NCBI Conserved Domain Search

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

897-1219

5.66e-12

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 5.66e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   897 RLKARQElKALKIEARSAEHLKRLNV---GMENKVVQLQRKIDdQNKEFKTLSEQLSAVtsSHAVEVEKLKKELAHYQQN 973
Cdd:TIGR02168  169 KYKERRK-ETERKLERTRENLDRLEDilnELERQLKSLERQAE-KAERYKELKAELREL--ELALLVLRLEELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   974 QEADTslQLQEEVQSLRTELQKAHSERRVLEDAHN----------KENGELRKRVADLEHENALLKDEKEYLNNQI---- 1039
Cdd:TIGR02168  245 QEELK--EAEEELEELTAELQELEEKLEELRLEVSeleeeieelqKELYALANEISRLEQQKQILRERLANLERQLeele 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1040 ---------LCQSKAESSQSSVEENLL------MKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKN-- 1102
Cdd:TIGR02168  323 aqleeleskLDELAEELAELEEKLEELkeelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNei 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1103 PSNQSSLESDSNYPSISTSEIGDTEDALQ--QVEEIGIEKAAMDMTVFlKLQKRVRELEQERKKLQAQLEKGQQ--DSKK 1178
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQalDAAE 481

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 569003409  1179 GQVEQQNNGLDVDQDAdiaynslkRQELESENKKLKNDLNE 1219
Cdd:TIGR02168  482 RELAQLQARLDSLERL--------QENLEGFSEGVKALLKN 514

PRK03918

DNA double-strand break repair ATPase Rad50;

901-1269

3.17e-10

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 3.17e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  901 RQELKALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTS------SHAVEVEKLKKELAHYQQNQ 974
Cdd:PRK03918  175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkeleELKEEIEELEKELESLEGSK 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  975 EAdtslqLQEEVQSLRTELQKAHSERRVLEDaHNKENGELRKRVADLEHENALLKDEKEYLNNQILCQSKAESSQSSVEE 1054
Cdd:PRK03918  255 RK-----LEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1055 NLL----MKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQsslesdsnypsistsEIGDTEDAL 1130
Cdd:PRK03918  329 RIKeleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL---------------TPEKLEKEL 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1131 QQVEE--IGIEKAamdmtvFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQV------EQQNNGLDVDQDADIAYNSLK 1202
Cdd:PRK03918  394 EELEKakEEIEEE------ISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgreltEEHRKELLEEYTAELKRIEKE 467

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569003409 1203 RQELESENKKLKNDLNELRKAVADQ---------AMQDNSTHSSPDSYSllLNQLKLANEELEVRKEEVLILRTQI 1269
Cdd:PRK03918  468 LKEIEEKERKLRKELRELEKVLKKEseliklkelAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEI 541

SCP-1

pfam05483

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

932-1375

2.40e-08

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.35 E-value: 2.40e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   932 QRKIDDQNKEFKTLS----------EQLSAVTSSHAVEVEKLKKELAhyqqnqEADTSLQLQEEVQSLRTELQKAHSERR 1001
Cdd:pfam05483  369 QQRLEKNEDQLKIITmelqkksselEEMTKFKNNKEVELEELKKILA------EDEKLLDEKKQFEKIAEELKGKEQELI 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1002 VLEDAHNKEngelrkrVADLEHENALLKDEKEYLNNQilcqskaessqssVEEnllMKKELEEERSRYQNLVKEYSQLEQ 1081
Cdd:pfam05483  443 FLLQAREKE-------IHDLEIQLTAIKTSEEHYLKE-------------VED---LKTELEKEKLKNIELTAHCDKLLL 499

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1082 RYENLRDEVT-ILKQTPGHRKNPSNQSSLEsdsnypsistseigdtEDALQQVEEIgiekAAMDMTVFLKLQKRVRELEQ 1160
Cdd:pfam05483  500 ENKELTQEASdMTLELKKHQEDIINCKKQE----------------ERMLKQIENL----EEKEMNLRDELESVREEFIQ 559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1161 ERKKLQAQLEKGQQDSKKGQVEQQNNGLDVDQDADIAyNSLKRQeLESENKKLKnDLNELRKAVADQAMQDNSthsSPDS 1240
Cdd:pfam05483  560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC-NNLKKQ-IENKNKNIE-ELHQENKALKKKGSAENK---QLNA 633

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1241 YSLLLNQLKLANEELEVRKEEvlILRTQIMNADQRRLSGKNMEPNINARTSWPNSEKHVDQEDAIEAYHGVCQTNSQTE- 1319
Cdd:pfam05483  634 YEIKVNKLELELASAKQKFEE--IIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEk 711

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569003409  1320 -----DWGYLNEDGELGLaYQGLKQVARLLEAQLQAQSLEHEEEVEHLKAQVEALKEEMDK 1375
Cdd:pfam05483  712 hkhqyDKIIEERDSELGL-YKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771

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

861-881

3.83e-04

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

Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 39.23 E-value: 3.83e-04

                            10        20
                    ....*....|....*....|.
gi 569003409    861 MEHKATIIQKYARGWMARKRF 881
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRY 22

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1202-1441

5.54e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 5.54e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1202 KRQELESENKKLKNDLNELRKAVADQAMQDNSthsspdsyslLLNQLKLANEELEVRKEEVLILRTQImNADQRRLSGKN 1281
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKA----------LLKQLAALERRIAALARRIRALEQEL-AALEAELAELE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1282 MEpnINArtswpNSEKHVDQEDAIEAYHGVCQTNSQTEDWGYL---NEDGELGLAYQGLKQVARLLEAQLQAQsleheee 1358
Cdd:COG4942    90 KE--IAE-----LRAELEAQKEELAELLRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEEL------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1359 vEHLKAQVEALKEEMDKQQQTFcqtlllspeAQVEFGVQQEISRLTNENLDFKELVEKLEKNERKLKKQLKIYMKKVQDL 1438
Cdd:COG4942   156 -RADLAELAALRAELEAERAEL---------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225


                  ...
gi 569003409 1439 EAA 1441
Cdd:COG4942   226 EAL 228

CBD_MYO6-like

cd21759

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

856-972

2.81e-03

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: 40.18 E-value: 2.81e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  856 YRQvlmeHKATIIQKYARGWMARKRFlRERdaaivIQCaFRRLKA-RQELKALKieaRSAEHLKRLNVGMENKVVQLQRK 934
Cdd:cd21759    43 YRR----EALIKIQKTVRGYLARKKH-RPR-----IKG-LRKIRAlEKQLKEME---EIASQLKKDKDKWTKQVKELKKE 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 569003409  935 IDDQNKEFKTlSEQLSAVTSSHAVE--VEKLKKELAHYQQ 972
Cdd:cd21759   109 IDALIKKIKT-NDMITRKEIDKLYNalVKKVDKQLAELQK 147

Name

Accession

Description

Interval

E-value

MYSc_Myo5

cd01380

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

83-750

0e+00

Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 1325.24 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd01380     1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASD-TNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRT 241
Cdd:cd01380    81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  242 YLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSH 321
Cdd:cd01380   161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  322 QISIFKIIASILHLGSVEIQSERDgDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNAR 401
Cdd:cd01380   241 QMEIFRILAAILHLGNVEIKATRN-DSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVAR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  402 DALAKHIYAQLFSWIVEHINKALHTSL--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYM 479
Cdd:cd01380   320 DALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYV 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  480 KEQIPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERHSN--SQHFQKPRMSNTAFIVNHFADKV 557
Cdd:cd01380   400 KEEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKkpNKHFKKPRFSNTAFIVKHFADDV 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  558 EYLSDGFLEKNRDTVYEEQINILKASKFplvadlfhddkdsapatntaknrssskinvrssrplikvpnkeHKKSVGYQF 637
Cdd:cd01380   480 EYQVEGFLEKNRDTVSEEHLNVLKASKN-------------------------------------------RKKTVGSQF 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  638 RTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKREL 717
Cdd:cd01380   517 RDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEW 596

                         650       660       670
                  ....*....|....*....|....*....|...
gi 569003409  718 TNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd01380   597 LRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629

MYSc

smart00242

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

64-761

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: 1046.75 E-value: 0e+00

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409     64 NPDILVGENDLTALSHLHEPAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVA 143
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409    144 EEAYKQMARDEKNQSIIVSGESGAGKTVSAKYAMRYFATVGGSA-SDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGK 222
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNtEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409    223 FIEIGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDA 302
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409    303 DDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLV 382
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409    383 TTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 462
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409    463 QQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKP 541
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409    542 -RMSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkdsapaTNTAKNRSSSKInvrssrp 620
Cdd:smart00242  480 kKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF---------PSGVSNAGSKKR------- 543

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409    621 likvpnkehKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWT 700
Cdd:smart00242  544 ---------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614

                           650       660       670       680       690       700
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569003409    701 YHDFFNRYRVLMKKR-ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFRAGQVAYLEKLR 761
Cdd:smart00242  615 FDEFLQRYRVLLPDTwPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676

Myosin_head

pfam00063

Myosin head (motor domain);

72-750

0e+00

Myosin head (motor domain);

Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 996.02 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409    72 NDLTALSHLHEPAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMA 151
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   152 RDEKNQSIIVSGESGAGKTVSAKYAMRYFATVGGSASDTN---IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGF 228
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   229 DKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKT 308
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   309 RQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDsCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETY 388
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDE-QAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   389 VKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKAL-HTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFN 467
Cdd:pfam00063  320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLdVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFN 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   468 SHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPR-MSN 545
Cdd:pfam00063  400 HHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRlQGE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   546 TAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddKDSAPATNTAKNRSSSKINVRSSrplikvp 625
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELF---PDYETAESAAANESGKSTPKRTK------- 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   626 nKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFF 705
Cdd:pfam00063  550 -KKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 569003409   706 NRYRVLMKKR-ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:pfam00063  629 QRYRILAPKTwPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674

COG5022

Myosin heavy chain [General function prediction only];

11-1268

0e+00

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 978.02 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   11 TRVWIPDPDEVWRSAELTK-DYKEGDKSLQLRLEDDTI--LEYPVDVQNNqvpflRNPDILVGENDLTALSHLHEPAVLH 87
Cdd:COG5022    10 SGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGESvsVKKKVLGNDR-----IKLPKFDGVDDLTELSYLNEPAVLH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   88 NLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSGESGA 167
Cdd:COG5022    85 NLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  168 GKTVSAKYAMRYFATVGGSASD--TNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYLLE 245
Cdd:COG5022   164 GKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  246 KSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSHQISI 325
Cdd:COG5022   244 KSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQI 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  326 FKIIASILHLGSVEIQSERDGDScsISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARDALA 405
Cdd:COG5022   324 FKILAAILHIGNIEFKEDRNGAA--IFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLA 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  406 KHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPW 485
Cdd:COG5022   402 KALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEW 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  486 TLIDFYDNQPCIDLIEAK--LGILDLLDEECKVPKGTDQNWAQKLYER--HSNSQHFQKPRMSNTAFIVNHFADKVEYLS 561
Cdd:COG5022   482 SFIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDV 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  562 DGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSApatntaknrssskinvrssrplikvpNKEHKKSVGYQFRTSL 641
Cdd:COG5022   562 EGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE--------------------------SKGRFPTLGSRFKESL 615

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  642 NLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKRELTNT- 720
Cdd:COG5022   616 NSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEy 695

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  721 ----DKKNICKSVLESLIKDPDKFQFGRTKIFFRAGQVAYLEKLRADKFREATIMIQKSVRGWLQRVKYRRLRAATLSLQ 796
Cdd:COG5022   696 twkeDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQ 775

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  797 RFCRGYLARRLAEHLRRTRAAIVFQKQYRMLKARRAYRRVCRATVIIQ-SFTRAMFVRRNYRQVLMEHKATIIQKYARGW 875
Cdd:COG5022   776 VIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQkTIKREKKLRETEEVEFSLKAEVLIQKFGRSL 855

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  876 MARKRFLRERDAAIVIQCAFRRLKARQELKALKIEARSAEHLKRLNVGMENKVVQLQRKIDdqnkefktlseqlsavtSS 955
Cdd:COG5022   856 KAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLS-----------------SD 918

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  956 HAVEVEKLKKELAHYQQ-NQEADTSLQLQEEVQSLRtELQKAHSERRVLEDAhnkengelrkrvadLEHENALLKDEKEY 1034
Cdd:COG5022   919 LIENLEFKTELIARLKKlLNNIDLEEGPSIEYVKLP-ELNKLHEVESKLKET--------------SEEYEDLLKKSTIL 983

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1035 LnnqilcqskaESSQSSVEENLLMKKELEEERSRYQNLVKEYSQLEQRyenlrdevtilkqtpghrknPSNQSSLESDSN 1114
Cdd:COG5022   984 V----------REGNKANSELKNFKKELAELSKQYGALQESTKQLKEL--------------------PVEVAELQSASK 1033

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1115 YPSISTSEIGdtedalqqveeigiekaamdmtVFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQVEQQNngLDVDQDA 1194
Cdd:COG5022  1034 IISSESTELS----------------------ILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ--LYQLEST 1089

                        1210      1220      1230      1240      1250      1260      1270
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569003409 1195 DIAYNSLKRQELESENKKLKNDLNELRKAVADQAMQDNSTHSSPdSYSLLLNQLKLANEELEVRKEEVLILRTQ 1268
Cdd:COG5022  1090 ENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISK-FLSQLVNTLEPVFQKLSVLQLELDGLFWE 1162

MYSc

cd00124

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

83-750

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: 868.06 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMG-DMDPHIFAVAEEAYKQMARDEKNQSIIV 161
Cdd:cd00124     1 AAILHNLRERY-ARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  162 SGESGAGKTVSAKYAMRYFATVGGSASD------TNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHII 235
Cdd:cd00124    80 SGESGAGKTETTKLVLKYLAALSGSGSSkssssaSSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  236 GANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAH----GGNTTIEGVNDADDFEKTRQA 311
Cdd:cd00124   160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDylnsSGCDRIDGVDDAEEFQELLDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  312 LTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSISPQD-EHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVK 390
Cdd:cd00124   240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADdESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  391 TMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQH--SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNS 468
Cdd:cd00124   320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  469 HVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHF-QKPRMSNT 546
Cdd:cd00124   400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFfSKKRKAKL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  547 AFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKfplvadlfhddkdsapatntaknrssskinvrssrplikvpn 626
Cdd:cd00124   480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  627 kehkksvgyQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFN 706
Cdd:cd00124   518 ---------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 569003409  707 RYRVLMKKR-ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd00124   589 RYRILAPGAtEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633

Myo5b_CBD

cd15477

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

1475-1846

0e+00

Pssm-ID: 271261 Cd Length: 372 Bit Score: 784.05 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1475 KEDEALLIRNLVTDLKPQMLSGTVPCLPAYILYMCIRHADYTNDDLKVHSLLSSTINGIKKVLKKHNDDFEMTSFWLSNT 1554
Cdd:cd15477     1 KEDEALLIRNLVTDLKPQAVSATVPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLANT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1555 CRFLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGLLQPMIVSAMLENESIQGLSGV 1634
Cdd:cd15477    81 CRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1635 RPTGYRKRSSSMVDGENSYCLEAIVRQMNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLR 1714
Cdd:cd15477   161 KPMGYRKRSSSMADGDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQLR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1715 YNISQLEEWLRGKNLHQSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERVTVSF 1794
Cdd:cd15477   241 YNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVSF 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569003409 1795 IRTIQAQLQERNDPQQLLLDSKHVFPVLFPYNPSALTMDSIHIPACLNLEFL 1846
Cdd:cd15477   321 IRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372

MYSc_class_II

cd01377

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

83-750

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: 775.10 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd01377     1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASDT--------NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHI 234
Cdd:cd01377    80 GESGAGKTENTKKVIQYLASVAASSKKKkesgkkkgTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  235 IGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKE--LALTCAEDFFYTAHgGNTTIEGVNDADDFEKTRQAL 312
Cdd:cd01377   160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGAD-PELKEklLLTGDPSYYFFLSQ-GELTIDGVDDAEEFKLTDEAF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  313 TLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSISPQDEhLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTM 392
Cdd:cd01377   238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEE-ADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQ 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  393 SLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFK 472
Cdd:cd01377   317 NKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFV 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  473 LEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSN---TA 547
Cdd:cd01377   397 LEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKkseAH 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  548 FIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSkinvrssrplikvpnk 627
Cdd:cd01377   477 FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGS---------------- 540

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  628 ehKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNR 707
Cdd:cd01377   541 --FRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQR 618

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 569003409  708 YRVLMKKRELTNTDKKN-ICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd01377   619 YSILAPNAIPKGFDDGKaACEKILKALQLDPELYRIGNTKVFFK 662

