NCBI Conserved Domain Search

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

902-1441

1.33e-16

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: 86.65 E-value: 1.33e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   902 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVA 981
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   982 TGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNhrivEQAKEMTEtmerkLV 1061
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD----ELAEELAE-----LE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1062 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmlnvpkpghKRTDSTHSSNESEYTFSSEF----AETEDIA 1137
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1138 PRTEEPIEKKVPLDMSL----FLKLQKRVTELEQEKQLMQDELDRKEEQvfrskaKEEERPQIRGAELEYESLKRQELES 1213
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1214 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ---- 1281
Cdd:TIGR02168  488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIAflkq 567

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1282 ---------PKNTMTDSTI----------------LLEDVQKMKDKGEIAQAYI--------GLKE-TNRSSTMDYQELN 1327
Cdd:TIGR02168  568 nelgrvtflPLDSIKGTEIqgndreilkniegflgVAKDLVKFDPKLRKALSYLlggvlvvdDLDNaLELAKKLRPGYRI 647

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1328 --EDGELW-----MVYEGLKQANRLLE-----SQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIE 1395
Cdd:TIGR02168  648 vtLDGDLVrpggvITGGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 568960783  1396 -ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1441
Cdd:TIGR02168  728 iSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774

COG5022

Myosin heavy chain [General function prediction only];

1251-1787

6.93e-16

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 84.36 E-value: 6.93e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1251 QLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkNTMTDSTILLEDVQKMKDkgeIAQAYIGLKETNRSSTMDYQELNEDg 1330
Cdd:COG5022   831 KLRETEEVEFSLKAEVLIQKFGRSLKAKKRF--SLLKKETIYLQSAQRVEL---AERQLQELKIDVKSISSLKLVNLEL- 904

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1331 eLWMVYEGLK--QANRLLESQLQSQKRSHEneaealrgeiqslkEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNE 1408
Cdd:COG5022   905 -ESEIIELKKslSSDLIENLEFKTELIARL--------------KKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKET 969

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1409 NLDLMEQLEKQDKTVRKLKKQ---LKVFAKKIGELEVGQME-NISPGQIIDEPIRPVNIPRKEKDFQGMLEYKR--EDEQ 1482
Cdd:COG5022   970 SEEYEDLLKKSTILVREGNKAnseLKNFKKELAELSKQYGAlQESTKQLKELPVEVAELQSASKIISSESTELSilKPLQ 1049

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1483 KLVKNLILE---LKPRGVAVNLIPGLPAYILfmcvrhaDYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSF------ 1553
Cdd:COG5022  1050 KLKGLLLLEnnqLQARYKALKLRRENSLLDD-------KQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQfivaqm 1122

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1554 WLSNTCRFLH-CLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLS------------------DLAIQIYQQLVRVL 1614
Cdd:COG5022  1123 IKLNLLQEISkFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSpppfaalsekrlyqsalyDEKSKLSSSEVNDL 1202

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1615 EN-----------------ILQPMIVSGMLEHETIQGVSGVKPTGLRKRTSSIadegtYTLDSILRQLNSFHSVMCQHGM 1677
Cdd:COG5022  1203 KNelialfskifsgwprgdKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPAS-----MSNEKLLSLLNSIDNLLSSYKL 1277

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1678 DPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWlrDKNLMNSGAKETLEPLIQAAQLLQVKKKT 1757
Cdd:COG5022  1278 EEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSEELDDW--CREFEISDVDEELEELIQAVKVLQLLKDD 1355

                         570       580       590
                  ....*....|....*....|....*....|
gi 568960783 1758 DDDAEAICSMCNALTTAQIVKVLNLYTPVN 1787
Cdd:COG5022  1356 LNKLDELLDACYSLNPAEIQNLKSRYDPAD 1385

PRK03918

DNA double-strand break repair ATPase Rad50;

901-1442

2.70e-14

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 2.70e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  901 AKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGvynsETEKLRNDVERLQLSEEEakv 980
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE----ELEKLEKEVKELEELKEE--- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  981 atgrVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTL---------LKQEKETLNHRIVEQAKE 1051
Cdd:PRK03918  240 ----IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaeeyikLSEFYEEYLDELREIEKR 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1052 MtETMERKLVEETKQLElDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmLNVPKPGHKRTDStHSSNESEYTFSSEFA 1131
Cdd:PRK03918  316 L-SRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEELER-LKKRLTGLTPEKLEK 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1132 ETEDIAPRTEEpIEKKVpldmslfLKLQKRVTELEQEKQLMQDELDRKEEQ-----VFRSKAKEEERPQIRG---AELEY 1203
Cdd:PRK03918  392 ELEELEKAKEE-IEEEI-------SKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEeytAELKR 463

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1204 ESLKRQELESENKKLKNELNELRKALSEKsaPEVTapgapAYRVLMEQLTSVSEELDVR---------------KEEVLI 1268
Cdd:PRK03918  464 IEKELKEIEEKERKLRKELRELEKVLKKE--SELI-----KLKELAEQLKELEEKLKKYnleelekkaeeyeklKEKLIK 536

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1269 LRSQLVSQKEAIQPKNTMTDSTILLEDvQKMKDKGEIAQAYIGLKETNRSSTMDYQE-LNEDGELWMVYEGLKQANRLLE 1347
Cdd:PRK03918  537 LKGEIKSLKKELEKLEELKKKLAELEK-KLDELEEELAELLKELEELGFESVEELEErLKELEPFYNEYLELKDAEKELE 615

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1348 SQLQSQKRSH-------------ENEAEALRGEIQSLKEENNRQQQLLAQNLQLppearieaSLQHEITRLTNENLDLME 1414
Cdd:PRK03918  616 REEKELKKLEeeldkafeelaetEKRLEELRKELEELEKKYSEEEYEELREEYL--------ELSRELAGLRAELEELEK 687

                         570       580
                  ....*....|....*....|....*...
gi 568960783 1415 QLEKQDKTVRKLKKQLKVFAKKIGELEV 1442
Cdd:PRK03918  688 RREEIKKTLEKLKEELEEREKAKKELEK 715

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

927-1431

3.76e-14

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: 78.22 E-value: 3.76e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   927 NKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEK 1006
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1007 KSIeerADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLVEETKQLELD------LNDERLRYQN 1080
Cdd:pfam05483  348 SFV---VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKLLDEK 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1081 llNEFSRLEERYDDLKEEMTLMLNV-PKPGHKRTDSTHSSNESEYTFSSEfaeTEDIAPRTEEPIEKKVPLDM-SLFLKL 1158
Cdd:pfam05483  425 --KQFEKIAEELKGKEQELIFLLQArEKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEKLKNIELTAhCDKLLL 499

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1159 QKRvtELEQEKQLMQDELDRKEEQVFRSKaKEEER--PQIRGAElEYESLKRQELESENKKLKNELNELRKAL--SEKSA 1234
Cdd:pfam05483  500 ENK--ELTQEASDMTLELKKHQEDIINCK-KQEERmlKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLdkSEENA 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1235 PEV---TAPGAPAYRVLMEQLTSVSEELDVRKEEVlilrSQLVSQKEAIQPKNTMTDSTILLEDVQKMKDKGEIAQAYIG 1311
Cdd:pfam05483  576 RSIeyeVLKKEKQMKILENKCNNLKKQIENKNKNI----EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1312 LKE--TNRSSTMDYQELNEDGELWMVYEGLKQANRLLESQLQSQKRSHENEAEAL----RGEIQSLKEENNRQQQLLAQN 1385
Cdd:pfam05483  652 FEEiiDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMValmeKHKHQYDKIIEERDSELGLYK 731

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 568960783  1386 LQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLK 1431
Cdd:pfam05483  732 NKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777

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

813-835

6.20e-06

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

Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 44.24 E-value: 6.20e-06

                            10        20
                    ....*....|....*....|...
gi 568960783    813 RRTKAATTIQKYWRMYVVRRRYK 835
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23

GumC

COG3206

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

1208-1460

3.48e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.48e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1208 RQELESENKKLKNELNELRKALSE-KSAPEVTAPGAPAyRVLMEQLTSVSEELdvrkEEVLILRSQLVSQKEAIQPKNTM 1286
Cdd:COG3206   177 LEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEA-KLLLQQLSELESQL----AEARAELAEAEARLAALRAQLGS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1287 TDSTI--LLEDVQKMKDKGEIAQAYIGLKETNRSSTM---DYQELNEDgelwmvyegLKQANRLLESQLQSQKRSHENEA 1361
Cdd:COG3206   252 GPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQ---------IAALRAQLQQEAQRILASLEAEL 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1362 EALRGEIQSLKEENNRQQQllaqnlqlppEARIEASLQHEITRLTNEnldlmeqlekqdktVRKLKKQLKVFAKKIGELE 1441
Cdd:COG3206   323 EALQAREASLQAQLAQLEA----------RLAELPELEAELRRLERE--------------VEVARELYESLLQRLEEAR 378

                         250
                  ....*....|....*....
gi 568960783 1442 VGQMENISPGQIIDEPIRP 1460
Cdd:COG3206   379 LAEALTVGNVRVIDPAVVP 397

CBD_MYO6-like

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...

780-837

3.53e-05

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).

Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 45.58 E-value: 3.53e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960783  780 WLLRKRYLCMQRAAITVQRYVRgyqarcyaKFLRRTKAATTIQKYWRMYVVRRRYKIR 837
Cdd:cd21759    18 WLIRSRWRKAQWCALSVIKLKN--------KILYRREALIKIQKTVRGYLARKKHRPR 67

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

1174-1441

7.62e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 7.62e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1174 DELDRKEEQVFRSKAKEEERPQI------------------RGAELEYESLKRQELESENKKLKNELNELRKALSeksap 1235
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERldliidekrqqlerlrreREKAERYQALLKEKREYEGYELLKEKEALERQKE----- 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1236 EVTAPGAPAYRVLmEQLTSVSEELDVRKEEVLILRSQL------VSQKEAIQPKNTMTDSTI-----------LLEDVQK 1298
Cdd:TIGR02169  241 AIERQLASLEEEL-EKLTEEISELEKRLEEIEQLLEELnkkikdLGEEEQLRVKEKIGELEAeiaslersiaeKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1299 MKDKGEIAQAYIG-LKETNRSSTMDYQELNEDGELWM-VYEGLKQANRLLESQLQSQKRSHE---NEAEALRGEIQSLKE 1373
Cdd:TIGR02169  320 AEERLAKLEAEIDkLLAEIEELEREIEEERKRRDKLTeEYAELKEELEDLRAELEEVDKEFAetrDELKDYREKLEKLKR 399

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568960783  1374 ENNRQQQLLAQNLQLPPEARIE-ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1441
Cdd:TIGR02169  400 EINELKRELDRLQEELQRLSEElADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468

Name

Accession

Description

Interval

E-value

MYSc_Myo5

cd01380

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

83-751

0e+00

Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 1319.08 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01380     1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd01380    81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESY 321
Cdd:cd01380   161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  322 QMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:cd01380   241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  402 ALAKHIYAKLFNWIVDHVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRMSNKAFIIKHFADKVE 558
Cdd:cd01380   401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  559 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrvpvkptkgrpgqtakeHKKTVGHQ 638
Cdd:cd01380   481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 718
Cdd:cd01380   516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595

                         650       660       670
                  ....*....|....*....|....*....|....
gi 568960783  719 VLG-DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01380   596 WLRdDKKKTCENILENLILDPDKYQFGKTKIFFR 629

Myosin_head

pfam00063

Myosin head (motor domain);

72-751

0e+00

Myosin head (motor domain);

Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1091.17 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    72 NDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMA 151
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   152 RDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN---VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF 228
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   229 DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHT 308
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   309 RQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHS-AVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPR-MSN 545
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   546 KAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtpltrvpvkptKGRPG 625
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESG-------------KSTPK 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:pfam00063  547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 568960783   706 FFSRYRVLMKQKDV--LGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:pfam00063  627 FVQRYRILAPKTWPkwKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674

MYSc

smart00242

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

64-762

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: 1019.78 E-value: 0e+00

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783     64 NPDILVGENDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVA 143
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    144 EEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-VEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGsVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDA 302
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    303 KEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSD-SCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLA 381
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    382 TATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK 540
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    541 PRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaispTSATSSGRtpltrvpvkpt 620
Cdd:smart00242  480 KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-----SNAGSKKR----------- 543

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    621 kgrpgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:smart00242  544 -----------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612

                           650       660       670       680       690       700
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568960783    701 WTYQEFFSRYRVLMKQK--DVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLR 762
Cdd:smart00242  613 LPFDEFLQRYRVLLPDTwpPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676

COG5022

Myosin heavy chain [General function prediction only];

7-1291

0e+00

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 969.55 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783    7 YTKFARVWIPDPEEVWKSAELLK-DYKPGDKVLLLHLEEG-------KDLEYRLDpktgelphlrNPDILVGENDLTALS 78
Cdd:COG5022     6 AEVGSGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGesvsvkkKVLGNDRI----------KLPKFDGVDDLTELS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   79 YLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQS 158
Cdd:COG5022    76 YLNEPAVLHNLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  159 IIVSGESGAGKTVSAKYAMRYFATVSGSASE--ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:COG5022   155 IIISGESGAGKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLG 316
Cdd:COG5022   235 AKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  317 ISESYQMGIFRILAGILHLGNVGFASrDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQA 396
Cdd:COG5022   315 IDEEEQDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQA 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:COG5022   394 LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEE 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  477 YMKEQIPWTLIDFYDNQPCINLIESK--LGILDLLDEECKMPKGTDDTWAQKLYNT-HLNKCALFEKPRMSNKAFIIKHF 553
Cdd:COG5022   474 YVKEGIEWSFIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVVKHY 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaisptsatssgrtpltrvpvKPTKGRPgqtakehkK 633
Cdd:COG5022   554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------IESKGRF--------P 605

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:COG5022   606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  714 MKQK------DVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKRYL 787
Cdd:COG5022   686 SPSKswtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYL 765

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  788 CMQRAAITVQRYVRGYQARCYAKFLRRTKAATTIQKYWRMYVVRRRYKIRRAATIVIQSYLRGYLTRN-RYRKILREYKA 866
Cdd:COG5022   766 QALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLReTEEVEFSLKAE 845

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  867 VIIQKRVRGWLARTHYKRTMKAIVYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQ-NKDYKC 945
Cdd:COG5022   846 VLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDlIENLEF 925

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  946 LMEKLTNLEGVYNSETEKLRNDVERLQLSEeeakvatgrVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVS 1025
Cdd:COG5022   926 KTELIARLKKLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN 996

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1026 NLKEENTLLKQ------EKETLNHRIVEQA---------KEMTETMER--KLVEETKQLELDLNDERLRYQNLLNEfSRL 1088
Cdd:COG5022   997 FKKELAELSKQygalqeSTKQLKELPVEVAelqsaskiiSSESTELSIlkPLQKLKGLLLLENNQLQARYKALKLR-REN 1075

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1089 EERYDDLKEEM----TLMLNVPKPGHKRTDsTHSSNESEYTF--------SSEFAETEDIAPR---TEEPIEKKVPLDMs 1153
Cdd:COG5022  1076 SLLDDKQLYQLesteNLLKTINVKDLEVTN-RNLVKPANVLQfivaqmikLNLLQEISKFLSQlvnTLEPVFQKLSVLQ- 1153

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1154 LFLKLQKRVTELEQEkqLMQDELDRKEEQVFRSKAKEEERPQIRGAELEyesLKRQELESENKKLKNELN---ELRKALS 1230
Cdd:COG5022  1154 LELDGLFWEANLEAL--PSPPPFAALSEKRLYQSALYDEKSKLSSSEVN---DLKNELIALFSKIFSGWPrgdKLKKLIS 1228

                        1290      1300      1310      1320      1330      1340
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960783 1231 EKSAPEVTAPGAPAYRVLMEQLTsvsEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTI 1291
Cdd:COG5022  1229 EGWVPTEYSTSLKGFNNLNKKFD---TPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATI 1286

MYSc

cd00124

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

83-751

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: 880.77 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMG-DMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd00124     1 AAILHNLRERY-ARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  162 SGESGAGKTVSAKYAMRYFATVSGSAS------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd00124    80 SGESGAGKTETTKLVLKYLAALSGSGSskssssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRL----GNADSFHYTKQGGSPMIEGVDDAKEMAHTRQA 311
Cdd:cd00124   160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLelllSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  312 CTLLGISESYQMGIFRILAGILHLGNVGFASRDSD--SCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIK 389
Cdd:cd00124   240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  390 PISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQH--SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd00124   320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNK 546
Cdd:cd00124   400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  547 AFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltrvpvkptkgrpgq 626
Cdd:cd00124   480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  627 takehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd00124   518 -----------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 568960783  707 FSRYRVLMKQKDVLGDR--KQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd00124   587 LKRYRILAPGATEKASDskKAAVLALLLLLKLDSSGYQLGKTKVFLR 633

MYSc_class_II

cd01377

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

83-751

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: 802.45 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01377     1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSA--------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd01377    80 GESGAGKTENTKKVIQYLASVAASSkkkkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  235 IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTL 314
Cdd:cd01377   160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  315 LGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKL 394
Cdd:cd01377   240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  395 QATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd01377   320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  475 EEYMKEQIPWTLIDF-YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRmSNKA---FI 549
Cdd:cd01377   400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK-PKKSeahFI 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  550 IKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrvpvkptkgrpgqtak 629
Cdd:cd01377   479 LKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSF----------------- 541

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  630 ehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd01377   542 ---RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQR 618

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 568960783  710 YRVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01377   619 YSILAPNAIPKGfdDGKAACEKILKALQLDPELYRIGNTKVFFK 662

MYSc_Myo11

cd01384

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

83-751

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: 763.76 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd01384     1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  162 SGESGAGKTVSAKYAMRYFATVSGSAS--EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd01384    80 SGESGAGKTETTKMLMQYLAYMGGRAVteGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd01384   160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  320 SYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEP---LTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd01384   240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01384   320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRMSNKAFIIKHFAD 555
Cdd:cd01384   400 YTKEEIDWSYIEFVDNQDVLDLIEKKpGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLSRTDFTIDHYAG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELF--QDDEKAISPTSATSsgrtpltrvpvkptkgrpgqtakehkk 633
Cdd:cd01384   479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFppLPREGTSSSSKFSS--------------------------- 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  634 tVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd01384   532 -IGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL 610

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568960783  714 MKQK-DVLGDRKQTCKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd01384   611 APEVlKGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647

MYSc_Myo7

cd01381

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

84-751

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: 754.09 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIDsKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01381     2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAISGQHSW--IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQM 323
Cdd:cd01381   159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  324 GIFRILAGILHLGNVGFASRDS---DSCTIpPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd01381   239 DIFKLLAAILHLGNIKFEATVVdnlDASEV-RDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  401 DALAKHIYAKLFNWIVDHVNQALHSAVKQHSF---IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd01381   318 DAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEY 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  478 MKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRM-SNKAFIIKHFAD 555
Cdd:cd01381   398 DKEGINWQHIEFVDNQDVLDLIALKpMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNN-KNYLKPKSdLNTSFGINHFAG 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisPTSATSSGRTPltrvpvkptkgrpgqtakehkkTV 635
Cdd:cd01381   477 VVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI----SMGSETRKKSP----------------------TL 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd01381   531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568960783  716 --QKDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01381   611 giPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648

MYSc_Myo8

cd01383

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

83-751

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: 733.35 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDmdPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01383     1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01383    78 GESGAGKTETAKIAMQYLAALGGGSS--GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  243 LLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQ 322
Cdd:cd01383   156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  323 MGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01383   236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  403 LAKHIYAKLFNWIVDHVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 481
Cdd:cd01383   316 LAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  482 IPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRmsNKAFIIKHFADKVEYQ 560
Cdd:cd01383   396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  561 CEGFLEKNKDTVFEEQIKVLKSSKFKmLPELF-----QDDEKAISPTSATSSGRTpltrvpvkptkgrpgqtakehKKTV 635
Cdd:cd01383   473 TSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFaskmlDASRKALPLTKASGSDSQ---------------------KQSV 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM- 714
Cdd:cd01383   531 ATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLp 610

                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 568960783  715 KQKDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01383   611 EDVSASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647

MYSc_Myo22

cd14883

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

84-751

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: 726.43 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14883     2 GINTNLKVRY-KKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14883    81 ESGAGKTETTKLILQYLCAVTNNHSW--VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  244 LEKSRVVFQAEEERNYHIFYQLCASAKL-PEFK-MLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESY 321
Cdd:cd14883   159 LEQSRITFQAPGERNYHVFYQLLAGAKHsKELKeKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  322 QMGIFRILAGILHLGNVGFASRDSDSCTIPPKH-EPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14883   239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDkEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  401 DALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 480
Cdd:cd14883   319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  481 QIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKP--RMSNKAFIIKHFADKV 557
Cdd:cd14883   399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELF--QDDE-----KAISPTSATSSGRtpltrvpvkpTKGRPgqtake 630
Cdd:cd14883   478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtyPDLLaltglSISLGGDTTSRGT----------SKGKP------ 541

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  631 hkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd14883   542 ---TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRY 618

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 568960783  711 RVLMKQKDVLGDRKQ--TCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14883   619 LCLDPRARSADHKETcgAVRALMGLGGLPEDEWQVGKTKVFLR 661

Myo5a_CBD

cd15478

Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...

1478-1852

0e+00

Pssm-ID: 271262 Cd Length: 375 Bit Score: 722.59 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1478 REDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1557
Cdd:cd15478     1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1558 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1637
Cdd:cd15478    81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1638 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIR 1717
Cdd:cd15478   161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1718 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1797
Cdd:cd15478   241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568960783 1798 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFIARV 1852
Cdd:cd15478   321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375

MYSc_Myo1

cd01378

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

84-751

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: 722.41 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01378     2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSaSEANVE---EKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR 240
Cdd:cd01378    81 ESGAGKTEASKRIMQYIAAVSGG-SESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd01378   160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  321 YQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIfCDLMGVDYEEMCHWLCHRKLATATE---TYIKPISKLQAT 397
Cdd:cd01378   240 EQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSVLDFV-AYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  398 NARDALAKHIYAKLFNWIVDHVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01378   319 YARDALAKAIYSRLFDWIVERINKSLAAKSGGKKkVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKLyNTHLNKCALFEKP----RMSNKAFII 550
Cdd:cd01378   399 YVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLtAGDATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRI 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  551 KHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgrtpltrvPVKPTKGRPgqtake 630
Cdd:cd01378   478 KHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEG--------------------VDLDSKKRP------ 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01378   532 --PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERY 609

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 568960783  711 RVLMKQK--DVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01378   610 KLLSPKTwpAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652

Myo5b_CBD

cd15477

Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ...

1478-1849

0e+00

Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.

Pssm-ID: 271261 Cd Length: 372 Bit Score: 646.15 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1478 REDEQKLVKNLILELKPRGVAVNlIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1557
Cdd:cd15477     1 KEDEALLIRNLVTDLKPQAVSAT-VPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1558 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1637
Cdd:cd15477    80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1638 VKPTGLRKRTSSIAD-EGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQI 1716
Cdd:cd15477   160 VKPMGYRKRSSSMADgDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1717 RYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVS 1796
Cdd:cd15477   240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568960783 1797 FIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFI 1849
Cdd:cd15477   320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372

MYSc_Myo42

cd14903

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

83-751

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: 643.75 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14903     1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14903    80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEfkMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESY 321
Cdd:cd14903   159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  322 QMGIFRILAGILHLGNVGFASRDSD--SCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14903   237 QEVLFEVLAGILHLGQLQIQSKPNDdeKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  400 RDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14903   317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKAFIIKHFADKVEY 559
Cdd:cd14903   397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  560 QCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqdDEKAISPTSATSSGRTPltrvpvkptkGRPGQTAKEHKKTVGHQF 639
Cdd:cd14903   477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLF--KEKVESPAAASTSLARG----------ARRRRGGALTTTTVGTQF 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  640 RNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK-D 718
Cdd:cd14903   545 KDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGrN 624

                         650       660       670
                  ....*....|....*....|....*....|....
gi 568960783  719 VLGDRKQTCKNVLEKLILDK-DKYQFGKTKIFFR 751
Cdd:cd14903   625 TDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658

MYSc_Myo6

cd01382

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

86-751

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: 631.21 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01382     4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  165 SGAGKTVSAKYAMRYFATVSGSASeANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01382    83 SGAGKTESTKYILRYLTESWGSGA-GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  245 EKSRVVFQAEEERNYHIFYQLCASAklPE---FKMLRLGNadsfhytkqggspmiegVDDAKEMAHTRQACTLLGISESY 321
Cdd:cd01382   162 EKSRICVQSKEERNYHIFYRLCAGA--PEdlrEKLLKDPL-----------------LDDVGDFIRMDKAMKKIGLSDEE 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  322 QMGIFRILAGILHLGNVGFASRDSDS---CTIPPKHEP-LTIFCDLMGVDYEEMCHWLCHRKLATATE----TYIK-PIS 392
Cdd:cd01382   223 KLDIFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLK 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  393 KLQATNARDALAKHIYAKLFNWIVDHVNQAL---HSAvkqhSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHV 469
Cdd:cd01382   303 VEEANNARDALAKAIYSKLFDHIVNRINQCIpfeTSS----YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERI 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  470 FKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRMS---- 544
Cdd:cd01382   379 LKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKSklki 457

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  545 ------NKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAiSPTSATSSGRTPLtrvpvk 618
Cdd:cd01382   458 hrnlrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN-NKDSKQKAGKLSF------ 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  619 ptkgrpgqtakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd01382   531 --------------ISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFP 596

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568960783  699 SRWTYQEFFSRYRVLMKQKDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01382   597 SRTSFHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649

MYSc_Myo4

cd14872

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

83-751

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: 627.19 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14872     1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd14872    80 GESGAGKTEATKQCLSFFAEVAGSTN--GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  243 LLEKSRVVFQAEEERNYHIFYQLCASAklPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQ 322
Cdd:cd14872   158 LLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  323 MGIFRILAGILHLGNVGFAS---RDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLAT-ATETYIKPISKLQATN 398
Cdd:cd14872   236 NNVMSLIAAILKLGNIEFASgggKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQATD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  399 ARDALAKHIYAKLFNWIVDHVNQALHSA-VKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14872   316 ACDALAKAAYSRLFDWLVKKINESMRPQkGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  478 MKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTH-LNKCALFEKPRMSNKAFIIKHFAD 555
Cdd:cd14872   396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisptsaTSSGRTPLTRVpvkptkgrpgqtakehkkTV 635
Cdd:cd14872   476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP-----------PSEGDQKTSKV------------------TL 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14872   527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK 606

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568960783  716 --QKDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14872   607 tiAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644

MYSc_Myo9

cd01385

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

86-751

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: 623.24 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGES 165
Cdd:cd01385     4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  166 GAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLE 245
Cdd:cd01385    83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  246 KSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQMGI 325
Cdd:cd01385   163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  326 FRILAGILHLGNVGFASRD---SDSCTIPPKhEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01385   243 FSVLSAVLHLGNIEYKKKAyhrDESVTVGNP-EVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  403 LAKHIYAKLFNWIVDHVNQAL----HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 478
Cdd:cd01385   322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  479 KEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKlYNTHLNKCALFEKPRMSNKAFIIKHFADKV 557
Cdd:cd01385   402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAI-----------------SPTSATSSGRT-PLTRVPVKP 619
Cdd:cd01385   481 KYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVfrwavlrafframaafrEAGRRRAQRTAgHSLTLHDRT 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  620 TKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd01385   561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568960783  700 RWTYQEFFSRYRVLMKQkdVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01385   641 RYTFQEFITQFQVLLPK--GLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690

Myo5_CBD

cd15470

Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ...

1479-1845

0e+00

Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.

Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 615.76 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1479 EDEQKLVKNLILELKPRGvAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1558
Cdd:cd15470     1 EDESRLIKNLITDLKPRG-AVGLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1559 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1638
Cdd:cd15470    80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1639 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRY 1718
Cdd:cd15470   142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1719 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1798
Cdd:cd15470   204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783 1799 RTIQMRLRDRKDSP--QLLMDAKHIFPVTFPFNPSSLALETIQIPASLG 1845
Cdd:cd15470   284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332

MYSc_Myo15

cd01387

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

84-751

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: 608.68 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01387     2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSAsEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMRTYL 243
Cdd:cd01387    81 ESGSGKTEATKLIMQYLAAVNQRR-NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQM 323
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  324 GIFRILAGILHLGNVGFASRDSDSctippKHEPLTIFCD--------LMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd01387   239 SIFRILASVLHLGNVYFHKRQLRH-----GQEGVSVGSDaeiqwvahLLQISPEGLQKALTFKVTETRRERIFTPLTIDQ 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd01387   314 ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  476 EYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKL-YNTHLNKcaLFEKPRMSNKAFIIKHF 553
Cdd:cd01387   394 EYIREQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHY 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgRTPLTRVPVKPTKGRpGQTAKEHKK 633
Cdd:cd01387   472 AGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-------------RAQTDKAPPRLGKGR-FVTMKPRTP 537

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd01387   538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568960783  714 MKQKDVLGDRKQTCKNVLEKL--ILDKDKYQFGKTKIFFR 751
Cdd:cd01387   618 VALKLPRPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657

MYSc_Myo29

cd14890

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

84-751

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: 601.38 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMAR----DERNQS 158
Cdd:cd14890     2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLARITsgfaqgasgegeaaseaIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  222 KYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNA-DSFHYTKQGGSpmIEGVD 300
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPvEYFYLRGECSS--IPSCD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  301 DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFAS-RDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRK 379
Cdd:cd14890   239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESeNDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  380 LATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANE 459
Cdd:cd14890   319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  460 KLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL----GILDLLDEECKM-------------------P 516
Cdd:cd14890   399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRFkgeeankkfvsqlhasfgrK 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  517 KGTDDTWAQKLYNTHlnkcalFEKPRMSN-KAFIIKHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFQDD 595
Cdd:cd14890   479 SGSGGTRRGSSQHPH------FVHPKFDAdKQFGIKHYAGDVIYDASGFNEKNNETLNAE------------MKELIKQS 540

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  596 EKAISPTSatssgrtpltrvpvkptkgrpgqtakehkktVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEK 675
Cdd:cd14890   541 RRSIREVS-------------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGL 589

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960783  676 RAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLgdrKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14890   590 DCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENI---EQLVAVLSKMLGLGKADWQIGSSKIFLK 662

MYSc_Myo10

cd14873

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

84-751

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: 597.16 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14873     2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVISqqslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLL 315
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  316 GISESYQMGIFRILAGILHLGNVGFASrdSDSCTIPPKhEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14873   241 QFSKEEVREVSRLLAGILHLGNIEFIT--AGGAQVSFK-TALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAvKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14873   318 AVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQL 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  476 EYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRMSNKAFIIKHFAD 555
Cdd:cd14873   397 EYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANN-HFYVKPRVAVNNFGVKHYAG 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptSATSSGRTpltrvpvkptkgrPGQTAKEHKKTV 635
Cdd:cd14873   476 EVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHV-------SSRNNQDT-------------LKCGSKHRRPTV 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14873   536 SSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMR 615

                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 568960783  716 QKDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14873   616 NLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651

MYSc_Myo40

cd14901

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

83-749

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: 587.91 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGD---MDPHIFAVAEEAYKQMARDER- 155
Cdd:cd14901     1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  156 ---NQSIIVSGESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIE 225
Cdd:cd14901    80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  226 IGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGS-PMIEGVDDAKE 304
Cdd:cd14901   160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCyDRRDGVDDSVQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  305 MAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEP-LTIFCDLMGVDYEEMCHWLCHRKLATA 383
Cdd:cd14901   240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIRAG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  384 TETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL--HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:cd14901   320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALF-- 538
Cdd:cd14901   400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASFsv 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  539 EKPRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPelfqddekaisptsatssgrtpltrvpvk 618
Cdd:cd14901   479 SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------------- 529

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  619 ptkgrpgqtakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14901   530 --------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYP 595

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960783  699 SRWTYQEFFSRYRVLMKQK-------DVLGDRKQTCKNVLEKLILDKDKYQFGKTKIF 749
Cdd:cd14901   596 VRFPHDAFVHTYSCLAPDGasdtwkvNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653

MYSc_Myo27

cd14888

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

83-751

0e+00

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

Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 571.25 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14888     1 ASILHSLNLRF-DIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  162 SGESGAGKTVSAKYAMRYFATVsGSASE---ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK-------- 230
Cdd:cd14888    79 SGESGAGKTESTKYVMKFLACA-GSEDIkkrSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  231 -RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPE----FKMLRLGNADSFHYTKQGGSPM---------- 295
Cdd:cd14888   158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKntglSYEENDEKLAKGADAKPISIDMssfephlkfr 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  296 ---------IEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFA-SRDSDSCTI--PPKHEPLTIFCDL 363
Cdd:cd14888   238 yltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAVvsASCTDDLEKVASL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  364 MGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALhSAVKQHS--FIGVLDIYGF 441
Cdd:cd14888   318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESI-GYSKDNSllFCGVLDIFGF 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  442 ETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTD 520
Cdd:cd14888   397 ECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKD 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  521 DTWAQKLYNTHLNKcALFEKPRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddEKAIS 600
Cdd:cd14888   477 QGLCNKLCQKHKGH-KRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLF---SAYLR 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  601 ptsatssgrtpltrvpvkptKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQ 680
Cdd:cd14888   553 --------------------RGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQ 612

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960783  681 LRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlgdRKQTCKNVLEklildkdkYQFGKTKIFFR 751
Cdd:cd14888   613 LKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL--------NGEGKKQLSI--------WAVGKTLCFFK 667

MYSc_Myo31

cd14892

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

89-751

0e+00

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

Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 567.08 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   89 LRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGE--DIINAYSGQNMGDMD-PHIFAVAEEAYKQMARD----ERNQSIIV 161
Cdd:cd14892     7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSPpPHVFSIAERAYRAMKGVgkgqGTPQSIVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  162 SGESGAGKTVSAKYAMRYFATVSGSASEA-----------NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14892    86 SGESGAGKTEASKYIMKYLATASKLAKGAstskgaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQ 310
Cdd:cd14892   166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  311 ACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEP--LTIFCDLMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:cd14892   246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGvnVAKAAGLLGVDAAELMFKLVTQTTSTARGSVL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  389 K-PISKLQATNARDALAKHIYAKLFNWIVDHVNqALHSAV-----------KQHSFIGVLDIYGFETFEINSFEQFCINY 456
Cdd:cd14892   326 EiKLTAREAKNALDALCKYLYGELFDWLISRIN-ACHKQQtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQLCINF 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  457 ANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMP-KGTDDTWAQKLYNTHLNK 534
Cdd:cd14892   405 TNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDK 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  535 CALFEKPRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltr 614
Cdd:cd14892   485 HPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------ 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  615 vpvkptkgrpgqtakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISA 694
Cdd:cd14892   535 -----------------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960783  695 AGFPSRWTYQEFFSRYRVLMKQKDVLGDRKQTCKNVLE--------KLILDKDKYQFGKTKIFFR 751
Cdd:cd14892   592 EGFPIRRQFEEFYEKFWPLARNKAGVAASPDACDATTArkkceeivARALERENFQLGRTKVFLR 656

MYSc_Myo3

cd01379

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

83-751

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: 564.21 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01379     1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFaTVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01379    80 GESGAGKTESANLLVQQL-TVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  243 LLEKSRVVFQAEEERNYHIFYQLCA----SAKLPEFKmlrLGNADSFHYTKQGGspmiEGVDDAKEMAHTR------QAC 312
Cdd:cd01379   159 LLEKSRVVHQAIGERNFHIFYYIYAglaeDKKLAKYK---LPENKPPRYLQNDG----LTVQDIVNNSGNRekfeeiEQC 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  313 -TLLGISESYQMGIFRILAGILHLGNVGFASRDS-----DSCTIpPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATET 386
Cdd:cd01379   232 fKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESnhqtdKSSRI-SNPEALNNVAKLLGIEADELQEALTSHSVVTRGET 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  387 YIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL----HSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQ 462
Cdd:cd01379   311 IIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQ 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  463 QQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNthlN-KCALFEK 540
Cdd:cd01379   390 YYFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHN---NiKSKYYWR 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  541 PRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLpelfqddekaisptsatssgrtpltrvpvkpt 620
Cdd:cd01379   467 PKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-------------------------------- 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  621 kgrpgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:cd01379   515 -----------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568960783  701 WTYQEFFSRYRVL---MKQKdVLGDRkQTCKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd01379   584 ILFADFLKRYYFLafkWNEE-VVANR-ENCRLILERLKL--DNWALGKTKVFLK 633

MYSc_Myh15_mammals

cd14929

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

83-751

5.93e-180

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: 559.21 E-value: 5.93e-180

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14929     1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSASE----ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14929    80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGgSPMIEGVDDAKEMAHTRQACTLLGIS 318
Cdd:cd14929   160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCG-AVAVESLDDAEELLATEQAMDILGFL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  319 ESYQMGIFRILAGILHLGNVGFASRdsdsctipPKHEPL----TIFCD----LMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14929   239 PDEKYGCYKLTGAIMHFGNMKFKQK--------PREEQLeadgTENADkaafLMGINSSELVKGLIHPRIKVGNEYVTRS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14929   311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKA-- 547
Cdd:cd14929   391 VLEQEEYRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKfe 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  548 --FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaISPTSATSSGRtpltrvpvkptkgrpg 625
Cdd:cd14929   471 ahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY---ISTDSAIQFGE---------------- 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  626 qtaKEHKKTVGHQFRNSLH-----LLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:cd14929   532 ---KKRKKGASFQTVASLHkenlnKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNR 608

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568960783  701 WTYQEFFSRY-----RVLMKQKDVlGDRKQTcKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14929   609 LLYADFKQRYcilnpRTFPKSKFV-SSRKAA-EELLGSLEIDHTQYRFGITKVFFK 662

MYSc_Myh3

cd14913

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

83-751

1.29e-178

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: 555.82 E-value: 1.29e-178

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14913     1 PAVLYNLKDRY-TSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14913    80 GESGAGKTVNTKRVIQYFATIAAtgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADSFHYTKQGgSPMIEGVDDAKEMAHTRQAC 312
Cdd:cd14913   160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQG-EILVASIDDAEELLATDSAI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  313 TLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14913   239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14913   319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-MSNKA--- 547
Cdd:cd14913   399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKvVKGRAeah 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  548 FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisPTSATSSGrtPLTRVPVKPTKGRPGQt 627
Cdd:cd14913   479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATADA--DSGKKKVAKKKGSSFQ- 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14913   548 ------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 621

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 568960783  708 SRYRVLMKQKDVLG---DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14913   622 QRYRVLNASAIPEGqfiDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668

MYSc_Myo43

cd14904

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

83-751

2.19e-176

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: 549.16 E-value: 2.19e-176

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14904     1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14904    80 SGESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPM-IEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14904   159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqIPGLDDAKLFASTQKSLSLIGLDND 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  321 YQMGIFRILAGILHLGNVGFASRDSDSCTIpPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14904   239 AQRTLFKILSGVLHLGEVMFDKSDENGSRI-SNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  401 DALAKHIYAKLFNWIVDHVNQAL---HSAVKQHsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14904   318 DALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  478 MKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHL----NKCALFekPRMSNKAFIIKHF 553
Cdd:cd14904   396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkdNESIDF--PKVKRTQFIINHY 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkAISPTSATSSGRtpltrvpvkptkgrpgqtAKEHKK 633
Cdd:cd14904   474 AGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE-APSETKEGKSGK------------------GTKAPK 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14904   535 SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568960783  714 MKQKDVLGDRKQTCKNVLEKLILDKD-KYQFGKTKIFFR 751
Cdd:cd14904   615 FPPSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653

MYSc_Myh7b

cd14927

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

84-751

5.61e-176

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: 549.17 E-value: 5.61e-176

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14927     2 SVLHNLRRRY-SRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVS-------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14927    81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFK--MLRLGNADSFHYTKQGGSpMIEGVDDAKEMAHT 308
Cdd:cd14927   161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK-PELQdmLLVSMNPYDYHFCSQGVT-TVDNMDDGEELMAT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  309 RQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:cd14927   239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14927   319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  469 VFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKA 547
Cdd:cd14927   399 MFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKR 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  548 -----FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddEKAISPTSAtssgrtpltrvpvkptkG 622
Cdd:cd14927   479 kyeahFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDST-----------------E 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  623 RPGQTAKEHKK------TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAG 696
Cdd:cd14927   539 DPKSGVKEKRKkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKG 618

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960783  697 FPSRWTYQEFFSRYRVLMKQ---KDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14927   619 FPNRILYADFKQRYRILNPSaipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676

MYSc_Myh10

cd14920

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

84-751

2.96e-173

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: 541.52 E-value: 2.96e-173

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14920     2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14920    81 ESGAGKTENTKKVIQYLAHVASShkgrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPmIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14920   161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  317 ISESYQMGIFRILAGILHLGNVGF-ASRDSDSCTIpPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14920   240 FSHEEILSMLKVVSSVLQFGNISFkKERNTDQASM-PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14920   319 ADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKA-FI 549
Cdd:cd14920   399 EEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAdFC 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  550 IKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTpltrvpvkpTKGRPGQTAK 629
Cdd:cd14920   479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTET---------AFGSAYKTKK 549

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  630 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14920   550 GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 568960783  710 YRVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14920   630 YEILTPNAIPKGfmDGKQACERMIRALELDPNLYRIGQSKIFFR 673

MYSc_Myo46

cd14907

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

85-751

7.85e-171

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: 535.00 E-value: 7.85e-171

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP---------IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14907     3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  156 NQSIIVSGESGAGKTVSAKYAMRYFATVSG------------------SASEANVEEKVLASNPIMESIGNAKTTRNDNS 217
Cdd:cd14907    82 KQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  218 SRFGKYIEIGFDKRYR-IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAK---LPEFKMLRLGNADSFHYTKQGGS 293
Cdd:cd14907   162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADqqlLQQLGLKNQLSGDRYDYLKKSNC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  294 PMIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASR--DSDSCTIPPKHEPLTIFCDLMGVDYEEM 371
Cdd:cd14907   242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEEL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  372 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL--HSAVKQHSF------IGVLDIYGFET 443
Cdd:cd14907   322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFEV 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  444 FEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL--IDFYDNQPCINLIES-KLGILDLLDEECKMPKGTD 520
Cdd:cd14907   402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  521 DTWAQKLYNTHLNKcALFEKPRMSNK-AFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAi 599
Cdd:cd14907   482 EKLLNKIKKQHKNN-SKLIFPNKINKdTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGS- 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  600 sptsatssgrtpltrvpvKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQ 679
Cdd:cd14907   560 ------------------QQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLN 621

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960783  680 QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlgdrkqtcKNVLeklildkdkyqFGKTKIFFR 751
Cdd:cd14907   622 QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK-------------KNVL-----------FGKTKIFMK 669

MYSc_Myh1_insects_crustaceans

cd14909

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

83-751

2.77e-170

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: 533.26 E-value: 2.77e-170

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14909     1 ASVLHNLRQRYY-AKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14909    80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLcASAKLPEFK-MLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTL 314
Cdd:cd14909   160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKeMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  315 LGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKL 394
Cdd:cd14909   239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  395 QATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14909   319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  475 EEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKA-----F 548
Cdd:cd14909   399 EEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaahF 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  549 IIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrvpvkptkGRPGQTA 628
Cdd:cd14909   479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGR------------GKKGGGF 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  629 kehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14909   547 ----ATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKM 622

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 568960783  709 RYRVLM-KQKDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14909   623 RYKILNpAGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666

Myo5c_CBD

cd15476

Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ...

1479-1846

2.22e-169

Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes.

Pssm-ID: 271260 [Multi-domain] Cd Length: 332 Bit Score: 517.41 E-value: 2.22e-169

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1479 EDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1558
Cdd:cd15476     1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1559 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1638
Cdd:cd15476    81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1639 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRY 1718
Cdd:cd15476   143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1719 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1798
Cdd:cd15476   205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 568960783 1799 RTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGL 1846
Cdd:cd15476   285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332

MYSc_Myo47

cd14908

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

83-751

2.02e-167

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: 526.40 E-value: 2.02e-167

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY------SGQNM---GDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14908     1 PAILHSLSRRF-FRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATV----------SGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:cd14908    80 IRaSQSILISGESGAGKTESTKIVMLYLTTLgngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--------KLPEFKMLRLGNADSFHYTKQGGSP 294
Cdd:cd14908   160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGdeeehekyEFHDGITGGLQLPNEFHYTGQGGAP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  295 MIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPK---HEPLTIFCDLMGVDYEEM 371
Cdd:cd14908   240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  372 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ--HSFIGVLDIYGFETFEINSF 449
Cdd:cd14908   320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  450 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMP-KGTDDTWAQKL 527
Cdd:cd14908   400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  528 YNTHLNKC--ALFEKPRMSNKA-------FIIKHFADKVEYQCE-GFLEKNKDtvfeeqiKVLKSSKfkmlpELFQDdek 597
Cdd:cd14908   480 YETYLPEKnqTHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKD-------EIPLTAD-----SLFES--- 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  598 aisptsatssgrtpltrvpvkptkgrpgqtakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRA 677
Cdd:cd14908   545 --------------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  678 VQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK--QKDVLG------DRKQTCKNVLEKLI-------------- 735
Cdd:cd14908   587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPliPEVVLSwsmerlDPQKLCVKKMCKDLvkgvlspamvsmkn 666

                         730
                  ....*....|....*.
gi 568960783  736 LDKDKYQFGKTKIFFR 751
Cdd:cd14908   667 IPEDTMQLGKSKVFMR 682

MYSc_Myh2_insects_mollusks

cd14911

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

84-751

6.12e-167

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in 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: 524.54 E-value: 6.12e-167

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14911     2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSASEAN----------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIG 227
Cdd:cd14911    81 ESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  228 FDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPmIEGVDDAKEMAH 307
Cdd:cd14911   161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLP-VPGVDDYAEFQA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  308 TRQACTLLGISESYQMGIFRILAGILHLGNVGF-ASRDSDSCTIPPKHEPLTIfCDLMGVDYEEMCHWLCHRKLATATET 386
Cdd:cd14911   240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKI-AHLLGLSVTDMTRAFLTPRIKVGRDF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  387 YIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 465
Cdd:cd14911   319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  466 NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRMS 544
Cdd:cd14911   399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  545 NKA-FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTpltrvpvkptkgr 623
Cdd:cd14911   478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQF------------- 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  624 PGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTY 703
Cdd:cd14911   545 GARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPF 624

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 568960783  704 QEFFSRYRVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14911   625 QEFRQRYELLTPNVIPKGfmDGKKACEKMIQALELDSNLYRVGQSKIFFR 674

MYSc_Myh7

cd14917

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

83-751

3.71e-164

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: 516.96 E-value: 3.71e-164

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14917     1 PAVLYNLKERY-ASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14917    80 GESGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACT 313
Cdd:cd14917   160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  314 LLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISK 393
Cdd:cd14917   240 VLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  394 LQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLE 473
Cdd:cd14917   320 QQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  474 QEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR----MSNKAF 548
Cdd:cd14917   400 QEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnikgKPEAHF 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  549 IIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSatssgrtpltrvpvkptKGRPGQTA 628
Cdd:cd14917   480 SLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIE-----------------KGKGKAKK 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  629 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14917   543 GSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 622

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 568960783  709 RYRVLMKQKDVLG---DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14917   623 RYRILNPAAIPEGqfiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668

MYSc_Myh6

cd14916

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

83-751

6.88e-162

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: 510.76 E-value: 6.88e-162

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14916     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSG----------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14916    80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRL-GNADSFHYTKQgGSPMIEGVDDAKEMAHTRQA 311
Cdd:cd14916   160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQ-GEVSVASIDDSEELLATDSA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  312 CTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd14916   239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14916   319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR----MSNK 546
Cdd:cd14916   399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  547 AFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAisptSATSSGrtpltrvpvkptKGRPGQ 626
Cdd:cd14916   479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASA----DTGDSG------------KGKGGK 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  627 TAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14916   543 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783  707 FSRYRVL----MKQKDVLGDRKQTCKnVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14916   623 RQRYRILnpaaIPEGQFIDSRKGAEK-LLGSLDIDHNQYKFGHTKVFFK 670

MYSc_Myh16

cd14934

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

84-751

1.49e-161

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: 509.57 E-value: 1.49e-161

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14934     2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSASEA-----NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14934    81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEF--KMLRLGNADSFHYTKQGGSpMIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14934   161 IESYLLEKSRVISQQAAERGYHIFYQILSNKK-PELieSLLLVPNPKEYHWVSQGVT-VVDNMDDGEELQITDVAFDVLG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  317 ISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd14934   239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14934   319 NNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  477 YMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP-----RMSNKAFII 550
Cdd:cd14934   399 YKREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFEL 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  551 KHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFkMLPELFQDDEKAISPTSATSSGRTPLtrvpvkptkgrpgqtake 630
Cdd:cd14934   479 VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL-GLLALLFKEEEAPAGSKKQKRGSSFM------------------ 539

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  631 hkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd14934   540 ---TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRY 616

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 568960783  711 RVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14934   617 QVLNPNVIPQGfvDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659

MYSc_Myo28

cd14889

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

85-751

6.91e-160

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: 504.83 E-value: 6.91e-160

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQM----ARDERNQSII 160
Cdd:cd14889     3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  161 VSGESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14889    82 ISGESGAGKTESTKLLLRQIMELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14889   159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  321 YQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHE-PLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14889   239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNgWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  400 RDALAKHIYAKLFNWIVDHVNQALHSAVK---QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14889   319 RDSIAKVAYGRVFGWIVSKINQLLAPKDDssvELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRMSNKAFIIKHFAD 555
Cdd:cd14889   399 YKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRSKSPKFTVNHYAG 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptSATSSGRTPLTRVPVKPTKGRPGQTAKEhKKTV 635
Cdd:cd14889   478 KVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF----------TATRSRTGTLMPRAKLPQAGSDNFNSTR-KQSV 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14889   547 GAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLC 626

                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 568960783  716 QKDVLGDrKQTCKNVLEKliLDKDKYQFGKTKIFFR 751
Cdd:cd14889   627 EPALPGT-KQSCLRILKA--TKLVGWKCGKTRLFFK 659

MYSc_Myh2_mammals

cd14912

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

83-751

9.30e-160

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: 505.04 E-value: 9.30e-160

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14912     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14912    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFKMLRLGNADSFHYT-KQGGSPMIEGVDDAKEMAHTRQ 310
Cdd:cd14912   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK-PELIEMLLITTNPYDYPfVSQGEISVASIDDQEELMATDS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  311 ACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14912   239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14912   319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRM----SN 545
Cdd:cd14912   399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  546 KAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtpltrvpvkpTKGrpG 625
Cdd:cd14912   479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGA------------KKG--G 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14912   545 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 624

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783  706 FFSRYRVLMKQKDVLG---DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14912   625 FKQRYKVLNASAIPEGqfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673

MYSc_Myh13

cd14923

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

83-751

6.02e-159

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: 503.06 E-value: 6.02e-159

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14923     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVS----------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14923    80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFKMLRL--GNADSFHYTKQGgSPMIEGVDDAKEMAHTRQ 310
Cdd:cd14923   160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKK-PELIDLLLisTNPFDFPFVSQG-EVTVASIDDSEELLATDN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  311 ACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14923   238 AIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14923   318 QNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-MSNKA- 547
Cdd:cd14923   398 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpAKGKAe 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  548 --FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaiSPTSATSSGRTPLTRvpvkptkgRPG 625
Cdd:cd14923   478 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-------SNYAGAEAGDSGGSK--------KGG 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14923   543 KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 622

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783  706 FFSRYRVLMKQKDVLG---DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14923   623 FKQRYRILNASAIPEGqfiDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671

MYSc_Myh8

cd14918

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

83-751

1.23e-158

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: 501.96 E-value: 1.23e-158

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14918     1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSAS---------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14918    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADSFHYTKQGgSPMIEGVDDAKEMAHTRQAC 312
Cdd:cd14918   160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQG-EITVPSIDDQEELMATDSAI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  313 TLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14918   239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14918   319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRM----SNKA 547
Cdd:cd14918   399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  548 FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrvpvkpTKGRPGQt 627
Cdd:cd14918   479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK----------KKGSSFQ- 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14918   548 ------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFK 621

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 568960783  708 SRYRVLMKQKDVLG---DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14918   622 QRYKVLNASAIPEGqfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668

MYSc_Myh18

cd14932

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

84-751

2.55e-157

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: 498.78 E-value: 2.55e-157

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14932     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSA-----------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14932    81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQgGSPMIEGVDDAKEMAHTRQAC 312
Cdd:cd14932   161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSN-GNVTIPGQQDKELFAETMEAF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  313 TLLGISESYQMGIFRILAGILHLGNVGF-ASRDSDSCTIPPKHEPLTIfCDLMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd14932   240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFkKERNSDQASMPDDTAAQKV-CHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14932   319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR--MS 544
Cdd:cd14932   399 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNN-PKFQKPKklKD 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  545 NKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSAtsSGRTPLTRVPVKPTKGRp 624
Cdd:cd14932   478 DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKV--AGMGESLHGAFKTRKGM- 554

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  625 gqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14932   555 -------FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783  705 EFFSRYRVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14932   628 EFRQRYEILTPNAIPKGfmDGKQACVLMVKALELDPNLYRIGQSKVFFR 676

MYSc_Myo36

cd14897

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

85-751

4.81e-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: 496.13 E-value: 4.81e-157

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDM-DPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14897     3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSASEaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14897    82 ESGAGKTESTKYMIKHLMKLSPSDDS-DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSfHYTKQGGSPMIEGVDDAKEMAHTRQACT-------LLG 316
Cdd:cd14897   161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDC-HRILRDDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  317 ISESYQMGIFRILAGILHLGNVGFAS-RDSDSCTIPPKHePLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14897   240 FSEEDISVIFTILAAILHLTNIVFIPdEDTDGVTVADEY-PLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQH-----SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14897   319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQimtrgPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRMSNKAFI 549
Cdd:cd14897   399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  550 IKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaispTSatssgrtpltrvpvkptkgrpgqtak 629
Cdd:cd14897   478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------TS-------------------------- 522

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  630 ehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14897   523 --------YFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 568960783  710 YRVLM-KQKDVLGDRKQTCKNVLEklILDKDKYQFGKTKIFFR 751
Cdd:cd14897   595 YKEICdFSNKVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635

MYSc_Myo30

cd14891

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

83-751

1.13e-156

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: 495.72 E-value: 1.13e-156

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRF-IDSKLIYTYCGIVLVAINPYEQLPiygEDIINAYSGQNMGDMDPHIFAVAEEAYKQM---ARDERNQS 158
Cdd:cd14891     1 AGILHNLEERSkLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMclgSGRMQNQS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  222 KYIEIGFDKR-YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVD 300
Cdd:cd14891   158 KFMKLQFTKDkFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  301 DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTI----PPKHEPLTIFCDLMGVDYEEMCHWLC 376
Cdd:cd14891   238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAeiasESDKEALATAAELLGVDEEALEKVIT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  377 HRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEI-NSFEQFCIN 455
Cdd:cd14891   318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLLIN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  456 YANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHL-N 533
Cdd:cd14891   398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTHKrH 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  534 KCALFEKPRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtplt 613
Cdd:cd14891   478 PCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA----------------------------- 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  614 rvpvkptkgrpgqtakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRIS 693
Cdd:cd14891   529 ------------------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960783  694 AAGFPSRWTYQEFFSRYRVLM----KQKDVLGDRKQTcKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14891   585 KVGLPTRVTYAELVDVYKPVLppsvTRLFAENDRTLT-QAILWAFRVPSDAYRLGRTRVFFR 645

MYSc_Myh1_mammals

cd14910

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

83-751

1.16e-156

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: 496.56 E-value: 1.16e-156

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14910     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14910    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADSFHYTKQGgSPMIEGVDDAKEMAHTRQ 310
Cdd:cd14910   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQG-EITVPSIDDQEELMATDS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  311 ACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14910   239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14910   319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKA-- 547
Cdd:cd14910   399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKve 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  548 --FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGrtpltrvpvkptkgrpG 625
Cdd:cd14910   479 ahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKG----------------G 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14910   543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783  706 FFSRYRVLMKQKDVLG---DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14910   623 FKQRYKVLNASAIPEGqfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671

MYSc_Myh4

cd14915

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

83-751

1.59e-156

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: 496.17 E-value: 1.59e-156

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14915     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14915    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADSFHYTKQGgSPMIEGVDDAKEMAHTRQ 310
Cdd:cd14915   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQG-EITVPSIDDQEELMATDS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  311 ACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14915   239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14915   319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR----MSN 545
Cdd:cd14915   399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKpakgKAE 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  546 KAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGrtpltrvpvkptkgrpG 625
Cdd:cd14915   479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKG----------------G 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14915   543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783  706 FFSRYRVLMKQKDVLG---DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14915   623 FKQRYKVLNASAIPEGqfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671

MYSc_Myh11

cd14921

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

84-751

4.17e-156

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: 495.31 E-value: 4.17e-156

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14921     2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14921    81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPmIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14921   161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETLEAMSIMG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  317 ISESYQMGIFRILAGILHLGNVGF-ASRDSDSCTIPPKHEPLTIfCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14921   240 FSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14921   319 ADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  475 EEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRM--SNKAF 548
Cdd:cd14921   399 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNH-PKFQKPKQlkDKTEF 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  549 IIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrvpvkPTKGRpgqTA 628
Cdd:cd14921   478 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSL------PSASK---TK 548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  629 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14921   549 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 568960783  709 RYRVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14921   629 RYEILAANAIPKGfmDGKQACILMIKALELDPNLYRIGQSKIFFR 673

