ELEQLQEELE------ 564

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1143 glkkatRVLESHFQSQKDCYEKEIEgLNFKVVHLSQEINHLQKL---FREETDINESIRHEV--TRLTSENMMipDFKQQ 1217
Cdd:PRK04863  565 ------ARLESLSESVSEARERRMA-LRQQLEQLQARIQRLAARapaWLAAQDALARLREQSgeEFEDSQDVT--EYMQQ 635

                         410       420
                  ....*....|....*....|....
gi 568961013 1218 ISELERQKQDLESRLKEQAEKIEG 1241
Cdd:PRK04863  636 LLERERELTVERDELAARKQALDE 659

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

890-1240

3.37e-07

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: 54.52 E-value: 3.37e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLE--KVQKLEAELEKAATHRH--SYEEKGRRYRDTVEErLSKLQKhn 965
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKEryKRDREQWERQRRELESRvaELKEELRQSREKHEE-LEEKYK-- 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   966 aelELQRERAEqMLQEKSEELKEKMDKLTR--QLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEikalKDERSQL 1043
Cdd:pfam07888  105 ---ELSASSEE-LSEEKDALLAQRAAHEARirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQL 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1044 HHQLEEGQVTSDRLKGE--VAR--LSKQAKTISEFEKEIELLQ-----AQKIDVE-KHVQSQKREMRER--MSEVTKQLL 1111
Cdd:pfam07888  177 QAKLQQTEEELRSLSKEfqELRnsLAQRDTQVLQLQDTITTLTqklttAHRKEAEnEALLEELRSLQERlnASERKVEGL 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1112 ESyDIEDV---RSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFR 1188
Cdd:pfam07888  257 GE-ELSSMaaqRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQ 335

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1189 EETDINESIRHEVTRLTSENMMipdfkqQISELERQKQDLESRL------KEQ--AEKIE 1240
Cdd:pfam07888  336 EERMEREKLEVELGREKDCNRV------QLSESRRELQELKASLrvaqkeKEQlqAEKQE 389

CCDC73

pfam15818

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...

944-1238

4.65e-07

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.

Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 54.57 E-value: 4.65e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   944 EEKGRRYRDT-VEERLSKLQKHNAELELQREraeqMLQEKSEEL----KEKMDKLTRQLFDDVQKEEQqrlvlEKG-FEL 1017
Cdd:pfam15818   15 ELRMRREAETqYEEQIGKIIVETQELKWQKE----TLQNQKETLakqhKEAMAVFKKQLQMKMCALEE-----EKGkYQL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1018 KTQAYEKQIESLREEIKALkdersqlhhqleegqvtsdrlkgEVARLSKQaKTISEFEKEIELLQAQKIDVEKhvqsQKR 1097
Cdd:pfam15818   86 ATEIKEKEIEGLKETLKAL-----------------------QVSKYSLQ-KKVSEMEQKLQLHLLAKEDHHK----QLN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1098 EMRERMSEVTKQL---------LESYDIEDVR--SRLSVedlehLNE--DGELWFAYEGLKKATRVL-ESHFQSQkdcYE 1163
Cdd:pfam15818  138 EIEKYYATITGQFglvkenhgkLEQNVQEAIQlnKRLSA-----LNKkqESEICSLKKELKKVTSDLiKSKVTCQ---YK 209

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013  1164 KEIEGLNFKVVHlsQEINHLQKLFREETDINESIRHEVTRLTSENM-MIPDFKQQISELERQKQ---DLESRLKEQAEK 1238
Cdd:pfam15818  210 MGEENINLTIKE--QKFQELQERLNMELELNKKINEEITHIQEEKQdIIISFQHMQQLLQQQTQantEMEAELKALKEN 286

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

884-1185

4.78e-07

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.

Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 4.78e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdlekvQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam05557   50 NQELQKRIRLLEKREAEAEEALREQAELNRLK-----------KKYLEALNKKLNEKESQLADAREVISCLKNELSELRR 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   964 --HNAELELQRERAE-QMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRLVlekgFELKTQAYEKQIESLREEIKALKDER 1040
Cdd:pfam05557  119 qiQRAELELQSTNSElEELQERLDLLKAKASEAE-QLRQNLEKQQSSLAE----AEQRIKELEFEIQSQEQDSEIVKNSK 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1041 SQLhHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQ----------AQKIDVEKHVQSQKREMRERMSEVTKQL 1110
Cdd:pfam05557  194 SEL-ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklereekyrEEAATLELEKEKLEQELQSWVKLAQDTG 272

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961013  1111 LESYDIEDVRSR---LSVEDLEHLNEDGELWFAYEGLKKATRVLeshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam05557  273 LNLRSPEDLSRRieqLQQREIVLKEENSSLTSSARQLEKARREL----EQELAQYLKKIEDLNKKLKRHKALVRRLQR 346

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

888-1102

5.31e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 5.31e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  888 TYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAAthrhsyeekgRRYRDTvEERLSKLQKHNAE 967
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----------RRIRAL-EQELAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  968 LELQRERAEQMLQEKSEELKEKMDKLTRQ--------LFDdvQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDE 1039
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRALYRLgrqpplalLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961013 1040 RSQLHHQLEEGQVTSDRLKGEVARLSKQ-----------AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRER 1102
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALkaerqkllarlEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

891-1240

5.31e-07

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.41 E-value: 5.31e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   891 VQRLQKKLEDQNRENHglveklTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEE---RLSKLQKHNAE 967
Cdd:pfam01576  329 VTELKKALEEETRSHE------AQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAElqaELRTLQQAKQD 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   968 LELQRERAEQMLQE----------KSEELKEKMDKLTRQLfDDV----QKEEQQRLVLEKGF-ELKTQAYEKQiESLREE 1032
Cdd:pfam01576  403 SEHKRKKLEGQLQElqarlseserQRAELAEKLSKLQSEL-ESVssllNEAEGKNIKLSKDVsSLESQLQDTQ-ELLQEE 480

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1033 ----------IKALKDERSQLHHQLEEGQVTSDRLKGEV----ARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam01576  481 trqklnlstrLRQLEDERNSLQEQLEEEEEAKRNVERQLstlqAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1099 MRERMSEVTK---------QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEglkkatRVLESHFQSQKDCYEKEIEGL 1169
Cdd:pfam01576  561 LEEKAAAYDKlektknrlqQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEE------KAISARYAEERDRAEAEAREK 634

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961013  1170 NFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENmmiPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:pfam01576  635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK---DDVGKNVHELERSKRALEQQVEEMKTQLE 702

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

887-1240

6.29e-07

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 6.29e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDT---VEERLSKLQK 963
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEydrVEKELSKLQR 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   964 HNAELELQRE---------RAEQMLQEKS---------------------------------------------EELKE- 988
Cdd:TIGR02169  491 ELAEAEAQARaseervrggRAVEEVLKASiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaiELLKRr 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   989 -----------KMDKLTRQL-----------------FDD---------------VQKEE-------QQRLV------LE 1012
Cdd:TIGR02169  571 kagratflplnKMRDERRDLsilsedgvigfavdlveFDPkyepafkyvfgdtlvVEDIEaarrlmgKYRMVtlegelFE 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1013 K------------GFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIEL 1080
Cdd:TIGR02169  651 KsgamtggsraprGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQ 727

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1081 LQAQkidvEKHVQSQKREMRERMSEvTKQLLESYD--IEDVRSRLS------------VEDLEHlNEDGELWFAYEGLKK 1146
Cdd:TIGR02169  728 LEQE----EEKLKERLEELEEDLSS-LEQEIENVKseLKELEARIEeleedlhkleeaLNDLEA-RLSHSRIPEIQAELS 801

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1147 ATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLtseNMMIPDFKQQISELERQKQ 1226
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL---NGKKEELEEELEELEAALR 878

                          490
                   ....*....|....
gi 568961013  1227 DLESRLKEQAEKIE 1240
Cdd:TIGR02169  879 DLESRLGDLKKERD 892

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

895-1185

6.73e-07

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 52.89 E-value: 6.73e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   895 QKKLEDQNRenHGLVEKLTSLAALRVGDLEK-VQKLEAELEKAathrhsyEEKgrrYRDTVEERLSkLQKHNAELELQR- 972
Cdd:pfam15905   66 QKNLKESKD--QKELEKEIRALVQERGEQDKrLQALEEELEKV-------EAK---LNAAVREKTS-LSASVASLEKQLl 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   973 --ERAEQMLQEKSEE--LKEKMDKLTRQLF---DDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHH 1045
Cdd:pfam15905  133 elTRVNELLKAKFSEdgTQKKMSSLSMELMklrNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1046 QLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQllesydIEDVRSRLSV 1125
Cdd:pfam15905  213 EKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ------IKDLNEKCKL 286

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1126 edLEHLNEDgelwfayeglkkatrvLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam15905  287 --LESEKEE----------------LLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328

PTZ00121

MAEBL; Provisional

924-1230

1.12e-06

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.12e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  924 EKVQKLEAELEKAATHRHSYEE--KGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKltrQLFDDV 1001
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK---KKAEEA 1569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1002 QKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGE----------VARLSKQAKTI 1071
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeekkkveqlKKKEAEEKKKA 1649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1072 SEFEKEIELLQAQKIDVEKHVQSQKREMRE-RMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDgELWFAyEGLKKATRV 1150
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-EKKKA-EELKKAEEE 1727

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1151 LESHF-QSQKDCYEKEIEGLNFKVVHlsQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDFKQQIsELERQKQDLE 1229
Cdd:PTZ00121 1728 NKIKAeEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM-EVDKKIKDIF 1804


                  .
gi 568961013 1230 S 1230
Cdd:PTZ00121 1805 D 1805

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

874-1240

1.27e-06

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 1.27e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  874 RFQNIRRFVLNIQLTYRvQRLQKKLEDQNRENHGLVEKLTSLAALrvGDLEKvqKLEAELEKAATH--------RHsyEE 945
Cdd:COG3096   275 RHANERRELSERALELR-RELFGARRQLAEEQYRLVEMARELEEL--SARES--DLEQDYQAASDHlnlvqtalRQ--QE 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  946 KGRRYRDTVEERLSKLQKHNAELElqrERAEQ--MLQEKSEELKEKMDKLTRQLFDDVQK-EEQQRLVLekgfelktqAY 1022
Cdd:COG3096   348 KIERYQEDLEELTERLEEQEEVVE---EAAEQlaEAEARLEAAEEEVDSLKSQLADYQQAlDVQQTRAI---------QY 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1023 EKQIESLRE----------EIKALKDErsQLHHQLEEGQVTSDRLKGEvARLSKQAKTISEFEKEIELLQAQKIDVEK-- 1090
Cdd:COG3096   416 QQAVQALEKaralcglpdlTPENAEDY--LAAFRAKEQQATEEVLELE-QKLSVADAARRQFEKAYELVCKIAGEVERsq 492

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1091 -----------------------HVQSQKREMRERMSEVTK--QLLESYDIEDVRSRLSVEDLEHLnedgelwfayegLK 1145
Cdd:COG3096   493 awqtarellrryrsqqalaqrlqQLRAQLAELEQRLRQQQNaeRLLEEFCQRIGQQLDAAEELEEL------------LA 560

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1146 KATRVLESHFQSQKDCYEKEIEgLNFKVVHLSQEINHLQK---LFREETDINESIRHEV-TRLTSENMMIpDFKQQISEL 1221
Cdd:COG3096   561 ELEAQLEELEEQAAEAVEQRSE-LRQQLEQLRARIKELAArapAWLAAQDALERLREQSgEALADSQEVT-AAMQQLLER 638

                         410
                  ....*....|....*....
gi 568961013 1222 ERQKQDLESRLKEQAEKIE 1240
Cdd:COG3096   639 EREATVERDELAARKQALE 657

EzrA

pfam06160

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...