MYSc_Myo11

cd01384

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

83-750

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: 772.62 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIV 161
Cdd:cd01384     1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  162 SGESGAGKTVSAKYAMRYFATVGGSASD--TNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANM 239
Cdd:cd01384    80 SGESGAGKTETTKMLMQYLAYMGGRAVTegRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  240 RTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRD 319
Cdd:cd01384   160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  320 SHQISIFKIIASILHLGSVEIQSERDGDSCSISPQD--EHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQV 397
Cdd:cd01384   240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKseFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  398 VNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEE 477
Cdd:cd01384   320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  478 YMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFADK 556
Cdd:cd01384   400 YTKEEIDWSYIEFVDNQDVLDLIEKKpGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGD 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  557 VEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkdsaPATNTAKNRSSSKINvrssrplikvpnkehkkSVGYQ 636
Cdd:cd01384   480 VTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-------PPLPREGTSSSSKFS-----------------SIGSR 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  637 FRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKRE 716
Cdd:cd01384   536 FKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL 615

                         650       660       670
                  ....*....|....*....|....*....|....
gi 569003409  717 LTNTDKKNICKSVLESLikDPDKFQFGRTKIFFR 750
Cdd:cd01384   616 KGSDDEKAACKKILEKA--GLKGYQIGKTKVFLR 647

MYSc_Myo7

cd01381

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

84-750

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: 733.29 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd01381     2 GILRNLLIRY-REKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSASdtNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYL 243
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAISGQHS--WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  244 LEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSHQI 323
Cdd:cd01381   159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  324 SIFKIIASILHLGSVE-IQSERDG-DSCSIsPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNAR 401
Cdd:cd01381   239 DIFKLLAAILHLGNIKfEATVVDNlDASEV-RDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  402 DALAKHIYAQLFSWIVEHINKALHTSLKQHSF---IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEY 478
Cdd:cd01381   318 DAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEY 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  479 MKEQIPWTLIDFYDNQPCIDLI-EAKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRM-SNTAFIVNHFADK 556
Cdd:cd01381   398 DKEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSdLNTSFGINHFAGV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  557 VEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhdDKDSAPATNTAKNRssskinvrssrplikvpnkehkKSVGYQ 636
Cdd:cd01381   478 VFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF--NEDISMGSETRKKS----------------------PTLSSQ 533

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  637 FRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKRE 716
Cdd:cd01381   534 FRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIP 613

                         650       660       670
                  ....*....|....*....|....*....|....*
gi 569003409  717 -LTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd01381   614 pAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648

MYSc_Myo8

cd01383

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

83-750

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: 731.04 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDmdPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd01383     1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSasDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTY 242
Cdd:cd01383    78 GESGAGKTETAKIAMQYLAALGGG--SSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  243 LLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSHQ 322
Cdd:cd01383   156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  323 ISIFKIIASILHLGSVEIQsERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARD 402
Cdd:cd01383   236 EHIFQMLAAVLWLGNISFQ-VIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARD 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  403 ALAKHIYAQLFSWIVEHINKALHTSLKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKE 481
Cdd:cd01383   315 ALAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELD 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  482 QIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRmsNTAFIVNHFADKVEYL 560
Cdd:cd01383   395 GIDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  561 SDGFLEKNRDTVYEEQINILKASK---FPLVADLFHDDKDsAPATNTAKNRSSSKinvrssrplikvpnkehKKSVGYQF 637
Cdd:cd01383   473 TSGFLEKNRDLLHSDLIQLLSSCScqlPQLFASKMLDASR-KALPLTKASGSDSQ-----------------KQSVATKF 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  638 RTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKREL 717
Cdd:cd01383   535 KGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVS 614

                         650       660       670
                  ....*....|....*....|....*....|...
gi 569003409  718 TNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd01383   615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647

MYSc_Myo22

cd14883

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

84-750

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: 722.96 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14883     2 GINTNLKVRY-KKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSASdtNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYL 243
Cdd:cd14883    81 ESGAGKTETTKLILQYLCAVTNNHS--WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  244 LEKSRVVFQADDERNYHIFYQLCAAASL-PEFKE-LALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSH 321
Cdd:cd14883   159 LEQSRITFQAPGERNYHVFYQLLAGAKHsKELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  322 QISIFKIIASILHLGSVEIQsERDGDSCSISPQD-EHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNA 400
Cdd:cd14883   239 QEGIFSVLSAILHLGNLTFE-DIDGETGALTVEDkEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  401 RDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMK 480
Cdd:cd14883   318 RDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEK 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  481 EQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKP--RMSNTAFIVNHFADKV 557
Cdd:cd14883   398 EGINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPdrRRWKTEFGVKHYAGEV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  558 EYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKINVRSSRplikvpnkehKKSVGYQF 637
Cdd:cd14883   478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRGTSKG----------KPTVGDTF 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  638 RTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKK-RE 716
Cdd:cd14883   548 KHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRaRS 627

                         650       660       670
                  ....*....|....*....|....*....|....
gi 569003409  717 LTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14883   628 ADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661

MYSc_Myo1

cd01378

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

84-750

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: 704.31 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd01378     2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSaSDTNIE---EKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMR 240
Cdd:cd01378    81 ESGAGKTEASKRIMQYIAAVSGG-SESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  241 TYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDS 320
Cdd:cd01378   160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  321 HQISIFKIIASILHLGSVEIQSERDGDScSISpqDEHLSNF-CSLLGIEHSQMEHWLCHRKLVTTSE---TYVKTMSLQQ 396
Cdd:cd01378   240 EQDSIFRILAAILHLGNIQFAEDEEGNA-AIS--DTSVLDFvAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQ 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  397 VVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQ 475
Cdd:cd01378   317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKkVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  476 EEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECK-VPKGTDQNWAQKLYERHSNSQHFQKP----RMSNTAFI 549
Cdd:cd01378   397 EEYVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLtAGDATDQTFLQKLNQLFSNHPHFECPsghfELRRGEFR 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  550 VNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDsapatntaknRSSSKinvrssRPLikvpnkeh 629
Cdd:cd01378   477 IKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD----------LDSKK------RPP-------- 532

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  630 kkSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYR 709
Cdd:cd01378   533 --TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 569003409  710 VLMKKRELT-NTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd01378   611 LLSPKTWPAwDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652

MYSc_Myo6

cd01382

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

86-750

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: 642.38 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   86 LHNLKVRFLEsNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSGE 164
Cdd:cd01382     4 LNNIRVRYSK-DKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  165 SGAGKTVSAKYAMRYFATVGGSaSDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYLL 244
Cdd:cd01382    83 SGAGKTESTKYILRYLTESWGS-GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  245 EKSRVVFQADDERNYHIFYQLCAAASLPEFKELaltcaedffytahggnTTIEGVNDADDFEKTRQALTLLGVRDSHQIS 324
Cdd:cd01382   162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEKLD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  325 IFKIIASILHLGSVEIQSERDGDS--CSISPQDEH-LSNFCSLLGIEHSQMEHWLCHRKLVTTSE-----TYVKTMSLQQ 396
Cdd:cd01382   226 IFRVVAAVLHLGNIEFEENGSDSGggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgtVIKVPLKVEE 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  397 VVNARDALAKHIYAQLFSWIVEHINKALHTSlKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQE 476
Cdd:cd01382   306 ANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  477 EYMKEQIPWTLIDFYDNQPCIDLIEAKL-GILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMS----------N 545
Cdd:cd01382   385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPRKSklkihrnlrdD 464

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  546 TAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDdkdsapATNTAKNRSSSKinvrssrplikvp 625
Cdd:cd01382   465 EGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFES------STNNNKDSKQKA------------- 525

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  626 NKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFF 705
Cdd:cd01382   526 GKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLY 605

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 569003409  706 NRYRVLMKKrELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd01382   606 NMYKKYLPP-KLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649

MYSc_Myo42

cd14903

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

83-750

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: 624.11 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIV 161
Cdd:cd14903     1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  162 SGESGAGKTVSAKYAMRYFATVGGSASDTNIEeKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRT 241
Cdd:cd14903    80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  242 YLLEKSRVVFQADDERNYHIFYQLCAAASLPEfkELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSH 321
Cdd:cd14903   159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  322 QISIFKIIASILHLGSVEIQSERDGDSCSIS-PQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNA 400
Cdd:cd14903   237 QEVLFEVLAGILHLGQLQIQSKPNDDEKSAIaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  401 RDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMK 480
Cdd:cd14903   317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  481 EQIPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQH-FQKPRMSNTAFIVNHFADKVEY 559
Cdd:cd14903   397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDvIEFPRTSRTQFTIKHYAGPVTY 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  560 LSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKinvRSSRPLikvpnkeHKKSVGYQFRT 639
Cdd:cd14903   477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARR---RRGGAL-------TTTTVGTQFKD 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  640 SLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKRELTN 719
Cdd:cd14903   547 SLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTD 626

                         650       660       670
                  ....*....|....*....|....*....|..
gi 569003409  720 TDKKNICKSVLESL-IKDPDKFQFGRTKIFFR 750
Cdd:cd14903   627 VPVAERCEALMKKLkLESPEQYQMGLTRIYFQ 658

MYSc_Myo4

cd14872

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

83-750

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: 620.25 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLEsNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14872     1 AMIVHNLRKRFKN-DQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSasDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTY 242
Cdd:cd14872    80 GESGAGKTEATKQCLSFFAEVAGS--TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  243 LLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTahGGNTTIEGVNDADDFEKTRQALTLLGVRDSHQ 322
Cdd:cd14872   158 LLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSL--SGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  323 ISIFKIIASILHLGSVEIQSERDGDSCSISPQ--DEHLSNFCSLLGIEHSQMEHWLCHRKL-VTTSETYVKTMSLQQVVN 399
Cdd:cd14872   236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanRDVLKEVATLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQATD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  400 ARDALAKHIYAQLFSWIVEHINKALH-TSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEY 478
Cdd:cd14872   316 ACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  479 MKEQIPWTLIDFYDNQPCIDLIEAKL-GILDLLDEECKVPKGTDQNWAQKLYERHSNSQHF--QKPRMSNTAFIVNHFAD 555
Cdd:cd14872   396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFvyAEVRTSRTEFIVKHYAG 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  556 KVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkdsapatntaknrssskinvrssrPLIKVPNKEHKKSVGY 635
Cdd:cd14872   476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF---------------------------PPSEGDQKTSKVTLGG 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  636 QFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKR 715
Cdd:cd14872   529 QFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTI 608

                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 569003409  716 ELTN-TDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14872   609 AKRVgPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644

MYSc_Myo9

cd01385

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

86-750

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: 615.15 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   86 LHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSGES 165
Cdd:cd01385     4 LENLRARF-KHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  166 GAGKTVSAKYAMRYFATVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYLLE 245
Cdd:cd01385    83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  246 KSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSHQISI 325
Cdd:cd01385   163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  326 FKIIASILHLGSVEIQSERDGDSCSISPQD-EHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARDAL 404
Cdd:cd01385   243 FSVLSAVLHLGNIEYKKKAYHRDESVTVGNpEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAM 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  405 AKHIYAQLFSWIVEHINKAL----HTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMK 480
Cdd:cd01385   323 AKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKK 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  481 EQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFADKVEY 559
Cdd:cd01385   403 EGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGKVKY 482

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  560 LSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDD--------------------KDSAPATNTAKNRSSSKINVRSSR 619
Cdd:cd01385   483 QIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDpvavfrwavlrafframaafREAGRRRAQRTAGHSLTLHDRTTK 562

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  620 PLIKVPNKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRW 699
Cdd:cd01385   563 SLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRY 642

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 569003409  700 TYHDFFNRYRVLMKKRELTNtdKKNICKsVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd01385   643 TFQEFITQFQVLLPKGLISS--KEDIKD-FLEKLNLDRDNYQIGKTKVFLK 690

MYSc_Myo10

cd14873

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

84-750

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: 614.11 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14873     2 SIMYNLFQRY-KRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATV-------GGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHII 235
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVIsqqslelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  236 GANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLL 315
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  316 GVRDSHQISIFKIIASILHLGSVEIQSErdgDSCSISPQDEhLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQ 395
Cdd:cd14873   241 QFSKEEVREVSRLLAGILHLGNIEFITA---GGAQVSFKTA-LGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQ 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  396 QVVNARDALAKHIYAQLFSWIVEHINKALHTSlKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQ 475
Cdd:cd14873   317 QAVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  476 EEYMKEQIPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFAD 555
Cdd:cd14873   396 LEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAG 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  556 KVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhdDKDSApatntaknrssskinvRSSRPLIKVPNKEHKKSVGY 635
Cdd:cd14873   476 EVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF--EHVSS----------------RNNQDTLKCGSKHRRPTVSS 537

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  636 QFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKR 715
Cdd:cd14873   538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617

                         650       660       670
                  ....*....|....*....|....*....|....*
gi 569003409  716 ELtNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14873   618 AL-PEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651

MYSc_Myo15

cd01387

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

84-750

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: 603.67 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd01387     2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSASdTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFdKKYHIIGANMRTYL 243
Cdd:cd01387    81 ESGSGKTEATKLIMQYLAAVNQRRN-NLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  244 LEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSHQI 323
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  324 SIFKIIASILHLGSV--EIQSERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNAR 401
Cdd:cd01387   239 SIFRILASVLHLGNVyfHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDAR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  402 DALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKE 481
Cdd:cd01387   319 DAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIRE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  482 QIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFADKVEYL 560
Cdd:cd01387   399 QIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYAGQVWYQ 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  561 SDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkdsAPATNTAKNRSSSKINVRSSRPLIKVPnkehkkSVGYQFRTS 640
Cdd:cd01387   479 VHGFLDKNRDQLRQDVLELLVSSRTRVVAHLF------SSHRAQTDKAPPRLGKGRFVTMKPRTP------TVAARFQDS 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  641 LNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKReLTNT 720
Cdd:cd01387   547 LLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK-LPRP 625

                         650       660       670
                  ....*....|....*....|....*....|..
gi 569003409  721 DKKNICKSVLESLIKDP--DKFQFGRTKIFFR 750
Cdd:cd01387   626 APGDMCVSLLSRLCTVTpkDMYRLGATKVFLR 657

MYSc_Myo40

cd14901

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

83-748

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: 599.47 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAY---SGQNMGD---MDPHIFAVAEEAYKQMARDEK- 155
Cdd:cd14901     1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  156 ---NQSIIVSGESGAGKTVSAKYAMRYFATV-------GGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIE 225
Cdd:cd14901    80 qkcDQSILVSGESGAGKTETTKIIMNYLASVssatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  226 IGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFY-TAHGGNTTIEGVNDADD 304
Cdd:cd14901   160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYlNSSQCYDRRDGVDDSVQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  305 FEKTRQALTLLGVRDSHQISIFKIIASILHLGSVE-IQSERDGDSCSISpqdeHLSNF---CSLLGIEHSQMEHWLCHRK 380
Cdd:cd14901   240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMS----SLANVraaCDLLGLDMDVLEKTLCTRE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  381 LVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKAL--HTSLKQHSFIGVLDIYGFETFEINSFEQFCINYA 458
Cdd:cd14901   316 IRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFA 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  459 NEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQH 537
Cdd:cd14901   396 NEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHAS 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  538 F--QKPRMSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVadlfhddkdsaPATNTAKnrssskinv 615
Cdd:cd14901   476 FsvSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL-----------SSTVVAK--------- 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  616 rssrplikvpnkehkksvgyqFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGY 695
Cdd:cd14901   536 ---------------------FKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGY 594

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569003409  696 PSRWTYHDFFNRYRVLM--------KKRELTNTDKKNICKSVLesLIKDPDKFQFGRTKIF 748
Cdd:cd14901   595 PVRFPHDAFVHTYSCLApdgasdtwKVNELAERLMSQLQHSEL--NIEHLPPFQVGKTKVF 653

MYSc_Myo29

cd14890

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

84-750

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: 591.36 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMAR----DEKNQS 158
Cdd:cd14890     2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  159 IIVSGESGAGKTVSAKYAMRYFATV-----------------GGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFG 221
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLARItsgfaqgasgegeaaseAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  222 KFIEIGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGgNTTIEGVND 301
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGE-CSSIPSCDD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  302 ADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKL 381
Cdd:cd14890   240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  382 VTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEK 461
Cdd:cd14890   320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  462 LQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAKL----GILDLLDeECKVPKGTDQNW------------- 524
Cdd:cd14890   400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLD-DCWRFKGEEANKkfvsqlhasfgrk 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  525 AQKLYERHSNSQH--FQKPRMSNT-AFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKaskfplvadlfhddkdsapa 601
Cdd:cd14890   479 SGSGGTRRGSSQHphFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIK-------------------- 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  602 tntaknrsSSKINVRSsrplikvpnkehkKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRA 681
Cdd:cd14890   539 --------QSRRSIRE-------------VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKY 597