MYSc_Myo19

cd14880

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

85-749

2.36e-154

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: 489.75 E-value: 2.36e-154

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY-SGQNMGDMDPHIFAVAEEAYK--QMARDERNQSII 160
Cdd:cd14880     3 VLRCLQARYT-ADTFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  161 VSGESGAGKTVSAKYAMRYFATVSGSAS--EAN-----VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14880    82 VSGESGAGKTWTSRCLMKFYAVVAASPTswESHkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTkqggsPMIEGVDDAKEMAHTRQACT 313
Cdd:cd14880   162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNLEEDCFEVTREAML 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  314 LLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPK---HEPLTIFCDLMGVDYEEMCHWLCHRKLATATE--TYI 388
Cdd:cd14880   237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMddtKESVRTSALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd14880   317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIE-SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNK 546
Cdd:cd14880   397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSRE 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  547 -AFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTrvpvkptkgrpg 625
Cdd:cd14880   477 pSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVL------------ 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  626 qtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14880   545 --------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 568960783  706 FFSRYRVLMKqkdvLGDRKQTCKNVLEKLILDKDKYQFGKTKIF 749
Cdd:cd14880   617 FVERYKLLRR----LRPHTSSGPHSPYPAKGLSEPVHCGRTKVF 656

MYSc_Myh9

cd14919

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

84-751

4.01e-152

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: 484.21 E-value: 4.01e-152

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14919     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGS----ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd14919    81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQgGSPMIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd14919   161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  320 SYQMGIFRILAGILHLGNVGF-ASRDSDSCTIPPKHEPLTIfCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATN 398
Cdd:cd14919   240 EEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKV-SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  399 ARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14919   319 AIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  478 MKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYN---THLNkcalFEKPR-MSNKA-F 548
Cdd:cd14919   399 QREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQeqgTHPK----FQKPKqLKDKAdF 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  549 IIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrvpvkptkgrPG--Q 626
Cdd:cd14919   475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAL-----------PGafK 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  627 TAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14919   544 TRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 623

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 568960783  707 FSRYRVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14919   624 RQRYEILTPNSIPKGfmDGKQACVLMIKALELDSNLYRIGQSKVFFR 670

MYSc_Myo34

cd14895

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

83-751

1.98e-150

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: 480.99 E-value: 1.98e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGediINAYSGQNMGDMD--PHIFAVAEEAYKQMAR------- 152
Cdd:cd14895     1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRrlhepga 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  153 DERNQSIIVSGESGAGKTVSAKYAMRYFA--------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14895    77 SKKNQTILVSGESGAGKTETTKFIMNYLAesskhttaTSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  225 EIGF-----DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG--NADSFHYTKQGGS-PMI 296
Cdd:cd14895   157 RMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGGQCyQRN 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  297 EGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFAS-------RDSDSCTIPPK-----------HEPLT 358
Cdd:cd14895   237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVAssedegeEDNGAASAPCRlasaspssltvQQHLD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  359 IFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAlhSAVKQHS------- 431
Cdd:cd14895   317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSA--SPQRQFAlnpnkaa 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  432 ------FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LG 504
Cdd:cd14895   395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  505 ILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPR--MSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKS 582
Cdd:cd14895   475 IFSLLDEECVVPKGSDAGFARKLYQR-LQEHSNFSASRtdQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  583 SKFKMLPELFqdDEKAISPTSATSSGRTPLTRvpvkptkgrpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIK 662
Cdd:cd14895   554 TSDAHLRELF--EFFKASESAELSLGQPKLRR-----------RSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  663 PNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVlgdRKQTCKNVLEKliLDKDKYQ 742
Cdd:cd14895   621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA---SDATASALIET--LKVDHAE 695


                  ....*....
gi 568960783  743 FGKTKIFFR 751
Cdd:cd14895   696 LGKTRVFLR 704

MYSc_Myo41

cd14902

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

83-751

8.52e-150

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: 479.39 E-value: 8.52e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY--------SGQNMGDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14902     1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVE--------EKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14902    80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveigKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  225 EIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGS----PMIEGVD 300
Cdd:cd14902   160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPsfarKRAVADK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  301 DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFA---SRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCH 377
Cdd:cd14902   240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  378 RKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIV-------DHVNQALHSAVKQHSF--IGVLDIYGFETFEINS 448
Cdd:cd14902   320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVrrlsdeiNYFDSAVSISDEDEELatIGILDIFGFESLNRNG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  449 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKL 527
Cdd:cd14902   400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  528 YNTHLNKcalfekprmsnKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEK--AISPTSAT 605
Cdd:cd14902   480 YRYHGGL-----------GQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRdsPGADNGAA 548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  606 SSGRTPLTRVPvkptkgrpgqtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACG 685
Cdd:cd14902   549 GRRRYSMLRAP-----------------SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  686 VLETIRISAAGFPSRWTYQEF---FSRYRVLMKQKD----------------------VLGDRKQTCKNVLEKLILDKDK 740
Cdd:cd14902   612 VLEAVRIARHGYSVRLAHASFielFSGFKCFLSTRDraakmnnhdlaqalvtvlmdrvLLEDGVEREEKNPGALTAVTGD 691

                         730       740
                  ....*....|....*....|....*
gi 568960783  741 Y--------------QFGKTKIFFR 751
Cdd:cd14902   692 GsgtafendcrrkdvQVGRTLVFCK 716

MYSc_Myh19

cd15896

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

84-751

1.07e-148

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: 474.94 E-value: 1.07e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd15896     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGS-----------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd15896    81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQgGSPMIEGVDDAKEMAHTRQAC 312
Cdd:cd15896   161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSN-GNVTIPGQQDKDLFTETMEAF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  313 TLLGISESYQMGIFRILAGILHLGNVGF-ASRDSDSCTIPPKHEPLTIfCDLMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd15896   240 RIMGIPEDEQIGMLKVVASVLQLGNMSFkKERHTDQASMPDNTAAQKV-CHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd15896   319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNK 546
Cdd:cd15896   399 ILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDE 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  547 A-FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrvpvkptkgRPG 625
Cdd:cd15896   479 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP-----------GAF 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd15896   548 KTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 568960783  706 FFSRYRVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd15896   628 FRQRYEILTPNAIPKGfmDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675

MYSc_Myo39

cd14900

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

85-725

1.04e-147

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: 470.56 E-value: 1.04e-147

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 152
Cdd:cd14900     3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  153 ----DERNQSIIVSGESGAGKTVSAKYAMRYFA---------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14900    82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  220 FGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKmlrlgnadsfhytkqggSPMIEGV 299
Cdd:cd14900   162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK-----------------RDMYRRV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  300 DDAKEMahtrqactlLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTI-------PPKHEPLTIFCDLMGVDYEEMC 372
Cdd:cd14900   225 MDAMDI---------IGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGqlksdlaPSSIWSRDAAATLLSVDATKLE 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  373 HWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALH--SAVKQHS---FIGVLDIYGFETFEIN 447
Cdd:cd14900   296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmdDSSKSHGglhFIGILDIFGFEVFPKN 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  448 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQK 526
Cdd:cd14900   376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASK 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  527 LYnTHLNKCALFEKPRM--SNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIkvlksskfkmlpELFQDdekaisptsa 604
Cdd:cd14900   456 LY-RACGSHPRFSASRIqrARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------DLFVY---------- 512

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  605 tssgrtpltrvpvkptkgrpgqtakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRAC 684
Cdd:cd14900   513 -------------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 568960783  685 GVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLGDRKQ 725
Cdd:cd14900   562 GVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLLAKKQ 602

MYSc_Myh14_mammals

cd14930

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

84-751

6.28e-147

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: 469.96 E-value: 6.28e-147

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14930     2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFATVSGSAS-------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14930    81 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGgsPMIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14930   161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--PSSSPGQERELFQETLESLRVLG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  317 ISESYQMGIFRILAGILHLGNVGF-ASRDSDSCTIpPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14930   239 FSHEEITSMLRMVSAVLQFGNIVLkRERNTDQATM-PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14930   318 ADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPR-MSNKA-F 548
Cdd:cd14930   398 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRhLRDQAdF 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  549 IIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrvpvKPTKGRPgqtA 628
Cdd:cd14930   477 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGD--------GPPGGRP---R 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  629 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14930   546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 568960783  709 RYRVLMKQKDVLG--DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14930   626 RYEILTPNAIPKGfmDGKQACEKMIQALELDPNLYRVGQSKIFFR 670

MYSc_Myo35

cd14896

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

83-751

3.70e-139

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: 447.69 E-value: 3.70e-139

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14896     1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSASEANVE--EKVLasnPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14896    80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14896   156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  321 YQMGIFRILAGILHLGNVGFASRDSDSctippkHEPLTIFCD--------LMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14896   236 ELTAIWAVLAAILQLGNICFSSSERES------QEVAAVSSWaeihtaarLLQVPPERLEGAVTHRVTETPYGRVSRPLP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSF--IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14896   310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRMSNKAFI 549
Cdd:cd14896   390 AQEEEECQRELLPWVPIPQPPRESCLDLLVDQPhSLLSILDDQTWLSQATDHTFLQKCHYHHGDH-PSYAKPQLPLPVFT 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  550 IKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisptsatssgrtpltrvpvkptKGRPGQTAK 629
Cdd:cd14896   469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQ---------------------------EAEPQYGLG 521

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  630 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14896   522 QGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLAR 601

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 568960783  710 YRVLMKQK-DVLGDRKQtCKNVLEKLI-LDKDKYQFGKTKIFFR 751
Cdd:cd14896   602 FGALGSERqEALSDRER-CGAILSQVLgAESPLYHLGATKVLLK 644

PTZ00014

myosin-A; Provisional

53-786

8.18e-139

myosin-A; Provisional

Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 452.95 E-value: 8.18e-139

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   53 DPKTGE-----LPHLRNPDILVGEN---DLTALSYLHEPAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDII 124
Cdd:PTZ00014   72 DPPTNStfevkPEHAFNANSQIDPMtygDIGLLPHTNIPCVLDFLKHRYL-KNQIYTTADPLLVAINPFKDLGNTTNDWI 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  125 NAY-SGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIM 203
Cdd:PTZ00014  151 RRYrDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  204 ESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNAD 283
Cdd:PTZ00014  231 EAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLE 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  284 SFHYTKQGgSPMIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSD-----SCTIPPKHEPLT 358
Cdd:PTZ00014  311 EYKYINPK-CLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltdaAAISDESLEVFN 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  359 IFCDLMGVDYEEMCHWLchrklaTATETYI------KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSF 432
Cdd:PTZ00014  390 EACELLFLDYESLKKEL------TVKVTYAgnqkieGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVF 463

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  433 IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDE 511
Cdd:PTZ00014  464 IGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILED 543

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  512 ECKMPKGTDD----TWAQKLYNthlNKCALFEKpRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKM 587
Cdd:PTZ00014  544 QCLAPGGTDEkfvsSCNTNLKN---NPKYKPAK-VDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPL 619

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  588 LPELFQDDEkaisptsatssgrtpLTRvpvkptkgrpGQTAKehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFK 667
Cdd:PTZ00014  620 VRDLFEGVE---------------VEK----------GKLAK--GQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENK 672

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  668 FPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRV--LMKQKDVLGDRKQTCKNVLEKLILDKDKYQFGK 745
Cdd:PTZ00014  673 KPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYldLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGK 752

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|...
gi 568960783  746 TKIFFRAGQVAYLEKLRADKLRA--ACIRIqktIRGWLLRKRY 786
Cdd:PTZ00014  753 TMVFLKKDAAKELTQIQREKLAAwePLVSV---LEALILKIKK 792

MYSc_Myo45

cd14906

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

85-749

5.29e-138

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: 447.12 E-value: 5.29e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14906     3 ILNNLGKRYK-SDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSASEAN---------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR-Y 232
Cdd:cd14906    82 GESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  233 RIIGANMRTYLLEKSRVVFQAEEER-NYHIFYQLCASAKLPEFKMLRLGN--------------ADSFHYTKQGGSPMIE 297
Cdd:cd14906   162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdpskyryldarddvISSFKSQSSNKNSNHN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  298 GVDDAKE-MAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFaSRDSDSCTI----PPKHEPLTIFCDLMGVDYEEMC 372
Cdd:cd14906   242 NKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEF-EEDSDFSKYayqkDKVTASLESVSKLLGYIESVFK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  373 HWLCHRKLATATE--TYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQ-----------ALHSAVKQHSFIGVLDIY 439
Cdd:cd14906   321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIF 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  440 GFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKG 518
Cdd:cd14906   401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKG 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  519 TDDTWAQKlYNTHLNKCALFEKPRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKA 598
Cdd:cd14906   481 SEQSLLEK-YNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITS 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  599 ISPTSATSSGRTpltrvpvkptkgrpgqtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAV 678
Cdd:cd14906   560 TTNTTKKQTQSN-----------------------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVL 616

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  679 QQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLGDRKQTCKNVLEKLIL---------------------- 736
Cdd:cd14906   617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIqsklktmgisnnkkknnsnsns 696

                         730
                  ....*....|....*..
gi 568960783  737 ----DKDKYQFGKTKIF 749
Cdd:cd14906   697 nttnDKPLFQIGKTKIF 713

MYSc_Myo14

cd14876

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

83-749

3.69e-135

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

Pssm-ID: 276843 Cd Length: 649 Bit Score: 436.73 E-value: 3.69e-135

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSG-QNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14876     1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14876    80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  242 YLLEKSRVVFQAEEERNYHIFYQLCASA-----------KLPEFKMLrlgNADSFHytkqggspmIEGVDDAKEMAHTRQ 310
Cdd:cd14876   160 FLLEKSRIVTQDDNERSYHIFYQLLKGAdsemkskyhllGLKEYKFL---NPKCLD---------VPGIDDVADFEEVLE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  311 ACTLLGISESYQMGIFRILAGILHLGNVGFASRD----SDSCTIPPkhEPLTIF---CDLMGVDYEEMCHWLChRKLATA 383
Cdd:cd14876   228 SLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTeqgvDDAAAISN--ESLEVFkeaCSLLFLDPEALKRELT-VKVTKA 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  384 TETYIK-PISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQ 462
Cdd:cd14876   305 GGQEIEgRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQ 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  463 QQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCIN-LIESKLGILDLLDEECKMPKGTDD----TWAQKLYNthlNKCAL 537
Cdd:cd14876   385 KNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEkfvsACVSKLKS---NGKFK 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  538 FEKpRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrVPV 617
Cdd:cd14876   462 PAK-VDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG--------------------VVV 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  618 KPTKGRPGQtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGF 697
Cdd:cd14876   521 EKGKIAKGS-------LIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGY 593

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568960783  698 PSRWTYQEFFSRYRVLmkqkdVLG-------DRKQTCKNVLEKLILDKDKYQFGKTKIF 749
Cdd:cd14876   594 SYRRPFEEFLYQFKFL-----DLGiandkslDPKVAALKLLESSGLSEDEYAIGKTMVF 647

MYSc_Myo38

cd14899

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

84-736

2.12e-128

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: 420.27 E-value: 2.12e-128

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 152
Cdd:cd14899     2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  153 DERNQSIIVSGESGAGKTVSAKYAMRYFATVSG----------------SASEANVEEKVLASNPIMESIGNAKTTRNDN 216
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  217 SSRFGKYIEIGF-DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL------CASAKLPEFKMLRlGNADSFHYTK 289
Cdd:cd14899   161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALS-GGPQSFRLLN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  290 QG-GSPMIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFA--------------SRDSDSCTIPPKH 354
Cdd:cd14899   240 QSlCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiphkgddtvfadeARVMSSTTGAFDH 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  355 epLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVK------ 428
Cdd:cd14899   320 --FTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgad 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  429 ---------QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLI 499
Cdd:cd14899   398 esdvddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELF 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  500 ESK-LGILDLLDEECKMPKGTDDTWAQKLY--------NTHLNKCALFEKprmsNKAFIIKHFADKVEYQCEGFLEKNKD 570
Cdd:cd14899   478 EHRpIGIFSLTDQECVFPQGTDRALVAKYYlefekknsHPHFRSAPLIQR----TTQFVVAHYAGCVTYTIDGFLAKNKD 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  571 TVFEEQIKVLKSSKFKMLPELfqddekAISPTSATSSGRTPLTRVPVKPTKGRPGQTAkehKKTVGHQFRNSLHLLMETL 650
Cdd:cd14899   554 SFCESAAQLLAGSSNPLIQAL------AAGSNDEDANGDSELDGFGGRTRRRAKSAIA---AVSVGTQFKIQLNELLSTV 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  651 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLGD----RKQT 726
Cdd:cd14899   625 RATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRVLLSLYKWGDndfeRQMR 704

                         730
                  ....*....|
gi 568960783  727 CKNVLEKLIL 736
Cdd:cd14899   705 CGVSLGKTRV 714

MYSc_Myo25

cd14886

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

85-751

4.17e-124

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: 405.81 E-value: 4.17e-124

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMG-----DMDPHIFAVAEEAYKQMARDERNQS 158
Cdd:cd14886     3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  159 IIVSGESGAGKTVSAKYAMRYFAtVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14886    82 CIVSGESGAGKTETAKQLMNFFA-YGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLgIS 318
Cdd:cd14886   161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  319 ESYQMGIFRILAGILHLGNVGFASRDS---DSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14886   240 KNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14886   320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  476 EYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMPKGTDDTWAQKLyNTHLNKcALFEKPRMSNKAFIIKHFA 554
Cdd:cd14886   400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIKN-NSFIPGKGSQCNFTIVHTA 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  555 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrvpvkptkgRPGQTAKEHKKT 634
Cdd:cd14886   478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD----------------------------IPNEDGNMKGKF 529

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14886   530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILI 609

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 568960783  715 KQKDVLG----DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14886   610 SHNSSSQnageDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650

MYSc_Myo13

cd14875

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

85-751

3.27e-120

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: 395.33 E-value: 3.27e-120

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQM-ARDERNQSIIVS 162
Cdd:cd14875     3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVS----GSASEANVEEKVLA----SNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd14875    83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  235 -IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCA------SAKL------PEFKMLRLGNAdsfhYTKQG--GSPmiegV 299
Cdd:cd14875   163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAglspeeKKELgglktaQDYKCLNGGNT----FVRRGvdGKT----L 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  300 DDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPpKHEPLTIFCDLMGVDYEEM--CHWLch 377
Cdd:cd14875   235 DDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIA-DETPFLTACRLLQLDPAKLreCFLV-- 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  378 rKLATATETYIKpiSKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHS--FIGVLDIYGFETFEINSFEQFCIN 455
Cdd:cd14875   312 -KSKTSLVTILA--NKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGckYIGLLDIFGFENFTRNSFEQLCIN 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  456 YANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNK 534
Cdd:cd14875   389 YANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  535 CALFEKPRMS-NKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgrtplt 613
Cdd:cd14875   469 SPYFVLPKSTiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE------------------ 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  614 rvpvkptkgrpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRIS 693
Cdd:cd14875   531 ------------KGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALK 598

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960783  694 AAGFPSRWTYQEFFSRYRVLM--------KQKDvLGDRKQTCKNVLEKLI-LDKDKYQFGKTKIFFR 751
Cdd:cd14875   599 RQGYPVRRPIEQFCRYFYLIMprstaslfKQEK-YSEAAKDFLAYYQRLYgWAKPNYAVGKTKVFLR 664

MYSc_Myo37

cd14898

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

84-713

2.22e-114

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: 375.77 E-value: 2.22e-114

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQlpIYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARdERNQSIIVSG 163
Cdd:cd14898     2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  164 ESGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRyrIIGANMRTYL 243
Cdd:cd14898    77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--ITGAKFETYL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  244 LEKSRVVFQAEEERNYHIFYQLCASaklpefKMLRLGNadSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISeSYQm 323
Cdd:cd14898   153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNIKN--DFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIA-NFK- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  324 GIFRILAGILHLGNVGFASrdsDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATEtYIKPISKL-QATNARDA 402
Cdd:cd14898   223 SIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGE-TIEVFNTLkQARTIRNS 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  403 LAKHIYAKLFNWIVDHVNQALhSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQI 482
Cdd:cd14898   299 MARLLYSNVFNYITASINNCL-EGSGERS-ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGI 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  483 PWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKL--YNTHlnkcalFEKPRMSNKaFIIKHFADKVEYQ 560
Cdd:cd14898   377 EWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDK-IKVSHYAGDVEYD 449

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  561 CEGFLEKNKDtvfEEQIKVLKSskfkmlpelfqddekaisptsatssgrtpltrvpvkptkgrPGQTAKEHKKTVGHQFR 640
Cdd:cd14898   450 LRDFLDKNRE---KGQLLIFKN-----------------------------------------LLINDEGSKEDLVKYFK 485

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568960783  641 NSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14898   486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558

MYSc_Myo17

cd14879

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

84-750

4.58e-108

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: 360.33 E-value: 4.58e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIdSKLIYTYCGI-VLVAINPYEQLPI--------YGEDIINAYSGQNMGDMdPHIFAVAEEAYKQMARDE 154
Cdd:cd14879     5 AITSHLASRFR-SDLPYTRLGSsALVAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLP-PHAYDLAARAYLRMRRRS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14879    83 EDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGG---SPMIEGVDDAKEMAHTRQ 310
Cdd:cd14879   163 LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGchpLPLGPGSDDAEGFQELKT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  311 ACTLLGISESYQMGIFRILAGILHLGNVGF---ASRDSDSCTIPPKHEpLTIFCDLMGVDYEEmchwlchrkLATATeTY 387
Cdd:cd14879   243 ALKTLGFKRKHVAQICQLLAAILHLGNLEFtydHEGGEESAVVKNTDV-LDIVAAFLGVSPED---------LETSL-TY 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  388 iKpiSKL-------------QATNARDALAKHIYAKLFNWIVDHVNQALhSAVKQ--HSFIGVLDIYGFETF---EINSF 449
Cdd:cd14879   312 -K--TKLvrkelctvfldpeGAAAQRDELARTLYSLLFAWVVETINQKL-CAPEDdfATFISLLDFPGFQNRsstGGNSL 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  450 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKL 527
Cdd:cd14879   388 DQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKpGGLLGILDDQTRrMPKKTDEQMLEAL 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  528 YNTHLNKCALFEKPRMSNK----AFIIKHFADKVEYQCEGFLEKNKDTVfeeqikvlkSSKFKMLpelfqddekaISPTs 603
Cdd:cd14879   468 RKRFGNHSSFIAVGNFATRsgsaSFTVNHYAGEVTYSVEGFLERNGDVL---------SPDFVNL----------LRGA- 527

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  604 atssgrtpltrvpvkptkgrpgqtakehkktvgHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRA 683
Cdd:cd14879   528 ---------------------------------TQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRS 574

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960783  684 CGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVlgDRKQTCknVLEKLILDKDKYQFGKTKIFF 750
Cdd:cd14879   575 LGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAA--ERIRQC--ARANGWWEGRDYVLGNTKVFL 637

MYSc_Myo16

cd14878

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

84-751

2.55e-97

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: 329.47 E-value: 2.55e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGDMDPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14878     2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  161 VSGESGAGKTVSAKYAMRYFATVSGSaSEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF-DKRYRIIGANM 239
Cdd:cd14878    81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQG---GSPMIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14878   160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmreDVSTAERSLNREKLAVLKQALNVVG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  317 ISESYQMGIFRILAGILHLGNVGF-ASRDSDSCTIpPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14878   240 FSSLEVENLFVILSAILHLGDIRFtALTEADSAFV-SDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSF----IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14878   319 AEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  472 LEQEEYMKEQIPW----------TLIDFYDNQPcinlieskLGILDLLDEECKMPKGTDDTWAQKLY----NTHLNKCAL 537
Cdd:cd14878   399 QEQTECVQEGVTMetayspgnqtGVLDFFFQKP--------SGFLSLLDEESQMIWSVEPNLPKKLQslleSSNTNAVYS 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  538 FEK-------PRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisptsatssgrT 610
Cdd:cd14878   471 PMKdgngnvaLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----------------S 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  611 PLTrvpvkptkgrpgqtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETI 690
Cdd:cd14878   535 KLV--------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMV 594

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960783  691 RISAAGFPSRWTYQEFFSRYRVLMKQkdVLGDRKQT-----CKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd14878   595 KIFRYGYPVRLSFSDFLSRYKPLADT--LLGEKKKQsaeerCRLVLQQCKL--QGWQMGVRKVFLK 656

MYSc_Myo24A

cd14937

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

85-751

6.68e-95

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

Pssm-ID: 276897 Cd Length: 637 Bit Score: 321.96 E-value: 6.68e-95

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYgediINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14937     3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  165 SGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14937    78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  245 EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGgSPMIEGVDDAKEMAHTRQACTLLGISEsYQMG 324
Cdd:cd14937   156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNK-NVVIPEIDDAKDFGNLMISFDKMNMHD-MKDD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  325 IFRILAGILHLGNVGFASRDS---DSCTIPPKH--EPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14937   234 LFLTLSGLLLLGNVEYQEIEKggkTNCSELDKNnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  400 RDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14937   314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTwaqkLYNTHLNKCALFEK----PRMSNKAFIIKHFAD 555
Cdd:cd14937   394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKyastKKDINKNFVIKHTVS 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpltrvpVKPTKGRpgqtakehKKTV 635
Cdd:cd14937   470 DVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE--------------------VSESLGR--------KNLI 521

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAgFPSRWTYQEFFSRYRVL-- 713
Cdd:cd14937   522 TFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdy 600

                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568960783  714 MKQKDVLGDRKQTCKNVLEKLIlDKDKYQFGKTKIFFR 751
Cdd:cd14937   601 STSKDSSLTDKEKVSMILQNTV-DPDLYKVGKTMVFLK 637

MYSc_Myo18

cd01386

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

85-751

3.24e-94

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 321.57 E-value: 3.24e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01386     3 VLHTLRQRY-GANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  165 SGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01386    82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  245 EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGN-ADSFHYtkqGGSPMIEGVD---DAKEMAHTRQACTLLGISES 320
Cdd:cd01386   162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQlAESNSF---GIVPLQKPEDkqkAAAAFSKLQAAMKTLGISEE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  321 YQMGIFRILAGILHLGNVGfASRDSDSCTIP-PKHEPLTIFCDLMGVDYEEMCHWLCHRKL------ATATETYIKPIS- 392
Cdd:cd01386   239 EQRAIWSILAAIYHLGAAG-ATKAASAGRKQfARPEWAQRAAYLLGCTLEELSSAIFKHHLsggpqqSTTSSGQESPARs 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  393 -----KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFE------INSFEQFCINYANEKL 461
Cdd:cd01386   318 ssggpKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAhsgsqrGATFEDLCHNYAQERL 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  462 QQQFNMHVFKLEQEEYMKEQIPwtlIDFYDNQPC----INLI---------------ESKLGILDLLDEECKMPKGTDDT 522
Cdd:cd01386   398 QLLFHERTFVAPLERYKQENVE---VDFDLPELSpgalVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSDDT 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  523 WAQKLYnTHLNKCALFEKPRMSNKA-----FIIKHF--ADKVEYQCEGFLEKNKDTVFEEQikvlksskfkmLPELFQDD 595
Cdd:cd01386   475 FLERLF-SHYGDKEGGKGHSLLRRSegplqFVLGHLlgTNPVEYDVSGWLKAAKENPSAQN-----------ATQLLQES 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  596 EKaisptsatssgrtpltrvpvkptkgrpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPN------DFKFP 669
Cdd:cd01386   543 QK----------------------------ETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTS 594

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  670 FTFDEKRAVQ------QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK-------QKDVLGDRKQTCKNVLEKLIL 736
Cdd:cd01386   595 SPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkklgLNSEVADERKAVEELLEELDL 674

                         730
                  ....*....|....*
gi 568960783  737 DKDKYQFGKTKIFFR 751
Cdd:cd01386   675 EKSSYRIGLSQVFFR 689

MYSc_Myo26

cd14887

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

83-751

1.19e-93

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: 320.83 E-value: 1.19e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFI-------DSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14887     1 PNLLENLYQRYNkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  156 NQSIIVSGESGAGKTVSAKYAMRYFATVS---GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14887    81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYtkqggspmiegvddakEMAHTRQAC 312
Cdd:cd14887   161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------------DLRRITAAM 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  313 TLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHR---KLATATETYIK 389
Cdd:cd14887   225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKCLSsglKVTEASRKHLK 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  390 PISKL--------------------------------QATNARDALAKHIYAKLFNWIVDHVNQALHSAVK--------- 428
Cdd:cd14887   305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  429 -----QHSFIGVLDIYGFETFE---INSFEQFCINYANEKLqqqfnmHVFKLEQ-----------EEYMKEQI------- 482
Cdd:cd14887   385 tpsttGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERL------HCFLLEQlilnehmlytqEGVFQNQDcsafpfs 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  483 ----------PWTLIDF-----------YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14887   459 fplastltssPSSTSPFsptpsfrsssaFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKNIT 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  542 R---MSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFqddekaisptsatSSGRTPLTRVPVK 618
Cdd:cd14887   539 PalsRENLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLF-------------LACSTYTRLVGSK 593