896-1224

1.68e-06

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.

Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 52.16 E-value: 1.68e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   896 KKLEDQNRENHGLVEKLtslaalrvgdLEKVQKLEAELekaATHRHSYEEkgrrYRDTVEERLSKLQKHNAELE------ 969
Cdd:pfam06160  110 DELLESEEKNREEVEEL----------KDKYRELRKTL---LANRFSYGP----AIDELEKQLAEIEEEFSQFEeltesg 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   970 --LQRERAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRL---------VLEKGFELKTQAYEKQIESLREEIKALKd 1038
Cdd:pfam06160  173 dyLEAREVLEKLEEETDALEELMEDIP-PLYEELKTELPDQLeelkegyreMEEEGYALEHLNVDKEIQQLEEQLEENL- 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1039 ersqlhHQLEEGQVtsDRLKGEVARLSKQAKTISE-FEKEIEllqaQKIDVEKHvQSQKREMRERMSEVTKQLLESYDIE 1117
Cdd:pfam06160  251 ------ALLENLEL--DEAEEALEEIEERIDQLYDlLEKEVD----AKKYVEKN-LPEIEDYLEHAEEQNKELKEELERV 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1118 DVRSRLSVEDLEHlnedgelwfayeglkkaTRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINE-- 1195
Cdd:pfam06160  318 QQSYTLNENELER-----------------VRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEeq 380

                          330       340       350
                   ....*....|....*....|....*....|....
gi 568961013  1196 -SIRHEVTRLTSENM----MIPDFKQQISELERQ 1224
Cdd:pfam06160  381 eEFKESLQSLRKDELeareKLDEFKLELREIKRL 414

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1018-1238

2.17e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.17e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1018 KTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT----ISEFEKEIELLQAQKIDVEKHVQ 1093
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqeLAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1094 SQKREMRERMSEVTKQ--------LLESYDIEDVRSRLSVedLEHLNE-DGELWFAYEGLKKATRVLESHFQSQKDCYEK 1164
Cdd:COG4942   101 AQKEELAELLRALYRLgrqpplalLLSPEDFLDAVRRLQY--LKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961013 1165 EIEGlnfkvvhLSQEINHLQKLFREETDINESIRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRLKEQAEK 1238
Cdd:COG4942   179 LLAE-------LEEERAALEALKAERQKLLARLEKELAELAAE---LAELQQEAEELEALIARLEAEAAAAAER 242

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

891-1138

2.47e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 2.47e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  891 VQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAEL----EKAATHRHSYEEKGRRYRDTVEERLS--KLQKH 964
Cdd:COG1340    38 LKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERdelnEKLNELREELDELRKELAELNKAGGSidKLRKE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  965 NAELELQRERA------EQMLQEKSEELKE------KMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK------QI 1026
Cdd:COG1340   118 IERLEWRQQTEvlspeeEKELVEKIKELEKelekakKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEaqelheEM 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1027 ESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQKIDVEKhvQSQKREMRERMSEV 1106
Cdd:COG1340   198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE---LRELRKELKKLRKKQRALKR--EKEKEELEEKAEEI 272

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568961013 1107 TKQLLESydiedvrSRLSVEDLEHLNEDGELW 1138
Cdd:COG1340   273 FEKLKKG-------EKLTTEELKLLQKSGLLE 297

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

932-1238

2.94e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 2.94e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   932 ELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEK-----SEELKEKMDKLTRQLFDDVQKEEQ 1006
Cdd:pfam02463  157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyYQLKEKLELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1007 QRLVL------------EKGFELKTQAYEKQIESLREEIKALKDERSQ----LHHQLEEGQVTSDRLKGEVARLSKqakt 1070
Cdd:pfam02463  237 ERIDLlqellrdeqeeiESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeeelKLLAKEEEELKSELLKLERRKVDD---- 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1071 isefEKEIELLQAQKIDVEKHVQSQKREMRERmsevtKQLLESYDIEDVRSRLSVEDLEHLNEDGELwfAYEGLKKATRV 1150
Cdd:pfam02463  313 ----EEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEEEEEELEKLQEKLEQ--LEEELLAKKKL 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1151 LESHFQSQKDCYEKEIEGLNFKVvhlsQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDFKQ---QISELERQKQD 1227
Cdd:pfam02463  382 ESERLSSAAKLKEEELELKSEEE----KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgklTEEKEELEKQE 457

                          330
                   ....*....|.
gi 568961013  1228 LESRLKEQAEK 1238
Cdd:pfam02463  458 LKLLKDELELK 468

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

960-1240

2.98e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.98e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  960 KLQKHNAELELQR-----ERAEQMLqeksEELKEKMDKLtrqlfddvqkeEQQRLVLEKGFELKTQAYEKQIESLREEIK 1034
Cdd:COG1196   171 KERKEEAERKLEAteenlERLEDIL----GELERQLEPL-----------ERQAEKAERYRELKEELKELEAELLLLKLR 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1035 ALKDERSQLHHQLEEGQvtsdrlkgevARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTkQLLESY 1114
Cdd:COG1196   236 ELEAELEELEAELEELE----------AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDI 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1115 DIEDVRSRLSVEDLEHLNEDGELWfaYEGLKKATRVLESHFQSQKDcYEKEIEGLNfkvVHLSQEINHLQKLFREETDIN 1194
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEE-AEEELEEAE---AELAEAEEALLEAEAELAEAE 378

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 568961013 1195 ESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

886-1241

3.36e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 3.36e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   886 QLTYRVQRLQKKLEDQNRenhgLVEKLTSLAALRVGDLE-KVQKLEAELEKAATHRhsyeekgRRYRDTVEERLSKLQKH 964
Cdd:pfam15921   82 EYSHQVKDLQRRLNESNE----LHEKQKFYLRQSVIDLQtKLQEMQMERDAMADIR-------RRESQSQEDLRNQLQNT 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   965 NAELELQRERAEQMLQEKSEELkekmDKLTRQLFDDVQKEEQQRLVLEKgFElktQAYEKQIESlreeikalKDERSQLH 1044
Cdd:pfam15921  151 VHELEAAKCLKEDMLEDSNTQI----EQLRKMMLSHEGVLQEIRSILVD-FE---EASGKKIYE--------HDSMSTMH 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1045 HQ---------LEEGQVTSDRLKGEVARLSKQAKTI-SEFEKEIELLQAQKID-VEKHVQSQKRE---MRERMSEVTKQl 1110
Cdd:pfam15921  215 FRslgsaiskiLRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDrIEQLISEHEVEitgLTEKASSARSQ- 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1111 lesydIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVV--------------HL 1176
Cdd:pfam15921  294 -----ANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlanseltearterdQF 368

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961013  1177 SQEI----NHLQKLF----REETDIN---ESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEG 1241
Cdd:pfam15921  369 SQESgnldDQLQKLLadlhKREKELSlekEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQG 444

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

886-1229

4.74e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 4.74e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKhn 965
Cdd:TIGR00618  532 RGEQTYAQLETSEEDVYHQLTSERKQRASLK-------EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK-- 602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   966 aELELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLR--EEIKALKDERSQL 1043
Cdd:TIGR00618  603 -LSEAEDMLACE-QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsiRVLPKELLASRQL 680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1044 HHQLEEG---QVTSDR--LKGEVARLSKQAKTISEFEKEIELLQ----AQKIDVEKHVQSQKREMRERMSEVTKQLLESY 1114
Cdd:TIGR00618  681 ALQKMQSekeQLTYWKemLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAAREDALNQSLKELMHQARTVLKART 760

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1115 DIEDVRSRLSVEDLEHLNE----DGELWF---AYEGLKKATRVLESHFQSQKDCYEKEiegLNFKVVHLSQEINHLQKLF 1187
Cdd:TIGR00618  761 EAHFNNNEEVTAALQTGAElshlAAEIQFfnrLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRL 837

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 568961013  1188 REETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLE 1229
Cdd:TIGR00618  838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

890-1112

6.24e-06

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 6.24e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   890 RVQRLQKKLEDQNRENHGLVEKLTSLAaLRVGDLEKV-----QKLEAELEKAATHRHSYEEKGRRYRDTVEErLSKLQKH 964
Cdd:TIGR04523  427 EIERLKETIIKNNSEIKDLTNQDSVKE-LIIKNLDNTresleTQLKVLSRSINKIKQNLEQKQKELKSKEKE-LKKLNEE 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   965 NAELELQreraEQMLQEKSEELKEKMDKLTRQLFDDVQK-EEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQL 1043
Cdd:TIGR04523  505 KKELEEK----VKDLTKKISSLKEKIEKLESEKKEKESKiSDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSL 580

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961013  1044 HHQLEEGQVTSDRLKGEVARLSKQ----AKTISEFEKEIELLQAQKIDVE---KHVQSQKREMRERMSEVTKQLLE 1112
Cdd:TIGR04523  581 KKKQEEKQELIDQKEKEKKDLIKEieekEKKISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIKETIKE 656

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

922-1109

7.30e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 7.30e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  922 DLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEE-------LKEKMDKLT 994
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEiaelraeLEAQKEELA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  995 RQLFDDVQKEEQQRLVLEKGFELKTQAYeKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEF 1074
Cdd:COG4942   108 ELLRALYRLGRQPPLALLLSPEDFLDAV-RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568961013 1075 EKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQ 1109
Cdd:COG4942   187 RAALEALKAERQKLLARLEKELAELAAELAELQQE 221

Filament

pfam00038

Intermediate filament protein;

980-1241

7.34e-06

Intermediate filament protein;

Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.53 E-value: 7.34e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   980 QEKsEELKEKMDKLTRQLfDDVQKEEQQRLVLEKGFELKTQ-----------AYEKQIESLREEIKALKDERSQLHHQLE 1048
Cdd:pfam00038    1 NEK-EQLQELNDRLASYI-DKVRFLEQQNKLLETKISELRQkkgaepsrlysLYEKEIEDLRRQLDTLTVERARLQLELD 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1049 EGQVTSDRLKgevARLSKQAKTISEFEKEIELLQAQ-------KIDVEKHVQS-------QKREMRERMSEVTKQLLESY 1114
Cdd:pfam00038   79 NLRLAAEDFR---QKYEDELNLRTSAENDLVGLRKDldeatlaRVDLEAKIESlkeelafLKKNHEEEVRELQAQVSDTQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1115 DIEDVRSRLSVEDLEHLNEdgeLWFAYEGL-KKATRVLESHFQSQkdcYEKeieglnfkvvhLSQEIN-HLQKLFREETD 1192
Cdd:pfam00038  156 VNVEMDAARKLDLTSALAE---IRAQYEEIaAKNREEAEEWYQSK---LEE-----------LQQAAArNGDALRSAKEE 218

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 568961013  1193 INESiRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRLKEQAEKIEG 1241
Cdd:pfam00038  219 ITEL-RRTIQSLEIE---LQSLKKQKASLERQLAETEERYELQLADYQE 263