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003409  682 CGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKREltntDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14890   598 SGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAE----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662

MYSc_Myo27

cd14888

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

83-750

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: 585.89 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYSgQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIV 161
Cdd:cd14888     1 ASILHSLNLRF-DIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  162 SGESGAGKTVSAKYAMRYFATVGGSASD--TNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDK--------- 230
Cdd:cd14888    79 SGESGAGKTESTKYVMKFLACAGSEDIKkrSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsgd 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  231 KYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlpEFKELALTCAEDFFYTAHGGNT---------------- 294
Cdd:cd14888   159 RGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAR--EAKNTGLSYEENDEKLAKGADAkpisidmssfephlkf 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  295 ---------TIEGVNDADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSI--SPQDEHLSNFCS 363
Cdd:cd14888   237 ryltksschELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVvsASCTDDLEKVAS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  364 LLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKAL-HTSLKQHSFIGVLDIYGF 442
Cdd:cd14888   317 LLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLFCGVLDIFGF 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  443 ETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTD 521
Cdd:cd14888   397 ECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKD 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  522 QNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPA 601
Cdd:cd14888   477 QGLCNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAYLRRGTD 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  602 TNTAKNRssskinvrssrplikvpnkehKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRA 681
Cdd:cd14888   557 GNTKKKK---------------------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKY 615

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003409  682 CGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKREltntdKKNIcksvleslikdpDKFQFGRTKIFFR 750
Cdd:cd14888   616 GGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNGEG-----KKQL------------SIWAVGKTLCFFK 667

Myo5_CBD

cd15470

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

1476-1842

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: 569.92 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1476 EDEALLIRNLVTDLKPQMLSGTVPCLPAYILYMCIRHADYTNDDLKVHSLLSSTINGIKKVLKKHNDDFEMTSFWLSNTC 1555
Cdd:cd15470     1 EDESRLIKNLITDLKPRGAVGLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNTC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1556 RFLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGLLQPmivsamlenesiqglsgvr 1635
Cdd:cd15470    81 RLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1636 ptgyrkrsssmvdgensyCLEAIVRQMNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLRY 1715
Cdd:cd15470   142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1716 NISQLEEWLRGKNLHQSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERVTVSFI 1795
Cdd:cd15470   204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 569003409 1796 RTIQAQLQERND--PQQLLLDSKHVFPVLFPYNPSALTMDSIHIPACLN 1842
Cdd:cd15470   284 RKVQARLNERADsnQLQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332

MYSc_Myo3

cd01379

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

83-750

3.05e-179

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: 556.12 E-value: 3.05e-179

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd01379     1 DTIVSQLQKRY-SRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFaTVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTY 242
Cdd:cd01379    80 GESGAGKTESANLLVQQL-TVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  243 LLEKSRVVFQADDERNYHIFYQLCAAasLPEFKELA---LTCAEDFFYTAHGGNTTIEGVNDA---DDFEKTRQALTLLG 316
Cdd:cd01379   159 LLEKSRVVHQAIGERNFHIFYYIYAG--LAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  317 VRDSHQISIFKIIASILHLGSVE---IQSERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMS 393
Cdd:cd01379   237 FTKEEVDSVYSILAAILHIGDIEfteVESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  394 LQQVVNARDALAKHIYAQLFSWIVEHINKAL----HTSLKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSH 469
Cdd:cd01379   317 VEEATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  470 VFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLyerHSN--SQHFQKPRMSNT 546
Cdd:cd01379   396 IFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKF---HNNikSKYYWRPKSNAL 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  547 AFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVadlfhddkdsapatntaknrssskinvrssrplikvpn 626
Cdd:cd01379   473 SFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-------------------------------------- 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  627 kehKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFN 706
Cdd:cd01379   515 ---RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLK 591

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 569003409  707 RYRVLMKKRELTNTDKKNICKSVLESLikDPDKFQFGRTKIFFR 750
Cdd:cd01379   592 RYYFLAFKWNEEVVANRENCRLILERL--KLDNWALGKTKVFLK 633

MYSc_Myo43

cd14904

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

83-750

5.50e-179

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

Pssm-ID: 276869 Cd Length: 653 Bit Score: 556.09 E-value: 5.50e-179

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLESNHiYTYCGIVLVAINPYEQLP-IYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIV 161
Cdd:cd14904     1 PSILFNLKKRFAASKP-YTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  162 SGESGAGKTVSAKYAMRYFATVGGSASDTNIEeKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRT 241
Cdd:cd14904    80 SGESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  242 YLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHG-GNTTIEGVNDADDFEKTRQALTLLGVRDS 320
Cdd:cd14904   159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLDND 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  321 HQISIFKIIASILHLGsvEIQSERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNA 400
Cdd:cd14904   239 AQRTLFKILSGVLHLG--EVMFDKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEEN 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  401 RDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYM 479
Cdd:cd14904   317 RDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYI 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  480 KEQIPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERHS---NSQHFQKPRMSNTAFIVNHFADK 556
Cdd:cd14904   397 REGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkDNESIDFPKVKRTQFIINHYAGP 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  557 VEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkDSAPATNTAKNRSSSKinvrssrplikvpNKEHKKSVGYQ 636
Cdd:cd14904   477 VTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF----GSSEAPSETKEGKSGK-------------GTKAPKSLGSQ 539

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  637 FRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYrVLMKKRE 716
Cdd:cd14904   540 FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY-AIMFPPS 618

                         650       660       670
                  ....*....|....*....|....*....|....*
gi 569003409  717 LTNTDKKNICKSVLESL-IKDPDKFQFGRTKIFFR 750
Cdd:cd14904   619 MHSKDVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653

MYSc_Myh15_mammals

cd14929

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

83-750

8.12e-178

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: 553.43 E-value: 8.12e-178

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlesNH--IYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSII 160
Cdd:cd14929     1 ASVLHTLRRRY---DHwmIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  161 VSGESGAGKTVSAKYAMRYFATVGGSASDT----NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIG 236
Cdd:cd14929    78 FTGESGAGKTVNTKHIIQYFATIAAMIESKkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  237 ANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlpEFKELALTCA--EDFFYTAHGGnTTIEGVNDADDFEKTRQALTL 314
Cdd:cd14929   158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSAnpSDFHFCSCGA-VAVESLDDAEELLATEQAMDI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  315 LGVRDSHQISIFKIIASILHLGSV-------EIQSERDGDscsispqdEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSET 387
Cdd:cd14929   235 LGFLPDEKYGCYKLTGAIMHFGNMkfkqkprEEQLEADGT--------ENADKAAFLMGINSSELVKGLIHPRIKVGNEY 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  388 YVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFN 467
Cdd:cd14929   307 VTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFN 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  468 SHVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPRMSN 545
Cdd:cd14929   387 QHMFVLEQEEYRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDK 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  546 TAFIVN----HFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKnrssskinvrssrpl 621
Cdd:cd14929   467 KKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGE--------------- 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  622 ikvpnKEHKKSVGYQFRTSL-----NLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYP 696
Cdd:cd14929   532 -----KKRKKGASFQTVASLhkenlNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFP 606

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569003409  697 SRWTYHDFFNRYRVL----MKKRELTNTDKKniCKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14929   607 NRLLYADFKQRYCILnprtFPKSKFVSSRKA--AEELLGSLEIDHTQYRFGITKVFFK 662

Myo5a_CBD

cd15478

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

1475-1849

4.03e-176

Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.

Pssm-ID: 271262 Cd Length: 375 Bit Score: 537.31 E-value: 4.03e-176

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1475 KEDEALLIRNLVTDLKPQMLS-GTVPCLPAYILYMCIRHADYTNDDLKVHSLLSSTINGIKKVLKKHNDDFEMTSFWLSN 1553
Cdd:cd15478     1 KEDEQKLVKNLILELKPRGVAvNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1554 TCRFLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGLLQPMIVSAMLENESIQGLSG 1633
Cdd:cd15478    81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1634 VRPTGYRKRSSSMVDgENSYCLEAIVRQMNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQL 1713
Cdd:cd15478   161 VKPTGLRKRTSSIAD-EGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1714 RYNISQLEEWLRGKNLHQSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERVTVS 1793
Cdd:cd15478   240 RYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVS 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003409 1794 FIRTIQAQLQERNDPQQLLLDSKHVFPVLFPYNPSALTMDSIHIPACLNLEFLNEV 1849
Cdd:cd15478   320 FIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375

MYSc_Myo31

cd14892

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

84-750

4.14e-176

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: 548.59 E-value: 4.14e-176

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMD---PHIFAVAEEAYKQMARDEKN---- 156
Cdd:cd14892     1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASsppPHVFSIAERAYRAMKGVGKGqgtp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  157 QSIIVSGESGAGKTVSAKYAMRYFATV-----GGSASDT------NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIE 225
Cdd:cd14892    81 QSIVVSGESGAGKTEASKYIMKYLATAsklakGASTSKGaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  226 IGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDF 305
Cdd:cd14892   161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  306 EKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQS-ERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTT 384
Cdd:cd14892   241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  385 SETYVK-TMSLQQVVNARDALAKHIYAQLFSWIVEHINKAL--HTSL--------KQHSFIGVLDIYGFETFEINSFEQF 453
Cdd:cd14892   321 RGSVLEiKLTAREAKNALDALCKYLYGELFDWLISRINACHkqQTSGvtggaaspTFSPFIGILDIFGFEIMPTNSFEQL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  454 CINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVP-KGTDQNWAQKLYER 531
Cdd:cd14892   401 CINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKrKTTDKQLLTIYHQT 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  532 H-SNSQHFQKPRMSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILkaskfplvadlfhddkdsapatntaknRSS 610
Cdd:cd14892   481 HlDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLL---------------------------RSS 533

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  611 SKinvrssrplikvpnkehkksvgyqFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRI 690
Cdd:cd14892   534 SK------------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003409  691 SAAGYPSRWTYHDFFNRYRVLMKKR---------ELTNTDKKNICKSVLESLikDPDKFQFGRTKIFFR 750
Cdd:cd14892   590 RREGFPIRRQFEEFYEKFWPLARNKagvaaspdaCDATTARKKCEEIVARAL--ERENFQLGRTKVFLR 656

MYSc_Myh10

cd14920

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

84-750

7.67e-175

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: 545.76 E-value: 7.67e-175

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14920     2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGS-------ASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIG 236
Cdd:cd14920    81 ESGAGKTENTKKVIQYLAHVASShkgrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  237 ANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAhGGNTTIEGVNDADDFEKTRQALTLLG 316
Cdd:cd14920   161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  317 VRDSHQISIFKIIASILHLGSVEIQSERDGDSCSIsPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQ 396
Cdd:cd14920   240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM-PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  397 VVNARDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQ 475
Cdd:cd14920   319 ADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  476 EEYMKEQIPWTLIDF-YDNQPCIDLIEAKL---GILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRM--SNTAFI 549
Cdd:cd14920   399 EEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlkDKADFC 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  550 VNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTaknrssSKINVRSSRPLIKVpNKEH 629
Cdd:cd14920   479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQV------TGMTETAFGSAYKT-KKGM 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  630 KKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYR 709
Cdd:cd14920   552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 569003409  710 VLMKKR-ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14920   632 ILTPNAiPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673

MYSc_Myh7b

cd14927

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

84-750

8.33e-174

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: 543.01 E-value: 8.33e-174

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14927     2 SVLHNLRRRY-SRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVG-------------GSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDK 230
Cdd:cd14927    81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  231 KYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELALTCAEDF-FYTAHGGNTTIEGVNDADDFEKTR 309
Cdd:cd14927   161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK-PELQDMLLVSMNPYdYHFCSQGVTTVDNMDDGEELMATD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  310 QALTLLGVRDSHQISIFKIIASILHLGSV-------EIQSERDGDscsispqdEHLSNFCSLLGIEHSQMEHWLCHRKLV 382
Cdd:cd14927   240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMkfkqkqrEEQAEADGT--------ESADKAAYLMGVSSADLLKGLLHPRVK 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  383 TTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 462
Cdd:cd14927   312 VGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKL 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  463 QQQFNSHVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQK 540
Cdd:cd14927   392 QQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQK 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  541 PRMSN-----TAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddKDSAPATNTAKNRSSSKINV 615
Cdd:cd14927   472 PRPDKkrkyeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTEDPKSGVKEKR 548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  616 RSSRPLIKVpNKEHKKsvgyqfrtSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGY 695
Cdd:cd14927   549 KKAASFQTV-SQLHKE--------NLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGF 619

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569003409  696 PSRWTYHDFFNRYRVLMKKR--ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14927   620 PNRILYADFKQRYRILNPSAipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676

MYSc_Myh2_insects_mollusks

cd14911

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

84-750

6.46e-171

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: 535.33 E-value: 6.46e-171

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14911     2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSASDTN----------------IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIG 227
Cdd:cd14911    81 ESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  228 FDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHgGNTTIEGVNDADDFEK 307
Cdd:cd14911   161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSN-GSLPVPGVDDYAEFQA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  308 TRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSIsPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSET 387
Cdd:cd14911   240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATL-PDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  388 YVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 466
Cdd:cd14911   319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  467 NSHVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSN 545
Cdd:cd14911   399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  546 TA-FIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAknrSSSKINVRSSRPLIkv 624
Cdd:cd14911   479 VAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQAL---TDTQFGARTRKGMF-- 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  625 pnkehkKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDF 704
Cdd:cd14911   554 ------RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 627

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569003409  705 FNRYRVLMKkreltNT------DKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14911   628 RQRYELLTP-----NVipkgfmDGKKACEKMIQALELDSNLYRVGQSKIFFR 674

MYSc_Myh3

cd14913

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

83-750

3.51e-170

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: 533.09 E-value: 3.51e-170

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14913     1 PAVLYNLKDRY-TSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGG---------SASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYH 233
Cdd:cd14913    80 GESGAGKTVNTKRVIQYFATIAAtgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  234 IIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELAL--TCAEDFFYTAHGgNTTIEGVNDADDFEKTRQA 311
Cdd:cd14913   160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKK-PELIELLLitTNPYDYPFISQG-EILVASIDDAEELLATDSA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  312 LTLLGVRDSHQISIFKIIASILHLGSV-------EIQSERDGDscsispqdEHLSNFCSLLGIEHSQMEHWLCHRKLVTT 384
Cdd:cd14913   238 IDILGFTPEEKSGLYKLTGAVMHYGNMkfkqkqrEEQAEPDGT--------EVADKTAYLMGLNSSDLLKALCFPRVKVG 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  385 SETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQ 464
Cdd:cd14913   310 NEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQ 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  465 QFNSHVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPR 542
Cdd:cd14913   390 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPK 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  543 M----SNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkdsapATNTAKNRSSSKINVRSS 618
Cdd:cd14913   470 VvkgrAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATADADSGKKKVAKK 541

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  619 RplikvpnKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSR 698
Cdd:cd14913   542 K-------GSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNR 614

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 569003409  699 WTYHDFFNRYRVLMKKR--ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14913   615 ILYGDFKQRYRVLNASAipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668

MYSc_Myo47

cd14908

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

83-750

1.27e-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: 526.78 E-value: 1.27e-167

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAY------SGQNM---GDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14908     1 PAILHSLSRRF-FRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  154 -EKNQSIIVSGESGAGKTVSAKYAMRYFATVG----------GSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGK 222
Cdd:cd14908    80 iRASQSILISGESGAGKTESTKIVMLYLTTLGngeegapnegEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  223 FIEIGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAAS--------LPEFKELALTCAEDFFYTAHGGNT 294
Cdd:cd14908   160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDeeehekyeFHDGITGGLQLPNEFHYTGQGGAP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  295 TIEGVNDADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSISPQDEH--LSNFCSLLGIEHSQM 372
Cdd:cd14908   240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEkcLARVAKLLGVDVDKL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  373 EHWLCHRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQ--HSFIGVLDIYGFETFEINSF 450
Cdd:cd14908   320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  451 EQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEA-KLGILDLLDEECKVP-KGTDQNWAQKL 528
Cdd:cd14908   400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  529 YERH---SNSQHFQKPRMSNTA-------FIVNHFADKVEY-LSDGFLEKNRDTVyeeqinilkaskfPLVAD-LFHDdk 596
Cdd:cd14908   480 YETYlpeKNQTHSENTRFEATSiqktkliFAVRHFAGQVQYtVETTFCEKNKDEI-------------PLTADsLFES-- 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  597 dsapatntaknrssskinvrssrplikvpnkehkksvGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAV 676
Cdd:cd14908   545 -------------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVT 587