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  619 PTKGRpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14887   594 KNSGV--RAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568960783  699 SRWTYQEFFSRY--RVLMKQKDVLgDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14887   672 CRLPYVELWRRYetKLPMALREAL-TPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725

MYSc_Myo23

cd14884

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

83-750

1.66e-90

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: 310.68 E-value: 1.66e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYS-------GQNMGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14884     1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR--- 231
Cdd:cd14884    80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVent 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  232 ------YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL---CASAKLPEFKMLR------LGNADSFHYTKQGGSPMI 296
Cdd:cd14884   160 qknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARRNLVRncgvygLLNPDESHQKRSVKGTLR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  297 EGVD-----------DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNvgfasrDSDSCTippkhepltifCDLMG 365
Cdd:cd14884   240 LGSDsldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN------RAYKAA-----------AECLQ 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  366 VDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL------------HSAVKQHSFI 433
Cdd:cd14884   303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  434 GVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESklgILDLLDEEC 513
Cdd:cd14884   383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK---IFRRLDDIT 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  514 KMP----KGTDDTWAQKLYNTHlNKCALFEK-------PRM---SNKA-------FIIKHFADKVEYQCEGFLEKNKDTV 572
Cdd:cd14884   460 KLKnqgqKKTDDHFFRYLLNNE-RQQQLEGKvsygfvlNHDadgTAKKqnikkniFFIRHYAGLVTYRINNWIDKNSDKI 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  573 feeqikvlksskfkmlpelfqddEKAISPTSATSSGRTpLTRVPVKPTKGrpgqtakeHKKTVGHQFRNSLHLLMETLNA 652
Cdd:cd14884   539 -----------------------ETSIETLISCSSNRF-LREANNGGNKG--------NFLSVSKKYIKELDNLFTQLQS 586

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  653 TTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkQKDVLGDRKQTCKNVLE 732
Cdd:cd14884   587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQI-AKELEKCNSNTDIEYQR 665

                         730
                  ....*....|....*...
gi 568960783  733 KLILDKDKYQFGKTKIFF 750
Cdd:cd14884   666 RLAALDVQFIPDGRLYAF 683

MYSc_Myo20

cd14881

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

84-750

1.01e-89

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: 306.66 E-value: 1.01e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFIDSKLiYTYCGIVLVAINPYEqlpiygeDIINAY---SGQNMGDMdPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14881     2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYR-------DVGNPLtltSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAII 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  161 VSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKryriiGANMR 240
Cdd:cd14881    73 LSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  241 T----YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG--NADSFHYTkQGGSPMIEGVDDAKEMAHTRQACTL 314
Cdd:cd14881   148 TkihcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYL-SHGDTRQNEAEDAARFQAWKACLGI 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  315 LGISESyqmGIFRILAGILHLGNVGFAsrDSDSCTIPPKHE-PLTIFCDLMGVDYEEMchwlcHRKLATATET----YIK 389
Cdd:cd14881   227 LGIPFL---DVVRVLAAVLLLGNVQFI--DGGGLEVDVKGEtELKSVAALLGVSGAAL-----FRGLTTRTHNargqLVK 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  390 PISKLQATNA-RDALAKHIYAKLFNWIVDHVN--QALHSAVKQHS---FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14881   297 SVCDANMSNMtRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQH 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  464 QFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCINLIES-KLGILDLLDEECKmPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14881   377 FYNTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAK 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  542 RMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVL--KSSKFKMLPELfQDdekaisptsatssgrtpltrvpvkp 619
Cdd:cd14881   456 PQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFykQNCNFGFATHT-QD------------------------- 509

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  620 tkgrpgqtakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd14881   510 -------------------FHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPH 570

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960783  700 RWTYQEFFSRYRVLMKQKDVLGDRKQ--TCKNVLEKLILDKDK---------YQFGKTKIFF 750
Cdd:cd14881   571 RMRFKAFNARYRLLAPFRLLRRVEEKalEDCALILQFLEAQPPsklssvstsWALGKRHIFL 632

MYSc_Myo44

cd14905

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

97-751

1.46e-87

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: 301.63 E-value: 1.46e-87

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   97 KLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGdMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKY 175
Cdd:cd14905    14 EIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENTKI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  176 AMRYFATVSGSASEAnVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEE 255
Cdd:cd14905    92 IIQYLLTTDLSRSKY-LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  256 ERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHL 335
Cdd:cd14905   171 ERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIIL 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  336 GNVGFASRDSDSctiPPKHEPLTifcdlmgvdyEEMCHWLCHRklATATETYI---KPISKLQATNARDALAKHIYAKLF 412
Cdd:cd14905   251 GNVTFFQKNGKT---EVKDRTLI----------ESLSHNITFD--STKLENILisdRSMPVNEAVENRDSLARSLYSALF 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  413 NWIVDHVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPW-TLIDFYD 491
Cdd:cd14905   316 HWIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKD 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  492 NQPCINLIESklgILDLLDEECKMPKGTDDTWAQKLYNtHLNKCALF-EKPrmsNKaFIIKHFADKVEYQCEGFLEKNKD 570
Cdd:cd14905   395 NEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQN-FLSRHHLFgKKP---NK-FGIEHYFGQFYYDVRGFIIKNRD 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  571 TVFEEQIKVLKSSKFKMLpeLFQDDEKAISPTSA---------TSSGRTPLTRVPVKPTKG--RPGQTAKEHKKTVG--- 636
Cdd:cd14905   467 EILQRTNVLHKNSITKYL--FSRDGVFNINATVAelnqmfdakNTAKKSPLSIVKVLLSCGsnNPNNVNNPNNNSGGggg 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  637 --------------HQFRNSLHLLMETLNATTpHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 702
Cdd:cd14905   545 ggnsgggsgsggstYTTYSSTNKAINNSNCDF-HFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYN 623

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568960783  703 YQEFFSRYRVLMKQkdvlgdrKQTCKNVLEKLI---LDKDK-----YQFGKTKIFFR 751
Cdd:cd14905   624 NKIFFDRFSFFFQN-------QRNFQNLFEKLKendINIDSilpppIQVGNTKIFLR 673

Myo5-like_CBD

cd14945

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

1479-1802

5.43e-86

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

Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 283.14 E-value: 5.43e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1479 EDEQKLVKNLILELKPRGVAVNLipgLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1558
Cdd:cd14945     1 SEEDSLLRGIVTDFEPSSGDHKL---TPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1559 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1638
Cdd:cd14945    78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1639 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRY 1718
Cdd:cd14945   140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1719 NVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1798
Cdd:cd14945   202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280


                  ....
gi 568960783 1799 RTIQ 1802
Cdd:cd14945   281 RTLA 284

MYSc_Myo12

cd14874

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

84-751

2.70e-80

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: 279.06 E-value: 2.70e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYsgqnmgdmdpHIFAVAEEAYKQMARDERN-QSIIVS 162
Cdd:cd14874     2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  163 GESGAGKTVSAKYAMRYFATVSGSASEAnveEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR-T 241
Cdd:cd14874    71 GESGSGKSYNAFQVFKYLTSQPKSKVTT---KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKyT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  242 YLLEKSRVVFQAEEERNYHIFYQLCASakLPEFKMLRLGNADS--FHYTKQGGSpmIEGV-DDAKEMAHTRQACTLLGIS 318
Cdd:cd14874   147 VPLEVPRVISQKPGERNFNVFYEVYHG--LNDEMKAKFGIKGLqkFFYINQGNS--TENIqSDVNHFKHLEDALHVLGFS 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  319 ESYQMGIFRILAGILHLGNVGFASR-----DSDSCTIPPKHEpLTIFCDLMGVDYEEMCHWLchrklaTATETYIKPISK 393
Cdd:cd14874   223 DDHCISIYKIISTILHIGNIYFRTKrnpnvEQDVVEIGNMSE-VKWVAFLLEVDFDQLVNFL------LPKSEDGTTIDL 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  394 LQATNARDALAKHIYAKLFNWIVD----HVNQALHSAVkqhsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHV 469
Cdd:cd14874   296 NAALDNRDSFAMLIYEELFKWVLNriglHLKCPLHTGV-----ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  470 FKLEQEEYMKEQIPwtlIDF-----YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCAlFEKPRM 543
Cdd:cd14874   371 FHDQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKARN 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  544 SNK-AFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaiSPTSATSsgrtpltrvpvkptkg 622
Cdd:cd14874   447 KERlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------SYSSNTS---------------- 504

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  623 rpgqtakEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 702
Cdd:cd14874   505 -------DMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKIS 577

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960783  703 YQEFFSRYRVLMKqkdvlGDRKQtCKNVLEkLILD---------KDKYQFGKTKIFFR 751
Cdd:cd14874   578 KTTFARQYRCLLP-----GDIAM-CQNEKE-IIQDilqgqgvkyENDFKIGTEYVFLR 628

MYSc_Myo32

cd14893

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

86-750

3.45e-74

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: 264.14 E-value: 3.45e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   86 LHNLRVRF-IDSklIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN----------MGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14893     4 LYTLRARYrMEQ--VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-----------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKY 223
Cdd:cd14893    82 EDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  224 IEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKL-PEFK-MLRLGN-ADSFHYTKQGGSPMIEGVD 300
Cdd:cd14893   162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdPTLRdSLEMNKcVNEFVMLKQADPLATNFAL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  301 DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGF----------------ASRDSDSCTIPPKHEpLTIFCDLM 364
Cdd:cd14893   242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvgganstTVSDAQSCALKDPAQ-ILLAAKLL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  365 GVDYEEMCHWLCHRKL----ATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL---------HSAVKQHS 431
Cdd:cd14893   321 EVEPVVLDNYFRTRQFfskdGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryekSNIVINSQ 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  432 FIGVLDIYGFETFE--INSFEQFCINYANEKLQQQF-------NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIES 501
Cdd:cd14893   401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDItSEQEKCLQLFED 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  502 K-LGILDLLDEECKMPKGTDDTWAQKLYN--------THLNKCALFEKPRMSNKA-----FIIKHFADKVEYQCEGFLEK 567
Cdd:cd14893   481 KpFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglSRPNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSK 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  568 NKDTVFEEQIKVLKSSKFKMLPELfqdDEKAISPTSATSSGRTPLTRVPVKPTKGRPGQTAKEHK---KTVGHQFRNSLH 644
Cdd:cd14893   561 NMLSISSTCAAIMQSSKNAVLHAV---GAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKnitDSAATDVYNQAD 637

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  645 LLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYrvlmkqKDVLGDRK 724
Cdd:cd14893   638 ALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------KNVCGHRG 711

                         730       740       750
                  ....*....|....*....|....*....|
gi 568960783  725 qTCKNVLEKL----ILDKDKYQFGKTKIFF 750
Cdd:cd14893   712 -TLESLLRSLsaigVLEEEKFVVGKTKVYL 740

MYSc_Myo21

cd14882

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

85-751

3.86e-65

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: 234.63 E-value: 3.86e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   85 VLHNLRVRfIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14882     3 ILEELRHR-YLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  165 SGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14882    82 SYSGKTTNARLLIKHLCYLGDGNR--GATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  245 EKSRVVFQAEEERNYHIFY----QLCASAKLPEF--------KMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAhtrQAC 312
Cdd:cd14882   160 EKLRVSTTDGNQSNFHIFYyfydFIEAQNRLKEYnlkagrnyRYLRIPPEVPPSKLKYRRDDPEGNVERYKEFE---EIL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  313 TLLGISESYQMGIFRILAGILHLGNVGFasRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14882   237 KDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHT 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  393 KLQATNARDALAKHIYAKLFNWIVDHVNQALH--SAV--KQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14882   315 TEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVfgDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQR 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  469 VFKLEQEEYMKEQIPWTLIDFYDNQPCI-NLIESKLGILDLLDEECKMPKGtddtwAQKLYNTHLNKCALFEKPrMSNKA 547
Cdd:cd14882   394 IFISEMLEMEEEDIPTINLRFYDNKTAVdQLMTKPDGLFYIIDDASRSCQD-----QNYIMDRIKEKHSQFVKK-HSAHE 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  548 FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptsaTSSgrtpltrvpvkptkgrpgQT 627
Cdd:cd14882   468 FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF------------TNS------------------QV 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  628 AKehKKTVGHQFRNSLHLLMETL----NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTY 703
Cdd:cd14882   518 RN--MRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783  704 QEFFSRYRVLMKQKDVLGD-RKQTCKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd14882   596 QEFLRRYQFLAFDFDETVEmTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642

Motor_domain

cd01363

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

106-229

6.26e-49

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: 172.14 E-value: 6.26e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  106 VLVAINPYEQLPIYGED-IINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVS 184
Cdd:cd01363     1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568960783  185 GSASEAN--------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFD 229
Cdd:cd01363    81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139

DIL

pfam01843

DIL domain; The DIL domain has no known function.

1684-1787

7.97e-42

DIL domain; The DIL domain has no known function.

Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 148.89 E-value: 7.97e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1684 QVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEA 1763
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79

                           90       100
                   ....*....|....*....|....
gi 568960783  1764 ICSMCNALTTAQIVKVLNLYTPVN 1787
Cdd:pfam01843   80 ILQVCPALNPLQLHRLLTLYQPDD 103

MYSc_Myo24B

cd14938

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

83-749

3.84e-39

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: 157.69 E-value: 3.84e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   83 PAVLHNLRVRFIDSKLiYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14938     1 PSVLYHLKERFKNNKF-YTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  162 SGESGAGKTVSAKYAMRYFA-TVSGSASEA---------------------NVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14938    80 SGESGSGKSEIAKNIINFIAyQVKGSRRLPtnlndqeednihneentdyqfNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  220 FGKYIEIGFDKRyRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGV 299
Cdd:cd14938   160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  300 DDAKEMAHTRQACTLLGISESYQMgIFRILAGILHLGNV----GFASRDS----DSCTIPPKHEplTIFCDL-----MGV 366
Cdd:cd14938   239 YSGKILELLKSLNYIFDDDKEIDF-IFSVLSALLLLGNTeivkAFRKKSLlmgkNQCGQNINYE--TILSELensedIGL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  367 DYEEMCHWLCHRKLATATETYIKPIS---------------KLQATNARDALAKHIYAKLFNWIVDHVNQ---ALHSAVK 428
Cdd:cd14938   316 DENVKNLLLACKLLSFDIETFVKYFTtnyifndsilikvhnETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNINI 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  429 QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCIN-LIESKLGIL 506
Cdd:cd14938   396 NTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSL 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  507 DLLDEECKMPKGTDDTwaqKLYNTHLNKCA-----LFEKPRMSN-KAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVL 580
Cdd:cd14938   476 FSLLENVSTKTIFDKS---NLHSSIIRKFSrnskyIKKDDITGNkKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMV 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  581 KSSKFKMLpelfqddEKAISPTSATSSGRTpltrvpVKPTKGRPGQTA-KEHKKTVGHQ-------FRNSLHLLMETLNA 652
Cdd:cd14938   553 KQSENEYM-------RQFCMFYNYDNSGNI------VEEKRRYSIQSAlKLFKRRYDTKnqmavslLRNNLTELEKLQET 619

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  653 TTPHYVRCIKPNDFK-FPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKqkdvlgDRKQTCKNVL 731
Cdd:cd14938   620 TFCHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE------DLKEKVEALI 693

                         730
                  ....*....|....*...
gi 568960783  732 EKLILDKDKYQFGKTKIF 749
Cdd:cd14938   694 KSYQISNYEWMIGNNMIF 711

Myo5p-like_CBD_DIL_ANK

cd15473

cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ...

1505-1834

7.58e-32

cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown.

Pssm-ID: 271257 [Multi-domain] Cd Length: 316 Bit Score: 127.67 E-value: 7.58e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1505 LPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgEEGFmkhntsrqne 1584
Cdd:cd15473    32 VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNVTLLLHYLKK---DAGL---------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1585 hcltNFDLAEYRQVLSDLAIQIYQQLVRVLEnilqpmivsgmlehetiqgvsgvkptglrKRTSSIADEGTYTLDSIlrq 1664
Cdd:cd15473    99 ----VEATPEFQQELAELINEIFVLIIRDAE-----------------------------RRIDKLLDASPRNITSL--- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1665 LNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLM-------NSGA 1737
Cdd:cd15473   143 LSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWARSNNLQpekgespPRIA 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1738 KETLEPLIQAAQLLQVKKKTDDDAEAICSM--CNALTTAQIVKVLNLYTP-VNefEERVSVSFIRTIQMRLRDRKDSpql 1814
Cdd:cd15473   223 RSHLAPVIQLLQWLQCLSSLDDFESLIATIqqLDALNPLQLLRAVKDYRYeVN--EGRMPEECVKYLAQLQKDWLDS--- 297

                         330       340
                  ....*....|....*....|
gi 568960783 1815 lmdaKHIFPVTFPFNPSSLA 1834
Cdd:cd15473   298 ----RYMLPFSLPTDTEMLV 313

Myo5p-like_CBD_fungal

cd15474

cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ...

1484-1828

1.79e-29

cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.

Pssm-ID: 271258 Cd Length: 352 Bit Score: 121.76 E-value: 1.79e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1484 LVKNLILELKPRGVAVN----LIPGLPAYILFMCVRHADYLNDDQKVRSL--LTSTINSIKKVLKKRgDDFETVSFWLSN 1557
Cdd:cd15474    11 LKSVEVLELKDISDEVSgdnlLFLGHVNFLIYSQMWKSLLELLTQSERFLshVLSYIASIVDSLPKK-ETIPDGAFWLAN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1558 TCRFLHCL--KQYSGEEGFMKHNTSRQNEHCLTNFDlaEYRQVLSdlaiQIYQQLVRVLENILQPMIVSGMLEHETIQGV 1635
Cdd:cd15474    90 LHELRSFVvyLLSLIEHSSSDEFSKESEEYWNTLFD--KTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1636 SGvkptgLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQ 1715
Cdd:cd15474   164 SE-----LIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1716 IRYNVSQLEEWLRDKNLmnSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNeFEERVSV 1795
Cdd:cd15474   239 ISYNVSRLKEWCHQHGL--SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPAN-YEAPVPK 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 568960783 1796 SFIRTI-QMRLRDRKDSPQLLMDAKHIFPVTFPF 1828
Cdd:cd15474   316 EFLNALeKLIKKENLSLPGRKNNSKMEIPESSNF 349

MYSc_Myo33

cd14894

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

196-734

3.90e-29

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: 126.78 E-value: 3.90e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  196 VLASNPIMESIGNAKTTRNDNSSRFGKY--IEIGFDK---RYRIIGANMRTYLLEKSRVVFQA------EEERNYHIFYQ 264
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  265 LCASAKLPEF-----KMLRLGNADSFHYTKQGGSP-----MIEGVD----DAKEMAHTRQACTLLGISESYQMGIFRILA 330
Cdd:cd14894   329 MVAGVNAFPFmrllaKELHLDGIDCSALTYLGRSDhklagFVSKEDtwkkDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  331 GILHLGNVGFASRD---------SDSCTIPPKhepLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:cd14894   409 AVLWLGNIELDYREvsgklvmssTGALNAPQK---VVELLELGSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRD 485

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  402 ALAKHIYAKLFNWIVDHVNQALH-----------------SAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQq 464
Cdd:cd14894   486 TLARLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnaSAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA- 564

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  465 fnmhvfKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLdEECKMPKGTDDTWAQ------KLYNTHL---NKC 535
Cdd:cd14894   565 ------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENMNAQqeekrnKLFVRNIydrNSS 637

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  536 ALFEKPRMSNKA------------FIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaispts 603
Cdd:cd14894   638 RLPEPPRVLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNE--------- 708

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  604 ATSSGRTPLT-RVPVKPTKGRPGQTakehKKTVGhQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLR 682
Cdd:cd14894   709 SSQLGWSPNTnRSMLGSAESRLSGT----KSFVG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCR 783

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568960783  683 ACGV---LETIRISAAGFPS-RWTYQEFFSRYRVLMKQKDVLGDRKQTCKNVLEKL 734
Cdd:cd14894   784 SQRLirqMEICRNSSSSYSAiDISKSTLLTRYGSLLREPYILDDVAGDNSNLMNWL 839

fMyo2p_CBD

cd15480

cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ...

1657-1852

4.95e-29

cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.

Pssm-ID: 271264 Cd Length: 363 Bit Score: 120.76 E-value: 4.95e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1657 TLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNlMNSG 1736
Cdd:cd15480   167 TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWCKSHD-IPEG 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1737 AkETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTpVNEFEERVSVSFIRTIQMRLR--DRKDSPQL 1814
Cdd:cd15480   246 T-LQLEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVAARVKpeDKSDHLLL 323

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568960783 1815 LMDAKHIFPVTFPFNPSSLALETIqIPASLGLGFIARV 1852
Cdd:cd15480   324 IPLVEEVGPFEDPFPREIAGLEAY-IPAWLNLPHIRRL 360

SMC_prok_B

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

902-1441

1.33e-16

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.65 E-value: 1.33e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   902 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVA 981
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   982 TGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNhrivEQAKEMTEtmerkLV 1061
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD----ELAEELAE-----LE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1062 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmlnvpkpghKRTDSTHSSNESEYTFSSEF----AETEDIA 1137
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1138 PRTEEPIEKKVPLDMSL----FLKLQKRVTELEQEKQLMQDELDRKEEQvfrskaKEEERPQIRGAELEYESLKRQELES 1213
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1214 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ---- 1281
Cdd:TIGR02168  488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIAflkq 567

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1282 ---------PKNTMTDSTI----------------LLEDVQKMKDKGEIAQAYI--------GLKE-TNRSSTMDYQELN 1327
Cdd:TIGR02168  568 nelgrvtflPLDSIKGTEIqgndreilkniegflgVAKDLVKFDPKLRKALSYLlggvlvvdDLDNaLELAKKLRPGYRI 647

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1328 --EDGELW-----MVYEGLKQANRLLE-----SQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIE 1395
Cdd:TIGR02168  648 vtLDGDLVrpggvITGGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 568960783  1396 -ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1441
Cdd:TIGR02168  728 iSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774

COG5022

Myosin heavy chain [General function prediction only];

1251-1787

6.93e-16

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 84.36 E-value: 6.93e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1251 QLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkNTMTDSTILLEDVQKMKDkgeIAQAYIGLKETNRSSTMDYQELNEDg 1330
Cdd:COG5022   831 KLRETEEVEFSLKAEVLIQKFGRSLKAKKRF--SLLKKETIYLQSAQRVEL---AERQLQELKIDVKSISSLKLVNLEL- 904

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1331 eLWMVYEGLK--QANRLLESQLQSQKRSHEneaealrgeiqslkEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNE 1408
Cdd:COG5022   905 -ESEIIELKKslSSDLIENLEFKTELIARL--------------KKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKET 969

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1409 NLDLMEQLEKQDKTVRKLKKQ---LKVFAKKIGELEVGQME-NISPGQIIDEPIRPVNIPRKEKDFQGMLEYKR--EDEQ 1482
Cdd:COG5022   970 SEEYEDLLKKSTILVREGNKAnseLKNFKKELAELSKQYGAlQESTKQLKELPVEVAELQSASKIISSESTELSilKPLQ 1049

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1483 KLVKNLILE---LKPRGVAVNLIPGLPAYILfmcvrhaDYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSF------ 1553
Cdd:COG5022  1050 KLKGLLLLEnnqLQARYKALKLRRENSLLDD-------KQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQfivaqm 1122

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1554 WLSNTCRFLH-CLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLS------------------DLAIQIYQQLVRVL 1614
Cdd:COG5022  1123 IKLNLLQEISkFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSpppfaalsekrlyqsalyDEKSKLSSSEVNDL 1202

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1615 EN-----------------ILQPMIVSGMLEHETIQGVSGVKPTGLRKRTSSIadegtYTLDSILRQLNSFHSVMCQHGM 1677
Cdd:COG5022  1203 KNelialfskifsgwprgdKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPAS-----MSNEKLLSLLNSIDNLLSSYKL 1277

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1678 DPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWlrDKNLMNSGAKETLEPLIQAAQLLQVKKKT 1757
Cdd:COG5022  1278 EEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSEELDDW--CREFEISDVDEELEELIQAVKVLQLLKDD 1355

                         570       580       590
                  ....*....|....*....|....*....|
gi 568960783 1758 DDDAEAICSMCNALTTAQIVKVLNLYTPVN 1787
Cdd:COG5022  1356 LNKLDELLDACYSLNPAEIQNLKSRYDPAD 1385

Myo5p-like_CBD_afadin

cd15471

cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ...

1506-1785

1.43e-15

cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain.