GumC

COG3206

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

859-1043

8.72e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 8.72e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  859 AVILQKYARAWLARRRFQNIRRFVLNIQ-LTYRVQRLQKKLEDQN------RENHGLV--EKLTSLAALRVGDLE-KVQK 928
Cdd:COG3206   151 AAVANALAEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEaaleefRQKNGLVdlSEEAKLLLQQLSELEsQLAE 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  929 LEAELEKAATHRHSYEEKGRRYRDTVEE-----RLSKLQKHNAELELQRERAEQMLQEKS---EELKEKMDKLTRQLFDD 1000
Cdd:COG3206   231 ARAELAEAEARLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQE 310

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568961013 1001 VQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQL 1043
Cdd:COG3206   311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

891-1235

9.85e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 9.85e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   891 VQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKA-----------ATHRHSYEEKGRRYRD---TVEE 956
Cdd:pfam15921  428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTkemlrkvveelTAKKMTLESSERTVSDltaSLQE 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   957 RLSKLQKHNAELELQRERAEQMLQE----KSEE------------------LKEKMDKLTRQlfddvQKEEQQRLVLEKG 1014
Cdd:pfam15921  508 KERAIEATNAEITKLRSRVDLKLQElqhlKNEGdhlrnvqtecealklqmaEKDKVIEILRQ-----QIENMTQLVGQHG 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1015 -----FELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARL----SKQAKTISEFEKEI-ELLQAQ 1084
Cdd:pfam15921  583 rtagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERdQLLNEV 662

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1085 KI------DVEKHVQSQKREMR---ERMSEVTKQL---LESYDIEDVRSRLSVEDLEhlNEDGELWFAYEGLKK---ATR 1149
Cdd:pfam15921  663 KTsrnelnSLSEDYEVLKRNFRnksEEMETTTNKLkmqLKSAQSELEQTRNTLKSME--GSDGHAMKVAMGMQKqitAKR 740

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1150 VLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHL-QKLFREETDIN------ESIRHEVTRLTSE--NMMIPDFKQ--QI 1218
Cdd:pfam15921  741 GQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLsQELSTVATEKNkmagelEVLRSQERRLKEKvaNMEVALDKAslQF 820

                          410       420
                   ....*....|....*....|
gi 568961013  1219 SELER--QKQDLES-RLKEQ 1235
Cdd:pfam15921  821 AECQDiiQRQEQESvRLKLQ 840

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

890-1237

1.38e-05

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 1.38e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   890 RVQRLQKKLEDQNRENHGLVEKLtslaalrvgDLEKVQkLEAELEKAATHRHSYEE---KGRRYRDTVEERLSKLQKHNA 966
Cdd:pfam01576  100 KMQQHIQDLEEQLDEEEAARQKL---------QLEKVT-TEAKIKKLEEDILLLEDqnsKLSKERKLLEERISEFTSNLA 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   967 ELElqrERAEQMlqeksEELKEKMDKLTRQLFDDVQKEEQQRLVLEKG---FELKTQAYEKQIESLREEIKALkdeRSQL 1043
Cdd:pfam01576  170 EEE---EKAKSL-----SKLKNKHEAMISDLEERLKKEEKGRQELEKAkrkLEGESTDLQEQIAELQAQIAEL---RAQL 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1044 HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQaQKIDVEK----HVQSQKREMRERMSEVTKQLLESYDIEDV 1119
Cdd:pfam01576  239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQ-EDLESERaarnKAEKQRRDLGEELEALKTELEDTLDTTAA 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1120 RSRLSVEDLEHLNEdgelwfayegLKKA----TRVLESHFQSQKDCYEKEIEGLN--------FKVV------HLSQEIN 1181
Cdd:pfam01576  318 QQELRSKREQEVTE----------LKKAleeeTRSHEAQLQEMRQKHTQALEELTeqleqakrNKANlekakqALESENA 387

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568961013  1182 HLQKLFREETDINESIRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRL-KEQAE 1237
Cdd:pfam01576  388 ELQAELRTLQQAKQDSEHKRKKLEGQ---LQELQARLSESERQRAELAEKLsKLQSE 441

COG2433

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

924-1077

1.44e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 1.44e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEErlskLQKHNAELELQRERAEQMLQEKSEELKEKmdkltrqlfddvqK 1003
Cdd:COG2433   392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVER----LEAEVEELEAELEEKDERIERLERELSEA-------------R 454

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013 1004 EEQQRLVLEkgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKgEVARLSKQ-----AKTISEFEKE 1077
Cdd:COG2433   455 SEERREIRK----------DREISRLDREIERLERELEEERERIEELKRKLERLK-ELWKLEHSgelvpVKVVEKFTKE 522

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

954-1097

1.59e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.59e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  954 VEERLSKLQKH-----NAELELQRERAEQMLQEKSEELKEKMDKLTRQLfdDVQKEEQQRLVLEKGfELKTQAYEKQIES 1028
Cdd:COG4913   223 TFEAADALVEHfddleRAHEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALRLWFA-QRRLELLEAELEE 299

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013 1029 LREEIKALKDERSQLHHQLEEGQVTSDRLkgEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKR 1097
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREELDEL--EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366

PRK01156

chromosome segregation protein; Provisional

890-1240

1.87e-05

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 1.87e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  890 RVQRLQKKLEDQNRENHGLVEKLTSLAALrvgdLEKVQKLEAELEKAATHRHSYEEKGRRYRDtVEERLSKLQkhNAELE 969
Cdd:PRK01156  219 EIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKII--NDPVY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  970 LQRERAEQMLQEKSEelKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktqayekQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:PRK01156  292 KNRNYINDYFKYKND--IENKKQILSNIDAEINKYHAIIKKLS------------VLQKDYNDYIKKKSRYDDLNNQILE 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIE--DVRSRLSVE 1126
Cdd:PRK01156  358 LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDiSSKVSslNQRIRALRE 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1127 DLEHLNEDGELWFAYE---------GLKKATRVLEsHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKL--FREETDINE 1195
Cdd:PRK01156  438 NLDELSRNMEMLNGQSvcpvcgttlGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkeYLESEEINK 516

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 568961013 1196 SIrHEVTRLTSENMMIPDFKQQISELeRQKQDLESRLKEQAEKIE 1240
Cdd:PRK01156  517 SI-NEYNKIESARADLEDIKIKINEL-KDKHDKYEEIKNRYKSLK 559

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

892-1241

1.92e-05

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.92e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   892 QRLQKKLEDQNRENHGLVEKLTslaalrvgDLEKVQKLEAELEKAathrhsyeeKGRRYRDTVEERLSKLQKHNAELELQ 971
Cdd:TIGR00618  246 TQKREAQEEQLKKQQLLKQLRA--------RIEELRAQEAVLEET---------QERINRARKAAPLAAHIKAVTQIEQQ 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   972 RERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLV--LEKGFELKTQAYEKQIESLREEIKALKDERS--QLHHQL 1047
Cdd:TIGR00618  309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtLHSQEIHIRDAHEVATSIREISCQQHTLTQHihTLQQQK 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1048 EEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKR--EMRERMSEVTKQLLESYDIEDVRSRLSV 1125
Cdd:TIGR00618  389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEKIHLQESAQSL 468

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1126 EDLEHLNEDGELWFAYEGLKKATR--VLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN--HLQKLFREETDINESIRHEV 1201
Cdd:TIGR00618  469 KEREQQLQTKEQIHLQETRKKAVVlaRLLELQEEPCPLCGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVY 548

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 568961013  1202 TRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEG 1241
Cdd:TIGR00618  549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

893-1120

1.92e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.92e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   893 RLQKKLEDQNREnhglvekLTSLAALRVGDLEKVQKLEA-----ELEKAAThRHSYEEKGRRYRDTVEER---LSKLQKH 964
Cdd:pfam15921  594 QLEKEINDRRLE-------LQEFKILKDKKDAKIRELEArvsdlELEKVKL-VNAGSERLRAVKDIKQERdqlLNEVKTS 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   965 NAELELQRERAEQM---LQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEK-------------GFELKTQAYEKQIES 1028
Cdd:pfam15921  666 RNELNSLSEDYEVLkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkvamGMQKQITAKRGQIDA 745

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1029 LREEIKAL--------------KDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISE----FEKEIELLQAQKIDVEK 1090
Cdd:pfam15921  746 LQSKIQFLeeamtnankekhflKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEkvanMEVALDKASLQFAECQD 825

                          250       260       270
                   ....*....|....*....|....*....|
gi 568961013  1091 HVQSQKREmrermsEVTKQLLESYDIEDVR 1120
Cdd:pfam15921  826 IIQRQEQE------SVRLKLQHTLDVKELQ 849

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

886-1240

1.93e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.93e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   886 QLTYRVQRLQKKLEdqNRENhglveKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHN 965
Cdd:TIGR04523   37 QLEKKLKTIKNELK--NKEK-----ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   966 AELELQREraeQMLQEKSEelkekMDKLTRQLfddVQKEEQQRLVLEKGFELKTQAYE--KQIESLREEIKALKDERSQL 1043
Cdd:TIGR04523  110 SEIKNDKE---QKNKLEVE-----LNKLEKQK---KENKKNIDKFLTEIKKKEKELEKlnNKYNDLKKQKEELENELNLL 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1044 HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRL 1123
Cdd:TIGR04523  179 EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1124 SVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSqkdcYEKEIEGLNfkvvhlSQEINHLQKLFREE-TDINESIRHEVT 1202
Cdd:TIGR04523  259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLN------NQKEQDWNKELKSElKNQEKKLEEIQN 328

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 568961013  1203 RLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:TIGR04523  329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366

SMC_prok_B

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

1015-1240

2.02e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.02e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1015 FELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA-----------RLSKQAKTISEFEKEIELLQA 1083
Cdd:TIGR02168  668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEqlrkeleelsrQISALRKDLARLEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1084 QKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQkdcyE 1163
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL----R 823

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961013  1164 KEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL---IEELESELEALLNERASLEEALALLRSELE 897

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

878-1101

2.16e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.16e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  878 IRRFVLNIQLTY-RVQRLQKKLEDQNReNHGLVEKltslAALRVGDLEKVQKLEAELEKAAT---------HRHSYEEKG 947
Cdd:COG4913   213 VREYMLEEPDTFeAADALVEHFDDLER-AHEALED----AREQIELLEPIRELAERYAAARErlaeleylrAALRLWFAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  948 RRYrDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKE-----------KMDKLTRQLfDDVQKEEQQRlvlekgfE 1016
Cdd:COG4913   288 RRL-ELLEAELEELRAELARLEAELERLEARLDALREELDEleaqirgnggdRLEQLEREI-ERLERELEER-------E 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1017 LKTQAYEKQIESL--------------REEIKALKDERSQLHHQLEEGQvtsDRLKGEVARLSKQAKTIsefEKEIELLQ 1082
Cdd:COG4913   359 RRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELREL---EAEIASLE 432

                         250
                  ....*....|....*....
gi 568961013 1083 AQKIDVEKHVQSQKREMRE 1101
Cdd:COG4913   433 RRKSNIPARLLALRDALAE 451

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

952-1240

2.31e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.31e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  952 DTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLfdDVQKEEQQRLVLEKgfelktQAYEKQIESLRE 1031
Cdd:COG4372     2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEEL--EQLREELEQAREEL------EQLEEELEQARS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1032 EIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT----ISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVT 1107
Cdd:COG4372    74 ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEElqeeLEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1108 KQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAyEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLF 1187
Cdd:COG4372   154 ELEEQLESLQEELAALEQELQALSEAEAEQALD-ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961013 1188 REETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIE 1240
Cdd:COG4372   233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