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  677 QQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVL------------MKKRELTNTDKKNICKSVLESLIKDP------- 737
Cdd:cd14908   588 EQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLlplipevvlswsMERLDPQKLCVKKMCKDLVKGVLSPAmvsmkni 667

                         730
                  ....*....|....*
gi 569003409  738 --DKFQFGRTKIFFR 750
Cdd:cd14908   668 peDTMQLGKSKVFMR 682

MYSc_Myh1_insects_crustaceans

cd14909

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

83-750

2.01e-166

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: 522.86 E-value: 2.01e-166

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14909     1 ASVLHNLRQRYY-AKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASDT-------NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHII 235
Cdd:cd14909    80 GESGAGKTENTKKVIAYFATVGASKKTDeaakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  236 GANMRTYLLEKSRVVFQADDERNYHIFYQLcAAASLPEFKELALTCAE--DFFYTAHGgNTTIEGVNDADDFEKTRQALT 313
Cdd:cd14909   160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLLSDNiyDYYIVSQG-KVTVPNVDDGEEFSLTDQAFD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  314 LLGVRDSHQISIFKIIASILHLGSV-------EIQSERDGDscsispqdEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSE 386
Cdd:cd14909   238 ILGFTKQEKEDVYRITAAVMHMGGMkfkqrgrEEQAEQDGE--------EEGGRVSKLFGCDTAELYKNLLKPRIKVGNE 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  387 TYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 466
Cdd:cd14909   310 FVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  467 NSHVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPRMS 544
Cdd:cd14909   390 NHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPP 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  545 NTA-----FIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKINVRSsr 619
Cdd:cd14909   470 KPGqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFA-- 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  620 plikvpnkehkkSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRW 699
Cdd:cd14909   548 ------------TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRM 615

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 569003409  700 TYHDFFNRYRVLMKKRELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14909   616 MYPDFKMRYKILNPAGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666

MYSc_Myo46

cd14907

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

85-750

1.12e-165

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: 521.13 E-value: 1.12e-165

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFLEsNHIYTYCGIVLVAINPYEQLP---------IYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEK 155
Cdd:cd14907     3 LLINLKKRYQQ-DKIFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  156 NQSIIVSGESGAGKTVSAKYAMRYFATVGG------------------SASDTNIEEKVLASSPIMEAIGNAKTTRNDNS 217
Cdd:cd14907    82 KQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  218 SRFGKFIEIGFDKKYH-IIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALT---CAEDFFYTAHGGN 293
Cdd:cd14907   162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlSGDRYDYLKKSNC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  294 TTIEGVNDADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEI-QSERDGDSCSISPQDEHLSNFCSLLGIEHSQM 372
Cdd:cd14907   242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFdDSTLDDNSPCCVKNKETLQIIAKLLGIDEEEL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  373 EHWLCHRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKAL--HTSLKQHSF------IGVLDIYGFET 444
Cdd:cd14907   322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFEV 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  445 FEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTL--IDFYDNQPCIDLIE-AKLGILDLLDEECKVPKGTD 521
Cdd:cd14907   402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLATGTD 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  522 QNWAQKLYERHSNSQHFQKPRMSN-TAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAP 600
Cdd:cd14907   482 EKLLNKIKKQHKNNSKLIFPNKINkDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGSQQ 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  601 ATNTAKNRSSSKinvrssrplikvpnkehKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLR 680
Cdd:cd14907   562 QNQSKQKKSQKK-----------------DKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIR 624

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  681 ACGVLETIRISAAGYPSRWTYHDFFNRYRVLmkkreltntdKKNICksvleslikdpdkfqFGRTKIFFR 750
Cdd:cd14907   625 YLGVLESIRVRKQGYPYRKSYEDFYKQYSLL----------KKNVL---------------FGKTKIFMK 669

MYSc_Myo36

cd14897

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

85-750

3.00e-165

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: 518.48 E-value: 3.00e-165

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDM-DPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14897     3 IVQTLKSRY-NKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSAsDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYL 243
Cdd:cd14897    82 ESGAGKTESTKYMIKHLMKLSPSD-DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  244 LEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDfFYTAHGGNTTIEGVNDADDFEKTRQALT-------LLG 316
Cdd:cd14897   161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDC-HRILRDDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  317 VRDSHQISIFKIIASILHLgsVEIQSERDGDSCSISPQDE-HLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQ 395
Cdd:cd14897   240 FSEEDISVIFTILAAILHL--TNIVFIPDEDTDGVTVADEyPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  396 QVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQH-----SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHV 470
Cdd:cd14897   318 QANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQimtrgPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYV 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  471 FKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSNTAFI 549
Cdd:cd14897   398 FPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNRVAFG 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  550 VNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDdkdsapatntaknrssskinvrssrplikvpnkeh 629
Cdd:cd14897   478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTS----------------------------------- 522

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  630 kksvgyQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYR 709
Cdd:cd14897   523 ------YFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYK 596

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 569003409  710 VLMKKRELTNTDKKNICKSVLESL-IKDpdkFQFGRTKIFFR 750
Cdd:cd14897   597 EICDFSNKVRSDDLGKCQKILKTAgIKG---YQFGKTKVFLK 635

MYSc_Myo30

cd14891

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

83-750

4.67e-163

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: 513.05 E-value: 4.67e-163

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRF-LESNHIYTYCGIVLVAINPYEQLPiygQDVIYAYSGQNMGDMDPHIFAVAEEAYKQM---ARDEKNQS 158
Cdd:cd14891     1 AGILHNLEERSkLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMclgSGRMQNQS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  159 IIVSGESGAGKTVSAKYAMRYFAT--VGGSA---------------SDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFG 221
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFLTTraVGGKKasgqdieqsskkrklSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  222 KFIEIGFDK-KYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVN 300
Cdd:cd14891   158 KFMKLQFTKdKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  301 DADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSE--RDGDSCSISPQD-EHLSNFCSLLGIEHSQMEHWLC 377
Cdd:cd14891   238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEdtSEGEAEIASESDkEALATAAELLGVDEEALEKVIT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  378 HRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEI-NSFEQFCIN 456
Cdd:cd14891   318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLLIN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  457 YANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAKL-GILDLLDEECKVPKGTDQNWAQKLYERHSNS 535
Cdd:cd14891   398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTHKRH 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  536 QHFQKPRMSNT--AFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKfplvadlfhddkdsapatntaknrssski 613
Cdd:cd14891   478 PCFPRPHPKDMreMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA----------------------------- 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  614 nvrssrplikvpnkehkksvgyQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAA 693
Cdd:cd14891   529 ----------------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKV 586

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  694 GYPSRWTYHDFFNRYRVLM---KKRELTNTDKKNIcKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14891   587 GLPTRVTYAELVDVYKPVLppsVTRLFAENDRTLT-QAILWAFRVPSDAYRLGRTRVFFR 645

MYSc_Myh18

cd14932

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

84-750

7.16e-162

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: 511.11 E-value: 7.16e-162

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14932     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSA-----------SDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKY 232
Cdd:cd14932    81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  233 HIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELaltCAEDF--FYTAHGGNTTIEGVNDADDFEKTRQ 310
Cdd:cd14932   161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSEL---CLEDYskYRFLSNGNVTIPGQQDKELFAETME 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  311 ALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSIsPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVK 390
Cdd:cd14932   238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASM-PDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  391 TMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSH 469
Cdd:cd14932   317 AQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  470 VFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIE---AKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPR--M 543
Cdd:cd14932   397 MFILEQEEYQREGIEWSFIDFgLDLQPCIELIEkpnGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKklK 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  544 SNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKINVRSSRPLIk 623
Cdd:cd14932   477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAFKTRKGMF- 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  624 vpnkehkKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHD 703
Cdd:cd14932   556 -------RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 628

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 569003409  704 FFNRYRVLMKKRELTN-TDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14932   629 FRQRYEILTPNAIPKGfMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676

MYSc_Myh11

cd14921

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

84-750

5.91e-159

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: 503.01 E-value: 5.91e-159

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14921     2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGS---ASDTNI----EEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIG 236
Cdd:cd14921    81 ESGAGKTENTKKVIQYLAVVASShkgKKDTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  237 ANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHgGNTTIEGVNDADDFEKTRQALTLLG 316
Cdd:cd14921   161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSN-GFVPIPAAQDDEMFQETLEAMSIMG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  317 VRDSHQISIFKIIASILHLGSVEIQSERDGDSCSIsPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQ 396
Cdd:cd14921   240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASM-PDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  397 VVNARDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQ 475
Cdd:cd14921   319 ADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  476 EEYMKEQIPWTLIDF-YDNQPCIDLIEAKL---GILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRM--SNTAFI 549
Cdd:cd14921   399 EEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQlkDKTEFS 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  550 VNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKnrssskiNVRSSRPLIKVPNKEH 629
Cdd:cd14921   479 IIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAK-------MTESSLPSASKTKKGM 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  630 KKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYR 709
Cdd:cd14921   552 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 569003409  710 VLMKKRELTN-TDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14921   632 ILAANAIPKGfMDGKQACILMIKALELDPNLYRIGQSKIFFR 673

MYSc_Myh7

cd14917

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

83-750

1.65e-157

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: 498.86 E-value: 1.65e-157

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14917     1 PAVLYNLKERY-ASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGG---------SASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYH 233
Cdd:cd14917    80 GESGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  234 IIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELALTCAEDFFYT-AHGGNTTIEGVNDADDFEKTRQAL 312
Cdd:cd14917   160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK-PELLDMLLITNNPYDYAfISQGETTVASIDDAEELMATDNAF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  313 TLLGVRDSHQISIFKIIASILHLGSV-------EIQSERDGDscsispqdEHLSNFCSLLGIEHSQMEHWLCHRKLVTTS 385
Cdd:cd14917   239 DVLGFTSEEKNSMYKLTGAIMHFGNMkfkqkqrEEQAEPDGT--------EEADKSAYLMGLNSADLLKGLCHPRVKVGN 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  386 ETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQ 465
Cdd:cd14917   311 EYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  466 FNSHVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPR- 542
Cdd:cd14917   391 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRn 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  543 ---MSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKINVRSSR 619
Cdd:cd14917   471 ikgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVS 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  620 PLikvpnkehkksvgyqFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRW 699
Cdd:cd14917   551 AL---------------HRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 615

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 569003409  700 TYHDFFNRYRVLMKKR--ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14917   616 LYGDFRQRYRILNPAAipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668

MYSc_Myo34

cd14895

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

83-750

5.12e-155

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: 493.32 E-value: 5.12e-155

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPiyGQDVIYAYSGQNMGDMD--PHIFAVAEEAYKQMAR-------D 153
Cdd:cd14895     1 PAFVDYLAQRYG-VDQVYCRSGAVLIAVNPFKHIP--GLYDLHKYREEMPGWTAlpPHVFSIAEGAYRSLRRrlhepgaS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  154 EKNQSIIVSGESGAGKTVSAKYAMRYFA--------TVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIE 225
Cdd:cd14895    78 KKNQTILVSGESGAGKTETTKFIMNYLAesskhttaTSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  226 IGF-----DKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALT--CAEDFFYTAHGG-NTTIE 297
Cdd:cd14895   158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGGQcYQRND 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  298 GVNDADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDS-------------CSISPQD----EHLSN 360
Cdd:cd14895   238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGeedngaasapcrlASASPSSltvqQHLDI 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  361 FCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKAlhTSLKQHS-------- 432
Cdd:cd14895   318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSA--SPQRQFAlnpnkaan 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  433 -----FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGI 506
Cdd:cd14895   396 kdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSGI 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  507 LDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPR--MSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASK 584
Cdd:cd14895   476 FSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRtdQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTS 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  585 FPLVADLFhddkDSAPATNTAKNRSSSKINVRSSRPLIKVpnkehkkSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDE 664
Cdd:cd14895   556 DAHLRELF----EFFKASESAELSLGQPKLRRRSSVLSSV-------GIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDE 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  665 KLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKRELTNTDKKNIcksvLESLIKdpDKFQFGR 744
Cdd:cd14895   625 SASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASAL----IETLKV--DHAELGK 698


                  ....*.
gi 569003409  745 TKIFFR 750
Cdd:cd14895   699 TRVFLR 704

MYSc_Myh6

cd14916

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

83-750

2.40e-154

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: 490.34 E-value: 2.40e-154

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14916     1 PAVLYNLKERY-AAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGG----------SASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKY 232
Cdd:cd14916    80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  233 HIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELALTCAEDFFYT-AHGGNTTIEGVNDADDFEKTRQA 311
Cdd:cd14916   160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK-PELLDMLLVTNNPYDYAfVSQGEVSVASIDDSEELLATDSA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  312 LTLLGVRDSHQISIFKIIASILHLGSVEI-QSERDGDSCSISPQDEHLSNFcsLLGIEHSQMEHWLCHRKLVTTSETYVK 390
Cdd:cd14916   239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFkQKQREEQAEPDGTEDADKSAY--LMGLNSADLLKGLCHPRVKVGNEYVTK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  391 TMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHV 470
Cdd:cd14916   317 GQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  471 FKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPR----MS 544
Cdd:cd14916   397 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRnvkgKQ 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  545 NTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhDDKDSAPATNTAKNRSSSKinvrssrplikv 624
Cdd:cd14916   477 EAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF-STYASADTGDSGKGKGGKK------------ 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  625 pNKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDF 704
Cdd:cd14916   544 -KGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 569003409  705 FNRYRVL--MKKRELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14916   623 RQRYRILnpAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670

MYSc_Myo28

cd14889

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

85-750

2.75e-154

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: 489.80 E-value: 2.75e-154

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFLEsNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQM----ARDEKNQSII 160
Cdd:cd14889     3 LLEVLKVRFMQ-SNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  161 VSGESGAGKTVSAKYAMRYFATVggSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFdKKYHIIGANMR 240
Cdd:cd14889    82 ISGESGAGKTESTKLLLRQIMEL--CRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  241 TYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDS 320
Cdd:cd14889   159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  321 HQISIFKIIASILHLGSVEIQSERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNA 400
Cdd:cd14889   239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  401 RDALAKHIYAQLFSWIVEHINKAL---HTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEE 477
Cdd:cd14889   319 RDSIAKVAYGRVFGWIVSKINQLLapkDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  478 YMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFADK 556
Cdd:cd14889   399 YKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKFTVNHYAGK 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  557 VEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkdSAPATNTAKNRSSSKINVRSSRPLikvpNKEHKKSVGYQ 636
Cdd:cd14889   479 VTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF-----TATRSRTGTLMPRAKLPQAGSDNF----NSTRKQSVGAQ 549

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  637 FRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKRE 716
Cdd:cd14889   550 FKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPA 629

                         650       660       670
                  ....*....|....*....|....*....|....
gi 569003409  717 LTNTdkKNICKSVLESliKDPDKFQFGRTKIFFR 750
Cdd:cd14889   630 LPGT--KQSCLRILKA--TKLVGWKCGKTRLFFK 659

MYSc_Myh8

cd14918

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

83-750

7.47e-154

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: 488.86 E-value: 7.47e-154

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14918     1 PGVLYNLKERY-AAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATV---GGSASDTN------IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYH 233
Cdd:cd14918    80 GESGAGKTVNTKRVIQYFATIavtGEKKKEESgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  234 IIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELALTCAEDFFYT-AHGGNTTIEGVNDADDFEKTRQAL 312
Cdd:cd14918   160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK-PDLIEMLLITTNPYDYAfVSQGEITVPSIDDQEELMATDSAI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  313 TLLGVRDSHQISIFKIIASILHLGSVEI-QSERDGDScsiSPQDEHLSNFCSLL-GIEHSQMEHWLCHRKLVTTSETYVK 390
Cdd:cd14918   239 DILGFTPEEKVSIYKLTGAVMHYGNMKFkQKQREEQA---EPDGTEVADKAAYLqSLNSADLLKALCYPRVKVGNEYVTK 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  391 TMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHV 470
Cdd:cd14918   316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  471 FKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPRM----S 544
Cdd:cd14918   396 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVvkgkA 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  545 NTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhDDKDSAPATNTAKNRSSSKinvrssrplikv 624
Cdd:cd14918   476 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-STYASAEADSGAKKGAKKK------------ 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  625 pnKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDF 704
Cdd:cd14918   543 --GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDF 620

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 569003409  705 FNRYRVLMKKR--ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14918   621 KQRYKVLNASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668