Pssm-ID: 271255 Cd Length: 322 Bit Score: 80.05 E-value: 1.43e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1506 PAYILFMCVRH---ADYLNDD------QKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgeegfmk 1576
Cdd:cd15471    25 PAYTLYLAARYrlsTHYRPELtpteraHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1577 hntsrqnEHCLTNFDLaEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTglrkrtssiadegTY 1656
Cdd:cd15471    96 -------DRDLSAFSV-QAQDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPAIGDV-------------LH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1657 TLDSILRQLNsfhsvmcQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKD--MCSWSKGMQIRYNVSQLEEWLrDKNLMN 1734
Cdd:cd15471   155 TLSSAMRLLR-------RCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWA-ERQGLE 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568960783 1735 SGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTP 1785
Cdd:cd15471   227 LAADCHLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP 277

Smc

COG1196

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

902-1501

1.85e-14

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 1.85e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  902 KRELKKLKIEARSVERYKKLHI---------------GMENKIMQLQRKVDEQNKDYKCLMEKLTNLEgvynSETEKLRN 966
Cdd:COG1196   199 ERQLEPLERQAEKAERYRELKEelkeleaellllklrELEAELEELEAELEELEAELEELEAELAELE----AELEELRL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  967 DVERLQLSEEEAKvatGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNH--- 1043
Cdd:COG1196   275 ELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaee 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1044 --RIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMLnvpkpghKRTDSTHSSNE 1121
Cdd:COG1196   352 elEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-------ERLERLEEELE 424

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1122 SEYTFSSEFAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEE-ERPQIRGAE 1200
Cdd:COG1196   425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLlLLEAEADYE 504

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1201 LEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLilrsqlvsQKEAI 1280
Cdd:COG1196   505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--------GRATF 576

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1281 QPKNTMTDSTILLEDVQkmkdKGEIAQAYIGLKETNRSSTMDYQEL-NEDGELWMVYEGLKQANRLLESQLQSQKR-SHE 1358
Cdd:COG1196   577 LPLDKIRARAALAAALA----RGAIGAAVDLVASDLREADARYYVLgDTLLGRTLVAARLEAALRRAVTLAGRLREvTLE 652

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1359 NEAEALRGEIQSLKEENNRQQQLLAQNLqlppEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIG 1438
Cdd:COG1196   653 GEGGSAGGSLTGGSRRELLAALLEAEAE----LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568960783 1439 ELEVGQMenispgQIIDEPIRPVNIPRKEKDFQGMLEYKREDEQKLVKNLILELKPRGvAVNL 1501
Cdd:COG1196   729 QLEAERE------ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG-PVNL 784

PRK03918

DNA double-strand break repair ATPase Rad50;

901-1442

2.70e-14

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 2.70e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  901 AKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGvynsETEKLRNDVERLQLSEEEakv 980
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE----ELEKLEKEVKELEELKEE--- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  981 atgrVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTL---------LKQEKETLNHRIVEQAKE 1051
Cdd:PRK03918  240 ----IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaeeyikLSEFYEEYLDELREIEKR 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1052 MtETMERKLVEETKQLElDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmLNVPKPGHKRTDStHSSNESEYTFSSEFA 1131
Cdd:PRK03918  316 L-SRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEELER-LKKRLTGLTPEKLEK 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1132 ETEDIAPRTEEpIEKKVpldmslfLKLQKRVTELEQEKQLMQDELDRKEEQ-----VFRSKAKEEERPQIRG---AELEY 1203
Cdd:PRK03918  392 ELEELEKAKEE-IEEEI-------SKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEeytAELKR 463

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1204 ESLKRQELESENKKLKNELNELRKALSEKsaPEVTapgapAYRVLMEQLTSVSEELDVR---------------KEEVLI 1268
Cdd:PRK03918  464 IEKELKEIEEKERKLRKELRELEKVLKKE--SELI-----KLKELAEQLKELEEKLKKYnleelekkaeeyeklKEKLIK 536

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1269 LRSQLVSQKEAIQPKNTMTDSTILLEDvQKMKDKGEIAQAYIGLKETNRSSTMDYQE-LNEDGELWMVYEGLKQANRLLE 1347
Cdd:PRK03918  537 LKGEIKSLKKELEKLEELKKKLAELEK-KLDELEEELAELLKELEELGFESVEELEErLKELEPFYNEYLELKDAEKELE 615

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1348 SQLQSQKRSH-------------ENEAEALRGEIQSLKEENNRQQQLLAQNLQLppearieaSLQHEITRLTNENLDLME 1414
Cdd:PRK03918  616 REEKELKKLEeeldkafeelaetEKRLEELRKELEELEKKYSEEEYEELREEYL--------ELSRELAGLRAELEELEK 687

                         570       580
                  ....*....|....*....|....*...
gi 568960783 1415 QLEKQDKTVRKLKKQLKVFAKKIGELEV 1442
Cdd:PRK03918  688 RREEIKKTLEKLKEELEEREKAKKELEK 715

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

927-1431

3.76e-14

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 78.22 E-value: 3.76e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   927 NKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEK 1006
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1007 KSIeerADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLVEETKQLELD------LNDERLRYQN 1080
Cdd:pfam05483  348 SFV---VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKLLDEK 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1081 llNEFSRLEERYDDLKEEMTLMLNV-PKPGHKRTDSTHSSNESEYTFSSEfaeTEDIAPRTEEPIEKKVPLDM-SLFLKL 1158
Cdd:pfam05483  425 --KQFEKIAEELKGKEQELIFLLQArEKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEKLKNIELTAhCDKLLL 499

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1159 QKRvtELEQEKQLMQDELDRKEEQVFRSKaKEEER--PQIRGAElEYESLKRQELESENKKLKNELNELRKAL--SEKSA 1234
Cdd:pfam05483  500 ENK--ELTQEASDMTLELKKHQEDIINCK-KQEERmlKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLdkSEENA 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1235 PEV---TAPGAPAYRVLMEQLTSVSEELDVRKEEVlilrSQLVSQKEAIQPKNTMTDSTILLEDVQKMKDKGEIAQAYIG 1311
Cdd:pfam05483  576 RSIeyeVLKKEKQMKILENKCNNLKKQIENKNKNI----EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1312 LKE--TNRSSTMDYQELNEDGELWMVYEGLKQANRLLESQLQSQKRSHENEAEAL----RGEIQSLKEENNRQQQLLAQN 1385
Cdd:pfam05483  652 FEEiiDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMValmeKHKHQYDKIIEERDSELGLYK 731

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 568960783  1386 LQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLK 1431
Cdd:pfam05483  732 NKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777

PRK03918

DNA double-strand break repair ATPase Rad50;

898-1435

2.10e-13

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 2.10e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  898 RMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYnSETEKLRNDVERLQLSEEE 977
Cdd:PRK03918  171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEELEKELES 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  978 AKvatGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQetdqlVSNLKEENTLLKQEKETLNHRIVEQAKEMtETME 1057
Cdd:PRK03918  250 LE---GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIEKRL-SRLE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1058 RKLVEETKQLElDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmLNVPKPGHKRTDStHSSNESEYTFSSEFAETEDIA 1137
Cdd:PRK03918  321 EEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEELER-LKKRLTGLTPEKLEKELEELE 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1138 PRTEEpIEKKVpldmslfLKLQKRVTELEQEKQLMQDELDRKEEQ-----VFRSKAKEEERPQIRG---AELEYESLKRQ 1209
Cdd:PRK03918  398 KAKEE-IEEEI-------SKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEeytAELKRIEKELK 469

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1210 ELESENKKLKNELNELRKALSEKsaPEVTApgapaYRVLMEQLTSVSEELDVR---------------KEEVLILRSQLV 1274
Cdd:PRK03918  470 EIEEKERKLRKELRELEKVLKKE--SELIK-----LKELAEQLKELEEKLKKYnleelekkaeeyeklKEKLIKLKGEIK 542

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1275 SQKEAIQPKNTMTDSTILLEDVQKMKDKgEIAQAYIGLKETNRSSTMDYQE-LNEDGELWMVYEGLKQANRLLESQLQSQ 1353
Cdd:PRK03918  543 SLKKELEKLEELKKKLAELEKKLDELEE-ELAELLKELEELGFESVEELEErLKELEPFYNEYLELKDAEKELEREEKEL 621

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1354 KRSH-------------ENEAEALRGEIQSLKE-------ENNRQQQLLAQNLQLPPEARIEA--SLQHEITRLTNenlD 1411
Cdd:PRK03918  622 KKLEeeldkafeelaetEKRLEELRKELEELEKkyseeeyEELREEYLELSRELAGLRAELEEleKRREEIKKTLE---K 698

                         570       580
                  ....*....|....*....|....
gi 568960783 1412 LMEQLEKQDKTVRKLKKQLKVFAK 1435
Cdd:PRK03918  699 LKEELEEREKAKKELEKLEKALER 722

SMC_prok_B

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

957-1231

2.45e-13

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 2.45e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   957 YNSETEKLRNDVERLQLSEEEAKVAtgrvlslQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQ 1036
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKA-------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1037 EKETLNHRIVEQAKEMTETMER--KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmLNVpKPGHKRTD 1114
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNE-EAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1115 STHSSNESEYTfSSEFAETEDIAPRTEEPIEKkvpldmslflkLQKRVTELEQEKQLMQDELDRKEEQvfrsKAKEEERP 1194
Cdd:TIGR02168  826 LESLERRIAAT-ERRLEDLEEQIEELSEDIES-----------LAAEIEELEELIEELESELEALLNE----RASLEEAL 889

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 568960783  1195 QIRGAELEYESLKRQELESENKKLKNELNELRKALSE 1231
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

903-1449

6.22e-13

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 6.22e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   903 RELKKLKIEARSVERYKKLHIgMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQ-LSEEEAKVA 981
Cdd:TIGR02169  214 QALLKEKREYEGYELLKEKEA-LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRV 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   982 TGRVLSLQEEIAKLRKDLEqtrsEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNhriVEQAKEMTETMERKLV 1061
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIA----EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER---KRRDKLTEEYAELKEE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1062 EETKQLELDLNDERLRyqNLLNEFSRLEERYDDLKEEMtlmlnvpkpghkrtdsthssNESEYTFSSEFAETEDIAPRTE 1141
Cdd:TIGR02169  366 LEDLRAELEEVDKEFA--ETRDELKDYREKLEKLKREI--------------------NELKRELDRLQEELQRLSEELA 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1142 EpIEKKVPldmslflKLQKRVTELEQEKQLMQDELDRKEEQVFRSKA-KEEERPQIRGAELEYeslkrQELESENKKLKN 1220
Cdd:TIGR02169  424 D-LNAAIA-------GIEAKINELEEEKEDKALEIKKQEWKLEQLAAdLSKYEQELYDLKEEY-----DRVEKELSKLQR 490

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1221 ELNEL---RKALSE-----KSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ----- 1281
Cdd:TIGR02169  491 ELAEAeaqARASEErvrggRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVvveddaVAKEAIEllkrr 570

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1282 --------PKNTMTDSTILLE------------DVQKMKDKGEIAQAYIgLKETNRSSTMD--------YQELNEDGELw 1333
Cdd:TIGR02169  571 kagratflPLNKMRDERRDLSilsedgvigfavDLVEFDPKYEPAFKYV-FGDTLVVEDIEaarrlmgkYRMVTLEGEL- 648

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1334 mvYE--GLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRltnenlD 1411
Cdd:TIGR02169  649 --FEksGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG------E 720

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 568960783  1412 LMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENIS 1449
Cdd:TIGR02169  721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758

PRK03918

DNA double-strand break repair ATPase Rad50;

942-1441

1.72e-11

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 1.72e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  942 DYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKqETD 1021
Cdd:PRK03918  159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1022 QLVSNLKEENTLLKQEKETLNHRIVEqakemTETMERKLVEETKQLEldlndERLRYqnlLNEFSRLEERYDDLKEEMTL 1101
Cdd:PRK03918  238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKEIEELE-----EKVKE---LKELKEKAEEYIKLSEFYEE 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1102 MLNVPKPGHKRTDSTHSSNESeytFSSEFAETEDIAPRTEEPIEKKVpldmslflKLQKRVTELEQEKQLMQDELDRKEE 1181
Cdd:PRK03918  305 YLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLK--------ELEKRLEELEERHELYEEAKAKKEE 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1182 QVFRSKAKEEERPQIRGAELEYESLKRQELESENKK-------LKNELNELRKALSEKSAPEVTAP--GAPA----YRVL 1248
Cdd:PRK03918  374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKitarigeLKKEIKELKKAIEELKKAKGKCPvcGRELteehRKEL 453

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1249 MEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkntmtdstILLEDVQKMKDKGEIAQAYIGLKEtnRSSTMDYQELNE 1328
Cdd:PRK03918  454 LEEYTAELKRIEKELKEIEEKERKLRKELRELE---------KVLKKESELIKLKELAEQLKELEE--KLKKYNLEELEK 522

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1329 DGELwmvYEGLKQANRLLESQLQSQKRS------HENEAEALRGEIQSLKEEN---NRQQQLLAQNLQLPPEARIEA--S 1397
Cdd:PRK03918  523 KAEE---YEKLKEKLIKLKGEIKSLKKElekleeLKKKLAELEKKLDELEEELaelLKELEELGFESVEELEERLKEleP 599

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 568960783 1398 LQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1441
Cdd:PRK03918  600 FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643

SMC_N

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

902-1492

1.53e-10

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: 66.53 E-value: 1.53e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   902 KRELKKLKIEARSVERYkklhigmenkimqLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSeeeakva 981
Cdd:pfam02463  196 KLQELKLKEQAKKALEY-------------YQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES------- 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   982 tgrvlslQEEIAKLRKDLEQTRSEKKSIEERADKyKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLV 1061
Cdd:pfam02463  256 -------SKQEIEKEEEKLAQVLKENKEEEKEKK-LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1062 EETKQLELdlndERLRYQNLLNEFSRLEERYDDLKEEMTLmlnvpkpghKRTDSTHSSNESEYTFSSEFAETEDIAPRTE 1141
Cdd:pfam02463  328 KELKKEKE----EIEELEKELKELEIKREAEEEEEEELEK---------LQEKLEQLEEELLAKKKLESERLSSAAKLKE 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1142 EPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVfRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNE 1221
Cdd:pfam02463  395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE-ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1222 LNELRKALseksapevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQKMKD 1301
Cdd:pfam02463  474 LKETQLVK--------------------LQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1302 KGEIAQAYIGLKETN------RSSTMDYQELNEDGELWMVYEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEEN 1375
Cdd:pfam02463  534 LGVAVENYKVAISTAvivevsATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATL 613

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1376 NRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIID 1455
Cdd:pfam02463  614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693

                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 568960783  1456 EPIRPVNIPRKEKDFQGMLEYKREDEQKLVKNLILEL 1492
Cdd:pfam02463  694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEA 730

SMC_prok_B

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

897-1486

3.47e-10

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 3.47e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   897 RRMMAKRELKKLKIEARSVERYKKLHigmENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEE 976
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEEL---ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   977 EAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETM 1056
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1057 ERKL------VEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM-TLMLNVPK-PGHKRTDSTHSSNESEYTFSS 1128
Cdd:TIGR02168  460 EEALeelreeLEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkALLKNQSGlSGILGVLSELISVDEGYEAAI 539

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1129 E----------------------------------FAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTE---------- 1164
Cdd:TIGR02168  540 EaalggrlqavvvenlnaakkaiaflkqnelgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkals 619

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1165 ---------------LEQEKQL--------MQDELDRKEEQVFRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNE 1221
Cdd:TIGR02168  620 yllggvlvvddldnaLELAKKLrpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1222 LNELRKALSEksapevtapgapaYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQKMKD 1301
Cdd:TIGR02168  700 LAELRKELEE-------------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1302 KGEIAQAYIGLKETNRSStmdyQELNEDgelwmvYEGLKQANRLLESQLQSQkrshENEAEALRGEIQSLKEENNRQQQL 1381
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEI----EELEAQ------IEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERR 832

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1382 LAQNlqlppEARIEAsLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRpv 1461
Cdd:TIGR02168  833 IAAT-----ERRLED-LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR-- 904

                          650       660
                   ....*....|....*....|....*
gi 568960783  1462 nipRKEKDFQGMLEYKREDEQKLVK 1486
Cdd:TIGR02168  905 ---ELESKRSELRRELEELREKLAQ 926

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

896-1439

3.67e-10

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: 65.15 E-value: 3.67e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   896 FRRMMAKRELKKLKIEarsverYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQL-- 973
Cdd:pfam05557    9 ARLSQLQNEKKQMELE------HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLkk 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   974 ----------SEEEAKVATGR--VLSLQEEIAKLRK-------DLEQTRSEKKSIEERADKYK---QETDQLVSNLKEEN 1031
Cdd:pfam05557   83 kylealnkklNEKESQLADARevISCLKNELSELRRqiqraelELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQ 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1032 TLLK---QEKETLNHRIVEQA--KEMTETMERKLVEETkqlELDLNDERLRYQN-LLNEFSR----LEERYDDLKEEMtl 1101
Cdd:pfam05557  163 SSLAeaeQRIKELEFEIQSQEqdSEIVKNSKSELARIP---ELEKELERLREHNkHLNENIEnkllLKEEVEDLKRKL-- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1102 mlnvpkpghkrtdsthssnESEYTFSSEFAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEE 1181
Cdd:pfam05557  238 -------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEE 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1182 Q-VFRSKAKEEERPQirgAELEYE-SLKRQELESENKKLKNELNELR----------------KALSEKSAPEVTAPGA- 1242
Cdd:pfam05557  299 NsSLTSSARQLEKAR---RELEQElAQYLKKIEDLNKKLKRHKALVRrlqrrvllltkerdgyRAILESYDKELTMSNYs 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1243 PAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTI-LLEDVQKMKDKGEIAQAYIGLKETNRSSTM 1321
Cdd:pfam05557  376 PQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELqALRQQESLADPSYSKEEVDSLRRKLETLEL 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1322 DYQEL---NEDGELWMVYEGLKQANRLLES---QLQSQ-----KRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPP 1390
Cdd:pfam05557  456 ERQRLreqKNELEMELERRCLQGDYDPKKTkvlHLSMNpaaeaYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPE 535

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 568960783  1391 EARIEASlqheitrltNENLDLMEQLEKQDKTVRKLKkqlKVFAKKIGE 1439
Cdd:pfam05557  536 TTSTMNF---------KEVLDLRKELESAELKNQRLK---EVFQAKIQE 572

Mplasa_alph_rch

TIGR04523

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

917-1488

9.32e-10

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.89 E-value: 9.32e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   917 RYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLR 996
Cdd:TIGR04523   23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   997 KDLEQTRSEKKSIEERADKYKQEtdqlVSNLKEEntlLKQEKETLNhriveqakemtetmerKLVEETKQLELDLNDERL 1076
Cdd:TIGR04523  103 SDLSKINSEIKNDKEQKNKLEVE----LNKLEKQ---KKENKKNID----------------KFLTEIKKKEKELEKLNN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1077 RYQNLLNEFSRLEERYDDLKEEMTlmlnvpKPGHKRTDSTHSSNESEYTFSSEFAETEDIAPRTEEPIEKKvpldmSLFL 1156
Cdd:TIGR04523  160 KYNDLKKQKEELENELNLLEKEKL------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK-----KQNN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1157 KLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEE---RPQIRGAELEYESLKRQELESENKKLKNELNELRKalsEKS 1233
Cdd:TIGR04523  229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKE 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1234 ApevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAI--------QPKNTMTDSTilLEDVQKMKDKGEI 1305
Cdd:TIGR04523  306 Q---------------DWNKELKSELKNQEKKLEEIQNQISQNNKIIsqlneqisQLKKELTNSE--SENSEKQRELEEK 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1306 AQAYIGLKETNRSSTMDYQEL-NEDGELWMVYEGLKQANRLLESQLQSQkrshENEAEALRGEIQSLKEENNrqqqllaq 1384
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLeSQINDLESKIQNQEKLNQQKDEQIKKL----QQEKELLEKEIERLKETII-------- 436

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1385 nlqlppearieaSLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISpgqiidepirpvNIP 1464
Cdd:TIGR04523  437 ------------KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK------------ELK 492

                          570       580
                   ....*....|....*....|....
gi 568960783  1465 RKEKDFQGMLEYKREDEQKlVKNL 1488
Cdd:TIGR04523  493 SKEKELKKLNEEKKELEEK-VKDL 515

SMC_N

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

900-1232

9.95e-10

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 63.84 E-value: 9.95e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   900 MAKRELKKLKIEARSVERYKKLHIGMEN-KIMQLQRKVDEQNKDYKCLMEKLTNLEGVYN-SETEKLRNDVERLQLSEEE 977
Cdd:pfam02463  694 ILRRQLEIKKKEQREKEELKKLKLEAEElLADRVQEAQDKINEELKLLKQKIDEEEEEEEkSRLKKEEKEEEKSELSLKE 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   978 AKvatgrvlsLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSN--LKEENTLLKQEKETLNHRIVEQAKEMTET 1055
Cdd:pfam02463  774 KE--------LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAelLEEEQLLIEQEEKIKEEELEELALELKEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1056 MERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMLNvpkpghKRTDSTHSSNESEYTFSSEFAETED 1135
Cdd:pfam02463  846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK------EKEEKKELEEESQKLNLLEEKENEI 919

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1136 IAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQvfrsKAKEEERPQIRGAELEYESLK--RQELES 1213
Cdd:pfam02463  920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLL----LAKEELGKVNLMAIEEFEEKEerYNKDEL 995

                          330
                   ....*....|....*....
gi 568960783  1214 ENKKLKNELNELRKALSEK 1232
Cdd:pfam02463  996 EKERLEEEKKKLIRAIIEE 1014

Mplasa_alph_rch

TIGR04523

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

926-1441

2.26e-09

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.35 E-value: 2.26e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSE 1005
Cdd:TIGR04523  123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1006 KKSIEERADKYKQETDQLvSNLKEENTLLKQEKETLNHRIVEQAKEMTETMER--KLVEETKQLELDLNDERLRYQNLLN 1083
Cdd:TIGR04523  203 LSNLKKKIQKNKSLESQI-SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKKQLSEKQKELEQNNK 281

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1084 EFSRLEERYDDLKEEMTLMLNVPKPG-HKRTDSTHSSNESEYT-FSSEFAETEDIAPRTEEPIEKkvpldmslflkLQKR 1161
Cdd:TIGR04523  282 KIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEeIQNQISQNNKIISQLNEQISQ-----------LKKE 350

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1162 VTELEQEKQLMQDELDRKEEQVfrskakeeerpqirgaeleyESLKR--QELESENKKLKNELNELRKALSEKSAPEvta 1239
Cdd:TIGR04523  351 LTNSESENSEKQRELEEKQNEI--------------------EKLKKenQSYKQEIKNLESQINDLESKIQNQEKLN--- 407

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1240 pgapayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP-KNTMTDSTILLEDVQKMKD---------KGEIAQAY 1309
Cdd:TIGR04523  408 ------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDlTNQDSVKELIIKNLDNTREsletqlkvlSRSINKIK 481

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1310 IGLKETNRSSTMDYQEL----NEDGELWMVYEGLKQANRLLES---QLQSQKRSHENEAEALRGEIQSLKEENNRQQQLL 1382
Cdd:TIGR04523  482 QNLEQKQKELKSKEKELkklnEEKKELEEKVKDLTKKISSLKEkieKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568960783  1383 AQNLQlppEARIEaSLQHEITRLTNEN--------------LDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1441
Cdd:TIGR04523  562 EIDEK---NKEIE-ELKQTQKSLKKKQeekqelidqkekekKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630

PTZ00121

MAEBL; Provisional

904-1377

4.63e-09

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 4.63e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  904 ELKKLKIEARSVERYKKlHIGMENKIMQLQRKVDEQNK--DYKCLMEKLTNLEGVYNSETEKLRndVERLQLSEEEAKVA 981
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKA 1485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  982 TgRVLSLQEEIAKLRKDLEQTRSEKKSIEE--RADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERK 1059
Cdd:PTZ00121 1486 D-EAKKKAEEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1060 LVEETKQLELDLNDERLRYQNLLN-EFSRLEERYDDLKEEmtlmlnvpkpghKRTDSTHSSNESEYTFSSEfaetediAP 1138
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEE------------KKMKAEEAKKAEEAKIKAE-------EL 1625

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1139 RTEEPIEKKVPLDMSLFLKLQKRVTEL---EQEKQLMQDELDRKEEQvfRSKAKEEERPQIRGAELEYESLKRQELESEN 1215
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEE--DKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1216 KK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELdvRKEEVLILRSQLVSQKEAIQPKNTMTDSTILL 1293
Cdd:PTZ00121 1704 AEelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1294 EDVQKMKDKGEIAQAYIGLKETnRSSTMDYQELNEDGELwmVYEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKE 1373
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDI-FDNFANIIEGGKEGNL--VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNN 1858


                  ....
gi 568960783 1374 ENNR 1377
Cdd:PTZ00121 1859 ENGE 1862

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

896-1258

4.90e-09

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.29 E-value: 4.90e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   896 FRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSE 975
Cdd:pfam17380  293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAM 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   976 EEAKVATGRVLSL--QEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHrivEQAKEMT 1053
Cdd:pfam17380  373 EISRMRELERLQMerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE---ERAREME 449

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1054 ETMERKLvEETKQLELDLNDERLRYQNLLnEFSRLEERYDDLKEEMTLMLNVPKPGHKRtdsthssneseytfssEFAET 1133
Cdd:pfam17380  450 RVRLEEQ-ERQQQVERLRQQEEERKRKKL-ELEKEKRDRKRAEEQRRKILEKELEERKQ----------------AMIEE 511

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1134 EDIAPRTEEPIEKKvplDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKakeEERPQIRGAELEYEsLKRQELES 1213
Cdd:pfam17380  512 ERKRKLLEKEMEER---QKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT---EERSRLEAMERERE-MMRQIVES 584

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 568960783  1214 ENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEE 1258
Cdd:pfam17380  585 EKARAEYEATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSPE 629

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

902-1209

1.03e-08

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 1.03e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   902 KRELKKLKIEARS-VERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLE---GVYNSETEKLRNDVERLQ--LSE 975
Cdd:TIGR02169  697 LRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeiENVKSELKELEARIEELEedLHK 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   976 EEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERAdkykQETDQLVSNLKEENTLLKQEKETLNHRI---------V 1046
Cdd:TIGR02169  777 LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL----REIEQKLNRLTLEKEYLEKEIQELQEQRidlkeqiksI 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1047 EQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLK---EEMTLMLNVPKPGHKRTDSTHSsnese 1123
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkiEELEAQIEKKRKRLSELKAKLE----- 927

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1124 yTFSSEFAETEDIAPRTEEPIEKKVPLDmslflKLQKRVTELEQEKQLMQ-------DELDRKEEQVFRSKAK----EEE 1192
Cdd:TIGR02169  928 -ALEEELSEIEDPKGEDEEIPEEELSLE-----DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKraklEEE 1001

                          330
                   ....*....|....*..
gi 568960783  1193 RPQIRGAELEYESLKRQ 1209
Cdd:TIGR02169 1002 RKAILERIEEYEKKKRE 1018

SMC_prok_B

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

1009-1440

1.46e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 1.46e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1009 IEERA--DKYKQ---ETD-QLVS---NLKEENTLLKQEKETLNH--RIVEQAKEMtetmeRKLVEETKQLELDLnderlr 1077
Cdd:TIGR02168  161 FEEAAgiSKYKErrkETErKLERtreNLDRLEDILNELERQLKSleRQAEKAERY-----KELKAELRELELAL------ 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1078 yqnLLNEFSRLEERYDDLKEEMTLMlnvpkpGHKRTDSTHSSNESEytfsSEFAETEDIAPRTEEPIEKKVpldmSLFLK 1157
Cdd:TIGR02168  230 ---LVLRLEELREELEELQEELKEA------EEELEELTAELQELE----EKLEELRLEVSELEEEIEELQ----KELYA 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1158 LQKRVTELEQEKQLMQDELDRKEEQvfrSKAKEEERPQIRGAELEYESLKrQELESENKKLKNELNELRKALSEKSApev 1237
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQ---LEELEAQLEELESKLDELAEEL-AELEEKLEELKEELESLEAELEELEA--- 365

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1238 tapgapayrvLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkntmtdstillEDVQKMKDKGEIAQAYIGLKETNR 1317
Cdd:TIGR02168  366 ----------ELEELESRLEELEEQLETLRSKVAQLELQIASLN------------NEIERLEARLERLEDRRERLQQEI 423

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1318 SSTMDYQELNEDGELWMVYEGLKQAnrllESQLQSQKRSHENEAEALRGEIQSLKEENNrqqqllaqnlqlpPEARIEAS 1397
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEE----LEELQEELERLEEALEELREELEEAEQALD-------------AAERELAQ 486

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 568960783  1398 LQHEITRLTnenlDLMEQLEKQDKTVRKLKKQLKVFAKKIGEL 1440
Cdd:TIGR02168  487 LQARLDSLE----RLQENLEGFSEGVKALLKNQSGLSGILGVL 525

PTZ00121

MAEBL; Provisional

904-1483

1.92e-08

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.92e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  904 ELKKLKiEARSVERYKKLHigMENKIMQLQRKVDEQNkdykclMEKLTNLEGVYNSE-----TEKLRNDVERLQLSEEEA 978
Cdd:PTZ00121 1192 ELRKAE-DARKAEAARKAE--EERKAEEARKAEDAKK------AEAVKKAEEAKKDAeeakkAEEERNNEEIRKFEEARM 1262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  979 KVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEentllKQEKETLNHRiVEQAKEMTETMER 1058
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-----AKKADEAKKK-AEEAKKKADAAKK 1336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1059 KLVEETKQLELDLNDERLRYQNLlnEFSRLEERYDDLK--EEMTLMLNVPKPGH--KRTDSTHSSNESEYTFSSEFAETE 1134
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEA--EAAEEKAEAAEKKkeEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAA 1414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1135 DIAPRTEE----PIEKKVPLDMSLFLKLQKRVTELEQ--EKQLMQDELDRKEEQVFRS---KAKEEERPQIRGAELEYES 1205
Cdd:PTZ00121 1415 AAKKKADEakkkAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKAdeaKKKAEEAKKADEAKKKAEE 1494

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1206 LKRQELESENK-KLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLilrSQLVSQKEAIQPKN 1284
Cdd:PTZ00121 1495 AKKKADEAKKAaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL---KKAEEKKKAEEAKK 1571

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1285 TMTDSTILLEDVQKMKdKGEIAQAYIGLKETNRSSTMDYQELNEDGELWMVYEGLKQANRLLESQLQSQKRSHEN--EAE 1362
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkKAE 1650

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1363 ALRGEIQSLK-----------------EENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKT--- 1422
Cdd:PTZ00121 1651 ELKKAEEENKikaaeeakkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnki 1730

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960783 1423 -VRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKREDEQK 1483
Cdd:PTZ00121 1731 kAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792

CCDC158

pfam15921

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

924-1442

2.74e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.36 E-value: 2.74e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   924 GMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAK-VATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam15921  282 GLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKrMYEDKIEELEKQLVLANSELTEA 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1003 RSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETlNHRIVEQAKEMTETMErklveetkQLELDLNDERLRYQnll 1082
Cdd:pfam15921  362 RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNSITID--------HLRRELDDRNMEVQ--- 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1083 nefsRLEERYDDLKEEMTLMLnvpkpgHKRTDSTHSSNESEYTFSSEFAETED----IAPRTEEPIEKKVPLDMS----- 1153
Cdd:pfam15921  430 ----RLEALLKAMKSECQGQM------ERQMAAIQGKNESLEKVSSLTAQLEStkemLRKVVEELTAKKMTLESSertvs 499

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1154 -LFLKLQKRVTELE---QEKQLMQDELDRKEEQVFRSKAKEEerpQIRGAELEYESLK-------------RQELES--- 1213
Cdd:pfam15921  500 dLTASLQEKERAIEatnAEITKLRSRVDLKLQELQHLKNEGD---HLRNVQTECEALKlqmaekdkvieilRQQIENmtq 576

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1214 --------------ENKKLKNELNELRKALSEksapevtapgapaYRVLMEQLTSVSEELDVRKEEVLILRSQLVsqkea 1279
Cdd:pfam15921  577 lvgqhgrtagamqvEKAQLEKEINDRRLELQE-------------FKILKDKKDAKIRELEARVSDLELEKVKLV----- 638

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1280 iqpkNTMTDSTILLEDVQKMKDKgeiaqayigLKETNRSSTMDYQELNEDgelwmvYEGLKQANR-------LLESQLQS 1352
Cdd:pfam15921  639 ----NAGSERLRAVKDIKQERDQ---------LLNEVKTSRNELNSLSED------YEVLKRNFRnkseemeTTTNKLKM 699