1016-1238

2.59e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.59e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1016 ELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQkidvekhVQSQ 1095
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAE-------IEER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1096 KREMRERMSEVTKQ---------LLESYDIEDVRSRLSVedLEHLNE-DGELwfaYEGLKKATRVLEshfqSQKDCYEKE 1165
Cdd:COG3883    85 REELGERARALYRSggsvsyldvLLGSESFSDFLDRLSA--LSKIADaDADL---LEELKADKAELE----AKKAELEAK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961013 1166 IEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLtsenmmipdfKQQISELERQKQDLESRLKEQAEK 1238
Cdd:COG3883   156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA----------EAQLAELEAELAAAEAAAAAAAAA 218

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

885-1240

2.84e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.84e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   885 IQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAAthrhsyEEKGRRYRDTVEERLSKLQKH 964
Cdd:TIGR04523  256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELE-------KQLNQLKSEISDLN------NQKEQDWNKELKSELKNQEKK 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   965 NAELELQRERAEQMLqeksEELKEKMDKLTRQLFD-DVQKEEQQRLVLEKGFELKTqaYEKQIESLREEIKALKDERSQL 1043
Cdd:TIGR04523  323 LEEIQNQISQNNKII----SQLNEQISQLKKELTNsESENSEKQRELEEKQNEIEK--LKKENQSYKQEIKNLESQINDL 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1044 HHQLEEGQVTSDRLKGEVARLSKQAKTIsefEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKqlLESYdIEDVRSRL 1123
Cdd:TIGR04523  397 ESKIQNQEKLNQQKDEQIKKLQQEKELL---EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN--LDNT-RESLETQL 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1124 SVEDLEHLNEDGELWFAYEGLKKATRVLEShFQSQKDCYEKEIEGLNFKVVHLSQEINHLQ----KLFREETDINESIRH 1199
Cdd:TIGR04523  471 KVLSRSINKIKQNLEQKQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLEsekkEKESKISDLEDELNK 549

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 568961013  1200 EVTRLTSENM--MIPDFKQQISELerqKQDLESRLKEQAEKIE 1240
Cdd:TIGR04523  550 DDFELKKENLekEIDEKNKEIEEL---KQTQKSLKKKQEEKQE 589

COG2433

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

993-1138

2.88e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 2.88e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  993 LTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT-- 1070
Cdd:COG2433   382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRei 461

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961013 1071 -----ISEFEKEIELLQAQKIDVEKHVQSQKREMrERMSEVTKqLLESYDIEDVR--SRLSVEDLEHLNEDGELW 1138
Cdd:COG2433   462 rkdreISRLDREIERLERELEEERERIEELKRKL-ERLKELWK-LEHSGELVPVKvvEKFTKEAIRRLEEEYGLK 534

mukB

PRK04863

chromosome partition protein MukB;

923-1124

2.95e-05

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.95e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  923 LEKVQKLEAELEKAATHRhSYEEKGRRYRD--TVEERLSKLQKHNAELElQRERAEQMLQekseelkekmdkltrQLFDD 1000
Cdd:PRK04863  479 YQLVRKIAGEVSRSEAWD-VARELLRRLREqrHLAEQLQQLRMRLSELE-QRLRQQQRAE---------------RLLAE 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1001 VQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGEVARLSKQAKTISEFEKEIEL 1080
Cdd:PRK04863  542 FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ-------LQARIQRLAARAPAWLAAQDALAR 614

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961013 1081 LQAQ-------KIDVEKHVQSQKRemRERMSEVTKQLLES--YDIEDVRSRLS 1124
Cdd:PRK04863  615 LREQsgeefedSQDVTEYMQQLLE--RERELTVERDELAArkQALDEEIERLS 665

Laminin_I

pfam06008

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...

897-1118

3.25e-05

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.

Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 47.02 E-value: 3.25e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   897 KLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAE 976
Cdd:pfam06008   41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDL 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   977 QMLQEKSEELKEKMDklTRQLFDDVQKEEQQrlvLEKGFELKTQAyEKQIESLREEIKALKDersQLHHQLEEgqvTSDR 1056
Cdd:pfam06008  121 SRMLAEAQRMLGEIR--SRDFGTQLQNAEAE---LKAAQDLLSRI-QTWFQSPQEENKALAN---ALRDSLAE---YEAK 188

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961013  1057 LKGEVARLSK-QAKTisefeKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIED 1118
Cdd:pfam06008  189 LSDLRELLREaAAKT-----RDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARDSLD 246

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

971-1190

3.26e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.26e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  971 QRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKgFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEG 1050
Cdd:COG4942    18 QADAAAE-AEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1051 QVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKI-DVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:COG4942    96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961013 1130 H---LNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREE 1190
Cdd:COG4942   176 LealLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

895-1238

3.29e-05

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 3.29e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  895 QKKLEDQNRENHGLVEKLTSLAAlRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRER 974
Cdd:COG5185   208 KESETGNLGSESTLLEKAKEIIN-IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANN 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  975 AEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIkalKDERSQLHHQLEEGQVTS 1054
Cdd:COG5185   287 LIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEI---EQGQESLTENLEAIKEEI 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1055 DRLKGEVaRLSKQAKTISEFEKEIEL----LQAQKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRLSV---- 1125
Cdd:COG5185   364 ENIVGEV-ELSKSSEELDSFKDTIEStkesLDEIPQNQRGYAQEILATLEDTLKAADRQIEElQRQIEQATSSNEEvskl 442

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1126 --------EDLEHLNEDGELWFAYEGLKKATRVLeshfQSQKDCYEKEIEGLNFKVVHLSQEINHL-----QKLFREETD 1192
Cdd:COG5185   443 lneliselNKVMREADEESQSRLEEAYDEINRSV----RSKKEDLNEELTQIESRVSTLKATLEKLrakleRQLEGVRSK 518

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 568961013 1193 INESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEK 1238
Cdd:COG5185   519 LDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAAN 564

Motor_domain

cd01363

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

627-652

3.84e-05

Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 45.41 E-value: 3.84e-05

                          10        20
                  ....*....|....*....|....*.
gi 568961013  627 KFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd01363   145 IINESLNTLMNVLRATRPHFVRCISP 170

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

924-1156

4.55e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.55e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQM------LQEKSEELKEKMDKLTRQL 997
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQKER 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  998 fDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEegQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:COG4372   125 -QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEAEQALDELLKEANRNAEKEEE 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013 1078 IELLQaQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRsrlSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQ 1156
Cdd:COG4372   202 LAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE---LEEDKEELLEEVILKEIEELELAILVEKDTEEE 276

PRK05771

V-type ATP synthase subunit I; Validated

986-1242

4.70e-05

V-type ATP synthase subunit I; Validated

Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 4.70e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  986 LKEKMDKLTRQL-------FDDVqKEEQQRLVLEKGFELKTQAYEK--QIESLREEIKALKDERSQLHHQLEEgqvtsDR 1056
Cdd:PRK05771   14 LKSYKDEVLEALhelgvvhIEDL-KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVKSLE-----EL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1057 LKGEVARLSKQAKTISEFEKEIELLQaqkidvekhvqSQKREMRERMSEVTKqlLESYDIedvrsrlsveDLEHLNeDGE 1136
Cdd:PRK05771   88 IKDVEEELEKIEKEIKELEEEISELE-----------NEIKELEQEIERLEP--WGNFDL----------DLSLLL-GFK 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1137 LWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFrEETDINESIRHEVTRLTSENMMIPDFKQ 1216
Cdd:PRK05771  144 YVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVE-EELKKLGFERLELEEEGTPSELIREIKE 222

                         250       260
                  ....*....|....*....|....*.
gi 568961013 1217 QISELERQKQDLESRLKEQAEKIEGF 1242
Cdd:PRK05771  223 ELEEIEKERESLLEELKELAKKYLEE 248

Apolipoprotein

pfam01442

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...

924-1084

5.39e-05

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.

Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.33 E-value: 5.39e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   924 EKVQKLEAELEKAAThrhsyEEKGRRYRDTVE--ERLSK-LQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDD 1000
Cdd:pfam01442   11 TYAEELQEQLGPVAQ-----ELVDRLEKETEAlrERLQKdLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKR 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1001 VQK--EEQQRLVLEKGFELKTQAyEKQIESLREEIKALKDE-RSQLHHQLEEGQVTSDRLKGEV-ARLSKQAKTISE-FE 1075
Cdd:pfam01442   86 LNAdaEELQEKLAPYGEELRERL-EQNVDALRARLAPYAEElRQKLAERLEELKESLAPYAEEVqAQLSQRLQELREkLE 164


                   ....*....
gi 568961013  1076 KEIELLQAQ 1084
Cdd:pfam01442  165 PQAEDLREK 173

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

976-1234

6.60e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 6.60e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  976 EQMLQEKS-----EELKEKMDKLTRqLFDDVQKEEQQRLVLEKgfelkTQAYEKQIESLREEIKALKDERSQLhhQLEEG 1050
Cdd:COG4913   215 EYMLEEPDtfeaaDALVEHFDDLER-AHEALEDAREQIELLEP-----IRELAERYAAARERLAELEYLRAAL--RLWFA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1051 QVTSDRLKGEVARLskqaktisefEKEIELLQAQKidveKHVQSQKREMRERMSEVTKQLLESydiedvrsrlSVEDLEH 1130
Cdd:COG4913   287 QRRLELLEAELEEL----------RAELARLEAEL----ERLEARLDALREELDELEAQIRGN----------GGDRLEQ 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1131 LNEDgelwfayegLKKATRVLESHFQSQKDcYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENmm 1210
Cdd:COG4913   343 LERE---------IERLERELEERERRRAR-LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA-- 410

                         250       260
                  ....*....|....*....|....
gi 568961013 1211 ipdfKQQISELERQKQDLESRLKE 1234
Cdd:COG4913   411 ----EAALRDLRRELRELEAEIAS 430

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

955-1106

7.28e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 7.28e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   955 EERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMD-KLT-----RQLFDDVQKEEQQRLVLEKGFE-LKTQAY--EKQ 1025
Cdd:pfam10174  337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEeKSTlageiRDLKDMLDVKERKINVLQKKIEnLQEQLRdkDKQ 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1026 IESLREEIKALKDERSQ-------LHHQLEEGQVTSDRLKGEVARLSKqaktisEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam10174  417 LAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDR------ERLEELESLKKENKDLKEKVSALQPE 490


                   ....*...
gi 568961013  1099 MRERMSEV 1106
Cdd:pfam10174  491 LTEKESSL 498

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

846-1049

8.50e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 8.50e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  846 ARRRYRKLLQEH-KAVILQKYARAWLARRRFQNIRRFVLNIQ-----LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALR 919
Cdd:COG4913   260 LAERYAAARERLaELEYLRAALRLWFAQRRLELLEAELEELRaelarLEAELERLEARLDALREELDELEAQIRGNGGDR 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  920 VGDLEK-VQKLEAELEKAATHRHSYEEKGRRYRDTVEERLsklqkhnAELELQRERAEQMLQEKSEELKEkmdkLTRQLF 998
Cdd:COG4913   340 LEQLEReIERLERELEERERRRARLEALLAALGLPLPASA-------EEFAALRAEAAALLEALEEELEA----LEEALA 408

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568961013  999 DDVQKEEQQRlvlekgfelktqayeKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:COG4913   409 EAEAALRDLR---------------RELRELEAEIASLERRKSNIPARLLA 444

YhaN

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

721-1096

1.03e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.03e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  721 LHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALT--IQRYFRGQQTVRK 798
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEeeLEEAQEELEELEE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  799 AITATAlKEAWAAIILQKycrgyLVRNLYQLIRVATITIQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLARRRFQNI 878
Cdd:COG4717   228 ELEQLE-NELEAAALEER-----LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  879 RRFvLNIQLTYRVQRLQKKLEDQNRENHGLVEKLT-SLAALRVGDLEKVQKLEAELEKAathrhsyeEKGRRYRDTVEER 957
Cdd:COG4717   302 KEA-EELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEEL--------EEELQLEELEQEI 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  958 LSKLQKHNAELELQRERAEQMLQEKsEELKEKMDKLTRQLfddvqkEEQQRLVLEKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQL------EELLGELEELLEALDEEELEEELEELEEELEELE 445

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013 1038 DERSQLHHQLEEgqvtsdrLKGEVARLSKQaKTISEFEKEIELLQAQKIDVEKHVQSQK 1096
Cdd:COG4717   446 EELEELREELAE-------LEAELEQLEED-GELAELLQELEELKAELRELAEEWAALK 496

Mitofilin

pfam09731

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...