MYSc_Myh2_mammals

cd14912

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

83-750

3.41e-153

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: 487.32 E-value: 3.41e-153

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14912     1 PAVLYNLKERY-AAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASDT-----------NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKK 231
Cdd:cd14912    80 GESGAGKTVNTKRVIQYFATIAVTGEKKkeeitsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  232 YHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELALTCAEDFFYT-AHGGNTTIEGVNDADDFEKTRQ 310
Cdd:cd14912   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK-PELIEMLLITTNPYDYPfVSQGEISVASIDDQEELMATDS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  311 ALTLLGVRDSHQISIFKIIASILHLGSVEI-QSERDGDScsiSPQDEHLSNFCSLL-GIEHSQMEHWLCHRKLVTTSETY 388
Cdd:cd14912   239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFkQKQREEQA---EPDGTEVADKAAYLqSLNSADLLKALCYPRVKVGNEYV 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  389 VKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNS 468
Cdd:cd14912   316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  469 HVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPRM--- 543
Cdd:cd14912   396 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVvkg 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  544 -SNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKINVRSSrpli 622
Cdd:cd14912   476 kAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGGKKKGSSF---- 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  623 kvpnkehkKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYH 702
Cdd:cd14912   552 --------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 623

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 569003409  703 DFFNRYRVLMKKR--ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14912   624 DFKQRYKVLNASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673

MYSc_Myh1_mammals

cd14910

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

83-750

7.76e-153

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: 486.16 E-value: 7.76e-153

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14910     1 PAVLYNLKERY-AAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASDT-----------NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKK 231
Cdd:cd14910    80 GESGAGKTVNTKRVIQYFATIAVTGEKKkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  232 YHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELALTCAEDFFYT-AHGGNTTIEGVNDADDFEKTRQ 310
Cdd:cd14910   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKK-PDLIEMLLITTNPYDYAfVSQGEITVPSIDDQEELMATDS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  311 ALTLLGVRDSHQISIFKIIASILHLGSVEI-QSERDGDScsiSPQDEHLSNFCSLL-GIEHSQMEHWLCHRKLVTTSETY 388
Cdd:cd14910   239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFkQKQREEQA---EPDGTEVADKAAYLqNLNSADLLKALCYPRVKVGNEYV 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  389 VKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNS 468
Cdd:cd14910   316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  469 HVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPRMSN- 545
Cdd:cd14910   396 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKg 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  546 ---TAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKinvrssrpli 622
Cdd:cd14910   476 kveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKK---------- 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  623 kvpnKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYH 702
Cdd:cd14910   546 ----GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 621

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 569003409  703 DFFNRYRVLMKKR--ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14910   622 DFKQRYKVLNASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671

MYSc_Myh13

cd14923

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

83-750

6.04e-152

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: 483.80 E-value: 6.04e-152

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14923     1 PAVLYNLKERY-AAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASDT----------NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKY 232
Cdd:cd14923    80 GESGAGKTVNTKRVIQYFATIAVTGDKKkeqqpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  233 HIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELALTCAEDF-FYTAHGGNTTIEGVNDADDFEKTRQA 311
Cdd:cd14923   160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKK-PELIDLLLISTNPFdFPFVSQGEVTVASIDDSEELLATDNA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  312 LTLLGVRDSHQISIFKIIASILHLGSVEI-QSERDGDScsiSPQDEHLSNFCS-LLGIEHSQMEHWLCHRKLVTTSETYV 389
Cdd:cd14923   239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFkQKQREEQA---EPDGTEVADKAGyLMGLNSAEMLKGLCCPRVKVGNEYVT 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  390 KTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSH 469
Cdd:cd14923   316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  470 VFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPR----M 543
Cdd:cd14923   396 MFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKpakgK 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  544 SNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDdkdsAPATNTAKNRSSSKINVRSSRPLik 623
Cdd:cd14923   476 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN----YAGAEAGDSGGSKKGGKKKGSSF-- 549

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  624 vpnkehkKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHD 703
Cdd:cd14923   550 -------QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 622

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 569003409  704 FFNRYRVLMKKR--ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14923   623 FKQRYRILNASAipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671

MYSc_Myh4

cd14915

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

83-750

9.82e-152

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: 483.08 E-value: 9.82e-152

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14915     1 PAVLYNLKERY-AAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASDT-----------NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKK 231
Cdd:cd14915    80 GESGAGKTVNTKRVIQYFATIAVTGEKKkeeaasgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  232 YHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELAL--TCAEDFFYTAHGgNTTIEGVNDADDFEKTR 309
Cdd:cd14915   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKK-PELIEMLLitTNPYDFAFVSQG-EITVPSIDDQEELMATD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  310 QALTLLGVRDSHQISIFKIIASILHLGSVEIQSER-----DGDSCSISPQDEHLSNFCSllgiehSQMEHWLCHRKLVTT 384
Cdd:cd14915   238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQreeqaEPDGTEVADKAAYLTSLNS------ADLLKALCYPRVKVG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  385 SETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQ 464
Cdd:cd14915   312 NEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  465 QFNSHVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPR 542
Cdd:cd14915   392 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  543 ----MSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKinvrss 618
Cdd:cd14915   472 pakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKK------ 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  619 rplikvpnKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSR 698
Cdd:cd14915   546 --------GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 569003409  699 WTYHDFFNRYRVLMKKR--ELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14915   618 ILYADFKQRYKVLNASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671

MYSc_Myh16

cd14934

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

84-750

5.08e-151

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.

Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 480.68 E-value: 5.08e-151

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLESnHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14934     2 SVLDNLRQRYTNM-RIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSASDT-----NIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGAN 238
Cdd:cd14934    81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  239 MRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKElALTCAED--FFYTAHGGNTTIEGVNDADDFEKTRQALTLLG 316
Cdd:cd14934   161 IESYLLEKSRVISQQAAERGYHIFYQILSNKK-PELIE-SLLLVPNpkEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  317 VRDSHQISIFKIIASILHLGSVEI-----QSERDGDSCSISPQDEHLsnfcslLGIEHSQMEHWLCHRKLVTTSETYVKT 391
Cdd:cd14934   239 FSAEEKIGVYKLTGGIMHFGNMKFkqkprEEQAEVDTTEVADKVAHL------MGLNSGELQKGITRPRVKVGNEFVQKG 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  392 MSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVF 471
Cdd:cd14934   313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  472 KLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKP-----RMS 544
Cdd:cd14934   393 VLEQEEYKREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPkggkgKGP 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  545 NTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhdDKDSAPATNTAKNRSSSKINVRSSrplikv 624
Cdd:cd14934   473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLF--KEEEAPAGSKKQKRGSSFMTVSNF------ 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  625 pnkehkksvgyqFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDF 704
Cdd:cd14934   545 ------------YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEF 612

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 569003409  705 FNRYRVLMKKRELTN-TDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14934   613 KQRYQVLNPNVIPQGfVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659

MYSc_Myo19

cd14880

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

85-748

1.84e-150

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: 479.35 E-value: 1.84e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFLEsNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAY-SGQNMGDMDPHIFAVAEEAYK--QMARDEKNQSII 160
Cdd:cd14880     3 VLRCLQARYTA-DTFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  161 VSGESGAGKTVSAKYAMRYFATVGGS-ASDTN------IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYH 233
Cdd:cd14880    82 VSGESGAGKTWTSRCLMKFYAVVAASpTSWEShkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  234 IIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTiegvnDADDFEKTRQALT 313
Cdd:cd14880   162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL-----EEDCFEVTREAML 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  314 LLGVRDSHQISIFKIIASILHLGSVEI-QSERDGDSCSISPQ-DEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYV-- 389
Cdd:cd14880   237 HLGIDTPTQNNIFKVLAGLLHLGNIQFaDSEDEAQPCQPMDDtKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVfk 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  390 KTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHT-SLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNS 468
Cdd:cd14880   317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICAdTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  469 HVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERH-SNSQHFQKPRMS-N 545
Cdd:cd14880   397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESAlAGNPCLGHNKLSrE 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  546 TAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkdsaPATNtaKNRSSSKINVRSSRPLIKVP 625
Cdd:cd14880   477 PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF-------PANP--EEKTQEEPSGQSRAPVLTVV 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  626 NKehkksvgyqFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFF 705
Cdd:cd14880   548 SK---------FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFV 618

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 569003409  706 NRYRVLMKKRELTNTDKKNICKSVLESlikdpDKFQFGRTKIF 748
Cdd:cd14880   619 ERYKLLRRLRPHTSSGPHSPYPAKGLS-----EPVHCGRTKVF 656

MYSc_Myh9

cd14919

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

84-750

2.58e-150

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: 479.20 E-value: 2.58e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14919     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSASDTN----IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANM 239
Cdd:cd14919    81 ESGAGKTENTKKVIQYLAHVASSHKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  240 RTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHgGNTTIEGVNDADDFEKTRQALTLLGVRD 319
Cdd:cd14919   161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  320 SHQISIFKIIASILHLGSVEIQSERDGDSCSIsPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVN 399
Cdd:cd14919   240 EEQMGLLRVISGVLQLGNIVFKKERNTDQASM-PDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  400 ARDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEY 478
Cdd:cd14919   319 AIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  479 MKEQIPWTLIDF-YDNQPCIDLIEAKL---GILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRM--SNTAFIVNH 552
Cdd:cd14919   399 QREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlkDKADFCIIH 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  553 FADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhDDKDSAPATNTAKNRSSSKInvrssrPLIKVPNKEHKKS 632
Cdd:cd14919   479 YAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELW-KDVDRIIGLDQVAGMSETAL------PGAFKTRKGMFRT 551

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  633 VGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLM 712
Cdd:cd14919   552 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 631

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 569003409  713 KKRELTN-TDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14919   632 PNSIPKGfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670

MYSc_Myh19

cd15896

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

84-750

4.07e-150

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: 478.79 E-value: 4.07e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd15896     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGS-----------ASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKY 232
Cdd:cd15896    81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  233 HIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHgGNTTIEGVNDADDFEKTRQAL 312
Cdd:cd15896   161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSN-GNVTIPGQQDKDLFTETMEAF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  313 TLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSIsPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTM 392
Cdd:cd15896   240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASM-PDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  393 SLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVF 471
Cdd:cd15896   319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  472 KLEQEEYMKEQIPWTLIDF-YDNQPCIDLIE---AKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPR--MSN 545
Cdd:cd15896   399 ILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKklKDE 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  546 TAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhDDKDSAPATNTAKNRSSSKINVRSSRPLIkvp 625
Cdd:cd15896   479 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELW-KDVDRIVGLDKVSGMSEMPGAFKTRKGMF--- 554

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  626 nkehkKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFF 705
Cdd:cd15896   555 -----RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 629

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 569003409  706 NRYRVLMKKRELTN-TDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd15896   630 QRYEILTPNAIPKGfMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675

MYSc_Myh14_mammals

cd14930

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

84-750

8.26e-150

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: 478.05 E-value: 8.26e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14930     2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSASDTN-------IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIG 236
Cdd:cd14930    81 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  237 ANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEgvNDADDFEKTRQALTLLG 316
Cdd:cd14930   161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQETLESLRVLG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  317 VRDSHQISIFKIIASILHLGSVEIQSERDGDSCSIsPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQ 396
Cdd:cd14930   239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATM-PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  397 VVNARDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQ 475
Cdd:cd14930   318 ADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  476 EEYMKEQIPWTLIDF-YDNQPCIDLIEAKL---GILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPR--MSNTAFI 549
Cdd:cd14930   398 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQADFS 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  550 VNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSApatntaknrSSSKINVRSSRPLIKVPNKEH 629
Cdd:cd14930   478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIV---------GLEQVSSLGDGPPGGRPRRGM 548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  630 KKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYR 709
Cdd:cd14930   549 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 628

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 569003409  710 VLMKKRELTN-TDKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14930   629 ILTPNAIPKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670

MYSc_Myo41

cd14902

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

83-750

1.71e-148

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: 475.92 E-value: 1.71e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAY--------SGQNMGDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14902     1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  154 EK-NQSIIVSGESGAGKTVSAKYAMRYFATVGGSASDTN--------IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFI 224
Cdd:cd14902    80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEqegsdaveIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  225 EIGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADD 304
Cdd:cd14902   160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSFARKRAVADK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  305 ----FEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSE--RDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCH 378
Cdd:cd14902   240 yaqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEngQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  379 RKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHIN-------KALHTSLKQHSF--IGVLDIYGFETFEINS 449
Cdd:cd14902   320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdSAVSISDEDEELatIGILDIFGFESLNRNG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  450 FEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAKL-GILDLLDEECKVPKGTDQNWAQKL 528
Cdd:cd14902   400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  529 YERHSNSQHfqkprmsntaFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNR 608
Cdd:cd14902   480 YRYHGGLGQ----------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGADNGAAG 549

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  609 SSSKINVRSSrplikvpnkehkkSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETI 688
Cdd:cd14902   550 RRRYSMLRAP-------------SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAV 616

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  689 RISAAGYPSRWTYHDFFNRYRVLMKKRELTNTDKKN-------------ICKSVLESLIKDPDK---------------- 739
Cdd:cd14902   617 RIARHGYSVRLAHASFIELFSGFKCFLSTRDRAAKMnnhdlaqalvtvlMDRVLLEDGVEREEKnpgaltavtgdgsgta 696

                         730       740
                  ....*....|....*....|
gi 569003409  740 ---------FQFGRTKIFFR 750
Cdd:cd14902   697 fendcrrkdVQVGRTLVFCK 716

PTZ00014

myosin-A; Provisional

73-809

1.15e-144

myosin-A; Provisional

Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 469.13 E-value: 1.15e-144

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   73 DLTALSHLHEPAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAY-SGQNMGDMDPHIFAVAEEAYKQMA 151
Cdd:PTZ00014  100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  152 RDEKNQSIIVSGESGAGKTVSAKYAMRYFATVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKK 231
Cdd:PTZ00014  179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  232 YHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKE-LALTCAEDFFYTaHGGNTTIEGVNDADDFEKTRQ 310
Cdd:PTZ00014  259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGAN-DEMKEkYKLKSLEEYKYI-NPKCLDVPGIDDVKDFEEVME 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  311 ALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDG---DSCSISPQDEH-LSNFCSLLGIEHSQMEHWLCHRKLVTTSE 386
Cdd:PTZ00014  337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDESLEvFNEACELLFLDYESLKKELTVKVTYAGNQ 416

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  387 TYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 466
Cdd:PTZ00014  417 KIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNF 496

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  467 NSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAKL-GILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMS- 544
Cdd:PTZ00014  497 VDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDs 576

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  545 NTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKdsapatntaknRSSSKINvrssrplikv 624
Cdd:PTZ00014  577 NKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVE-----------VEKGKLA---------- 635

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  625 pnkehKKS-VGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHD 703
Cdd:PTZ00014  636 -----KGQlIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAE 710

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  704 FFNRYRVL-MKKRELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFR---AGQVAYLEKLRADKFREATIMIQksvrGW 779
Cdd:PTZ00014  711 FLSQFKYLdLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLE----AL 786

                         730       740       750
                  ....*....|....*....|....*....|.
gi 569003409  780 LQRVKYRR-LRAATLSLQRFCrGYLARRLAE 809
Cdd:PTZ00014  787 ILKIKKKRkVRKNIKSLVRIQ-AHLRRHLVI 816

MYSc_Myo39

cd14900

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

85-711

7.68e-144

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

Pssm-ID: 276865 Cd Length: 627 Bit Score: 459.77 E-value: 7.68e-144

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFLEsNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 152
Cdd:cd14900     3 ILSALETRFYA-QKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  153 ----DEKNQSIIVSGESGAGKTVSAKYAMRYFATVGG---------SASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSR 219
Cdd:cd14900    82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDnnlaasvsmGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  220 FGKFIEIGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKElaltcaedffytahggnttiegv 299
Cdd:cd14900   162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR----------------------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  300 ndaDDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDG-----DSCSISPQD-EHLSNFCSLLGIEHSQME 373
Cdd:cd14900   219 ---DMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSdrlgqLKSDLAPSSiWSRDAAATLLSVDATKLE 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  374 HWLCHRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHT--SLKQHS---FIGVLDIYGFETFEIN 448
Cdd:cd14900   296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVFPKN 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  449 SFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQK 527
Cdd:cd14900   376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASK 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  528 LYERHSNSQHFQKPRMSNTA--FIVNHFADKVEYLSDGFLEKNRDTVYEEQInilkaskfplvaDLFHDdkdsapatnta 605
Cdd:cd14900   456 LYRACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------DLFVY----------- 512

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  606 knrssskinvrssrplikvpnkehkksvGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVL 685
Cdd:cd14900   513 ----------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVM 564

                         650       660
                  ....*....|....*....|....*.
gi 569003409  686 ETIRISAAGYPSRWTYHDFFNRYRVL 711
Cdd:cd14900   565 EAVRVARAGFPIRLLHDEFVARYFSL 590