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1353 QKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEAR--IEAsLQHEITRL----TNENLDlmEQLEKQDKTvrKL 1426
Cdd:pfam15921  700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRgqIDA-LQSKIQFLeeamTNANKE--KHFLKEEKN--KL 774

                          570       580
                   ....*....|....*....|
gi 568960783  1427 KKQLKVFA----KKIGELEV 1442
Cdd:pfam15921  775 SQELSTVAteknKMAGELEV 794

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

904-1485

6.55e-08

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 6.55e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   904 ELKKLKIEARSVERYKKLHIGMENKIMQLQRKV------------------DEQNKD---------YKCLMEKLTNLEGV 956
Cdd:pfam05483   89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAiqelqfenekvslkleeeIQENKDlikennatrHLCNLLKETCARSA 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   957 -----YNSETEKLR-------NDVERLQLSEEEAKVATGRvlSLQEEIAKLRKDLEQTRS-EKKSIEERADKYKQETDQL 1023
Cdd:pfam05483  169 ektkkYEYEREETRqvymdlnNNIEKMILAFEELRVQAEN--ARLEMHFKLKEDHEKIQHlEEEYKKEINDKEKQVSLLL 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1024 VSNLKEENtllKQEKETLnhrIVEQAKEMTETMErklvEETKqleldLNDERLRyqnllnefsRLEERYDDLKEEMTLMl 1103
Cdd:pfam05483  247 IQITEKEN---KMKDLTF---LLEESRDKANQLE----EKTK-----LQDENLK---------ELIEKKDHLTKELEDI- 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1104 nvpKPGHKRTDSTHSSNESEYTFSSE--FAETEDIAPRTEEPIEKKVPLDMSlflklqkrVTELEQEKQLMQdELDRKEE 1181
Cdd:pfam05483  302 ---KMSLQRSMSTQKALEEDLQIATKtiCQLTEEKEAQMEELNKAKAAHSFV--------VTEFEATTCSLE-ELLRTEQ 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1182 QVFRskaKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSapevtapgapayRVLME--QLTSVSEEL 1259
Cdd:pfam05483  370 QRLE---KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE------------KLLDEkkQFEKIAEEL 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1260 DVRKEEVLIL---RSQLVSQKEaIQPKNTMTDSTILLEDVQKMKDKGEIAQayigLKETNRSSTMDYQELnEDGELW--- 1333
Cdd:pfam05483  435 KGKEQELIFLlqaREKEIHDLE-IQLTAIKTSEEHYLKEVEDLKTELEKEK----LKNIELTAHCDKLLL-ENKELTqea 508

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1334 --MVYE----------GLKQANRLLES--QLQSQKRSHENEAEALRGEIQSL---------KEENNRQQQLLAQNLQLPP 1390
Cdd:pfam05483  509 sdMTLElkkhqediinCKKQEERMLKQieNLEEKEMNLRDELESVREEFIQKgdevkckldKSEENARSIEYEVLKKEKQ 588

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1391 EARIEASLQHEITRLTNENLDLmEQLEKQDKTVRKL----KKQLKVFAKKIGELEvgqMENISPGQIIDEPIrpvniprk 1466
Cdd:pfam05483  589 MKILENKCNNLKKQIENKNKNI-EELHQENKALKKKgsaeNKQLNAYEIKVNKLE---LELASAKQKFEEII-------- 656

                          650
                   ....*....|....*....
gi 568960783  1467 eKDFQGMLEYKREDEQKLV 1485
Cdd:pfam05483  657 -DNYQKEIEDKKISEEKLL 674

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

929-1291

8.04e-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: 57.44 E-value: 8.04e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   929 IMQLQRKVDEQNKDYKclMEKLtnlegvynsETEKLRndverlQLSEEEAKvatgrvlslqeEIAKLRKDLEQTRSEKKS 1008
Cdd:pfam17380  277 IVQHQKAVSERQQQEK--FEKM---------EQERLR------QEKEEKAR-----------EVERRRKLEEAEKARQAE 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1009 IEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQakEMTETMERKLVEETKQLELDLNDERLRyQNLlnEFSRL 1088
Cdd:pfam17380  329 MDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQE--EIAMEISRMRELERLQMERQQKNERVR-QEL--EAARK 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1089 -----EERYDDLKEEMTLMLNVPKpghkrtdsthssneseytfSSEFAETEDIApRTEEPIEKKVpldmslflklqKRVT 1163
Cdd:pfam17380  404 vkileEERQRKIQQQKVEMEQIRA-------------------EQEEARQREVR-RLEEERAREM-----------ERVR 452

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1164 ELEQEKQ-----LMQDELDRKEEQVFRSKAK------EEERPQIrgAELEYESLKRQELESENKK--LKNELNELRKALS 1230
Cdd:pfam17380  453 LEEQERQqqverLRQQEEERKRKKLELEKEKrdrkraEEQRRKI--LEKELEERKQAMIEEERKRklLEKEMEERQKAIY 530

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1231 EKSAPEV------TAPGAPAYRVLMEQLTSVSEE---LDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTI 1291
Cdd:pfam17380  531 EEERRREaeeerrKQQEMEERRRIQEQMRKATEErsrLEAMEREREMMRQIVESEKARAEYEATTPITTI 600

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

928-1259

9.74e-08

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 9.74e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   928 KIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVatgrvlsLQEEIAKLRKDLEQTRSEKK 1007
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-------LEQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1008 SIEERADKYKQETDQLVSNLKEENTLLKQEKETLN--------HRIVEQAKEMTETME--RKLVEETKQLELDLNDERLR 1077
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearlshSRIPEIQAELSKLEEevSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1078 YQNLLNEFSRLEERYDDLKEEMtlmlnvpkpghkrtdsthssneseytfSSEFAETEDIAPRTEEpIEKKVPldmslflK 1157
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQI---------------------------KSIEKEIENLNGKKEE-LEEELE-------E 872

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1158 LQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEErpqirgAELEYEsLKRQELESENKKLKNELNELRKALSEKSAPEV 1237
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEE------LEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945

                          330       340
                   ....*....|....*....|..
gi 568960783  1238 TAPGAPAYRVLMEQLTSVSEEL 1259
Cdd:TIGR02169  946 IPEEELSLEDVQAELQRVEEEI 967

YhaN

COG4717

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

900-1281

1.09e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.09e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYN-----SETEKLRNDVERLQLS 974
Cdd:COG4717    68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPER 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  975 EEEAKVATGRVLSLQEEIAKLRKDLEQTRSEkksIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIvEQAKEMTE 1054
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-EEAQEELE 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1055 TMERKLVEETKQLELDLNDERLRYQN-----------LLNEFSRLEERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESE 1123
Cdd:COG4717   224 ELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1124 YTFSSEFAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERP--QIRGAEL 1201
Cdd:COG4717   304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVED 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1202 EYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:COG4717   384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

980-1228

2.88e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 2.88e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  980 VATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLnhRIVEQAKEMTETMERK 1059
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--RALEQELAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1060 LVEETKQLELDLNDERLRYQNLLNEFSRLEERyddlkEEMTLMLNvpkpghkrtdsthssneseytfSSEFAETEdiapR 1139
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLS----------------------PEDFLDAV----R 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1140 TEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVfrsKAKEEERPQIRGAELEYESLkRQELESENKKLK 1219
Cdd:COG4942   137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL---AELEEERAALEALKAERQKL-LARLEKELAELA 212


                  ....*....
gi 568960783 1220 NELNELRKA 1228
Cdd:COG4942   213 AELAELQQE 221

sbcc

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

926-1441

2.92e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.75 E-value: 2.92e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   926 ENKIMQLQRKVD---EQNKDYKCLMEKLTNLEGvyNSETEKLRNDVERLQLSeeeakVATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:TIGR00618  378 TQHIHTLQQQKTtltQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLA-----HAKKQQELQQRYAELCAAAITCT 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1003 RSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETlnHRIVEQAKEMTETMERKLVEETKQLELDLNDERL------ 1076
Cdd:TIGR00618  451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK--KAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltr 528

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1077 RYQNLLNEFSRLEERYDDLKEEMTLMLNvpkpgHKRTDSTH--SSNESEYTFSSEFAETEDIAPRTEEPIEKKVP-LDMS 1153
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLTSERK-----QRASLKEQmqEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlTEKL 603

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1154 LFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRGAELEYESLKRQELES-------ENKKLKNELNELR 1226
Cdd:TIGR00618  604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsirvlPKELLASRQLALQ 683

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1227 KALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEvliLRSQLVSQKEAIQPKN-TMTDSTILLEDVQKMKDKG-E 1304
Cdd:TIGR00618  684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE---IENASSSLGSDLAAREdALNQSLKELMHQARTVLKArT 760

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1305 IAQAYIGLKETNRSSTMD-YQELNEDGELWM-VYEGLKQANRLLESQLQSQKRSHENEAEAlrGEIQSLKEENNRQQQLl 1382
Cdd:TIGR00618  761 EAHFNNNEEVTAALQTGAeLSHLAAEIQFFNrLREEDTHLLKTLEAEIGQEIPSDEDILNL--QCETLVQEEEQFLSRL- 837

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960783  1383 aqnlqlppeaRIEASLQHEITRLT---NENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1441
Cdd:TIGR00618  838 ----------EEKSATLGEITHQLlkyEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD 889

Myo5p-like_CBD_Rasip1

cd15472

cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ...

1506-1785

4.16e-07

cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.

Pssm-ID: 271256 Cd Length: 366 Bit Score: 54.20 E-value: 4.16e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1506 PAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVL----KKRGD---------------------DFETVSFWLSNTCR 1560
Cdd:cd15472    25 PAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVwektKELAEkqpehqdpaslsllsiaelapDLQPLLFWMSNSIE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1561 FLHCLKQ----YSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmIVSGMLE-----HET 1631
Cdd:cd15472   105 LLYFIQQkvplYEQSMEEELDVGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCVYYLTKTLYV-ALPALLDsnpftAEE 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1632 IQGVSG--VKPTGLRkRTSSIADEgtyTLDsILRQLnsfhsvmCQHgmdPELIKQVVKQMFYIVGAITLNNLLLRKDMCS 1709
Cdd:cd15472   184 RESWSGgsRLPEGVR-RVLEIYQA---TLD-LLRQY-------QVH---PEIASQMFAYLFFFSNASLFNQLMEKGSGGG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1710 ---WSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAE--AICSMCNALTTAQIVKVLNLYT 1784
Cdd:cd15472   249 ffqWSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQLLQMSwsSLRAEFPALNPAQLHHLLRQYQ 327


                  .
gi 568960783 1785 P 1785
Cdd:cd15472   328 L 328

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

953-1374

4.72e-07

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 4.72e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   953 LEGVYNSETEKLrndvERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEEnt 1032
Cdd:TIGR02169  665 GILFSRSEPAEL----QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER-- 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1033 lLKQEKETLnhRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLlnEFSRLEERYDDLKEEMTLMLNVPKPGHKR 1112
Cdd:TIGR02169  739 -LEELEEDL--SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEAR 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1113 TDSTHSSNESEyTFSSEFAETEdiaprteepIEKKVpldmSLFLKLQKRVTELEQEKQLMQDELDRKEEQVfrskakEEE 1192
Cdd:TIGR02169  814 LREIEQKLNRL-TLEKEYLEKE---------IQELQ----EQRIDLKEQIKSIEKEIENLNGKKEELEEEL------EEL 873

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1193 RPQIRGAELEYESLKRQ--ELESENKKLKNELNELRKALSEKsapevtapgapayRVLMEQLTSVSEELDVRKEEVLILR 1270
Cdd:TIGR02169  874 EAALRDLESRLGDLKKErdELEAQLRELERKIEELEAQIEKK-------------RKRLSELKAKLEALEEELSEIEDPK 940

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1271 SQLVSQKEAIQPkntmtdstilLEDVQKMKDKgeIAQAYIGLKETNRSSTMDYQELnedgelwmvyeglkqANRLLEsqL 1350
Cdd:TIGR02169  941 GEDEEIPEEELS----------LEDVQAELQR--VEEEIRALEPVNMLAIQEYEEV---------------LKRLDE--L 991

                          410       420
                   ....*....|....*....|....
gi 568960783  1351 QSQKRSHENEAEALRGEIQSLKEE 1374
Cdd:TIGR02169  992 KEKRAKLEEERKAILERIEEYEKK 1015

SMC_N

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

901-1493

1.19e-06

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.82 E-value: 1.19e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   901 AKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDyKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKV 980
Cdd:pfam02463  349 IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKE 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   981 ATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKE-ENTLLKQEKETLNHRIVEQAKEMTETMERK 1059
Cdd:pfam02463  428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKEtQLVKLQEQLELLLSRQKLEERSQKESKARS 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1060 -------LVEETKQLELDLNDERL-RYQNLLNEFSRLEERYDDLkEEMTLMLNVPKPGHKR---TDSTHSSNESEYTFSS 1128
Cdd:pfam02463  508 glkvllaLIKDGVGGRIISAHGRLgDLGVAVENYKVAISTAVIV-EVSATADEVEERQKLVralTELPLGARKLRLLIPK 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1129 EFAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEqvfRSKAKEEERPQIRGAELEYESLKR 1208
Cdd:pfam02463  587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE---SAKAKESGLRKGVSLEEGLAEKSE 663

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1209 QELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQ-LTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMT 1287
Cdd:pfam02463  664 VKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQrEKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ 743

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1288 DSTILLEDVQKMKDKGEIAQAYIGLKETNRSSTMDYQELNE-DGELWMVYEGLKQANRLLESQLQSQKRSHE-NEAEALR 1365
Cdd:pfam02463  744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEkLKVEEEKEEKLKAQEEELRALEEELKEEAElLEEEQLL 823

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1366 GEIQSLK--EENNRQQQLLAQNLQLPPEARIEASLQHEITR---LTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIG-- 1438
Cdd:pfam02463  824 IEQEEKIkeEELEELALELKEEQKLEKLAEEELERLEEEITkeeLLQELLLKEEELEEQKLKDELESKEEKEKEEKKEle 903

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568960783  1439 -ELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKREDEQKLVKNLILELK 1493
Cdd:pfam02463  904 eESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE 959

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

972-1304

1.57e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.57e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  972 QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRI--VEQA 1049
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeLESL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1050 KEMTETMERKLVE---ETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM---LNVPKPGHKRTDSTHSSNESE 1123
Cdd:COG4372   107 QEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqeeLAALEQELQALSEAEAEQALD 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1124 YTFSSEFAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRGAELEY 1203
Cdd:COG4372   187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1204 ESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPK 1283
Cdd:COG4372   267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346

                         330       340
                  ....*....|....*....|.
gi 568960783 1284 NTMTDSTILLEDVQKMKDKGE 1304
Cdd:COG4372   347 LVGLLDNDVLELLSKGAEAGV 367

PRK12704

phosphodiesterase; Provisional

900-1066

1.96e-06

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.96e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  900 MAKRELKKLKIEARSVERYKKLHIgmENKIMQLQRKVDEQNKDYKclmEKLTNLEGVYNSETEKLRNDVERLQLSEEEAK 979
Cdd:PRK12704   39 EAKRILEEAKKEAEAIKKEALLEA--KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRKLELLEKREEELE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  980 VATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQE--TDQLVSNLKEEntlLKQEKETLNHRIVEQAKEMTETME 1057
Cdd:PRK12704  114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE---ARHEAAVLIKEIEEEAKEEADKKA 190


                  ....*....
gi 568960783 1058 RKLVEETKQ 1066
Cdd:PRK12704  191 KEILAQAIQ 199

SMC_N

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

984-1493

2.72e-06

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 2.72e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   984 RVLSLQ--EEIAKLRKDLEQTRSE--------KKSIEERADKYKQETDQLVSNLKEENTLLKQEKetlnhRIVEQAKEMT 1053
Cdd:pfam02463  136 NFLVQGgkIEIIAMMKPERRLEIEeeaagsrlKRKKKEALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKAL 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1054 ETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEErydDLKEEMTLMLNVPKPGHKRTDSTHSSNESEytfSSEFAET 1133
Cdd:pfam02463  211 EYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR---DEQEEIESSKQEIEKEEEKLAQVLKENKEE---EKEKKLQ 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1134 EDIAPRTEEPIEKKVpldmSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQirgaELEYESLKRQELES 1213
Cdd:pfam02463  285 EEELKLLAKEEEELK----SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK----ELKELEIKREAEEE 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1214 ENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDS--TI 1291
Cdd:pfam02463  357 EEEELEKLQEKLEQLEEELLA---------KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEekKE 427

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1292 LLEDVQKMKDKGEIAQAYIGLKETNRSSTMDYQELNEDgelwmvyEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSL 1371
Cdd:pfam02463  428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-------ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQ 500

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1372 KEENNRQQQLLAQNLQLPPEARIEASLQHEITRL---------------TNENLDLMEQLEKQDKTVRKLKKQLKVFAKK 1436
Cdd:pfam02463  501 KESKARSGLKVLLALIKDGVGGRIISAHGRLGDLgvavenykvaistavIVEVSATADEVEERQKLVRALTELPLGARKL 580

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568960783  1437 IGELEVGQMENISpgqiiDEPIRPVNIPRKEKDFQGMLEYKREDEQKLVKNLILELK 1493
Cdd:pfam02463  581 RLLIPKLKLPLKS-----IAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632

PRK02224

DNA double-strand break repair Rad50 ATPase;

948-1374

2.77e-06

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 2.77e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  948 EKLTNLEGVyNSETEKLRNDV-----ERLQLSEEeAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQ 1022
Cdd:PRK02224  248 ERREELETL-EAEIEDLRETIaeterEREELAEE-VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1023 LVSNLKEENTLLKQ-------------EKETLNHRIVEQAKEMTETME------RKLVEETKQLELDLNDERLRYQNLLN 1083
Cdd:PRK02224  326 LRDRLEECRVAAQAhneeaeslredadDLEERAEELREEAAELESELEeareavEDRREEIEELEEEIEELRERFGDAPV 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1084 EFSRLEERYDDLKEEmtlmlnvpkpghkRTDSTHSSNESEYTFSSE---FAETEDI-----APRTEEPIEKKVPLDmslf 1155
Cdd:PRK02224  406 DLGNAEDFLEELREE-------------RDELREREAELEATLRTArerVEEAEALleagkCPECGQPVEGSPHVE---- 468

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1156 lklqkRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRGAELEYESL--KRQELESENKKLKNELNELRKALSE-- 1231
Cdd:PRK02224  469 -----TIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLeeRREDLEELIAERRETIEEKRERAEElr 543

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1232 KSAPEVTAPGAPAYrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQkmKDKGEIAQAYIG 1311
Cdd:PRK02224  544 ERAAELEAEAEEKR----EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAE--DEIERLREKREA 617

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568960783 1312 LKETNRSSTMDYQELNE-DGELwmvyEGLKQANRLleSQLQSQKRSHENEAEALRGEIQSLKEE 1374
Cdd:PRK02224  618 LAELNDERRERLAEKRErKREL----EAEFDEARI--EEAREDKERAEEYLEQVEEKLDELREE 675

Motor_domain

cd01363

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

639-663

3.10e-06

Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 49.27 E-value: 3.10e-06

                          10        20
                  ....*....|....*....|....*
gi 568960783  639 FRNSLHLLMETLNATTPHYVRCIKP 663
Cdd:cd01363   146 INESLNTLMNVLRATRPHFVRCISP 170

PTZ00121

MAEBL; Provisional

911-1483

3.41e-06

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.41e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  911 EARSVERYKKLHigmENKIMQLQRKVDEQNKdykclMEKLTNLEGVYNSETEKLRNDVER---LQLSEEEAKVATGRVLS 987
Cdd:PTZ00121 1138 DARKAEEARKAE---DAKRVEIARKAEDARK-----AEEARKAEDAKKAEAARKAEEVRKaeeLRKAEDARKAEAARKAE 1209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  988 LQEEIAKLRKDLEQTRSEKKSIEERADKyKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTEtmERKLVEETKQL 1067
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEAKK-DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE--EARKADELKKA 1286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1068 ELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESEYTFSSEFAETEDIAPRTEEPIEKK 1147
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1148 vpldmslflKLQKRVTELEQEKqlmQDELDRKEEQVFRSK--AKEEERPQIRGAELEYESLKRQELESENKKL--KNELN 1223
Cdd:PTZ00121 1367 ---------EAAEKKKEEAKKK---ADAAKKKAEEKKKADeaKKKAEEDKKKADELKKAAAAKKKADEAKKKAeeKKKAD 1434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1224 ELRKALSEKSAPEVTAPGAPAYRVlMEQLTSVSEEldVRKEEVLILRSQlvSQKEAIQPKNTMTDSTILLEDVQKMKDKG 1303
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKK-AEEAKKKAEE--AKKADEAKKKAE--EAKKADEAKKKAEEAKKKADEAKKAAEAK 1509

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1304 EIAQAYIGLKETNRSSTMDYQELNEDGELWMVYEGLKQANRLlesqlqsQKRSHENEAEALRGEIQSLKEENNRQQQLLA 1383
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL-------KKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1384 QNLQLPPE-ARIEA--SLQHEITRLTNENLDLMEQLEKQDKTVRK---LKKQLKVFAKKIGElEVGQMENISPGQiIDEP 1457
Cdd:PTZ00121 1583 AEEAKKAEeARIEEvmKLYEEEKKMKAEEAKKAEEAKIKAEELKKaeeEKKKVEQLKKKEAE-EKKKAEELKKAE-EENK 1660

                         570       580
                  ....*....|....*....|....*..
gi 568960783 1458 IRPVNIPRK-EKDFQGMLEYKREDEQK 1483
Cdd:PTZ00121 1661 IKAAEEAKKaEEDKKKAEEAKKAEEDE 1687

fMyo4p_CBD

cd15479

cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin ...

1665-1793

3.71e-06

cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum).

Pssm-ID: 271263 Cd Length: 329 Bit Score: 51.13 E-value: 3.71e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1665 LNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKnlmNSGAKETLEPL 1744
Cdd:cd15479   168 LNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPALNWKYGYEVDRNIERLVSWFEPR---IEDVRPNLIQI 244

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783 1745 IQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERV 1793
Cdd:cd15479   245 IQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAILLKYKPANKGEAGV 293

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

813-835

6.20e-06

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

Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 44.24 E-value: 6.20e-06

                            10        20
                    ....*....|....*....|...
gi 568960783    813 RRTKAATTIQKYWRMYVVRRRYK 835
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23

CCDC158

pfam15921

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

896-1435

6.58e-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: 51.27 E-value: 6.58e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   896 FRRMMAKRELKKLKIEAR----SVERYKKLHIGMEN--KIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVE 969
Cdd:pfam15921  609 FKILKDKKDAKIRELEARvsdlELEKVKLVNAGSERlrAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   970 RLQLSEEEAKVatgrvlslqeEIAKLRKDLEQTRSEKKSIEErADKYKQetdQLVSNLKEENTLLKQEKETLNHRIVEQA 1049
Cdd:pfam15921  689 EMETTTNKLKM----------QLKSAQSELEQTRNTLKSMEG-SDGHAM---KVAMGMQKQITAKRGQIDALQSKIQFLE 754

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1050 KEMTETMERK--LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM-LNVPKPghkrtdsthssneseytf 1126
Cdd:pfam15921  755 EAMTNANKEKhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMeVALDKA------------------ 816

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1127 SSEFAETEDIAPRTEEPiekkvpldmSLFLKLQKR--VTELEQEKQLMQDELDRKEEQVFRSKAKEEERP--QIRGAELE 1202
Cdd:pfam15921  817 SLQFAECQDIIQRQEQE---------SVRLKLQHTldVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPssQSTASFLS 887

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1203 YESLKRQEL-ESENKKLKNELNELRKALSEKSAPEVT-APG---APAYRVLMEQLTSVSEELDVRKEevLILRSQLVSQK 1277
Cdd:pfam15921  888 HHSRKTNALkEDPTRDLKQLLQELRSVINEEPTVQLSkAEDkgrAPSLGALDDRVRDCIIESSLRSD--ICHSSSNSLQT 965

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1278 EAIQPKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRSSTMDYQELNEDGELWMVYEGLKQANRLLESQLQSQKRSH 1357
Cdd:pfam15921  966 EGSKSSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIGSSSQYRSAKTIH 1045

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960783  1358 ENEAEAlrgEIQSLKEENNRQQQLLAqnlqlppEARIEaSLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAK 1435
Cdd:pfam15921 1046 SPDSVK---DSQSLPIETTGKTCRKL-------QNRLE-SLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQEKMLLK 1112

Caldesmon

pfam02029

Caldesmon;

959-1232

8.61e-06

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.64 E-value: 8.61e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   959 SETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQET-----------DQLVSNL 1027
Cdd:pfam02029   50 LKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEEnsswekeekrdSRLGRYK 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1028 KEENTLL-KQEKETLNHRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEfsrLEERYDDLK---------- 1096
Cdd:pfam02029  130 EEETEIReKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE---KKVKYESKVfldqkrghpe 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1097 ------EEMTLMLNVPkpgHKRTDSTHSSNESEYTFSSEFAETEDiapRTEEPIEKKVPLDMSLFLKL----QKRVTELE 1166
Cdd:pfam02029  207 vksqngEEEVTKLKVT---TKRRQGGLSQSQEREEEAEVFLEAEQ---KLEELRRRRQEKESEEFEKLrqkqQEAELELE 280

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960783  1167 qekqlmqdELDRKEEQvfRSKAKEEERPQiRGAEleyESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:pfam02029  281 --------ELKKKREE--RRKLLEEEEQR-RKQE---EAERKLREEEEKRRMKEEIERRRAEAAEK 332

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

926-1098

1.00e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.00e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDL-EQTRS 1004
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1005 EKK---------------SIEE---RADKYKQETDQ---LVSNLKEENTLLKQEKETLnhrivEQAKEMTETMERKLVEE 1063
Cdd:COG3883    95 LYRsggsvsyldvllgseSFSDfldRLSALSKIADAdadLLEELKADKAELEAKKAEL-----EAKLAELEALKAELEAA 169

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568960783 1064 TKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG3883   170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

971-1099

1.11e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.11e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  971 LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQ-- 1048
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyr 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960783 1049 -------------AKEMTETMER------------KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:COG3883    98 sggsvsyldvllgSESFSDFLDRlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173

COG2433

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

1131-1270

1.29e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.24 E-value: 1.29e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1131 AETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFR-----SKAKEEERPQIRgAELEYES 1205
Cdd:COG2433   391 PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERlerelSEARSEERREIR-KDREISR 469

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568960783 1206 LKR--QELESENKKLKNELNELR------KALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILR 1270
Cdd:COG2433   470 LDReiERLERELEEERERIEELKrklerlKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKEGDVVYLR 542

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

926-1104

1.88e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.88e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSE 1005
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1006 kksIEERADK-YKQ-ETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLvEETKQLELDLNDERLRYQNLLN 1083
Cdd:COG4942   106 ---LAELLRAlYRLgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-AELAALRAELEAERAELEALLA 181

                         170       180
                  ....*....|....*....|.
gi 568960783 1084 EFSRLEERYDDLKEEMTLMLN 1104
Cdd:COG4942   182 ELEEERAALEALKAERQKLLA 202

sbcc

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

901-1440

1.88e-05

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 1.88e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   901 AKRELKKLKIEARSVE--------RYKKLHIGMENK-IMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSeTEKLRNDVERL 971
Cdd:TIGR00618  265 LRARIEELRAQEAVLEetqerinrARKAAPLAAHIKaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA-HVKQQSSIEEQ 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   972 QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERAdkykqetdQLVSNLKEENTLLKQEKETLNHrivEQAKE 1051
Cdd:TIGR00618  344 RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ--------QQKTTLTQKLQSLCKELDILQR---EQATI 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1052 MTETMER-----KLVEETKQLELDLNDERLR-------YQNLLNEFSRLEERYDDLKEEMTLMLNVpKPGHKRTDSTHSS 1119
Cdd:TIGR00618  413 DTRTSAFrdlqgQLAHAKKQQELQQRYAELCaaaitctAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAV 491

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1120 NESeytFSSEFAETE-DIAPRTEEPIEKKV-----PLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEER 1193
Cdd:TIGR00618  492 VLA---RLLELQEEPcPLCGSCIHPNPARQdidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEI 568

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1194 PQirgaELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGApaYRVLMEQLTSVSEELDVRKEEVLILRSQ- 1272
Cdd:TIGR00618  569 QQ----SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE--QHALLRKLQPEQDLQDVRLHLQQCSQELa 642

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1273 ------------LVSQKEAIQPKNTMTDSTILLEDVQKMKDK--GEIAQAYIGLKETNRSSTMDYQELNEDGELWMVY-- 1336
Cdd:TIGR00618  643 lkltalhalqltLTQERVREHALSIRVLPKELLASRQLALQKmqSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFne 722

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1337 --------------------EGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEA 1396
Cdd:TIGR00618  723 ienassslgsdlaaredalnQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK 802

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 568960783  1397 SLQHEITRLTNENLDLME-QLEKQDKTVRKLKKQLKVFAKKIGEL 1440
Cdd:TIGR00618  803 TLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEI 847

GumC

COG3206

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

1208-1460

3.48e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.48e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1208 RQELESENKKLKNELNELRKALSE-KSAPEVTAPGAPAyRVLMEQLTSVSEELdvrkEEVLILRSQLVSQKEAIQPKNTM 1286
Cdd:COG3206   177 LEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEA-KLLLQQLSELESQL----AEARAELAEAEARLAALRAQLGS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1287 TDSTI--LLEDVQKMKDKGEIAQAYIGLKETNRSSTM---DYQELNEDgelwmvyegLKQANRLLESQLQSQKRSHENEA 1361
Cdd:COG3206   252 GPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQ---------IAALRAQLQQEAQRILASLEAEL 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1362 EALRGEIQSLKEENNRQQQllaqnlqlppEARIEASLQHEITRLTNEnldlmeqlekqdktVRKLKKQLKVFAKKIGELE 1441
Cdd:COG3206   323 EALQAREASLQAQLAQLEA----------RLAELPELEAELRRLERE--------------VEVARELYESLLQRLEEAR 378

                         250
                  ....*....|....*....
gi 568960783 1442 VGQMENISPGQIIDEPIRP 1460
Cdd:COG3206   379 LAEALTVGNVRVIDPAVVP 397

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

906-1439

3.48e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 3.48e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   906 KKLKIEARSVE-RYKKlhigMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNdVERLQLsEEEAKVATGR 984
Cdd:pfam01576  120 QKLQLEKVTTEaKIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKN-KHEAMISDLE 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   985 VLSLQEEiaKLRKDLEQTRseKKSIEERADKYKQ--ETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETME--RKL 1060
Cdd:pfam01576  194 ERLKKEE--KGRQELEKAK--RKLEGESTDLQEQiaELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKkiREL 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1061 VEETKQLELDLNDERLRYqnllnefSRLEERYDDLKEEMTLMlnvpkpghkRTdsthssnESEYTFSSEFAETEDIAPRT 1140
Cdd:pfam01576  270 EAQISELQEDLESERAAR-------NKAEKQRRDLGEELEAL---------KT-------ELEDTLDTTAAQQELRSKRE 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1141 EEPIEKKVPLDmSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAK--------EEERPQIRgAELEYESLKRQELE 1212
Cdd:pfam01576  327 QEVTELKKALE-EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANlekakqalESENAELQ-AELRTLQQAKQDSE 404

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1213 SENKKLKNELNELRKALSEksapevtapGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV-SQKEAIQPKNTMTDSTI 1291
Cdd:pfam01576  405 HKRKKLEGQLQELQARLSE---------SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIkLSKDVSSLESQLQDTQE 475

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1292 LL--EDVQKMKDKGEIAQAyiglkETNRSSTMDYQELNEDGElwmvyEGLKQANRLLESQLQSQKRSHENEAEALRGeiq 1369
Cdd:pfam01576  476 LLqeETRQKLNLSTRLRQL-----EDERNSLQEQLEEEEEAK-----RNVERQLSTLQAQLSDMKKKLEEDAGTLEA--- 542

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960783  1370 slKEENNRQQQLLAQNLQLPPEARIEA--SLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGE 1439
Cdd:pfam01576  543 --LEEGKKRLQRELEALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE 612

MyosinXI_CBD

cd15475

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

1530-1783

3.51e-05

cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle.