910-1086

1.41e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.

Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.29 E-value: 1.41e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   910 EKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYE-EKGRRYRDTVEERLSKLQKHNAELELQRERAEQmlQEKSEELKE 988
Cdd:pfam09731  283 DDLNSLIAHAHREIDQLSKKLAELKKREEKHIERAlEKQKEELDKLAEELSARLEEVRAADEAQLRLEF--EREREEIRE 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   989 KMDKLTRQLFDDVQKEEQQRLvlekGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGEVARLSKQA 1068
Cdd:pfam09731  361 SYEEKLRTELERQAEAHEEHL----KDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNE-------LLANLKGLEKAT 429

                          170
                   ....*....|....*...
gi 568961013  1069 KTISEFEKEIelLQAQKI 1086
Cdd:pfam09731  430 SSHSEVEDEN--RKAQQL 445

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

776-1036

1.79e-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: 1.79e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  776 FLRERQAALTIQRYFRGQQTVRKAITATALKEAWAAIILQKYCRGYLVRNLYQLIRV-----------ATITIQAHTRGF 844
Cdd:COG1196   506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieylkaakagrATFLPLDKIRAR 585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  845 LARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLE 924
Cdd:COG1196   586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  925 KVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKL--QKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQ 1002
Cdd:COG1196   666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEeeEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745

                         250       260       270
                  ....*....|....*....|....*....|....
gi 568961013 1003 KEEQQRLVLEKGFELKTQAYEKQIESLREEIKAL 1036
Cdd:COG1196   746 ELLEEEALEELPEPPDLEELERELERLEREIEAL 779

MAP7

pfam05672

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...

890-1009

1.85e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.

Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.11 E-value: 1.85e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   890 RVQRLQKKLEDQNR-----ENHGLVEKLTSLAAlrvgdlEKVQKLEAELEKAATHRH-SYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam05672   21 RQAREQREREEQERlekeeEERLRKEELRRRAE------EERARREEEARRLEEERRrEEEERQRKAEEEAEEREQREQE 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568961013   964 HNAELELQRERAEQMLQEKSEELKEKMDKLTrqlfddvQKEEQQRL 1009
Cdd:pfam05672   95 EQERLQKQKEEAEAKAREEAERQRQEREKIM-------QQEEQERL 133

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

867-1170

1.85e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.85e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  867 RAWLARRRFQNIRRFVLNIQltYRVQRLQKKLEDQNRENHGLVEKLTS--------LAALR--------VGDLEKVQ-KL 929
Cdd:COG3096   286 RALELRRELFGARRQLAEEQ--YRLVEMARELEELSARESDLEQDYQAasdhlnlvQTALRqqekieryQEDLEELTeRL 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  930 EAE---LEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQ-----EKSEEL--------------- 986
Cdd:COG3096   364 EEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQavqalEKARALcglpdltpenaedyl 443

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  987 ---KEKMDKLTRQLFDDVQK---EEQQRLVLEKGFEL---------KTQAYEKQIESLRE--EIKALKDERSQLHHQL-- 1047
Cdd:COG3096   444 aafRAKEQQATEEVLELEQKlsvADAARRQFEKAYELvckiageveRSQAWQTARELLRRyrSQQALAQRLQQLRAQLae 523

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1048 ----EEGQVTSDRLKGEVA-RLSKQAKTISEFEKEIELLQAQKIDVEKHV----------QSQKREMRERMSEVTKQLLE 1112
Cdd:COG3096   524 leqrLRQQQNAERLLEEFCqRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqrselRQQLEQLRARIKELAARAPA 603

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961013 1113 SYDIEDVRSRLSVEDLEHLNEDGELWFAYEGL---KKATRVLESHFQSQKDCYEKEIEGLN 1170
Cdd:COG3096   604 WLAAQDALERLREQSGEALADSQEVTAAMQQLlerEREATVERDELAARKQALESQIERLS 664

ClpA

COG0542

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...

988-1093

2.28e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 2.28e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  988 EKMDKLTRQLfdDVQKEEQQRLVLEKgfelkTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQ 1067
Cdd:COG0542   411 EELDELERRL--EQLEIEKEALKKEQ-----DEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQR 483

                          90       100
                  ....*....|....*....|....*.
gi 568961013 1068 AKTISEFEKEIELLQAQKIDVEKHVQ 1093
Cdd:COG0542   484 YGKIPELEKELAELEEELAELAPLLR 509

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

845-1137

2.43e-04

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 2.43e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   845 LARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdLE 924
Cdd:pfam02463  185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES-------SK 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   925 KVQKLEAELEKaatHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKE 1004
Cdd:pfam02463  258 QEIEKEEEKLA---QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1005 EQ--QRLVLEKGFELKTQAYEKQIESLREEIKAL---KDERSQLHHQLEEGQVTSDRLKGEVarLSKQAKTISEFEKEIE 1079
Cdd:pfam02463  335 EEieELEKELKELEIKREAEEEEEEELEKLQEKLeqlEEELLAKKKLESERLSSAAKLKEEE--LELKSEEEKEAQLLLE 412

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961013  1080 LLQAQKIDVEKHVQSQKREmrermSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGEL 1137
Cdd:pfam02463  413 LARQLEDLLKEEKKEELEI-----LEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

924-1100

2.76e-04

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 2.76e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELelqRERAEQMLQEKSEELKEKMDKLTRQLFDDVQk 1003
Cdd:PRK00409  523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKEAKKEADEIIKELRQLQK- 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1004 eEQQRLVLEKgfelKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQ---VTSDRLKGEVARLSKQAKTISEF------ 1074
Cdd:PRK00409  599 -GGYASVKAH----ELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDevkYLSLGQKGEVLSIPDDKEAIVQAgimkmk 673

                         170       180
                  ....*....|....*....|....*...
gi 568961013 1075 --EKEIELLQAQKIDVEKHVQSQKREMR 1100
Cdd:PRK00409  674 vpLSDLEKIQKPKKKKKKKPKTVKPKPR 701

PRK04778

septation ring formation regulator EzrA; Provisional

896-1224

2.85e-04

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 2.85e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  896 KKLEDQNRENHGLVEKLtslaalrvgdLEKVQKLEAELekaATHRHSYeekGRRYrDTVEERLSKLQKHNAELE------ 969
Cdd:PRK04778  129 QELLESEEKNREEVEQL----------KDLYRELRKSL---LANRFSF---GPAL-DELEKQLENLEEEFSQFVeltesg 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  970 --LQRERAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRL---------VLEKGFELKTQAYEKQIESLREEIKALKD 1038
Cdd:PRK04778  192 dyVEAREILDQLEEELAALEQIMEEIP-ELLKELQTELPDQLqelkagyreLVEEGYHLDHLDIEKEIQDLKEQIDENLA 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1039 ERSQLhhqleegqvtsdrlkgEVARLSKQAKTISE--------FEKEIEllqAQKiDVEKHvQSQKREMRERMSEVTKQL 1110
Cdd:PRK04778  271 LLEEL----------------DLDEAEEKNEEIQEridqlydiLEREVK---ARK-YVEKN-SDTLPDFLEHAKEQNKEL 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1111 LEsyDIEDVRS--RLSVEDLEHLNE-DGELWFAYEGLKKATRVLESH---FQSQKDCYEKEIEGLnfKVVHLSQE--INH 1182
Cdd:PRK04778  330 KE--EIDRVKQsyTLNESELESVRQlEKQLESLEKQYDEITERIAEQeiaYSELQEELEEILKQL--EEIEKEQEklSEM 405

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 568961013 1183 LQKLFREETDINESIRHevtrltsenmmipdFKQQISELERQ 1224
Cdd:PRK04778  406 LQGLRKDELEAREKLER--------------YRNKLHEIKRY 433

ATG16

pfam08614

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...

924-1082

3.44e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.

Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.61 E-value: 3.44e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   924 EKVQKLEAELEKAATHRHSY-EEKGRRYRDTVEERLSKLQKHNAEL-ELQRERAE--QMLQEKSEELKEKMDKLTRQlfd 999
Cdd:pfam08614   21 AENAKLQSEPESVLPSTSSSkLSKASPQSASIQSLEQLLAQLREELaELYRSRGElaQRLVDLNEELQELEKKLRED--- 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1000 dvqkeeqqrlvlekgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA----RLSKQAKTISEFE 1075
Cdd:pfam08614   98 -----------------------ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELValqlQLNMAEEKLRKLE 154


                   ....*...
gi 568961013  1076 KE-IELLQ 1082
Cdd:pfam08614  155 KEnRELVE 162

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

870-1100

3.57e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 3.57e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   870 LARRRFQNIRRFVlnIQLTYRVQRLQKKLEDQ-NRENHGLVEKLTSLAA-LRVGDLEKVQKLEAELEKAATHRhsyEEKG 947
Cdd:pfam12128  643 FARTALKNARLDL--RRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAqLKQLDKKHQAWLEEQKEQKREAR---TEKQ 717

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   948 RRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfdDVqkEEQQRLVLEKGFELKTQAYEkQIE 1027
Cdd:pfam12128  718 AYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASL------GV--DPDVIAKLKREIRTLERKIE-RIA 788

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1028 SLREEIKALKD--------ERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT-ISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam12128  789 VRRQEVLRYFDwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLrRAKLEMERKASEKQQVRLSENLRGLRCE 868


                   ..
gi 568961013  1099 MR 1100
Cdd:pfam12128  869 MS 870

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

881-1043

3.81e-04

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 3.81e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   881 FVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAathrHSYEEKGRRYR---DTVEER 957
Cdd:pfam15905  176 MAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITEL----SCVSEQVEKYKldiAQLEEL 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   958 LSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfddvqKEEQQRLVLEkgFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam15905  252 LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLL---------ESEKEELLRE--YEEKEQTLNAELEELKEKLTLEE 320