MYSc_Myo14

cd14876

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

83-748

1.97e-143

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: 459.45 E-value: 1.97e-143

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLeSNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSG-QNMGDMDPHIFAVAEEAYKQMARDEKNQSIIV 161
Cdd:cd14876     1 PCVLDFLKHRYL-KNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  162 SGESGAGKTVSAKYAMRYFATVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRT 241
Cdd:cd14876    80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  242 YLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKE--LALTCAEDFFYTAHggNTTIEGVNDADDFEKTRQALTLLGVRD 319
Cdd:cd14876   160 FLLEKSRIVTQDDNERSYHIFYQLLKGAD-SEMKSkyHLLGLKEYKFLNPK--CLDVPGIDDVADFEEVLESLKSMGLTE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  320 SHQISIFKIIASILHLGSVEIQSERDG---DSCSISPQDEH-LSNFCSLLGIEHSQMEHWLchrklvTTSETYVKTMSLQ 395
Cdd:cd14876   237 EQIDTVFSIVSGVLLLGNVKITGKTEQgvdDAAAISNESLEvFKEACSLLFLDPEALKREL------TVKVTKAGGQEIE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  396 QVVNARDA------LAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSH 469
Cdd:cd14876   311 GRWTKDDAemlklsLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDI 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  470 VFKLEQEEYMKEQIPWTLIDFYDNQPCID-LIEAKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRM-SNTA 547
Cdd:cd14876   391 VFERESKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVdSNIN 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  548 FIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDdkdsapatntaknrssskinvrssrplIKVpnk 627
Cdd:cd14876   471 FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG---------------------------VVV--- 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  628 EHKKS-----VGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYH 702
Cdd:cd14876   521 EKGKIakgslIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFE 600

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 569003409  703 DFFNRYRVL-MKKRELTNTDKKNICKSVLESLIKDPDKFQFGRTKIF 748
Cdd:cd14876   601 EFLYQFKFLdLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647

MYSc_Myo45

cd14906

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

85-748

3.53e-142

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: 458.67 E-value: 3.53e-142

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFlESNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYSGQN-MGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14906     3 ILNNLGKRY-KSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASDTN---------IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYH 233
Cdd:cd14906    82 GESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  234 II-GANMRTYLLEKSRVVFQADDER-NYHIFYQLCAAASLPEFKELAL--------------TCAEDFFYTAHGGNTTIE 297
Cdd:cd14906   162 KIdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLnndpskyryldardDVISSFKSQSSNKNSNHN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  298 GVNDADD-FEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIqsERDGDSCSISPQD----EHLSNFCSLLGIEHSQM 372
Cdd:cd14906   242 NKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEF--EEDSDFSKYAYQKdkvtASLESVSKLLGYIESVF 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  373 EHWLCHRKLVTTSE--TYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINK-----------ALHTSLKQHSFIGVLDI 439
Cdd:cd14906   320 KQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDI 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  440 YGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPK 518
Cdd:cd14906   400 FGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPK 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  519 GTDQNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDS 598
Cdd:cd14906   480 GSEQSLLEKYNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITS 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  599 APATNtakNRSSSKINVRSsrplikvpnkehkksvgyQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQ 678
Cdd:cd14906   560 TTNTT---KKQTQSNTVSG------------------QFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQ 618

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  679 LRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMK----KRELTNTDKKNICKSVLESLIK------------------- 735
Cdd:cd14906   619 LRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDmynrKNNNNPKLASQLILQNIQSKLKtmgisnnkkknnsnsnsnt 698

                         730
                  ....*....|....*
gi 569003409  736 --DPDKFQFGRTKIF 748
Cdd:cd14906   699 tnDKPLFQIGKTKIF 713

Myo5c_CBD

cd15476

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

1476-1843

8.17e-138

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: 431.51 E-value: 8.17e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1476 EDEALLIRNLVTDLKPQ-MLSGTVPCLPAYILYMCIRHADYTNDDLKVHSLLSSTINGIKKVLKKHNDDFEMTSFWLSNT 1554
Cdd:cd15476     1 EDEAKLIQNLILDLKPRgVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1555 CRFLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGLLQPMIVSamlenesiqglsgv 1634
Cdd:cd15476    81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQPTISS-------------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1635 rptgyrkrsssmvdgensycleaIVRQMNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLR 1714
Cdd:cd15476   147 -----------------------ILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIR 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1715 YNISQLEEWLRGKNLHQSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERVTVSF 1794
Cdd:cd15476   204 CNISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSF 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 569003409 1795 IRTIQAQLQERNDPQQLLLDSKHVFPVLFPYNPSALTMDSIHIPACLNL 1843
Cdd:cd15476   284 VRKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332

MYSc_Myo35

cd14896

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

83-750

8.99e-138

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: 443.84 E-value: 8.99e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVS 162
Cdd:cd14896     1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVGGSASDTNIE--EKVLassPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYhIIGANMR 240
Cdd:cd14896    80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHLQHGV-IVGASVS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  241 TYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDS 320
Cdd:cd14896   156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  321 HQISIFKIIASILHLGSVEIQS-ERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVN 399
Cdd:cd14896   236 ELTAIWAVLAAILQLGNICFSSsERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  400 ARDALAKHIYAQLFSWIVEHINKALHTSLKQHSF--IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEE 477
Cdd:cd14896   316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  478 YMKEQIPWTLIDFYDNQPCIDLIEAKL-GILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFADK 556
Cdd:cd14896   396 CQRELLPWVPIPQPPRESCLDLLVDQPhSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAGT 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  557 VEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDdkdsapatntAKNRSSskinvrssrplikvpNKEHKKSVGYQ 636
Cdd:cd14896   476 VTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE----------AEPQYG---------------LGQGKPTLASR 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  637 FRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKRE 716
Cdd:cd14896   531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610

                         650       660       670
                  ....*....|....*....|....*....|....*
gi 569003409  717 LTNTDKKNiCKSVLESLIKDP-DKFQFGRTKIFFR 750
Cdd:cd14896   611 EALSDRER-CGAILSQVLGAEsPLYHLGATKVLLK 644

MYSc_Myo38

cd14899

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

84-721

1.84e-129

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: 423.35 E-value: 1.84e-129

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLP-IYGQDVI--YAYS-GQNMGDM-------DPHIFAVAEEAYKQMAR 152
Cdd:cd14899     2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILrgYAYDhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  153 DEKNQSIIVSGESGAGKTVSAKYAMRYFATVGG----------------SASDTNIEEKVLASSPIMEAIGNAKTTRNDN 216
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  217 SSRFGKFIEIGF-DKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKE----LALTCAEDFFYTAHG 291
Cdd:cd14899   161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEqkqvLALSGGPQSFRLLNQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  292 G--NTTIEGVNDADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQ--SERDGDSC---------SISPQDEHL 358
Cdd:cd14899   241 SlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiPHKGDDTVfadearvmsSTTGAFDHF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  359 SNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLK--------- 429
Cdd:cd14899   321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  430 ------QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK 503
Cdd:cd14899   401 vddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  504 -LGILDLLDEECKVPKGTDQNWAQKLY---ERHSNSQHFQKPRM--SNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQI 577
Cdd:cd14899   481 pIGIFSLTDQECVFPQGTDRALVAKYYlefEKKNSHPHFRSAPLiqRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  578 NILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKINVRSSRPLIKVpnkehkkSVGYQFRTSLNLLMETLNATTPHYVR 657
Cdd:cd14899   561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAV-------SVGTQFKIQLNELLSTVRATTPRYVR 633

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569003409  658 CIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRY-RVLMKKRELTNTD 721
Cdd:cd14899   634 CIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYrRVLLSLYKWGDND 698

MYSc_Myo25

cd14886

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

85-750

7.89e-121

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: 396.56 E-value: 7.89e-121

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFlESNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYSGQNMG-----DMDPHIFAVAEEAYKQMARDEKNQS 158
Cdd:cd14886     3 VIDILRDRF-AKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  159 IIVSGESGAGKTVSAKYAMRYFAtVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGAN 238
Cdd:cd14886    82 CIVSGESGAGKTETAKQLMNFFA-YGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  239 MRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLgVR 318
Cdd:cd14886   161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  319 DSHQISIFKIIASILHLGSVEIQSERDG--DSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMS-LQ 395
Cdd:cd14886   240 KNEIDSFYKCISGILLAGNIEFSEEGDMgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTqAQ 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  396 QVVNARdALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQ 475
Cdd:cd14886   320 AEVNIR-AVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEI 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  476 EEYMKEQIPWTLIDFYDNQPCIDLIEA-KLGILDLLDEECKVPKGTDQNWAQKLyERHSNSQHFQKPRMSNTAFIVNHFA 554
Cdd:cd14886   399 QEYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIKNNSFIPGKGSQCNFTIVHTA 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  555 DKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVadlfhddkdsapatntakNRSSSKINVRSsrPLIKvpnkehKKSVG 634
Cdd:cd14886   478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV------------------NKAFSDIPNED--GNMK------GKFLG 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  635 YQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKK 714
Cdd:cd14886   532 STFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISH 611

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 569003409  715 RELTNT---DKKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14886   612 NSSSQNageDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650

MYSc_Myo13

cd14875

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

85-750

1.58e-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: 396.10 E-value: 1.58e-120

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFLESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAY-SGQNMGDMDPHIFAVAEEAYKQM-ARDEKNQSIIVS 162
Cdd:cd14875     3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATVG----GSASDTNIEEKVLA----SSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHI 234
Cdd:cd14875    83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  235 -IGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELA-LTCAEDFfYTAHGGNTTI------EGVNDADDFE 306
Cdd:cd14875   163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGgLKTAQDY-KCLNGGNTFVrrgvdgKTLDDAHEFQ 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  307 KTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSErDGDSCSISPQDEHLSNfCSLLGIEHSQMEHwlChrkLVTTSE 386
Cdd:cd14875   242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD-QNDKAQIADETPFLTA-CRLLQLDPAKLRE--C---FLVKSK 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  387 TYVKTM--SLQQVVNARDALAKHIYAQLFSWIVEHINKALH--TSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 462
Cdd:cd14875   315 TSLVTIlaNKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpqGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESL 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  463 QQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSN-SQHFQK 540
Cdd:cd14875   395 QNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANkSPYFVL 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  541 PR--MSNTaFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSApatntaknrssskinvrss 618
Cdd:cd14875   475 PKstIPNQ-FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA------------------- 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  619 rplikvpnkEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSR 698
Cdd:cd14875   535 ---------RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVR 605

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  699 WTYHDFFNRYRVLMKKRELTNTDKKNI---CKSVLESLIK-----DPDkFQFGRTKIFFR 750
Cdd:cd14875   606 RPIEQFCRYFYLIMPRSTASLFKQEKYseaAKDFLAYYQRlygwaKPN-YAVGKTKVFLR 664

MYSc_Myo37

cd14898

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

84-711

1.70e-120

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: 393.11 E-value: 1.70e-120

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQlpIYGQDVIYAYSgQNMGDMDPHIFAVAEEAYKQMARdEKNQSIIVSG 163
Cdd:cd14898     2 ATLEILEKRY-ASGKIYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFatVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKyhIIGANMRTYL 243
Cdd:cd14898    77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--ITGAKFETYL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  244 LEKSRVVFQADDERNYHIFYQLCAAaslpefKELALTcaEDFF-YTAHGGNTTiEGVNDADDFEKTRQALTLLGVRDSHQ 322
Cdd:cd14898   153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNIK--NDFIdTSSTAGNKE-SIVQLSEKYKMTCSAMKSLGIANFKS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  323 ISifKIIASILHLGSVEIQSerdgDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARD 402
Cdd:cd14898   224 IE--DCLLGILYLGSIQFVN----DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRN 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  403 ALAKHIYAQLFSWIVEHINKALHTSlKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQ 482
Cdd:cd14898   298 SMARLLYSNVFNYITASINNCLEGS-GERS-ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEG 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  483 IPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLyerHSNSQHFQKPRMSNTaFIVNHFADKVEYLSD 562
Cdd:cd14898   376 IEWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKI---KKYLNGFINTKARDK-IKVSHYAGDVEYDLR 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  563 GFLEKNRDtvyeeqinilKASKFPLVADLFHDDKdsapatntaknrssskinvrSSRPLIKVpnkehkksvgyqFRTSLN 642
Cdd:cd14898   452 DFLDKNRE----------KGQLLIFKNLLINDEG--------------------SKEDLVKY------------FKDSMN 489

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003409  643 LLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVL 711
Cdd:cd14898   490 KLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558

Myo5-like_CBD

cd14945

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

1476-1803

8.34e-109

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: 348.23 E-value: 8.34e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1476 EDEALLIRNLVTDLKPQmlSGTVPCLPAYILYMCIRHADYTNDDLKVHSLLSSTINGIKKVLKKHNDDFEMTSFWLSNTC 1555
Cdd:cd14945     1 SEEDSLLRGIVTDFEPS--SGDHKLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1556 RFLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGLLQPmivsamlenesiqglsgvr 1635
Cdd:cd14945    79 ELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1636 ptgyrkrsssmvdgensyCLEAIVRQMNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLRY 1715
Cdd:cd14945   140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1716 NISQLEEWLRGKNLHqSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERVTVSFI 1795
Cdd:cd14945   202 NISRLEEWCEGRGLE-HLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280


                  ....*...
gi 569003409 1796 RTIQAQLQ 1803
Cdd:cd14945   281 RTLAAEVS 288

MYSc_Myo17

cd14879

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

72-749

4.50e-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: 4.50e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   72 NDLTALSHLHEpavlhnlkvRFLeSNHIYTYCGI-VLVAINPYEQLPI--------YGQDVIYAYSGQNMGDMdPHIFAV 142
Cdd:cd14879     2 SDDAITSHLAS---------RFR-SDLPYTRLGSsALVAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLP-PHAYDL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  143 AEEAYKQMARDEKNQSIIVSGESGAGKTVSAKYAMRYFATVggSAS---DTNIEEKVLASSPIMEAIGNAKTTRNDNSSR 219
Cdd:cd14879    71 AARAYLRMRRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL--SSHskkGTKLSSQISAAEFVLDSFGNAKTLTNPNASR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  220 FGKFIEIGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKE-LALTCAEDFFYTAH-GGNTTIE 297
Cdd:cd14879   149 FGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGAS-PEERQhLGLDDPSDYALLASyGCHPLPL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  298 GV--NDADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDG--DSCSISPQDEhLSNFCSLLGIEHSQME 373
Cdd:cd14879   228 GPgsDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGgeESAVVKNTDV-LDIVAAFLGVSPEDLE 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  374 HWL------CHRKLVTtsetyvkTM-----SLQQvvnaRDALAKHIYAQLFSWIVEHINKALHTSLKQ-HSFIGVLDIYG 441
Cdd:cd14879   307 TSLtyktklVRKELCT-------VFldpegAAAQ----RDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPG 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  442 FETF---EINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAK-LGILDLLDEECK-V 516
Cdd:cd14879   376 FQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKpGGLLGILDDQTRrM 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  517 PKGTDQNWAQKLYERHSNSQHFQKPRMSNT-----AFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILkaskfplvadl 591
Cdd:cd14879   456 PKKTDEQMLEALRKRFGNHSSFIAVGNFATrsgsaSFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLL----------- 524

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  592 fhddkdsapatntaknRSSSkinvrssrplikvpnkehkksvgyQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFD 671
Cdd:cd14879   525 ----------------RGAT------------------------QLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFD 564

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569003409  672 PKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYrvlmkKRELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFF 749
Cdd:cd14879   565 KRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY-----KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637

MYSc_Myo24A

cd14937

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

85-750

8.31e-96

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

Pssm-ID: 276897 Cd Length: 637 Bit Score: 324.66 E-value: 8.31e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFlESNHIYTYCGIVLVAINPYEQLpiygqDV-IYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14937     3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVI-----DVdINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFatVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYL 243
Cdd:cd14937    77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  244 LEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGgNTTIEGVNDADDFEKTRQALTLLGVRDSHQi 323
Cdd:cd14937   155 LENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNK-NVVIPEIDDAKDFGNLMISFDKMNMHDMKD- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  324 SIFKIIASILHLGSVEIQSERDGDSCSISPQDEH----LSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVN 399
Cdd:cd14937   233 DLFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNnlelVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVS 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  400 ARDALAKHIYAQLFSWIVEHINKALHTSLKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYM 479
Cdd:cd14937   313 ICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYK 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  480 KEQIPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMS-NTAFIVNHFADKVE 558
Cdd:cd14937   393 AEDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDiNKNFVIKHTVSDVT 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  559 YLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDdkdsapatntaknrssskinVRSSRPLIKvpnkehKKSVGYQFR 638
Cdd:cd14937   473 YTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED--------------------VEVSESLGR------KNLITFKYL 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  639 TSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAgYPSRWTYHDFFNRYRVL--MKKRE 716
Cdd:cd14937   527 KNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdySTSKD 605