Pssm-ID: 271259 Cd Length: 326 Bit Score: 47.95 E-value: 3.51e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1530 LTSTINSIKKVlkkrGDDFETVSFWLSNTCRFLhCLKQysgeegfmkhntsrqneHCLTnfdlaeyrqvlsdlAIQIYQQ 1609
Cdd:cd15475    52 IIQTIGSAIED----QDNNDHLAYWLSNTSTLL-FLLQ-----------------RSLP--------------ALLFKQQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1610 LVRVLENILqPMI-------VSGMLEhETIQGVSGVKPTGLRKRTSSIADEGTYTL---DSILRQLNSFHSVMCQHGMDP 1679
Cdd:cd15475    96 LTAYVEKIY-GIIrdnlkkeLSPLLS-LCIQAPRTSRGSSSKSSSSANSLGQQSPSshwQSIIKSLNSLLSTLKENHVPP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1680 ELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDknlmnsgAKET--------LEPLIQAAQLL 1751
Cdd:cd15475   174 FLVQKIFTQVFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELELWCSQ-------ATEEyagsswdeLKHIRQAVGFL 246

                         250       260       270
                  ....*....|....*....|....*....|...
gi 568960783 1752 QVKKKTDDDAEAICS-MCNALTTAQIVKVLNLY 1783
Cdd:cd15475   247 VIHQKSRKSYDEITNdLCPVLSVQQLYRICTMY 279

CBD_MYO6-like

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...

780-837

3.53e-05

Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 45.58 E-value: 3.53e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960783  780 WLLRKRYLCMQRAAITVQRYVRgyqarcyaKFLRRTKAATTIQKYWRMYVVRRRYKIR 837
Cdd:cd21759    18 WLIRSRWRKAQWCALSVIKLKN--------KILYRREALIKIQKTVRGYLARKKHRPR 67

sbcc

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

904-1231

3.67e-05

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 3.67e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   904 ELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKlrNDVERLQLSEEEAKvatg 983
Cdd:TIGR00618  543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK--LSEAEDMLACEQHA---- 616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   984 RVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETdqlvsnlkeenTLLKQEKETLNHRIVEQAKEMTETMERKL-VE 1062
Cdd:TIGR00618  617 LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQL-----------TLTQERVREHALSIRVLPKELLASRQLALqKM 685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1063 ETKQLELDLNDERLRYQN-LLNEFSRLEERYDDLKEEMTLMLNVPKPGHKRTDST--HSSNESEYTFSSEFAETEDIAPR 1139
Cdd:TIGR00618  686 QSEKEQLTYWKEMLAQCQtLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlnQSLKELMHQARTVLKARTEAHFN 765

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1140 TEEpiekKVPLDMSLFLKLQKRVTELEQEKQLMQD---ELDRKEEQVfRSKAKEEErpQIRGAELEYESLKRQELESENK 1216
Cdd:TIGR00618  766 NNE----EVTAALQTGAELSHLAAEIQFFNRLREEdthLLKTLEAEI-GQEIPSDE--DILNLQCETLVQEEEQFLSRLE 838

                          330
                   ....*....|....*
gi 568960783  1217 KLKNELNELRKALSE 1231
Cdd:TIGR00618  839 EKSATLGEITHQLLK 853

sbcc

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

964-1430

3.77e-05

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 3.77e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   964 LRNDVERLQLSEEEAKVATGRVLSL----QEEIAKLRKDLEQTRSE--KKSIEERADKYKQETDQLVSNLKEENTLLKQE 1037
Cdd:TIGR00618  159 KAKSKEKKELLMNLFPLDQYTQLALmefaKKKSLHGKAELLTLRSQllTLCTPCMPDTYHERKQVLEKELKHLREALQQT 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1038 KETLNHRiveqakemteTMERKLVEETKQLELDLNDERLRYQNLLNEFSRLE---------------------------- 1089
Cdd:TIGR00618  239 QQSHAYL----------TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEetqerinrarkaaplaahikavtqieqq 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1090 --ERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESEYTFSSEFAETEDIAPRTEEPIEKKVPLDMSL-----FLKLQKRV 1162
Cdd:TIGR00618  309 aqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHtltqhIHTLQQQK 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1163 TELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRG----------AELEYESLKRQELESENKKLKNE---LNELRKAL 1229
Cdd:TIGR00618  389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGqlahakkqqeLQQRYAELCAAAITCTAQCEKLEkihLQESAQSL 468

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1230 SEKSAPEVTApgapayRVLMEQLTSVSEELDVRKEEVLILRSQLvsQKEAIQPKNTMTDSTIL---------LEDVQKMK 1300
Cdd:TIGR00618  469 KEREQQLQTK------EQIHLQETRKKAVVLARLLELQEEPCPL--CGSCIHPNPARQDIDNPgpltrrmqrGEQTYAQL 540

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1301 DKGEIAQAYIGLKETNRSSTMDYQELNEDGEL------WMVY----EGLKQANRLLESQLQSQKRSHENEAEALRGEIQS 1370
Cdd:TIGR00618  541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFsiltqcDNRSkediPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960783  1371 LKEENNRQQQLLAqnlqlppEARIEASLQHEITRLTNENLDLM-EQLEKQDKTVRKLKKQL 1430
Cdd:TIGR00618  621 LQPEQDLQDVRLH-------LQQCSQELALKLTALHALQLTLTqERVREHALSIRVLPKEL 674

HOOK

pfam05622

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...

998-1495

3.79e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.

Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.53 E-value: 3.79e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   998 DLEQTRSEKKSIEERAdkykQETDQLVSNLKEENTLLKQEKETLNHRI--VEQAKEMTETMERK----------LVEETK 1065
Cdd:pfam05622    1 DLSEAQEEKDELAQRC----HELDQQVSLLQEEKNSLQQENKKLQERLdqLESGDDSGTPGGKKylllqkqleqLQEENF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1066 QLELDLNDERLRYQNLLNEFSRLEERYDDLkeemtlmlnvpkpghkrtdstHSSNESEYTFSSE---FAETEDIAPRTEE 1142
Cdd:pfam05622   77 RLETARDDYRIKCEELEKEVLELQHRNEEL---------------------TSLAEEAQALKDEmdiLRESSDKVKKLEA 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1143 PIE--KKVPLDMSlflKLQKRVTELEQEKQL-MQDELDRKEEQVFRSKAK---EEERPQIRG--AELEYESLKRQELESE 1214
Cdd:pfam05622  136 TVEtyKKKLEDLG---DLRRQVKLLEERNAEyMQRTLQLEEELKKANALRgqlETYKRQVQElhGKLSEESKKADKLEFE 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1215 NKKLKNELNELRKalsEKsapevtapgapayrvlmEQLTSvseELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLE 1294
Cdd:pfam05622  213 YKKLEEKLEALQK---EK-----------------ERLII---ERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGD 269

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1295 DVQKMKDKGEIAQAYIGLKETNRSSTMDyQELNEDGELWMVYEGLKQANRLLEsQLQSQKRSHENEAEALRGEIQSLKee 1374
Cdd:pfam05622  270 NLAAEIMPAEIREKLIRLQHENKMLRLG-QEGSYRERLTELQQLLEDANRRKN-ELETQNRLANQRILELQQQVEELQ-- 345

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1375 nnrqqqllaqnlqlppEARIEASLQHEITRLTNENLD-LMEQLEKQDKTVRKLKKQLKvfakkigELEVGQMENisPGQI 1453
Cdd:pfam05622  346 ----------------KALQEQGSKAEDSSLLKQKLEeHLEKLHEAQSELQKKKEQIE-------ELEPKQDSN--LAQK 400

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 568960783  1454 IDEpiRPVNIPRKEKDFQGMLE-YKREDEQklVKNLILELKPR 1495
Cdd:pfam05622  401 IDE--LQEALRKKDEDMKAMEErYKKYVEK--AKSVIKTLDPK 439

SMC_prok_B

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

901-1099

4.63e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 4.63e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   901 AKRELKKLKIEARSV----ERYKKLHIGMENKIMQLQRKVDEQNKDYKCL---MEKLTNLEGVYNSETEKLRNDV----E 969
Cdd:TIGR02168  808 LRAELTLLNEEAANLrerlESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERasleE 887

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   970 RLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEketlnhriVEQA 1049
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE--------AEAL 959

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568960783  1050 KEMTETMERKLVEETKQLELDLNdeRLRYQNL--LNEFSRLEERYDDLKEEM 1099
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIK--ELGPVNLaaIEEYEELKERYDFLTAQK 1009

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

897-1234

6.24e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 6.24e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   897 RRMMAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVD---EQNKDYKCLME------KLTNLEGVYNSETEKLRND 967
Cdd:TIGR00606  320 ELVDCQRELEKLNKERRLLNQEKT---ELLVEQGRLQLQADrhqEHIRARDSLIQslatrlELDGFERGPFSERQIKNFH 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   968 VERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKK----SIEERADKYKQETDQLVSNLKEENTLLKQEKETL-- 1041
Cdd:TIGR00606  397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrTIELKKEILEKKQEELKFVIKELQQLEGSSDRILel 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1042 NHRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMLNVPKP---GHKRTDSTHS 1118
Cdd:TIGR00606  477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDkmdKDEQIRKIKS 556

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1119 SNESEYTFSSEFAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKeeerpqirg 1198
Cdd:TIGR00606  557 RHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK--------- 627

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 568960783  1199 aelEYESLKRQELESENKKLKNELNELRKALSEKSA 1234
Cdd:TIGR00606  628 ---LFDVCGSQDEESDLERLKEEIEKSSKQRAMLAG 660

PRK02224

DNA double-strand break repair Rad50 ATPase;

899-1233

7.52e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 7.52e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  899 MMAKRELKKLKIEARSVERYKklhigMENKIMQLQRKVDEQ-------NKDYKCLMEKLTNLEgvynSETEKLRNDVERL 971
Cdd:PRK02224  298 LLAEAGLDDADAEAVEARREE-----LEDRDEELRDRLEECrvaaqahNEEAESLREDADDLE----ERAEELREEAAEL 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  972 QLSEEEAKVA----TGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETL--NHRI 1045
Cdd:PRK02224  369 ESELEEAREAvedrREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeAEAL 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1046 VEQAK---------------EMTETMER--KLVEETKQLELDLND-----ERL--------RYQNLLNEFSRLEERYDDL 1095
Cdd:PRK02224  449 LEAGKcpecgqpvegsphveTIEEDRERveELEAELEDLEEEVEEveerlERAedlveaedRIERLEERREDLEELIAER 528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1096 KEEMtlmlnvpkpgHKRTDSTHSSNESEYTFSSEFAETEDIAPRTEEPIEKKvpldmslflklQKRVTELEQEKQLMQDE 1175
Cdd:PRK02224  529 RETI----------EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA-----------REEVAELNSKLAELKER 587

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960783 1176 LDRKEEQVFRSKAKEEerpqirgaeleyeslKRQELESENKKLKN--ELNELRK-ALSEKS 1233
Cdd:PRK02224  588 IESLERIRTLLAAIAD---------------AEDEIERLREKREAlaELNDERReRLAEKR 633

pfam00612

IQ calmodulin-binding motif; Calmodulin-binding motif.

815-835

7.69e-05

IQ calmodulin-binding motif; Calmodulin-binding motif.

Pssm-ID: 459869 Cd Length: 21 Bit Score: 41.15 E-value: 7.69e-05

                           10        20
                   ....*....|....*....|.
gi 568960783   815 TKAATTIQKYWRMYVVRRRYK 835
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

925-1225

8.40e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 8.40e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRS 1004
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1005 EKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNH---RIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNL 1081
Cdd:COG4372   123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESlqeELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1082 LNEFSRLEERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESEYTFSSEFAETEDiaprTEEPIEKKVPLDMSLFLKLQKR 1161
Cdd:COG4372   203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI----LKEIEELELAILVEKDTEEEEL 278

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568960783 1162 VTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNELNEL 1225
Cdd:COG4372   279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

910-1219

9.52e-05

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 9.52e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   910 IEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKC-LMEKLTNLEGVYNSETEKLR---NDVERLQLSEEEAKVATGRV 985
Cdd:TIGR00606  185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKsyeNELDPLKNRLKEIEHNLSKI 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   986 LSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKET----LNHRIVEQAKEMTETMERKLV 1061
Cdd:TIGR00606  265 MKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERelvdCQRELEKLNKERRLLNQEKTE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1062 EETKQLELDLNDERLRYQNLLNEFSRLE----------ERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNeseytfSSEFA 1131
Cdd:TIGR00606  345 LLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldgfERGPFSERQIKNFHTLVIERQEDEAKTAAQL------CADLQ 418

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1132 ETEDIAPRTEEPIE-KKVPLDMSLFLK---LQKRVTELEQEKQLMQ------DELDRKEEQVFRSKA---KEEERPQIRG 1198
Cdd:TIGR00606  419 SKERLKQEQADEIRdEKKGLGRTIELKkeiLEKKQEELKFVIKELQqlegssDRILELDQELRKAERelsKAEKNSLTET 498

                          330       340
                   ....*....|....*....|.
gi 568960783  1199 AELEYESLKRQELESENKKLK 1219
Cdd:TIGR00606  499 LKKEVKSLQNEKADLDRKLRK 519

PRK03918

DNA double-strand break repair ATPase Rad50;

903-1231

1.18e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.18e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  903 RELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGV-------------------YNSETEK 963
Cdd:PRK03918  384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelleeYTAELKR 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  964 LRNDVERLQLSEEEAKVATGRV---LSLQEEIAKLRKDLEQTRS-------------EKKS-----IEERADKYKQETDQ 1022
Cdd:PRK03918  464 IEKELKEIEEKERKLRKELRELekvLKKESELIKLKELAEQLKEleeklkkynleelEKKAeeyekLKEKLIKLKGEIKS 543

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1023 LVSNLKEENtLLKQEKETLNHRIVEQAKEMTETMER----------KLVEETKQLE------LDLNDERLRYQNLLNEFS 1086
Cdd:PRK03918  544 LKKELEKLE-ELKKKLAELEKKLDELEEELAELLKEleelgfesveELEERLKELEpfyneyLELKDAEKELEREEKELK 622

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1087 RLEERYDDLKEEMTLMLNVPKPGHKRTdsthssNESEYTFSSEfaetediapRTEEPIEKKVPLDMSLFlKLQKRVTELE 1166
Cdd:PRK03918  623 KLEEELDKAFEELAETEKRLEELRKEL------EELEKKYSEE---------EYEELREEYLELSRELA-GLRAELEELE 686

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1167 QEKQLMQDELDRKEEQvfrskaKEEerpqIRGAELEYESLKR-----QELESENKKLKNELNElrKALSE 1231
Cdd:PRK03918  687 KRREEIKKTLEKLKEE------LEE----REKAKKELEKLEKalervEELREKVKKYKALLKE--RALSK 744

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

925-1447

1.37e-04

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.37e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   925 MENKIMQLQRKVD--EQNKD-YKCLMEKLTNLEGVYNSE------TEKLRNDVERLQlseEEAKVATGRVLSLQEEIAKL 995
Cdd:TIGR00606  589 TRDRLAKLNKELAslEQNKNhINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLK---EEIEKSSKQRAMLAGATAVY 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   996 RKDLEQTRSEKKS---IEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLVE--ETKQLELD 1070
Cdd:TIGR00606  666 SQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRqsIIDLKEKE 745

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1071 LNDERLRYQNLLNEFSRLEeryDDLKEEMTLMLNVpkpgHKRTDSTHSSNESEYTFSSEFAETEDIAPRTEEPIEKKVPL 1150
Cdd:TIGR00606  746 IPELRNKLQKVNRDIQRLK---NDIEEQETLLGTI----MPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS 818

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1151 DmslflkLQKRVTELEQEKQLMQDELDRKEEQV-FRSKAKEEERPQIrgaeleyeslkrQELESENKKLKNELNELRKAL 1229
Cdd:TIGR00606  819 D------LDRTVQQVNQEKQEKQHELDTVVSKIeLNRKLIQDQQEQI------------QHLKSKTNELKSEKLQIGTNL 880

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1230 SEKSAPEvtapgapayrvlmeqltsvsEELDVRKEEVLILRSQLVSQKEAIQPKNTMtdstilLEDVQKMKDKgeiaqaY 1309
Cdd:TIGR00606  881 QRRQQFE--------------------EQLVELSTEVQSLIREIKDAKEQDSPLETF------LEKDQQEKEE------L 928

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1310 IGLKET-NRSSTMDYQELNEdgELWMVYEGLKQANRLLESQLQSQKRSHENEaeaLRGEIQSLKEENNRQQQLLAQNLQL 1388
Cdd:TIGR00606  929 ISSKETsNKKAQDKVNDIKE--KVKNIHGYMKDIENKIQDGKDDYLKQKETE---LNTVNAQLEECEKHQEKINEDMRLM 1003

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568960783  1389 ppeaRIEASLQHEITRLTNENLDLMeqleKQDKTVRKLKKQLKVFAKKIGELEVGQMEN 1447
Cdd:TIGR00606 1004 ----RQDIDTQKIQERWLQDNLTLR----KRENELKEVEEELKQHLKEMGQMQVLQMKQ 1054

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

925-1095

2.08e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.08e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEgvynSETEKLRNDVERLQlsEEEAKVATGRVL-SLQEEIAKLRKDLEQTR 1003
Cdd:COG1579    36 LEDELAALEARLEAAKTELEDLEKEIKRLE----LEIEEVEARIKKYE--EQLGNVRNNKEYeALQKEIESLKRRISDLE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1004 SEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEmtetmERKLVEETKQLELDLNDErlryqnLLN 1083
Cdd:COG1579   110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREELAAKIPPE------LLA 178

                         170
                  ....*....|..
gi 568960783 1084 EFSRLEERYDDL 1095
Cdd:COG1579   179 LYERIRKRKNGL 190

PRK02224

DNA double-strand break repair Rad50 ATPase;

977-1374

2.24e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.24e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  977 EAKVATGRVLS--------LQEEIA-KLRKDLEQT----RSEKKSIEERADKYKQETDQLVSNL-------------KEE 1030
Cdd:PRK02224  173 DARLGVERVLSdqrgsldqLKAQIEeKEEKDLHERlnglESELAELDEEIERYEEQREQARETRdeadevleeheerREE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1031 NTLLKQEKETLNHRIVEQAKEMTETMERklVEETKQLELDLNDER-----------LRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:PRK02224  253 LETLEAEIEDLRETIAETEREREELAEE--VRDLRERLEELEEERddllaeaglddADAEAVEARREELEDRDEELRDRL 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1100 TlmlnvpkpgHKRTDSTHSSNESEytfsSEFAETEDIAPRTEEPIEKKVPLDMSL------FLKLQKRVTELEQE----- 1168
Cdd:PRK02224  331 E---------ECRVAAQAHNEEAE----SLREDADDLEERAEELREEAAELESELeeareaVEDRREEIEELEEEieelr 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1169 KQLMQDELDRKEEQVFRSKAkEEERPQIRGaeleyeslKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVl 1248
Cdd:PRK02224  398 ERFGDAPVDLGNAEDFLEEL-REERDELRE--------REAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHV- 467

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1249 meqltSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLED-VQKMKDKGEIAQAYIGLKETnrsstmdyqELN 1327
Cdd:PRK02224  468 -----ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDrIERLEERREDLEELIAERRE---------TIE 533

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 568960783 1328 EDGElwmvyeglkQANRLLE--SQLQSQKRSHENEAEALRGEIQSLKEE 1374
Cdd:PRK02224  534 EKRE---------RAEELREraAELEAEAEEKREAAAEAEEEAEEAREE 573

IQCD

cd23767

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...

809-839

2.45e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.

Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 40.22 E-value: 2.45e-04

                          10        20        30
                  ....*....|....*....|....*....|.
gi 568960783  809 AKFLRRTKAATTIQKYWRMYVVRRRYKIRRA 839
Cdd:cd23767     3 EELQRMNRAATLIQALWRGYKVRKELKKKKK 33

CBD_MYO6-like

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...

829-867

2.62e-04

Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 43.26 E-value: 2.62e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568960783  829 VVRRRYKI--RRAATIVIQSYLRGYLTRNRYRKILREYKAV 867
Cdd:cd21759    34 VIKLKNKIlyRREALIKIQKTVRGYLARKKHRPRIKGLRKI 74

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

911-1325

2.67e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 2.67e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   911 EARSVERYKKLHIGMENKIMQL----QRKVDE-------------QNKDYK----CLMEKLTNLE---GVYNSETEKLRN 966
Cdd:pfam10174  273 EIKQMEVYKSHSKFMKNKIDQLkqelSKKESEllalqtkletltnQNSDCKqhieVLKESLTAKEqraAILQTEVDALRL 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   967 DVER-----------LQLSEEEAKVATG--------------RVLSLQEEIAKLrkdLEQTRSEKKSIEERADKYKQ-ET 1020
Cdd:pfam10174  353 RLEEkesflnkktkqLQDLTEEKSTLAGeirdlkdmldvkerKINVLQKKIENL---QEQLRDKDKQLAGLKERVKSlQT 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1021 DQlvSNLKEENTLLKQ---EKEtlnhRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKE 1097
Cdd:pfam10174  430 DS--SNTDTALTTLEEalsEKE----RIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKE 503

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1098 EMTlmlNVPKPGHKRtDSTHSSNEseytfsSEFAETEDIAPRTEEPIEKKVPLDMSLFLK--LQKRVTELEQEKQLMQDE 1175
Cdd:pfam10174  504 HAS---SLASSGLKK-DSKLKSLE------IAVEQKKEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEE 573

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1176 LDRKEEQVFR----SKAKEEERPQIRGAELEYESLKRQELESENKK---LKNELNELRK---ALSEKSAPEVTAPGAPAY 1245
Cdd:pfam10174  574 SGKAQAEVERllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKvanIKHGQQEMKKkgaQLLEEARRREDNLADNSQ 653

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1246 RVLMEQLTsvsEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTIL-----LEDVQKMKDKGEIA-----QAYIGLKET 1315
Cdd:pfam10174  654 QLQLEELM---GALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAerrkqLEEILEMKQEALLAaisekDANIALLEL 730

                          490
                   ....*....|
gi 568960783  1316 NRSSTMDYQE 1325
Cdd:pfam10174  731 SSSKKKKTQE 740

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

988-1231

2.82e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 2.82e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  988 LQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEentllkqeketlnhrIVEQAKEMTETMeRKLVEETKQl 1067
Cdd:COG1340    13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---------------LREEAQELREKR-DELNEKVKE- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1068 eldLNDERlryQNLLNEFSRLEERYDDLKEEMtlmlnvpkpghkrtdsthssneseytfssefaETEDIAPRTEEPIEKK 1147
Cdd:COG1340    76 ---LKEER---DELNEKLNELREELDELRKEL--------------------------------AELNKAGGSIDKLRKE 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1148 VPldmSLFLKLQKRVTELEQEKQLMqDELDRKEEQVFRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNEL 1225
Cdd:COG1340   118 IE---RLEWRQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLKELRAELKELRKEaeEIHKKIKELAEEAQEL 193


                  ....*.
gi 568960783 1226 RKALSE 1231
Cdd:COG1340   194 HEEMIE 199

HOOK

pfam05622

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...

904-1277

3.03e-04

Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.45 E-value: 3.03e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   904 ELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEqnkdykcLMEKLTNLEGV---YNSETEKLRNDVERLQLSEEEAKV 980
Cdd:pfam05622   36 ENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQ-------LQEENFRLETArddYRIKCEELEKEVLELQHRNEELTS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   981 ATGRVLSLQEEIAKLR------KDLEQT-RSEKKSIEERADKYKQetdqlVSNLKEENTLLKQEKETLNhrivEQAKEMT 1053
Cdd:pfam05622  109 LAEEAQALKDEMDILRessdkvKKLEATvETYKKKLEDLGDLRRQ-----VKLLEERNAEYMQRTLQLE----EELKKAN 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1054 ------ETMERKLVEetkqLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMLNvpkpghkRTDSTHSSNE------ 1121
Cdd:pfam05622  180 alrgqlETYKRQVQE----LHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLII-------ERDTLRETNEelrcaq 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1122 -SEYTFSSEFAETEDIAPRTEEPIEKKVPLDmslflkLQKRVTELEQEKQLMqdeldrKEEQvfrsKAKEEERPQIRGAE 1200
Cdd:pfam05622  249 lQQAELSQADALLSPSSDPGDNLAAEIMPAE------IREKLIRLQHENKML------RLGQ----EGSYRERLTELQQL 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1201 LEYESLKRQELESENKK-------LKNELNELRKALSEK-SAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQ 1272
Cdd:pfam05622  313 LEDANRRKNELETQNRLanqrileLQQQVEELQKALQEQgSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPK 392


                   ....*
gi 568960783  1273 LVSQK 1277
Cdd:pfam05622  393 QDSNL 397

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

969-1099

3.10e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.10e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  969 ERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQlVSNLKE------ENTLLKQEKETLN 1042
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKEyealqkEIESLKRRISDLE 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568960783 1043 HRI------VEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:COG1579   110 DEIlelmerIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172

DUF724

pfam05266

Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...

928-1047

3.14e-04

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.

Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 43.80 E-value: 3.14e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   928 KIMQLQrkVDEQNKDYKCLMEKLTNLegvynsetEKLRNDVERLQLSEEEakvatgrVLSLQEEIAKL---RKDLEQTRS 1004
Cdd:pfam05266   57 KVKKLQ--VDDSRSVFESLMESFAEL--------EKHGFDVKAPQSRINK-------LLSLKDRQTKLleeLKKLEKKIA 119

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568960783  1005 EKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVE 1047
Cdd:pfam05266  120 EEESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIAR 162

Mplasa_alph_rch

TIGR04523

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

925-1102

3.89e-04

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 3.89e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVAT-------GRVLSLQEEIAKLRK 997
Cdd:TIGR04523  445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNeekkeleEKVKDLTKKISSLKE 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   998 DLEQTRSEKKSIE-------------------ERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMER 1058
Cdd:TIGR04523  525 KIEKLESEKKEKEskisdledelnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 568960783  1059 KLVEETKQLEL--DLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM 1102
Cdd:TIGR04523  605 IEEKEKKISSLekELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650

COG2433

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

960-1113

4.21e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 4.21e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  960 ETEKLRNDVERLqlsEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSiEERADKYkqetdqlVSNLKEENTLLKQEke 1039
Cdd:COG2433   414 EIRRLEEQVERL---EAEVEELEAELEEKDERIERLERELSEARSEERR-EIRKDRE-------ISRLDREIERLERE-- 480

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568960783 1040 tlnhriVEQAKEMTETMERKLvEETKQLELDLNDERLRYQNLLNEFSR-----LEERYdDLKEEMTLMLNVPKPGHKRT 1113
Cdd:COG2433   481 ------LEEERERIEELKRKL-ERLKELWKLEHSGELVPVKVVEKFTKeairrLEEEY-GLKEGDVVYLRDASGAGRST 551

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

904-1102

5.58e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 5.58e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   904 ELKKL--KIEARSVERYKKlHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYN---SETEKLRNDVERLQlseeea 978
Cdd:pfam15905  160 ELMKLrnKLEAKMKEVMAK-QEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIeekSETEKLLEYITELS------ 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   979 kvatgrvlslqeeiaklrkdleqtrsekkSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMER 1058
Cdd:pfam15905  233 -----------------------------CVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEK 283

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 568960783  1059 -KLVEetKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM 1102
Cdd:pfam15905  284 cKLLE--SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKL 326

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

960-1277

6.58e-04

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 6.58e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   960 ETEKLRNDVERLQLSEEEAKVATGR-VLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEEntllkqek 1038
Cdd:pfam01576  493 QLEDERNSLQEQLEEEEEAKRNVERqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEK-------- 564

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1039 etlnhrivEQAKEMTETMERKLVEETKQLELDLNDERlryqNLLNEFSRLEERYDDLKEEmtlmlnvpkpghkrtdsths 1118
Cdd:pfam01576  565 --------AAAYDKLEKTKNRLQQELDDLLVDLDHQR----QLVSNLEKKQKKFDQMLAE-------------------- 612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1119 snesEYTFSSEFAETEDIAPRTEEPIEKKVpLDMSLFLK-LQKRVTELEQEKQLMQDELdrkeEQVFRSK------AKEE 1191
Cdd:pfam01576  613 ----EKAISARYAEERDRAEAEAREKETRA-LSLARALEeALEAKEELERTNKQLRAEM----EDLVSSKddvgknVHEL 683

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1192 ERPQiRGAELEYESLKRQ--ELE-----SENKKLKNELN-ELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEEL-DVR 1262
Cdd:pfam01576  684 ERSK-RALEQQVEEMKTQleELEdelqaTEDAKLRLEVNmQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELeDER 762

                          330
                   ....*....|....*
gi 568960783  1263 KEevlilRSQLVSQK 1277
Cdd:pfam01576  763 KQ-----RAQAVAAK 772

GumC

COG3206

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

957-1104

6.91e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 6.91e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  957 YNSETEKLRNDVERLQL-------------SEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQE---- 1019
Cdd:COG3206   180 LEEQLPELRKELEEAEAaleefrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpel 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1020 -TDQLVSNLKEENTLLKQEKETL------NHRIVEQAKEMTETMERKLVEETKQLEL---------------------DL 1071
Cdd:COG3206   260 lQSPVIQQLRAQLAELEAELAELsarytpNHPDVIALRAQIAALRAQLQQEAQRILAsleaelealqareaslqaqlaQL 339

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568960783 1072 NDERLRYQNLLNEFSRLEERYDDLKEEMTLMLN 1104
Cdd:COG3206   340 EARLAELPELEAELRRLEREVEVARELYESLLQ 372

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

1039-1275

8.86e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 8.86e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1039 ETLNHRIVEQAKEMTETMeRKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmlnvpkpghKRTDSTHS 1118
Cdd:pfam07888   30 ELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL-----------RQSREKHE 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1119 SNESEYT----FSSEFAETEDIAPRTEEPIEKKVpldmslfLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKA--KEEE 1192
Cdd:pfam07888   98 ELEEKYKelsaSSEELSEEKDALLAQRAAHEARI-------RELEEDIKTLTQRVLERETELERMKERAKKAGAqrKEEE 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1193 rpqirgAELEYESLKRQELESENKKLKNELNELRKALSEKSA---------PEVTAPGAPAYR------VLMEQLTSVSE 1257
Cdd:pfam07888  171 ------AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTqvlqlqdtiTTLTQKLTTAHRkeaeneALLEELRSLQE 244

                          250
                   ....*....|....*...
gi 568960783  1258 ELDVRKEEVLILRSQLVS 1275
Cdd:pfam07888  245 RLNASERKVEGLGEELSS 262

Tropomyosin

pfam00261

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...

928-1177

9.28e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.

Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.71 E-value: 9.28e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   928 KIMQLQRKVDEQNKDYKCLMEKLTNLEGVYnsetEKLRNDVE----RLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTR 1003
Cdd:pfam00261    2 KMQQIKEELDEAEERLKEAMKKLEEAEKRA----EKAEAEVAalnrRIQLLEEELERTEERLAEALEKLEEAEKAADESE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1004 SEKKSIEERAdkykqetdqlvsnLKEENTLLKQEKEtlnhriVEQAKEMTETMERKLVEETKQL-----ELDLNDERLRy 1078
Cdd:pfam00261   78 RGRKVLENRA-------------LKDEEKMEILEAQ------LKEAKEIAEEADRKYEEVARKLvvvegDLERAEERAE- 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1079 qnllnefsRLEERYDDLKEEMTLMLNVPK----PGHKRTDSTHSSNESEYTFSSEFAETEDiapRTEEPiEKKVPldmsl 1154
Cdd:pfam00261  138 --------LAESKIVELEEELKVVGNNLKsleaSEEKASEREDKYEEQIRFLTEKLKEAET---RAEFA-ERSVQ----- 200

                          250       260       270
                   ....*....|....*....|....*....|
gi 568960783  1155 flKLQKRVTELEQE-------KQLMQDELD 1177
Cdd:pfam00261  201 --KLEKEVDRLEDEleaekekYKAISEELD 228

YhaN

COG4717

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

968-1441

9.43e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 9.43e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  968 VERLQLSEEEAKVATGRVLSLQ-EEIAKLRKDLEQTRSEKKSIEERADKyKQETDQLVSNLKEENTLLKQEKETLNH--R 1044
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKllQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1045 IVEQAKEMTETmERKLVEETKQLElDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmlnvpkpghkrtdsthssnesey 1124
Cdd:COG4717   127 LLPLYQELEAL-EAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELE------------------------ 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1125 tfssefAETEDIAPRTEEPIEKkvpldmslflkLQKRVTELEQEKQLMQDELDRKEEQVfrskakEEERPQIRGAELEYE 1204
Cdd:COG4717   181 ------ELLEQLSLATEEELQD-----------LAEELEELQQRLAELEEELEEAQEEL------EELEEELEQLENELE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1205 SLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVL---ILRSQLVSQKEAIQ 1281
Cdd:COG4717   238 AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLgkeAEELQALPALEELE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1282 PKNTMTDSTIL-LEDVQKMKDKGEIAQAYIGLKETNRSSTMDYQELNEDGELWMVYEGLKQANRLLESQLQsQKRSHENE 1360
Cdd:COG4717   318 EEELEELLAALgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELR-AALEQAEE 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1361 AEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQheitrltnenlDLMEQLEKQDKTVRKLKKQLKVFAKKIGEL 1440
Cdd:COG4717   397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELE-----------ELEEELEELEEELEELREELAELEAELEQL 465


                  .
gi 568960783 1441 E 1441
Cdd:COG4717   466 E 466

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

960-1052

1.12e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 1.12e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  960 ETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKE 1039
Cdd:COG4942   151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230

                          90
                  ....*....|...
gi 568960783 1040 TLNHRIVEQAKEM 1052
Cdd:COG4942   231 RLEAEAAAAAERT 243

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

925-1273

1.44e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.44e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGvynsETEKLRNDVERLQLSEEE----AKVATGRVLSLQEEIAKLRKDLE 1000
Cdd:pfam01576  775 LELDLKELEAQIDAANKGREEAVKQLKKLQA----QMKDLQRELEEARASRDEilaqSKESEKKLKNLEAELLQLQEDLA 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1001 QTRSEKKSIEERADKYKQEtdqlVSNLKEENTLLKQEKETLNHRIVEQAKEMTE---TME------RKLVEETKQLELDL 1071
Cdd:pfam01576  851 ASERARRQAQQERDELADE----IASGASGKSALQDEKRRLEARIAQLEEELEEeqsNTEllndrlRKSTLQVEQLTTEL 926

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1072 NDERLRYQNLLNEFSRLEERYDDLKEEMTLMLNVPKPGHKrtdsthssneseytfsSEFAETEDIAPRTEEPIEKKVPlD 1151
Cdd:pfam01576  927 AAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFK----------------SSIAALEAKIAQLEEQLEQESR-E 989

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1152 MSLFLKLQKRvTELEQEKQLMQDELDRKEeqvfrskaKEEERPQIRGAELEYESLKRQELESENkklknelnelrkalse 1231
Cdd:pfam01576  990 RQAANKLVRR-TEKKLKEVLLQVEDERRH--------ADQYKDQAEKGNSRMKQLKRQLEEAEE---------------- 1044

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 568960783  1232 ksapEVTAPGApAYRVLMEQLTSVSEELDVRKEEVLILRSQL 1273
Cdd:pfam01576 1045 ----EASRANA-ARRKLQRELDDATESNESMNREVSTLKSKL 1081

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

969-1098

1.60e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.60e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  969 ERLQLSE---EEAK-VATGRVLSLQEEIAKL---RKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETL 1041
Cdd:PRK00409  495 KRLGLPEniiEEAKkLIGEDKEKLNELIASLeelERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568960783 1042 NHRIVEQAKEMTETMERKLVEETKQLELDLNDerlryQNLLNEFSRLEERYDDLKEE 1098
Cdd:PRK00409  575 AQQAIKEAKKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKANEKKEKK 626

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

765-786

1.62e-03

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

Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 37.31 E-value: 1.62e-03

                            10        20
                    ....*....|....*....|..
gi 568960783    765 KLRAACIRIQKTIRGWLLRKRY 786
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

931-1212

1.78e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.78e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  931 QLQRKVDEQNKDYKCLMEKLTNLEgvynSETEKLRNDVERLQlseEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIE 1010
Cdd:COG4372    42 KLQEELEQLREELEQAREELEQLE----EELEQARSELEQLE---EELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1011 ERADKYKQEtdqlVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEE 1090
Cdd:COG4372   115 EELEELQKE----RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1091 RYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESEYTFSSEFAETEDIAprTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQ 1170
Cdd:COG4372   191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA--LLDALELEEDKEELLEEVILKEIEELELAIL 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568960783 1171 LMQDELDRKEEQVFRSKAKEEERPQIRGAELEYESLKRQELE 1212
Cdd:COG4372   269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310

Rabaptin

pfam03528

Rabaptin;

932-1096

1.78e-03

Rabaptin;

Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 1.78e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   932 LQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRndveRLQLS-EEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIE 1010
Cdd:pfam03528    6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFK----ELYLAkEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1011 ERA---DKYKQET-DQLVSNLKEENTLLK-------QEKETLNHRIVEQAK----EMTETMERKLVEETKQLEldlndER 1075
Cdd:pfam03528   82 AVAtvsENTKQEAiDEVKSQWQEEVASLQaimketvREYEVQFHRRLEQERaqwnQYRESAEREIADLRRRLS-----EG 156

                          170       180
                   ....*....|....*....|.
gi 568960783  1076 LRYQNLLNEFSRLEERYDDLK 1096
Cdd:pfam03528  157 QEEENLEDEMKKAQEDAEKLR 177

235kDa-fam

TIGR01612

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...

902-1067

2.03e-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: 43.50 E-value: 2.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKvdeqnkdykclMEKLTNLEGVYN---SETEKLRNDVERLQLSEEEA 978
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENK-----------FLKISDIKKKINdclKETESIEKKISSFSIDSQDT 1643

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   979 KVATGrvlslQEEIAKLRKDLEQTRSEKKSIEERadkyKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMER 1058
Cdd:TIGR01612 1644 ELKEN-----GDNLNSLQEFLESLKDQKKNIEDK----KKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKE 1714


                   ....*....
gi 568960783  1059 KLvEETKQL 1067
Cdd:TIGR01612 1715 EI-ESIKEL 1722

FPP

pfam05911

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...

923-1099

2.23e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.

Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.13 E-value: 2.23e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   923 IGMENKIMqlqrKVDEQNKdYKCLMEKLTNLEGVYnSETEKLRNDVERLQlseeEAKVATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam05911  624 SSMEDEIK----KHDCIDK-VTLSENKVAQVDNGC-SEIDNLSSDPEIPS----DGPLVSGSNDLKTEENKRLKEEFEQL 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1003 RSEKKSIEERADKYK----------QETDQLVSNLKEENTLLKQeketLNHRIVEQAKEMTEtMERKLVEETKQLELDLN 1072
Cdd:pfam05911  694 KSEKENLEVELASCTenlestksqlQESEQLIAELRSELASLKE----SNSLAETQLKCMAE-SYEDLETRLTELEAELN 768

                          170       180       190
                   ....*....|....*....|....*....|....
gi 568960783  1073 DERLRYQNLLNEFS-------RLEERYDDLKEEM 1099
Cdd:pfam05911  769 ELRQKFEALEVELEeekncheELEAKCLELQEQL 802

PRK05771

V-type ATP synthase subunit I; Validated

902-1042

2.40e-03

V-type ATP synthase subunit I; Validated

Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 2.40e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  902 KRELKKLKIEARSVERYKKLHIGMENKIMQ--LQRKVDEQNKDYKCLMEKLTNLEGVYNSETEK---------------- 963
Cdd:PRK05771  113 ENEIKELEQEIERLEPWGNFDLDLSLLLGFkyVSVFVGTVPEDKLEELKLESDVENVEYISTDKgyvyvvvvvlkelsde 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  964 -----LRNDVERLQLSEEEakvatgrvlSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEK 1038
Cdd:PRK05771  193 veeelKKLGFERLELEEEG---------TPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERA 263


                  ....
gi 568960783 1039 ETLN 1042
Cdd:PRK05771  264 EALS 267

Golgin_A5

pfam09787

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...

988-1209

2.58e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.

Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 2.58e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   988 LQEEIAKLRKDLEQTRSEKKSIEERadkYKQETDQlvsnLKEENTLLKQEKETLNhriveQAKEMTETMERKLVEETKQL 1067
Cdd:pfam09787   59 LREEIQKLRGQIQQLRTELQELEAQ---QQEEAES----SREQLQELEEQLATER-----SARREAEAELERLQEELRYL 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1068 ELDLNDERLRYQNLLNEfsrLEERYDDLKEEMTLmlnvpkpghkRTDSTHSSNESEytfssefaetEDIAPRTEEPIEKk 1147
Cdd:pfam09787  127 EEELRRSKATLQSRIKD---REAEIEKLRNQLTS----------KSQSSSSQSELE----------NRLHQLTETLIQK- 182

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960783  1148 vpldmslflklQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRGAELEYESLKRQ 1209
Cdd:pfam09787  183 -----------QTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRL 233

PLN02939

transferase, transferring glycosyl groups

900-1043

2.62e-03

transferase, transferring glycosyl groups

Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 2.62e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKD--------YKCLMEKLTNLEGVYNSETEK-------- 963
Cdd:PLN02939  244 FLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDvsklsplqYDCWWEKVENLQDLLDRATNQvekaalvl 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  964 -----LRNDVERLQLSEEEAKV---ATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENtllk 1035
Cdd:PLN02939  324 dqnqdLRDKVDKLEASLKEANVskfSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEES---- 399


                  ....*...
gi 568960783 1036 qEKETLNH 1043
Cdd:PLN02939  400 -KKRSLEH 406

TPR_MLP1_2

pfam07926

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...

975-1104

2.66e-03

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: 39.93 E-value: 2.66e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   975 EEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEradKYKQE------TDQLVSNLKEENTLLKQEKETLNHRiVEQ 1048
Cdd:pfam07926    7 QSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQ---NYERElvlhaeDIKALQALREELNELKAEIAELKAE-AES 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568960783  1049 AKEMTETMERKLVEETKQLEldlnderlryqnllNEFSRLEERYDDLKEEMTLMLN 1104
Cdd:pfam07926   83 AKAELEESEESWEEQKKELE--------------KELSELEKRIEDLNEQNKLLHD 124

Smc

COG1196

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

965-1098

2.92e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 2.92e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  965 RNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHR 1044
Cdd:COG1196   641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1045 IVEQAKEMTETMERKLVEETKQLELDLNDERLRYQ---------------------------NL--LNEFSRLEERYDDL 1095
Cdd:COG1196   721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdleelerelerlereiealgpvNLlaIEEYEELEERYDFL 800


                  ...
gi 568960783 1096 KEE 1098
Cdd:COG1196   801 SEQ 803

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

925-1100

3.28e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLegvyNSETEKLRndvERLQLSEEEAKvatgrvlSLQEEIAKLRKDLEQTRS 1004
Cdd:COG1340    20 LREEIEELKEKRDELNEELKELAEKRDEL----NAQVKELR---EEAQELREKRD-------ELNEKVKELKEERDELNE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1005 EKKSIEERADKYKQETDQLVSNLKEENTlLKQEKETLNHRIveQAKEMTETMERKLVEETKQLE------LDLNDERLRY 1078
Cdd:COG1340    86 KLNELREELDELRKELAELNKAGGSIDK-LRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEkelekaKKALEKNEKL 162

                         170       180
                  ....*....|....*....|..
gi 568960783 1079 QNLLNEFSRLEERYDDLKEEMT 1100
Cdd:COG1340   163 KELRAELKELRKEAEEIHKKIK 184

GBP_C

cd16269

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

943-1085

3.65e-03

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: 41.41 E-value: 3.65e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  943 YKCLMEKLTNLEGVYNSETEKLRNDVERLQL------SEEEAKVATGRVLSLQE-EIAKLRKDLEQTRSEKKSIEERADK 1015
Cdd:cd16269   144 YQLYLEDREKLVEKYRQVPRKGVKAEEVLQEflqskeAEAEAILQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQRE 223

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1016 YKQETDQLVSNLKEENTLLKQEKETlnhRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEF 1085
Cdd:cd16269   224 LEQKLEDQERSYEEHLRQLKEKMEE---ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1182-1436

4.28e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 4.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1182 QVFRSKAKEEERPQIRgAELEYESLKRQELESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDV 1261
Cdd:COG4942    18 QADAAAEAEAELEQLQ-QEIAELEKELAALKKEEKALLKQLAALERRIAALAR---------RIRALEQELAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1262 RKEEVLILRSQLVSQKEAIQPkntmtdstiLLEDVQKMkdkGEIAQAYIGLK-----ETNRSSTMdYQELNE-DGELWMV 1335
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAE---------LLRALYRL---GRQPPLALLLSpedflDAVRRLQY-LKYLAPaRREQAEE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1336 YEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQqllaqnlqlppeaRIEASLQHEITRLTNENLDLMEQ 1415
Cdd:COG4942   155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ-------------KLLARLEKELAELAAELAELQQE 221

                         250       260
                  ....*....|....*....|.
gi 568960783 1416 LEKQDKTVRKLKKQLKVFAKK 1436
Cdd:COG4942   222 AEELEALIARLEAEAAAAAER 242

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

900-1242

4.49e-03

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: 41.87 E-value: 4.49e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  900 MAKRELKKLKIEArSVERYKKLHIGMENKIMQLQRKVDEqnkdYKCLMEKLTNLEgvynseTEKLRNDVERLQLSEEEAK 979
Cdd:COG5185   217 SESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDK----LEKLVEQNTDLR------LEKLGENAESSKRLNENAN 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  980 VATGRVLSLQEEIAklrkDLEQTRSEKKSIEERADKYKQ--ETDQLVSNLKEENTLLKQEKETLnhrivEQAKEMTETME 1057
Cdd:COG5185   286 NLIKQFENTKEKIA----EYTKSIDIKKATESLEEQLAAaeAEQELEESKRETETGIQNLTAEI-----EQGQESLTENL 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1058 RKLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKEEMTLMLNVPKPGHK---RTDSTHSSNESEYTFSSEFAETE 1134
Cdd:COG5185   357 EAIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQNQRGYAQEILAtleDTLKAADRQIEELQRQIEQATSS 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1135 diaprTEEPIEKKVPLDMSlflkLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKE--EERPQIRGAELEYeslkRQELE 1212
Cdd:COG5185   436 -----NEEVSKLLNELISE----LNKVMREADEESQSRLEEAYDEINRSVRSKKEDlnEELTQIESRVSTL----KATLE 502

                         330       340       350
                  ....*....|....*....|....*....|
gi 568960783 1213 SENKKLKNELNELRKALSEKSAPEVTAPGA 1242
Cdd:COG5185   503 KLRAKLERQLEGVRSKLDQVAESLKDFMRA 532

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

956-1081

4.97e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.97e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  956 VYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERA-----DKY-------KQETDQL 1023
Cdd:PRK00409  510 LIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeaeKEAqqaikeaKKEADEI 589

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960783 1024 VSNL----KEENTLLKQEKETLNHRIVEQAKEMTEtmERKLVEETKQLELDLNDeRLRYQNL 1081
Cdd:PRK00409  590 IKELrqlqKGGYASVKAHELIEARKRLNKANEKKE--KKKKKQKEKQEELKVGD-EVKYLSL 648

CBD_MYO6-like

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...

767-786

5.03e-03

Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 39.41 E-value: 5.03e-03

                          10        20
                  ....*....|....*....|
gi 568960783  767 RAACIRIQKTIRGWLLRKRY 786
Cdd:cd21759    45 REALIKIQKTVRGYLARKKH 64

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

987-1097

5.14e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 5.14e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   987 SLQEEIAKLRKDleqtrsekksiEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKlvEETKQ 1066
Cdd:pfam13851   30 SLKEEIAELKKK-----------EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK--ARLKV 96

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568960783  1067 LELDLNDERLRYQNLLNEFSRLEERYDDLKE 1097
Cdd:pfam13851   97 LEKELKDLKWEHEVLEQRFEKVERERDELYD 127

ATG16

pfam08614

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...

960-1098

5.16e-03

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: 39.92 E-value: 5.16e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   960 ETEKLRNDVERL-----QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRsekksieeradKYKQETDQLVSNLKEENTLL 1034
Cdd:pfam08614   22 ENAKLQSEPESVlpstsSSKLSKASPQSASIQSLEQLLAQLREELAELY-----------RSRGELAQRLVDLNEELQEL 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1035 KQEKETLNHRI------VEQAKEMTETMERKLVEETKQLElDLNDErlrYQNLLNEFSRLEERYDDLKEE 1098
Cdd:pfam08614   91 EKKLREDERRLaaleaeRAQLEEKLKDREEELREKRKLNQ-DLQDE---LVALQLQLNMAEEKLRKLEKE 156

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

897-1211

5.21e-03

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 5.21e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   897 RRMMAKRELKKLKIEARsveRYKKLHIGMENKIMQLQRKVDEQNKDYKCLME-------KLTNLEGVYNSETEKLRNDVE 969
Cdd:pfam07888   74 QRRELESRVAELKEELR---QSREKHEELEEKYKELSASSEELSEEKDALLAqraaheaRIRELEEDIKTLTQRVLERET 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783   970 RLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQ---ETDQLVSNLKEENTLLKQEKETLNHRIV 1046
Cdd:pfam07888  151 ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNslaQRDTQVLQLQDTITTLTQKLTTAHRKEA 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1047 EQA---KEMTETMERKLVEETKQ--LELDLND---ERLRYQNLLNEfSRLEeryddlKEEMTLMLnvpkpghkrTDSTHS 1118
Cdd:pfam07888  231 ENEallEELRSLQERLNASERKVegLGEELSSmaaQRDRTQAELHQ-ARLQ------AAQLTLQL---------ADASLA 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1119 SNESEYTFSSEFAETEDIAPRTEEPIEKkvpLDMSLfLKLQKRVTELEQEKQLMQDELDRKEE--QVFRSKAK---EEER 1193
Cdd:pfam07888  295 LREGRARWAQERETLQQSAEADKDRIEK---LSAEL-QRLEERLQEERMEREKLEVELGREKDcnRVQLSESRrelQELK 370

                          330       340
                   ....*....|....*....|
gi 568960783  1194 PQIRGAELEYESL--KRQEL 1211
Cdd:pfam07888  371 ASLRVAQKEKEQLqaEKQEL 390

PRK12704

phosphodiesterase; Provisional

971-1068

5.30e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.30e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  971 LQLSEEEAKVATG-RVLSLQEEIAKLRKDLEQTRSEKKS-IEERADKYKQETDQLVSNL----KEENTLLKQEKEtLNHR 1044
Cdd:PRK12704   44 LEEAKKEAEAIKKeALLEAKEEIHKLRNEFEKELRERRNeLQKLEKRLLQKEENLDRKLelleKREEELEKKEKE-LEQK 122

                          90       100
                  ....*....|....*....|....
gi 568960783 1045 IvEQAKEMTETMERKLVEETKQLE 1068
Cdd:PRK12704  123 Q-QELEKKEEELEELIEEQLQELE 145

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

932-1096

5.64e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 5.64e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  932 LQRKVDEQNKDYKCLMEKLTNLEgvynSETEKLRNDVERLQlsEEEAKVATGRVLSLQEEIAKLRKDLEQtrsekksIEE 1011
Cdd:COG4913   293 LEAELEELRAELARLEAELERLE----ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEE-------RER 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783 1012 RADKYkqetDQLVSNLKEEntlLKQEKETLNhRIVEQAKEMTETMErklvEETKQLELDLNDERLRYQNLLNEFSRLEER 1091
Cdd:COG4913   360 RRARL----EALLAALGLP---LPASAEEFA-ALRAEAAALLEALE----EELEALEEALAEAEAALRDLRRELRELEAE 427


                  ....*
gi 568960783 1092 YDDLK 1096
Cdd:COG4913   428 IASLE 432

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

1174-1441

7.62e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 7.62e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1174 DELDRKEEQVFRSKAKEEERPQI------------------RGAELEYESLKRQELESENKKLKNELNELRKALSeksap 1235
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERldliidekrqqlerlrreREKAERYQALLKEKREYEGYELLKEKEALERQKE----- 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1236 EVTAPGAPAYRVLmEQLTSVSEELDVRKEEVLILRSQL------VSQKEAIQPKNTMTDSTI-----------LLEDVQK 1298
Cdd:TIGR02169  241 AIERQLASLEEEL-EKLTEEISELEKRLEEIEQLLEELnkkikdLGEEEQLRVKEKIGELEAeiaslersiaeKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  1299 MKDKGEIAQAYIG-LKETNRSSTMDYQELNEDGELWM-VYEGLKQANRLLESQLQSQKRSHE---NEAEALRGEIQSLKE 1373
Cdd:TIGR02169  320 AEERLAKLEAEIDkLLAEIEELEREIEEERKRRDKLTeEYAELKEELEDLRAELEEVDKEFAetrDELKDYREKLEKLKR 399

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568960783  1374 ENNRQQQLLAQNLQLPPEARIE-ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1441
Cdd:TIGR02169  400 EINELKRELDRLQEELQRLSEElADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468

COG2433

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

925-1018

8.05e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 8.05e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960783  925 MENKIMQLQRKVDE---QNKDykcLMEKLTNLEgvynSETEKLRNDVERLQlSEEEAKVATGRVLS-LQEEIAKLRKDLE 1000
Cdd:COG2433   411 EEEEIRRLEEQVERleaEVEE---LEAELEEKD----ERIERLERELSEAR-SEERREIRKDREISrLDREIERLERELE 482

                          90
                  ....*....|....*...
gi 568960783 1001 QTRSEKKSIEERADKYKQ 1018
Cdd:COG2433   483 EERERIEELKRKLERLKE 500

pfam00612

IQ calmodulin-binding motif; Calmodulin-binding motif.

838-858

8.09e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.

Pssm-ID: 459869 Cd Length: 21 Bit Score: 35.37 E-value: 8.09e-03

                           10        20
                   ....*....|....*....|.
gi 568960783   838 RAATIVIQSYLRGYLTRNRYR 858
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21