                   ....*.
gi 568961013  1038 DERSQL 1043
Cdd:pfam15905  321 QEHQKL 326

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

961-1030

4.03e-04

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.72 E-value: 4.03e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961013  961 LQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDD-----VQKEEQQRLVLEKGFELKTQAYEKQIESLR 1030
Cdd:cd16269   217 LEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEqeralESKLKEQEALLEEGFKEQAELLQEEIRSLK 291

Spc7

smart00787

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

960-1131

4.77e-04

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

Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 4.77e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013    960 KLQKHNAELELQRERAEQMLQEkSEELKEKMDKLtrqlfDDVQKEEQQRLVlekgfelktqAYEKQIESLREEIKALKDE 1039
Cdd:smart00787  120 QLVKTFARLEAKKMWYEWRMKL-LEGLKEGLDEN-----LEGLKEDYKLLM----------KELELLNSIKPKLRDRKDA 183

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   1040 RSQLHHQLEEG-----QVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQLL 1111
Cdd:smart00787  184 LEEELRQLKQLedeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEAEKKLE 263

                           170       180
                    ....*....|....*....|...
gi 568961013   1112 ES--YDIEDVRS-RLSVEDLEHL 1131
Cdd:smart00787  264 QCrgFTFKEIEKlKEQLKLLQSL 286

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

890-1104

4.90e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.90e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELE 969
Cdd:TIGR02169  792 RIPEIQAELSKLEEEVSRIEARLREIEQ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   970 LQRERAEQMLQEKSEELKEkmdkltrqlfddvqkeeqqrlvlekgfelktqaYEKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR02169  868 EELEELEAALRDLESRLGD---------------------------------LKKERDELEAQLRELERKIEELEAQIEK 914

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568961013  1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhVQSQKREMRERMS 1104
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIR 968

PLN03229

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

966-1240

5.23e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 5.23e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  966 AELELQRERaeqmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEI-----------K 1034
Cdd:PLN03229  432 RELEGEVEK----LKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENLREEFskansqdqlmhP 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1035 ALKDERSQLHHQL-----EEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLqaqKIDVEKHVQS--QKREMRERM---- 1103
Cdd:PLN03229  508 VLMEKIEKLKDEFnkrlsRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKL---KAEINKKFKEvmDRPEIKEKMealk 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1104 SEVTKQLLESYDIEDvrsRLSVEDLEHLNEDGELWFAyEGLKKATRVLESHFQSQKDCYEKEI-EGLNFKVVHLSQEINH 1182
Cdd:PLN03229  585 AEVASSGASSGDELD---DDLKEKVEKMKKEIELELA-GVLKSMGLEVIGVTKKNKDTAEQTPpPNLQEKIESLNEEINK 660

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013 1183 LQKLFREETDIN---ESIRHEVTRLTSEnmmiPDF--KQQISELERQ-KQDL-----ESRLKEQAEKIE 1240
Cdd:PLN03229  661 KIERVIRSSDLKskiELLKLEVAKASKT----PDVteKEKIEALEQQiKQKIaealnSSELKEKFEELE 725

TPR_MLP1_2

pfam07926

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...

924-1049

5.27e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.

Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 5.27e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEE--RLSK---------LQKHNAEL-ELQRERAE-QMLQEKSEELKEKM 990
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAReaqqnyereLVLHAEDIkALQALREElNELKAEIAELKAEA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013   991 DKLTRQLfddvqkeeqqrLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:pfam07926   81 ESAKAEL-----------EESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128

PRK12704

phosphodiesterase; Provisional

954-1109

6.04e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 6.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  954 VEERLSKLQKHNAE------LELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIE 1027
Cdd:PRK12704   24 VRKKIAEAKIKEAEeeakriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1028 SLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEiellQAQKIDVEKhvqsQKREMRERMSEVT 1107
Cdd:PRK12704  104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE----EAKEILLEK----VEEEARHEAAVLI 175


                  ..
gi 568961013 1108 KQ 1109
Cdd:PRK12704  176 KE 177

PTZ00121

MAEBL; Provisional

924-1240

6.80e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 6.80e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEElKEKMDKLTRQLFDDVQK 1003
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-KKKADAAKKKAEEKKKA 1393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1004 EEQQRLVLE---KGFELKTQAYEKQIEslrEEIKALKDER---SQLHHQLEEGQVTSD-RLKGEVARLSKQAKTISEFEK 1076
Cdd:PTZ00121 1394 DEAKKKAEEdkkKADELKKAAAAKKKA---DEAKKKAEEKkkaDEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAK 1470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1077 EIELLQAQKIDVEKHVQSQKR--EMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEgLKKATRVlesh 1154
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE-AKKAEEK---- 1545

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1155 fqsqkdcyEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIR-----HEVTRLTSENMMIPDFKQQISELERQKQDLE 1229
Cdd:PTZ00121 1546 --------KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617

                         330
                  ....*....|..
gi 568961013 1230 SRLK-EQAEKIE 1240
Cdd:PTZ00121 1618 AKIKaEELKKAE 1629

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

924-1109

9.19e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 9.19e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  924 EKVQKLEAELEKAathrhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLFD---D 1000
Cdd:COG3883    23 KELSELQAELEAA-------QAELDALQAELEELNEEYNELQAELEALQAEIDK-LQAEIAEAEAEIEERREELGErarA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1001 VQKEEQQRLVLE-----KGFE--------LKT--QAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLS 1065
Cdd:COG3883    95 LYRSGGSVSYLDvllgsESFSdfldrlsaLSKiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568961013 1066 KQaktISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQ 1109
Cdd:COG3883   175 AQ---QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215

PRK02224

DNA double-strand break repair Rad50 ATPase;

968-1243

9.29e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 9.29e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  968 LELQRERA-------EQMLQEKSEELkekmDKLTRQLFDDVQKEEQQRLvlekgfelktQAYEKQIESLREEIKALKDER 1040
Cdd:PRK02224  164 LEEYRERAsdarlgvERVLSDQRGSL----DQLKAQIEEKEEKDLHERL----------NGLESELAELDEEIERYEEQR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1041 SQLHHQLEEGQVTsdrlkgeVARLSKQAKTISEFEKEIELLQAQKIDVEKhvqsQKREMRERMSEVTKQLLE-SYDIEDV 1119
Cdd:PRK02224  230 EQARETRDEADEV-------LEEHEERREELETLEAEIEDLRETIAETER----EREELAEEVRDLRERLEElEEERDDL 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1120 RSRLSVEDL--EHLNEDGElwfAYEGLKKATR-VLESHFQSQKDcYEKEIEGLNFKVVHLSQEINHLqklfREETDINES 1196
Cdd:PRK02224  299 LAEAGLDDAdaEAVEARRE---ELEDRDEELRdRLEECRVAAQA-HNEEAESLREDADDLEERAEEL----REEAAELES 370

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 568961013 1197 irhevtRLTSENMMIPDFKQQISELERQKQDLESRLK---EQAEKIEGFS 1243
Cdd:PRK02224  371 ------ELEEAREAVEDRREEIEELEEEIEELRERFGdapVDLGNAEDFL 414

K-box

pfam01486

K-box region; The K-box region is commonly found associated with SRF-type transcription ...

973-1048

1.06e-03

K-box region; The K-box region is commonly found associated with SRF-type transcription factors see pfam00319. The K-box is a possible coiled-coil structure. Possible role in multimer formation.

Pssm-ID: 460228 [Multi-domain] Cd Length: 91 Bit Score: 39.37 E-value: 1.06e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   973 ERAEQMLQEKSEELKEKMDKLTRQL------------FDDVQKEEQQrlvLEKGF----ELKTQAYEKQIESLREEIKAL 1036
Cdd:pfam01486    3 ENEQENWQQEAAKLKKEIENLQRSQrqllgedlsslsLKELQQLEQQ---LEKSLkrirSRKNQLLLEQIEELKKKERIL 79

                           90
                   ....*....|..
gi 568961013  1037 KDERSQLHHQLE 1048
Cdd:pfam01486   80 QEENKELRKKLE 91

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

890-1130

1.12e-03

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.12e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDL----EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQkhn 965
Cdd:pfam12128  277 RQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ--- 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   966 AELELQRER------AEQMLQEKSEELKEKMD-KLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKA--- 1035
Cdd:pfam12128  354 SELENLEERlkaltgKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgkl 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1036 -LKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhVQSQKREMRERMSEVTKQL-LES 1113
Cdd:pfam12128  434 eFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVER-LQSELRQARKRRDQASEALrQAS 512

                          250
                   ....*....|....*..
gi 568961013  1114 YDIEDVRSRLsvEDLEH 1130
Cdd:pfam12128  513 RRLEERQSAL--DELEL 527

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

922-1129

1.22e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 1.22e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   922 DLEKVQKLEAELEKAATHRHSY----EEKGRRYRDTVEERlsklqKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQL 997
Cdd:pfam13868    4 NSDELRELNSKLLAAKCNKERDaqiaEKKRIKAEEKEEER-----RLDEMMEEERERALEEEEEKEEERKEERKRYRQEL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   998 FDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREE----IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQA-KTIS 1072
Cdd:pfam13868   79 EEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEdqaeAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEdERIL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961013  1073 EFEKEIELLQAQKIDVEKHVQSQKREMRERMSE-VTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:pfam13868  159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAqQEKAQDEKAERDELRAKLYQEEQE 216

YhaN

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

958-1153

1.29e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.29e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  958 LSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQrlvlekgfelktQAYEKQIESLREEIKALK 1037
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL------------EELEEELEELEAELEELR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1038 DERSQLHHQLEEGQVTSDR--LKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLEsyD 1115
Cdd:COG4717   116 EELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--E 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568961013 1116 IEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLES 1153
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

SHE3

pfam17078

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...

884-1110

1.31e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.

Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.65 E-value: 1.31e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdlekvqKLEAELEKAATHRhsyeeKGRRYRDtVEERLSKLQK 963
Cdd:pfam17078   19 NLQLTVQSQNLLSKLEIAQQKESKFLENLASL------------KHENDNLSSMLNR-----KERRLKD-LEDQLSELKN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   964 HNAELELQ----RERAEQmLQEKSEELKEKMDKLTRQLfdDVQKEEQQRLvlekgfelkTQAYEKQIESLREEIKALKDE 1039
Cdd:pfam17078   81 SYEELTESnkqlKKRLEN-SSASETTLEAELERLQIQY--DALVDSQNEY---------KDHYQQEINTLQESLEDLKLE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1040 rsqLHHQLEE-GQVTSDRLKGEVARLS------KQAKTISEfEKEIELLQ-----AQKIDVEKHVQSQKrEMRERMSEVT 1107
Cdd:pfam17078  149 ---NEKQLENyQQRISSNDKDIDTKLDsynnkfKNLDNIYV-NKNNKLLTkldslAQLLDLPSWLNLYP-ESRNKILEYA 223


                   ...
gi 568961013  1108 KQL 1110
Cdd:pfam17078  224 EKM 226

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

764-1079

1.35e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.35e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  764 QKHVRGWLQRRKFLRERQAALTIQRyfRGQQTVRKAITAT--ALKEAWAAIILQKYCRGYLVRNLYQLIRVATITIQAHT 841
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAEL--EELEAELEELEAElaELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  842 RGflaRRRYRKLLQEHKAVILQKYARawLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVG 921
Cdd:COG1196   302 QD---IARLEERRRELEERLEELEEE--LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  922 DLEKVQKL---EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLF 998
Cdd:COG1196   377 AEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  999 DDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEI 1078
Cdd:COG1196   457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536