                         650       660       670
                  ....*....|....*....|....*....|....
gi 569003409  717 LTNTDKKNICKsVLESLIkDPDKFQFGRTKIFFR 750
Cdd:cd14937   606 SSLTDKEKVSM-ILQNTV-DPDLYKVGKTMVFLK 637

MYSc_Myo16

cd14878

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

84-750

2.30e-94

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

Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 320.99 E-value: 2.30e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAY---SGQNMGDMDPHIFAVAEEAYKQMARDEKNQSII 160
Cdd:cd14878     2 SLLYEIQKRF-GNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  161 VSGESGAGKTVSAKYAMRYFATVGGSaSDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGF-DKKYHIIGANM 239
Cdd:cd14878    81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  240 RTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALT--CAEDFFYTAHGGNT-TIEGVNDADDFEKTRQALTLLG 316
Cdd:cd14878   160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNnlCAHRYLNQTMREDVsTAERSLNREKLAVLKQALNVVG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  317 VRDSHQISIFKIIASILHLGSVEIQSERDGDSCSISPQdEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQ 396
Cdd:cd14878   240 FSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDL-QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  397 VVNARDALAKHIYAQLFSWIVEHINKALHTSLKQHSF----IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFK 472
Cdd:cd14878   319 AEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  473 LEQEEYMKEQIPW----------TLIDFYDNQPcidlieakLGILDLLDEECKVPKGTDQNWAQKL--YERHSNSQHFQK 540
Cdd:cd14878   399 QEQTECVQEGVTMetayspgnqtGVLDFFFQKP--------SGFLSLLDEESQMIWSVEPNLPKKLqsLLESSNTNAVYS 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  541 P----------RMSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHddkdsapatntaknrss 610
Cdd:cd14878   471 PmkdgngnvalKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----------------- 533

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  611 SKInvrssrplikvpnkehkKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRI 690
Cdd:cd14878   534 SKL-----------------VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKI 596

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569003409  691 SAAGYPSRWTYHDFFNRYRVLMK-----KRELTNTDKkniCKSVLESlIKDPDkFQFGRTKIFFR 750
Cdd:cd14878   597 FRYGYPVRLSFSDFLSRYKPLADtllgeKKKQSAEER---CRLVLQQ-CKLQG-WQMGVRKVFLK 656

MYSc_Myo20

cd14881

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

84-749

8.16e-94

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

Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 318.60 E-value: 8.16e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPiygqDVIYAYSGQNMGDMdPHIFAVAEEAYKQMARDEKNQSIIVSG 163
Cdd:cd14881     2 AVMKCLQARF-YAKEFFTNVGPILLSVNPYRDVG----NPLTLTSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAIILSG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  164 ESGAGKTVSAKYAMRYFATVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKkyhiiGANMRT-- 241
Cdd:cd14881    76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYRTki 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  242 --YLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALT--CAEDFFYTAHGgnTTIEGVN-DADDFEKTRQALTLLG 316
Cdd:cd14881   151 hcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHG--DTRQNEAeDAARFQAWKACLGILG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  317 VRDShqiSIFKIIASILHLGSVEIqSERDGDSCSISPQDEhLSNFCSLLGIEHSQMEHWLCHRKLVTTSETyVKTMSLQQ 396
Cdd:cd14881   229 IPFL---DVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGLTTRTHNARGQL-VKSVCDAN 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  397 VVNA-RDALAKHIYAQLFSWIVEHIN--KALHTSLKQHS---FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHV 470
Cdd:cd14881   303 MSNMtRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHI 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  471 FKLEQEEYMKEQIPWTL-IDFYDNQPCIDLIEA-KLGILDLLDEECKvPKGTDQNWAQKLYERHSNSQHFQKPR-MSNTA 547
Cdd:cd14881   383 FKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKpQDDRM 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  548 FIVNHFADKVEYLSDGFLEKNRDTVYEEQINIlkaskfplvadlFHDDKDS-APATNTAknrssskinvrssrplikvpn 626
Cdd:cd14881   462 FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAV------------FYKQNCNfGFATHTQ--------------------- 508

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  627 kehkksvgyQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFN 706
Cdd:cd14881   509 ---------DFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNA 579

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 569003409  707 RYRVLMKKRELTNTDKKNI--CKSVLESLIKDPDK--------FQFGRTKIFF 749
Cdd:cd14881   580 RYRLLAPFRLLRRVEEKALedCALILQFLEAQPPSklssvstsWALGKRHIFL 632

MYSc_Myo26

cd14887

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

83-750

2.79e-91

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: 313.89 E-value: 2.79e-91

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLES-------NHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEK 155
Cdd:cd14887     1 PNLLENLYQRYNKAyinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  156 NQSIIVSGESGAGKTVSAKYAMRYFATVG---GSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKY 232
Cdd:cd14887    81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  233 HIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLP-EFKELALtcaedffytahggnttiEGVNDADDFEKTRQA 311
Cdd:cd14887   161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAaTQKSSAG-----------------EGDPESTDLRRITAA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  312 LTLLGVRDSHQISIFKIIASILHLGSVEI------QSERDGDSCSISPQDE---------------------------HL 358
Cdd:cd14887   224 MKTVGIGGGEQADIFKLLAAILHLGNVEFttdqepETSKKRKLTSVSVGCEetaadrshssevkclssglkvteasrkHL 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  359 SNFCSLLGIEHSQMEHWLCHRKLVTTS--ETYvKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSLK------- 429
Cdd:cd14887   304 KTVARLLGLPPGVEGEEMLRLALVSRSvrETR-SFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  430 -------QHSFIGVLDIYGFETFE---INSFEQFCINYANEKLqqqfnsHVFKLEQ-----------EEYMKEQI----- 483
Cdd:cd14887   383 edtpsttGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERL------HCFLLEQlilnehmlytqEGVFQNQDcsafp 456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  484 ------------PWTLIDF-----YDNQPCIDLIEAKLGILDLLDEECK--VPKGTDQNWAQKLYER-HSNSQHFQK--- 540
Cdd:cd14887   457 fsfplastltssPSSTSPFsptpsFRSSSAFATSPSLPSSLSSLSSSLSssPPVWEGRDNSDLFYEKlNKNIINSAKykn 536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  541 --PRMS--NTAFIVNHFADKVEYLSDGFLEKNRDTVYEEqinilkaskfplVADLFhddkdSAPATNTAKNRSSSKINVR 616
Cdd:cd14887   537 itPALSreNLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLF-----LACSTYTRLVGSKKNSGVR 599

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  617 SSrplikvpnKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYP 696
Cdd:cd14887   600 AI--------SSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003409  697 SRWTYHDFFNRY--RVLMKKRELTNTdkKNICKSVLESLIKDPDKFQFGRTKIFFR 750
Cdd:cd14887   672 CRLPYVELWRRYetKLPMALREALTP--KMFCKIVLMFLEINSNSYTFGKTKIFFR 725

MYSc_Myo18

cd01386

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

85-750

1.07e-90

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: 311.17 E-value: 1.07e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSGE 164
Cdd:cd01386     3 VLHTLRQRY-GANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  165 SGAGKTVSAKYAMRYFATVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYLL 244
Cdd:cd01386    82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  245 EKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDA-DDFEKTRQALTLLGVRDSHQI 323
Cdd:cd01386   162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAaAAFSKLQAAMKTLGISEEEQR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  324 SIFKIIASILHLGSVE-IQSERDGDSCSISPqdEHLSNFCSLLGIEHSQM-----EHWLCHRKLVTTSETYVKTMSL--- 394
Cdd:cd01386   242 AIWSILAAIYHLGAAGaTKAASAGRKQFARP--EWAQRAAYLLGCTLEELssaifKHHLSGGPQQSTTSSGQESPARsss 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  395 ----QQVVNARDALAKHIYAQLFSWIVEHINKALHTSlkQHSF--IGVLDIYGFETFE------INSFEQFCINYANEKL 462
Cdd:cd01386   320 ggpkLTGVEALEGFAAGLYSELFAAVVSLINRSLSSS--HHSTssITIVDTPGFQNPAhsgsqrGATFEDLCHNYAQERL 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  463 QQQFNSHVFKLEQEEYMKEQIPwtlIDFYDNQPC----IDLI---------------EAKLGILDLLDEECKVPKGTDQN 523
Cdd:cd01386   398 QLLFHERTFVAPLERYKQENVE---VDFDLPELSpgalVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSDDT 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  524 WAQKLY-----ERHSNSQHFQKPRMSNTAFIVNHF--ADKVEYLSDGFleknrdtvyeeqiniLKASKfplvadlfhddk 596
Cdd:cd01386   475 FLERLFshygdKEGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGW---------------LKAAK------------ 527

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  597 dSAPATntaknRSSSKINVRSSRPLIKVpnkeHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPN------DEKLPFHF 670
Cdd:cd01386   528 -ENPSA-----QNATQLLQESQKETAAV----KRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPA 597

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  671 DPKRAVQ------QLRACGVLETIRISAAGYPSRWTYHDFFNRYRVL----MKKRELTN--TDKKNICKSVLESLIKDPD 738
Cdd:cd01386   598 AGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSevADERKAVEELLEELDLEKS 677

                         730
                  ....*....|..
gi 569003409  739 KFQFGRTKIFFR 750
Cdd:cd01386   678 SYRIGLSQVFFR 689

MYSc_Myo23

cd14884

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

83-748

4.68e-88

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 303.37 E-value: 4.68e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFLEsNHIYTYCGIVLVAINPYEQLP-IYGQDVIYAYS-------GQNMGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14884     1 PNVLQNLKNRYLK-NKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  155 KNQSIIVSGESGAGKTVSAKYAMRYFATVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKK--- 231
Cdd:cd14884    80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVent 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  232 ------YHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALT----------CAEDFFYTAHGGNTT 295
Cdd:cd14884   160 qknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVrncgvygllnPDESHQKRSVKGTLR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  296 IEGVN----------DADDFEKTRQALTLLGVrDSHQIS-IFKIIASILHLGsveiqserdgdscsispqDEHLSNFCSL 364
Cdd:cd14884   240 LGSDSldpseeekakDEKNFVALLHGLHYIKY-DERQINeFFDIIAGILHLG------------------NRAYKAAAEC 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  365 LGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKAL------------HTSLKQHS 432
Cdd:cd14884   301 LQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEA 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  433 FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAKLGILDLLDE 512
Cdd:cd14884   381 IISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITK 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  513 --ECKVPKGTDQNW--------AQKLYERHS--------NSQHFQKPRMSNTAFIVNHFADKVEYLSDGFLEKNRDTVyE 574
Cdd:cd14884   461 lkNQGQKKTDDHFFryllnnerQQQLEGKVSygfvlnhdADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNSDKI-E 539

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  575 EQINILkaskfplvadlfhddkdsapaTNTAKNRSSSKINVRSsrplikvpNKEHKKSVGYQFRTSLNLLMETLNATTPH 654
Cdd:cd14884   540 TSIETL---------------------ISCSSNRFLREANNGG--------NKGNFLSVSKKYIKELDNLFTQLQSTDMY 590

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  655 YVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRwtyhdffnryrvlMKKRELTNTDKKNICKSVLEslI 734
Cdd:cd14884   591 YIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK-------------IPKKETAAALKEQIAKELEK--C 655

                         730
                  ....*....|....
gi 569003409  735 KDPDKFQFGRTKIF 748
Cdd:cd14884   656 NSNTDIEYQRRLAA 669

MYSc_Myo12

cd14874

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

84-750

6.91e-86

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: 295.24 E-value: 6.91e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   84 AVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYsgqnmgdmdpHIFAVAEEAYKQMARDEKN-QSIIVS 162
Cdd:cd14874     2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  163 GESGAGKTVSAKYAMRYFATvggSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFdKKYHIIGANMR-T 241
Cdd:cd14874    71 GESGSGKSYNAFQVFKYLTS---QPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKyT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  242 YLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGgNTTIEGVNDADDFEKTRQALTLLGVRDSH 321
Cdd:cd14874   147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQG-NSTENIQSDVNHFKHLEDALHVLGFSDDH 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  322 QISIFKIIASILHLGSVEIQSERDGD---SCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTsetyvkTMSLQQVV 398
Cdd:cd14874   226 CISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSEDGT------TIDLNAAL 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  399 NARDALAKHIYAQLFSWIVEHINKALHTSLKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEY 478
Cdd:cd14874   300 DNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVDY 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  479 MKEQIPwtlIDF-----YDNQPCIDLIEAK-LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSN-TAFIVN 551
Cdd:cd14874   379 AKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKErLEFGVR 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  552 HFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHddkdsapatNTAKNRSSSKInvrssrplikvpnkehkk 631
Cdd:cd14874   456 HCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE---------SYSSNTSDMIV------------------ 508

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  632 SVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVL 711
Cdd:cd14874   509 SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 569003409  712 MKKRELTNTDKKNICKSVLESL-IKDPDKFQFGRTKIFFR 750
Cdd:cd14874   589 LPGDIAMCQNEKEIIQDILQGQgVKYENDFKIGTEYVFLR 628

MYSc_Myo44

cd14905

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

99-750

2.64e-84

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: 292.00 E-value: 2.64e-84

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   99 IYTYCGIVLVAINPYEQLP-IYGQDVIYAYSgQNMGdMDPHIFAVAEEAYKQMARDEKNQSIIVSGESGAGKTVSAKYAM 177
Cdd:cd14905    16 IYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENTKIII 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  178 RYFATVGGSASDTnIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYLLEKSRVVFQADDER 257
Cdd:cd14905    94 QYLLTTDLSRSKY-LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGER 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  258 NYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGS 337
Cdd:cd14905   173 NFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGN 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  338 VEIQSERDGDSCSISPQDEHLSNFCSLlgiEHSQMEHWLCHRklvttsetyvKTMSLQQVVNARDALAKHIYAQLFSWIV 417
Cdd:cd14905   253 VTFFQKNGKTEVKDRTLIESLSHNITF---DSTKLENILISD----------RSMPVNEAVENRDSLARSLYSALFHWII 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  418 EHINKALHTSLKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPW-TLIDFYDNQPC 496
Cdd:cd14905   320 DFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDNEES 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  497 IDLIEAklgILDLLDEECKVPKGTDQNWAQKLYERHSNSQHF-QKPrmsnTAFIVNHFADKVEYLSDGFLEKNRDTVYeE 575
Cdd:cd14905   399 VEMMEK---IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDEIL-Q 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  576 QINILKA---SKFPLVAD-LFHDDKDSAP------ATNTAKNRSSSKINVR----SSRP-LIKVPNKEHKKSVG------ 634
Cdd:cd14905   471 RTNVLHKnsiTKYLFSRDgVFNINATVAElnqmfdAKNTAKKSPLSIVKVLlscgSNNPnNVNNPNNNSGGGGGggnsgg 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  635 --------YQFRTSLNLLMETLNATTpHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFN 706
Cdd:cd14905   551 gsgsggstYTTYSSTNKAINNSNCDF-HFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFD 629

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 569003409  707 RYRVLMK-KRELTNTDKKNICKSV-LESLIkdPDKFQFGRTKIFFR 750
Cdd:cd14905   630 RFSFFFQnQRNFQNLFEKLKENDInIDSIL--PPPIQVGNTKIFLR 673

MYSc_Myo32

cd14893

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

86-749

6.40e-80

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: 281.09 E-value: 6.40e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   86 LHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQN----------MGDMDPHIFAVAEEAYKQMARDEK 155
Cdd:cd14893     4 LYTLRARY-RMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  156 NQSIIVSGESGAGKTVSAKYAMRYFATVGGSASDTN-----------IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFI 224
Cdd:cd14893    83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  225 EIGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAA----SLPEFKELAlTCAEDFFYTAHGGNTTIEGVN 300
Cdd:cd14893   163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVqhdpTLRDSLEMN-KCVNEFVMLKQADPLATNFAL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  301 DADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSISPQDEHLSNFCS--------------LLG 366
Cdd:cd14893   242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQScalkdpaqillaakLLE 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  367 IEHSQMEHWLCHRKLVT----TSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKAL---------HTSLKQHSF 433
Cdd:cd14893   322 VEPVVLDNYFRTRQFFSkdgnKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryekSNIVINSQG 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  434 IGVLDIYGFETFE--INSFEQFCINYANEKLQQQF-------NSHVFKLEQEEYMKEQIPWTLIDF-YDNQPCIDLIEAK 503
Cdd:cd14893   402 VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDItSEQEKCLQLFEDK 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  504 -LGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMS--------------NTAFIVNHFADKVEYLSDGFLEKN 568
Cdd:cd14893   482 pFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGadttneylapskdwRLLFIVQHHCGKVTYNGKGLSSKN 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  569 RDTVYEEQINILKASKFPLV-----ADLFHDDKDSAPATNTAKNRSSSKINVRSSRpliKVPNKEHKKSVGYQFRTSLNL 643
Cdd:cd14893   562 MLSISSTCAAIMQSSKNAVLhavgaAQMAAASSEKAAKQTEERGSTSSKFRKSASS---ARESKNITDSAATDVYNQADA 638