                  .
gi 568961013 1079 E 1079
Cdd:COG1196   537 E 537

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

852-1166

1.47e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.47e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   852 KLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEA 931
Cdd:TIGR00606  785 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKS 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   932 ELEKAATHRHSYEEKGRR---YRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqlfddvqKEEQQR 1008
Cdd:TIGR00606  865 KTNELKSEKLQIGTNLQRrqqFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS-------KETSNK 937

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1009 LVlekgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQvtSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDV 1088
Cdd:TIGR00606  938 KA------------QDKVNDIKEKVKNIHGYMKDIENKIQDGK--DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLM 1003

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1089 EKHVQSQKREMRERMSEVTKQLLESyDIEDVRSRLSVEDLEhLNEDG--ELWFAYEGLKKATRVL---ESHFQSQKDCYE 1163
Cdd:TIGR00606 1004 RQDIDTQKIQERWLQDNLTLRKREN-ELKEVEEELKQHLKE-MGQMQvlQMKQEHQKLEENIDLIkrnHVLALGRQKGYE 1081


                   ...
gi 568961013  1164 KEI 1166
Cdd:TIGR00606 1082 KEI 1084

PTZ00108

DNA topoisomerase 2-like protein; Provisional

852-1127

1.51e-03

DNA topoisomerase 2-like protein; Provisional

Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 1.51e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  852 KLLQEHKAVILQKYA--RAWL------ARRRFQNIRRFVLNIqltyrvqrLQKKLEDQNRENHGLVEKLTSLAALRVGDL 923
Cdd:PTZ00108  980 DILKEFYLVRLDLYKkrKEYLlgklerELARLSNKVRFIKHV--------INGELVITNAKKKDLVKELKKLGYVRFKDI 1051

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  924 EKVQK---LEAELEKAATHRHSYEEKGRRYRDTVEE------------RLSKLQKHNAELELQRERAEQMLQEKSEEL-K 987
Cdd:PTZ00108 1052 IKKKSekiTAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNTTPKDMwL 1131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  988 EKMDKLTRQLFDDVQKEEQQRLVLEKgFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRlKGEVARLSKQ 1067
Cdd:PTZ00108 1132 EDLDKFEEALEEQEEVEEKEIAKEQR-LKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSK-RVDSDEKRKL 1209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1068 AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVED 1127
Cdd:PTZ00108 1210 DDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEG 1269

ClpA

COG0542

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...

952-1055

1.55e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 1.55e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  952 DTVEERLSKLQKHNAELELQRERA----EQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK--Q 1025
Cdd:COG0542   407 DSKPEELDELERRLEQLEIEKEALkkeqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRygK 486

                          90       100       110
                  ....*....|....*....|....*....|
gi 568961013 1026 IESLREEIKALKDERSQLHHQLEEgQVTSD 1055
Cdd:COG0542   487 IPELEKELAELEEELAELAPLLRE-EVTEE 515

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

895-1206

1.67e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 1.67e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   895 QKKLEDQNRENHGLVEKLTSLAALRVGDLE----KVQKLEAELEKAATHRHSYEEKGRRYRDTVE-ERL--SKLQKHNAE 967
Cdd:pfam05483  417 DEKLLDEKKQFEKIAEELKGKEQELIFLLQarekEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkEKLknIELTAHCDK 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   968 LELQRERAEQMLQEKSEELKEKMDKLtrqlfDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDErsqLHHQL 1047
Cdd:pfam05483  497 LLLENKELTQEASDMTLELKKHQEDI-----INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE---VKCKL 568

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1048 EEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQlLESYDIEDVRSRLSVED 1127
Cdd:pfam05483  569 DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ-LNAYEIKVNKLELELAS 647

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1128 LEHlnedgelwfayeglkkatrvlesHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE----ETDINESIRHEVTR 1203
Cdd:pfam05483  648 AKQ-----------------------KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklQKEIDKRCQHKIAE 704


                   ...
gi 568961013  1204 LTS 1206
Cdd:pfam05483  705 MVA 707

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

921-1112

1.69e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.

Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 1.69e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   921 GDLEKVQKLEAELEKAATHRHSYEEKGRRYR---DTVEERLSKLQKHNAELELQR-------ERAEQMLQEKSEELKEKM 990
Cdd:pfam15709  307 GNMESEEERSEEDPSKALLEKREQEKASRDRlraERAEMRRLEVERKRREQEEQRrlqqeqlERAEKMREELELEQQRRF 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   991 D--KLTRQLFDDvqkEEQQRLVLEKGFELKTQAYE----KQIESLREEIKALKDERSQlhHQLEEGQVTSDRLKGEVARL 1064
Cdd:pfam15709  387 EeiRLRKQRLEE---ERQRQEEEERKQRLQLQAAQerarQQQEEFRRKLQELQRKKQQ--EEAERAEAEKQRQKELEMQL 461

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 568961013  1065 SKQAKTISEFEKEIEL-LQAQKIDVEKHVQSQKREMRERMSEVTKQLLE 1112
Cdd:pfam15709  462 AEEQKRLMEMAEEERLeYQRQKQEAEEKARLEAEERRQKEEEAARLALE 510

TBCA

pfam02970

Tubulin binding cofactor A;

1144-1241

1.79e-03

Tubulin binding cofactor A;

Pssm-ID: 460769 [Multi-domain] Cd Length: 99 Bit Score: 39.03 E-value: 1.79e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1144 LKKATRVLEsHFQSQKDCYEKEIEglnfkvvhlsQEINHLQKLFREETDINEsIRHEVTRLTSENMMIPDFKQQISEler 1223
Cdd:pfam02970    6 LKIKTGVVK-RLVKEEASYEKELE----------EQEARLEKLKADGADEYD-LKKQEEVLEETKAMIPDLKKRLEE--- 70

                           90
                   ....*....|....*...
gi 568961013  1224 QKQDLESRLKEQAEKIEG 1241
Cdd:pfam02970   71 AVEDLEEFLEEEEDLGAD 88

235kDa-fam

TIGR01612

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...

875-1208

2.17e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.

Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 2.17e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   875 FQNIRRFVLNIQLTYR-VQRLQKKLED--QNRENHGLVEKLTSLAALRvGDLEKVQKLEAELEKAATHRHSYEEKGRRYR 951
Cdd:TIGR01612 1442 FKNADENNENVLLLFKnIEMADNKSQHilKIKKDNATNDHDFNINELK-EHIDKSKGCKDEADKNAKAIEKNKELFEQYK 1520

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   952 DTVEERLSKLqkhnAELELQ------RERAEQMLQE----------KSEELKEKMDKLTRQLF---DDVQKEEQQ----- 1007
Cdd:TIGR01612 1521 KDVTELLNKY----SALAIKnkfaktKKDSEIIIKEikdahkkfilEAEKSEQKIKEIKKEKFrieDDAAKNDKSnkaai 1596

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1008 --RLVLEKgFE---LKTQAYEKQIESLREEIKALKDERSQL-----HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:TIGR01612 1597 diQLSLEN-FEnkfLKISDIKKKINDCLKETESIEKKISSFsidsqDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKE 1675

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1078 IELLQAQ----KIDVEKHVQSQKREMRERMSEV----------TKQLLESyDIEDVRSRLSVEDLEHLNEDGElwfayeg 1143
Cdd:TIGR01612 1676 LDELDSEiekiEIDVDQHKKNYEIGIIEKIKEIaiankeeiesIKELIEP-TIENLISSFNTNDLEGIDPNEK------- 1747

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961013  1144 lkkatrvLESHFQSQKDCYEKEIEGLNFKVvhlsqeiNHLQKLFREETDINEsIRHevTRLTSEN 1208
Cdd:TIGR01612 1748 -------LEEYNTEIGDIYEEFIELYNIIA-------GCLETVSKEPITYDE-IKN--TRINAQN 1795

PRK12704

phosphodiesterase; Provisional

924-1085

2.40e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.40e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  924 EKVQKLEAELEKaathrhsyeekgrryrdTVEERLSKLQKhnaeLELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQK 1003
Cdd:PRK12704   64 EEIHKLRNEFEK-----------------ELRERRNELQK----LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1004 EEQqrlVLEKGFELKtQAYEKQIESLrEEIKAL-KDE-RSQLHHQLEEgqvtsdRLKGEVARLskqaktISEFEKEIElL 1081
Cdd:PRK12704  123 QQE---LEKKEEELE-ELIEEQLQEL-ERISGLtAEEaKEILLEKVEE------EARHEAAVL------IKEIEEEAK-E 184


                  ....
gi 568961013 1082 QAQK 1085
Cdd:PRK12704  185 EADK 188

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

984-1240

2.50e-03

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.50e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   984 EELKEKMDKLTRQLfdDVQKEEQQRLvlEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVAR 1063
Cdd:pfam12128  600 EELRERLDKAEEAL--QSAREKQAAA--EEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAE 675

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1064 LSKQAKT-ISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSrlsvedlehlneDGELWFAYE 1142
Cdd:pfam12128  676 RKDSANErLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL------------KAAIAARRS 743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1143 GLKKATRVLEShfQSQKDCYEKEIEGLNfkVVHLSQEINHL-QKLFREETDINESIRHEVTRLTSENMMIPDFKQQISEL 1221
Cdd:pfam12128  744 GAKAELKALET--WYKRDLASLGVDPDV--IAKLKREIRTLeRKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNI 819

                          250
                   ....*....|....*....
gi 568961013  1222 ERQKQDLESRLKEQAEKIE 1240
Cdd:pfam12128  820 ERAISELQQQLARLIADTK 838

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

887-1060

2.64e-03

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.64e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAA-LRVGDLeKVQKLEAELEKAathRHSYEEKGRRYRDTVEER-------L 958
Cdd:pfam05483  599 LKKQIENKNKNIEELHQENKALKKKGSAENKqLNAYEI-KVNKLELELASA---KQKFEEIIDNYQKEIEDKkiseeklL 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   959 SKLQKHNA----ELELQRErAEQMLQEKSEELKEKMDKLTRQlFDDVQKEEQQRLVLEKGfelKTQAYEKQIESLREEIK 1034
Cdd:pfam05483  675 EEVEKAKAiadeAVKLQKE-IDKRCQHKIAEMVALMEKHKHQ-YDKIIEERDSELGLYKN---KEQEQSSAKAALEIELS 749

                          170       180
                   ....*....|....*....|....*.
gi 568961013  1035 ALKDERSQLHHQLEEGQVTSDRLKGE 1060
Cdd:pfam05483  750 NIKAELLSLKKQLEIEKEEKEKLKME 775

YhaN

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

1055-1243

2.72e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.72e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1055 DRLKGEVARLSK-QAKTISEFEKEIELLQaQKIDVEKHVQSQKREMRERMSEVTKQLLEsydIEDVRSRLSvEDLEHLNE 1133
Cdd:COG4717    49 ERLEKEADELFKpQGRKPELNLKELKELE-EELKEAEEKEEEYAELQEELEELEEELEE---LEAELEELR-EELEKLEK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1134 DGELWFAYEGLKKATRVLEsHFQSQKDCYEKEIEGLNFKVV---HLSQEINHLQ-KLFREETDINESIRHEVTRLTSEnm 1209
Cdd:COG4717   124 LLQLLPLYQELEALEAELA-ELPERLEELEERLEELRELEEeleELEAELAELQeELEELLEQLSLATEEELQDLAEE-- 200

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568961013 1210 mIPDFKQQISELERQKQDLESRLKEQAEKIEGFS 1243
Cdd:COG4717   201 -LEELQQRLAELEEELEEAQEELEELEEELEQLE 233

PRK09039

peptidoglycan -binding protein;

983-1084

3.04e-03

peptidoglycan -binding protein;

Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 3.04e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  983 SEEL--KEK-MDKLTRQLfddvqKEEQQRLVLEKgfeLKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKG 1059
Cdd:PRK09039   45 SREIsgKDSaLDRLNSQI-----AELADLLSLER---QGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116

                          90       100
                  ....*....|....*....|....*....
gi 568961013 1060 EVARLSKQ---AKTIS-EFEKEIELLQAQ 1084
Cdd:PRK09039  117 RAGELAQEldsEKQVSaRALAQVELLNQQ 145

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

891-1042

3.71e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.71e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  891 VQRLQKKLEDQNRENHGLVEKLTSLAAlRVGDLE-KVQKLEAELEKAAthRHSYEEKGRRyrDTVE-------------- 955
Cdd:COG3883    46 LEELNEEYNELQAELEALQAEIDKLQA-EIAEAEaEIEERREELGERA--RALYRSGGSV--SYLDvllgsesfsdfldr 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  956 -ERLSKLQKHNAEL--ELQRERAE-----QMLQEKSEELKEKMDKLTRQLFD-DVQKEEQQRLVleKGFELKTQAYEKQI 1026
Cdd:COG3883   121 lSALSKIADADADLleELKADKAEleakkAELEAKLAELEALKAELEAAKAElEAQQAEQEALL--AQLSAEEAAAEAQL 198

                         170
                  ....*....|....*.
gi 568961013 1027 ESLREEIKALKDERSQ 1042
Cdd:COG3883   199 AELEAELAAAEAAAAA 214

pfam00612

IQ calmodulin-binding motif; Calmodulin-binding motif.

831-851

4.06e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.

Pssm-ID: 459869 Cd Length: 21 Bit Score: 35.76 E-value: 4.06e-03

                           10        20
                   ....*....|....*....|.
gi 568961013   831 RVATITIQAHTRGFLARRRYR 851
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21

Crescentin

pfam19220

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...

887-1110

4.48e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.

Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.82 E-value: 4.48e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALrvgdlekVQKLEAELEKAATHRHSYEEKGRRYR---DTVEERLSKLQK 963
Cdd:pfam19220   88 LVARLAKLEAALREAEAAKEELRIELRDKTAQ-------AEALERQLAAETEQNRALEEENKALReeaQAAEKALQRAEG 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   964 HNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDDVQKEEQQR---LVLEKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam19220  161 ELATARERLALLEQenrRLQALSEEQAAELAELTRRLAELETQLDATRarlRALEGQLAAEQAERERAEAQLEEAVEAHR 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1038 DERSQLHHQLEEGQ---VTSDRLKGEVA---------------RLSKQAKTISEFEKEIELLQAQKIDVE---KHVQSQK 1096
Cdd:pfam19220  241 AERASLRMKLEALTaraAATEQLLAEARnqlrdrdeairaaerRLKEASIERDTLERRLAGLEADLERRTqqfQEMQRAR 320

                          250
                   ....*....|....
gi 568961013  1097 REMRERMSEVTKQL 1110
Cdd:pfam19220  321 AELEERAEMLTKAL 334

YhaN

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

1005-1223

4.58e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1005 EQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtSDRLKGEVARLSKQaktISEFEKEIELLQaQ 1084
Cdd:COG4717    52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAE---LEELREELEKLE-K 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1085 KIDVEKHVQsQKREMRERMSEVTKQLLESYDIEDVRSRLsVEDLEHLNEDgelwfayegLKKATRVLESHFQSQKDCYEK 1164
Cdd:COG4717   124 LLQLLPLYQ-ELEALEAELAELPERLEELEERLEELREL-EEELEELEAE---------LAELQEELEELLEQLSLATEE 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568961013 1165 EIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSEnMMIPDFKQQISELER 1223
Cdd:COG4717   193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE-LEAAALEERLKEARL 250

smart00015

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...

830-851

4.95e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.

Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.38 E-value: 4.95e-03

                            10        20
                    ....*....|....*....|..
gi 568961013    830 IRVATITIQAHTRGFLARRRYR 851
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

924-1234

5.02e-03

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 5.02e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   924 EKVQKLEAELEKAATHRHSYeekgRRYRDTVEERLSKL----------QKHNAELELQRERAEQ------MLQEKSEELK 987
Cdd:TIGR00606  591 DRLAKLNKELASLEQNKNHI----NNELESKEEQLSSYedklfdvcgsQDEESDLERLKEEIEKsskqraMLAGATAVYS 666

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   988 EKMDKLTRQ------LFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLhhqleegqvtsdrlkgeV 1061
Cdd:TIGR00606  667 QFITQLTDEnqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM-----------------L 729

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1062 ARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSV-EDLEHLNEDGELWFA 1140
Cdd:TIGR00606  730 GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTImERFQMELKDVERKIA 809

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1141 YEGLKKATRVLESHFQSQKdcyeKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDFKQQISE 1220
Cdd:TIGR00606  810 QQAAKLQGSDLDRTVQQVN----QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ 885

                          330
                   ....*....|....
gi 568961013  1221 LERQKQDLESRLKE 1234
Cdd:TIGR00606  886 FEEQLVELSTEVQS 899

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

1071-1239

5.06e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 5.06e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1071 ISEFEKEIELLQAQKIDVEKH---VQSQKREMRERMSEVTKQLLESYDIEDVRSRL-SVEDLEHLNEdgelwfayeglKK 1146
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENierLDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKE-----------KE 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1147 ATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE-ETDINESIRHEVTRLTSEnmmIPDFKQQISELERQK 1225
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSI 310

                          170
                   ....*....|....
gi 568961013  1226 QDLESRLKEQAEKI 1239
Cdd:TIGR02169  311 AEKERELEDAEERL 324

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

747-1069

5.07e-03

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 5.07e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   747 YLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVRKAITATALKEAWAAIILQKYCRGYLVRNL 826
Cdd:pfam02463  695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   827 yQLIRVATITIQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLarRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENH 906
Cdd:pfam02463  775 -ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL--EEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   907 GLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQE----- 981
Cdd:pfam02463  852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEaeill 931

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   982 ----KSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKtqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRL 1057
Cdd:pfam02463  932 kyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL----GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007

                          330
                   ....*....|..
gi 568961013  1058 KGEVARLSKQAK 1069
Cdd:pfam02463 1008 IRAIIEETCQRL 1019

YhaN

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

956-1151

5.07e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.07e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  956 ERLSKLQKHNAELELQR-ERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIK 1034
Cdd:COG4717    56 DELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013 1035 ALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQK-IDVEKHVQSQKREMRERMSEVTKQLLES 1113
Cdd:COG4717   136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEEL 215

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568961013 1114 YDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATRVL 1151
Cdd:COG4717   216 EEAQEELEELE-EELEQLENELEAAALEERLKEARLLL 252

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

953-1128

6.35e-03

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 6.35e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   953 TVEERLSKLQKHNAELELQRERAEQMLQEKSE-------ELKEKMDKLTRQLFDdvqKEEQQRLVLEKGFELKTQAYEK- 1024
Cdd:pfam10174  440 TLEEALSEKERIIERLKEQREREDRERLEELEslkkenkDLKEKVSALQPELTE---KESSLIDLKEHASSLASSGLKKd 516

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1025 -QIESLREEIKALKDERSQLHHQLEEGQVT----------SDRLK-----------------GEVARL-----------S 1065
Cdd:pfam10174  517 sKLKSLEIAVEQKKEECSKLENQLKKAHNAeeavrtnpeiNDRIRlleqevarykeesgkaqAEVERLlgilrevenekN 596

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961013  1066 KQAKTISEFEKEIELL---QAQKIDVEKHVQSQKRemRERMSEVTKQLLESYDIEDVRSRLSVEDL 1128
Cdd:pfam10174  597 DKDKKIAELESLTLRQmkeQNKKVANIKHGQQEMK--KKGAQLLEEARRREDNLADNSQQLQLEEL 660

DUF4515

pfam14988

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...

979-1185

6.38e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.

Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 39.37 E-value: 6.38e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   979 LQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktQAYEKQIESLREEIKALKDERSQLHHQLEEGQvtsdrlk 1058
Cdd:pfam14988    9 LAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA-------SRYTQQTAELQTQLLQKEKEQASLKKELQALR------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1059 gEVARLSKQAktisefEKEIELLQAQKIDVEKHVQSQKREMRERMSEvTKQLLESyDIEDVRSRLSVEDLEHlnedgELW 1138
Cdd:pfam14988   75 -PFAKLKESQ------EREIQDLEEEKEKVRAETAEKDREAHLQFLK-EKALLEK-QLQELRILELGERATR-----ELK 140

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568961013  1139 FAYEGLK-KATRVLESHFQSQKdcyeKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam14988  141 RKAQALKlAAKQALSEFCRSIK----RENRQLQKELLQLIQETQALEA 184

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

848-1240

6.43e-03

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 6.43e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   848 RRYRKLLQEHKAV----------ILQKYARAWLARRRFQNIRRFVLNIQltYRVQRLQKKLEDQNRENHGLVEKltSLAA 917
Cdd:pfam05483   78 RLYSKLYKEAEKIkkwkvsieaeLKQKENKLQENRKIIEAQRKAIQELQ--FENEKVSLKLEEEIQENKDLIKE--NNAT 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   918 LRVGDLEKvQKLEAELEKAATHRHSYEEKGRRYRDtVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQL 997
Cdd:pfam05483  154 RHLCNLLK-ETCARSAEKTKKYEYEREETRQVYMD-LNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEY 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   998 FDDVQKEEQQRLVL-----EKGFELKTQAY------------EKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGE 1060
Cdd:pfam05483  232 KKEINDKEKQVSLLliqitEKENKMKDLTFlleesrdkanqlEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1061 VARL------------------------SKQAKT-----ISEFEKEI----ELLQAQKIDVEKH----------VQSQKR 1097
Cdd:pfam05483  312 QKALeedlqiatkticqlteekeaqmeeLNKAKAahsfvVTEFEATTcsleELLRTEQQRLEKNedqlkiitmeLQKKSS 391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013  1098 EMrERMSEVTKQllESYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQkdcyEKEIEGLNFKVV--- 1174
Cdd:pfam05483  392 EL-EEMTKFKNN--KEVELEELKKILA-EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR----EKEIHDLEIQLTaik 463

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961013  1175 ----HLSQEINHLQKLFREETDINESIRHEVTRLTSENM-MIPDFKQQISELERQKQDL------ESRLKEQAEKIE 1240
Cdd:pfam05483  464 tseeHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeLTQEASDMTLELKKHQEDIinckkqEERMLKQIENLE 540

UPF0242

pfam06785

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...

904-1036

6.50e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.

Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 39.42 E-value: 6.50e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961013   904 ENHGLVEKLTSLAALrvgDLEKVQKLEAELEKaathRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKS 983
Cdd:pfam06785   66 EKSFLEEKEAKLTEL---DAEGFKILEETLEE----LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFR 138

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568961013   984 EELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFElKTQAYEKQIESLREEIKAL 1036
Cdd:pfam06785  139 LESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD-QIENLESKVRDLNYEIKTL 190

Myosin_tail_1