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  644 LMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYrvlmkkreltntdkK 723
Cdd:cd14893   639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY--------------K 704

                         730       740       750
                  ....*....|....*....|....*....|....*.
gi 569003409  724 NIC--KSVLESLIK--------DPDKFQFGRTKIFF 749
Cdd:cd14893   705 NVCghRGTLESLLRslsaigvlEEEKFVVGKTKVYL 740

MYSc_Myo21

cd14882

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

85-750

1.59e-68

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: 244.65 E-value: 1.59e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   85 VLHNLKVRfLESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSGE 164
Cdd:cd14882     3 ILEELRHR-YLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  165 SGAGKTVSAKYAMRYFATVGGSASDTNieEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYLL 244
Cdd:cd14882    82 SYSGKTTNARLLIKHLCYLGDGNRGAT--GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  245 EKSRVVFQADDERNYHIFYQLCAAASLPE-FKELALTCAEDFFYTAHGGNTTIEGV--------NDADDFEKTRQALTLL 315
Cdd:cd14882   160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpeGNVERYKEFEEILKDL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  316 GVRDSHQISIFKIIASILHLGSVEIqseRDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQ 395
Cdd:cd14882   240 DFNEEQLETVRKVLAAILNLGEIRF---RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  396 QVVNARDALAKHIYAQLFSWIVEHINKALHTSLK----QHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVF 471
Cdd:cd14882   317 EARDARDVLASTLYSRLVDWIINRINMKMSFPRAvfgdKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIF 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  472 KLEQEEYMKEQIPWTLIDFYDNQPCID-LIEAKLGILDLLDEECKvpKGTDQNWaqkLYER-HSNSQHFQKPrMSNTAFI 549
Cdd:cd14882   396 ISEMLEMEEEDIPTINLRFYDNKTAVDqLMTKPDGLFYIIDDASR--SCQDQNY---IMDRiKEKHSQFVKK-HSAHEFS 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  550 VNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFhddkdsapaTNTAKNRSSSKINVrssrplikvpnkeh 629
Cdd:cd14882   470 VAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF---------TNSQVRNMRTLAAT-------------- 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  630 kksvgyqFR-TSLNLLMETLNATTP---HYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFF 705
Cdd:cd14882   527 -------FRaTSLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFL 599

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 569003409  706 NRYRVLMKKRELTNTDKKNICKSVLESLikDPDKFQFGRTKIFFR 750
Cdd:cd14882   600 RRYQFLAFDFDETVEMTKDNCRLLLIRL--KMEGWAIGKTKVFLK 642

Motor_domain

cd01363

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

106-229

2.57e-46

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: 164.44 E-value: 2.57e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  106 VLVAINPYEQLPIYGQD-VIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSGESGAGKTVSAKYAMRYFATVG 184
Cdd:cd01363     1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569003409  185 GSASDTN--------------IEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFD 229
Cdd:cd01363    81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139

MYSc_Myo24B

cd14938

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

83-748

1.70e-42

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

Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 168.09 E-value: 1.70e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   83 PAVLHNLKVRFlESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQN-MGDMDPHIFAVAEEAYKQMARDEKNQSIIV 161
Cdd:cd14938     1 PSVLYHLKERF-KNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  162 SGESGAGKTVSAKYAMRYFA-TVGGSASDT---------------------NIEEKVLASSPIMEAIGNAKTTRNDNSSR 219
Cdd:cd14938    80 SGESGSGKSEIAKNIINFIAyQVKGSRRLPtnlndqeednihneentdyqfNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  220 FGKFIEIGFDKKyHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASlPEFKELA-LTCAEDffYTAHGGNTTIEG 298
Cdd:cd14938   160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSS-DKFKKMYfLKNIEN--YSMLNNEKGFEK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  299 VNDADDfeKTRQALTLLG--VRDSHQIS-IFKIIASILHLGSVEI-------QSERDGDSCSISPQDE-HLS--NFCSLL 365
Cdd:cd14938   236 FSDYSG--KILELLKSLNyiFDDDKEIDfIFSVLSALLLLGNTEIvkafrkkSLLMGKNQCGQNINYEtILSelENSEDI 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  366 GIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVN---------------ARDALAKHIYAQLFSWIVEHINK---ALHTS 427
Cdd:cd14938   314 GLDENVKNLLLACKLLSFDIETFVKYFTTNYIFNdsilikvhnetkiqkKLENFIKTCYEELFNWIIYKINEkctQLQNI 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  428 LKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTL-IDFYDNQPCID-LIEAKLG 505
Cdd:cd14938   394 NINTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEG 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  506 ILDLLDEECKVPKGTDQ-NWAQKLYERHSNSQHFQKPR---MSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILK 581
Cdd:cd14938   474 SLFSLLENVSTKTIFDKsNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVK 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  582 ASKFPLVADL-FHDDKDSAPATNTAKNRSSskinVRSSRPLIKVPNKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIK 660
Cdd:cd14938   554 QSENEYMRQFcMFYNYDNSGNIVEEKRRYS----IQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMK 629

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  661 PNDEK-LPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLmkkreltNTDKKNICKSVLESLIKDPDK 739
Cdd:cd14938   630 PNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIK-------NEDLKEKVEALIKSYQISNYE 702


                  ....*....
gi 569003409  740 FQFGRTKIF 748
Cdd:cd14938   703 WMIGNNMIF 711

DIL

pfam01843

DIL domain; The DIL domain has no known function.

1681-1784

7.80e-42

DIL domain; The DIL domain has no known function.

Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 148.89 E-value: 7.80e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1681 QVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLRYNISQLEEWLRGKNLhQSGAVQTMEPLIQAAQLLQLKKKTHEDAEA 1760
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79

                           90       100
                   ....*....|....*....|....
gi 569003409  1761 ICSLCTSLSTQQIVKILNLYTPLN 1784
Cdd:pfam01843   80 ILQVCPALNPLQLHRLLTLYQPDD 103

MYSc_Myo33

cd14894

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

196-697

3.54e-31

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: 133.33 E-value: 3.54e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  196 VLASSPIMEAIGNAKTTRNDNSSRFGKF--IEIGFDK---KYHIIGANMRTYLLEKSRVVFQA------DDERNYHIFYQ 264
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  265 LCAAASLPEF-----KELALTCAEDFFYTAHG-------GNTTIEGV--NDADDFEKTRQALTLLGVRDSHQISIFKIIA 330
Cdd:cd14894   329 MVAGVNAFPFmrllaKELHLDGIDCSALTYLGrsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  331 SILHLGSVEIQSERDGDSCSISPQD-----EHLSNFCSLLGIEhsQMEHWLCHRK--LVTTSETYVKTMSLQQVVNARDA 403
Cdd:cd14894   409 AVLWLGNIELDYREVSGKLVMSSTGalnapQKVVELLELGSVE--KLERMLMTKSvsLQSTSETFEVTLEKGQVNHVRDT 486

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  404 LAKHIYAQLFSWIVEHINKA-----LHTSLKQH------------SFIGVLDIYGFETFEINSFEQFCINYANEKLQQqf 466
Cdd:cd14894   487 LARLLYQLAFNYVVFVMNEAtkmsaLSTDGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA-- 564

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  467 nshvfKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQK----------LYERHSnSQ 536
Cdd:cd14894   565 -----REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQEekrnklfvrnIYDRNS-SR 638

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  537 HFQKPRMSNTA------------FIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNT 604
Cdd:cd14894   639 LPEPPRVLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQLGWSPNT 718

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  605 AKNRSSSKINVRSSrplikvpnkehKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGV 684
Cdd:cd14894   719 NRSMLGSAESRLSG-----------TKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRL 787

                         570
                  ....*....|....*.
gi 569003409  685 ---LETIRISAAGYPS 697
Cdd:cd14894   788 irqMEICRNSSSSYSA 803

Myo5p-like_CBD_DIL_ANK

cd15473

cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ...

1485-1824

6.47e-29

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: 119.20 E-value: 6.47e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1485 LVTDLKPQMLSgTVPCLPAYILYMCIRHADYTNDDLKVHSLLSSTINGIKKVLKKHNDDFEMTSFWLSNTCRFLHCLKQy 1564
Cdd:cd15473    17 LITNMTPQRSP-SQRPVPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNVTLLLHYLKK- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1565 sgDEGFmtqntakqnehclkNFDLTEYRQVLSDLSIQIYQQLIKIAEGLLQPMIVSAmlenesiqglsgvrPtgyRKrss 1644
Cdd:cd15473    95 --DAGL--------------VEATPEFQQELAELINEIFVLIIRDAERRIDKLLDAS--------------P---RN--- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1645 smvdgensycleaIVRQMNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLRYNISQLEEWL 1724
Cdd:cd15473   139 -------------ITSLLSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWA 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1725 RGKNLH-------QSGAVQTMEPLIQAAQLLQ-LKKKTHEDA--EAICSLcTSLSTQQIVKILNLYTPlnEFEE-RVTVS 1793
Cdd:cd15473   206 RSNNLQpekgespPRIARSHLAPVIQLLQWLQcLSSLDDFESliATIQQL-DALNPLQLLRAVKDYRY--EVNEgRMPEE 282

                         330       340       350
                  ....*....|....*....|....*....|.
gi 569003409 1794 FIRTIqAQLQErnDPqqllLDSKHVFPVLFP 1824
Cdd:cd15473   283 CVKYL-AQLQK--DW----LDSRYMLPFSLP 306

fMyo2p_CBD

cd15480

cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ...

1660-1843

1.66e-27

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: 116.52 E-value: 1.66e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1660 RQMNSFHtvlcdqgLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLRYNISQLEEWLRGKNLhQSGAVQtME 1739
Cdd:cd15480   180 KSMKSYY-------IEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWCKSHDI-PEGTLQ-LE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1740 PLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPlNEFEERVTVSFIRTIQAQLQ--ERNDPQQLLLDSKH 1817
Cdd:cd15480   251 HLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYYV-ADYENPISPEILKAVAARVKpeDKSDHLLLIPLVEE 329

                         170       180
                  ....*....|....*....|....*.
gi 569003409 1818 VFPVLFPYnPSALTMDSIHIPACLNL 1843
Cdd:cd15480   330 VGPFEDPF-PREIAGLEAYIPAWLNL 354

Myo5p-like_CBD_fungal

cd15474

cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ...

1502-1827

1.97e-24

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: 107.12 E-value: 1.97e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1502 PAYILYMCIRHADYTNDDLKvhSLLSSTINGIKKVLKKHND----DFEMTS--FWLSNTCRFL----HCLKQYSGDEGFM 1571
Cdd:cd15474    34 LGHVNFLIYSQMWKSLLELL--TQSERFLSHVLSYIASIVDslpkKETIPDgaFWLANLHELRsfvvYLLSLIEHSSSDE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1572 TQntakQNEHCLKNFDLTEYRQVLSdlsiQIYQQLIKIAEGLLQPMIVSAMLENESIQGLSG---VRPTGYRKRSSSMVD 1648
Cdd:cd15474   112 FS----KESEEYWNTLFDKTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDLSElidLNKEFFNKPKKKMAD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1649 gensycleaIVRQMNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLRYNISQLEEWLRGKN 1728
Cdd:cd15474   184 ---------LITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQISYNVSRLKEWCHQHG 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1729 LhqSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPLNeFEERVTVSFIRTIqAQLQERNDP 1808
Cdd:cd15474   255 L--SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPAN-YEAPVPKEFLNAL-EKLIKKENL 330

                         330
                  ....*....|....*....
gi 569003409 1809 QQLLLDSKHVFPVLFPYNP 1827
Cdd:cd15474   331 SLPGRKNNSKMEIPESSNF 349

Myo5p-like_CBD_afadin

cd15471

cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ...

1502-1782

7.23e-17

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: 83.90 E-value: 7.23e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1502 PAYILYMCIRHADYTNDDL---------KVHSLLSSTINGIKKVLKKHNDDFEMTSFWLSNTCRFLHCLKQysgdegfmt 1572
Cdd:cd15471    25 PAYTLYLAARYRLSTHYRPeltpterahKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1573 qntakqnEHCLKNFDLTEyRQVLSDLSIQIYQQLIKIAEGLLQPMIVSAMLENESIQGLSGVrptgyrkrsssmvdGENS 1652
Cdd:cd15471    96 -------DRDLSAFSVQA-QDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPAI--------------GDVL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1653 YCLEAIVRQMNSFhtvlcdqGLDPEIILQVFKQLFYMINAVTLNNLLLRKDA--CSWSTGMQLRYNISQLEEWLRGKNLh 1730
Cdd:cd15471   154 HTLSSAMRLLRRC-------RVNAALTIQLFSQLFHFINAWLFNSLVSNPDSglCTRYWGKRLRQRLAHVEAWAERQGL- 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569003409 1731 QSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTP 1782
Cdd:cd15471   226 ELAADCHLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP 277

SMC_prok_B

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

897-1219

5.66e-12

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 5.66e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   897 RLKARQElKALKIEARSAEHLKRLNV---GMENKVVQLQRKIDdQNKEFKTLSEQLSAVtsSHAVEVEKLKKELAHYQQN 973
Cdd:TIGR02168  169 KYKERRK-ETERKLERTRENLDRLEDilnELERQLKSLERQAE-KAERYKELKAELREL--ELALLVLRLEELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   974 QEADTslQLQEEVQSLRTELQKAHSERRVLEDAHN----------KENGELRKRVADLEHENALLKDEKEYLNNQI---- 1039
Cdd:TIGR02168  245 QEELK--EAEEELEELTAELQELEEKLEELRLEVSeleeeieelqKELYALANEISRLEQQKQILRERLANLERQLeele 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1040 ---------LCQSKAESSQSSVEENLL------MKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKN-- 1102
Cdd:TIGR02168  323 aqleeleskLDELAEELAELEEKLEELkeelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNei 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1103 PSNQSSLESDSNYPSISTSEIGDTEDALQ--QVEEIGIEKAAMDMTVFlKLQKRVRELEQERKKLQAQLEKGQQ--DSKK 1178
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQalDAAE 481

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 569003409  1179 GQVEQQNNGLDVDQDAdiaynslkRQELESENKKLKNDLNE 1219
Cdd:TIGR02168  482 RELAQLQARLDSLERL--------QENLEGFSEGVKALLKN 514

MyosinXI_CBD

cd15475

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

1472-1780

1.18e-11

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: 67.98 E-value: 1.18e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1472 EYHKEDEALLIRNLVTDL-----KPqmlsgtvpcLPAYILYMCIRH-----ADYTNddlkvhsLLSSTINGIKKVLKKHN 1541
Cdd:cd15475     1 ERQQENVDALIKCVSENLgfsegKP---------VAAFTIYKCLLHwksfeAEKTS-------VFDRIIQTIGSAIEDQD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1542 DDFEMtSFWLSNTCRFLhclkqysgdegFMTQNTA-----KQNehclknfdLTEYRQvlsdlsiQIYqqlikiaegllqP 1616
Cdd:cd15475    65 NNDHL-AYWLSNTSTLL-----------FLLQRSLpallfKQQ--------LTAYVE-------KIY------------G 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1617 MI-------VSAMLeNESIQGLSGVRPTGYRKRSSSMVDGENSYCL--EAIVRQMNSFHTVLCDQGLDPEIILQVFKQLF 1687
Cdd:cd15475   106 IIrdnlkkeLSPLL-SLCIQAPRTSRGSSSKSSSSANSLGQQSPSShwQSIIKSLNSLLSTLKENHVPPFLVQKIFTQVF 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1688 YMINAVTLNNLLLRKDACSWSTGMQLRYNISQLEEW-LRGKNLHQSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICS-LC 1765
Cdd:cd15475   185 SFINVQLFNSLLLRRECCSFSNGEYVKAGLAELELWcSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDEITNdLC 264

                         330
                  ....*....|....*
gi 569003409 1766 TSLSTQQIVKILNLY 1780
Cdd:cd15475   265 PVLSVQQLYRICTMY 279

SMC_prok_B

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

938-1226

5.05e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 5.05e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   938 QNKEFKTLSEQLSAVTSshavEVEKLKKELAHYQQNQEadtslQLQEEVQSLRTELQkahsERRVLEDAHNKENGELRKR 1017
Cdd:TIGR02168  675 RRREIEELEEKIEELEE----KIAELEKALAELRKELE-----ELEEELEQLRKELE----ELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1018 VADLEHENALLKDEKEYLNNQIlcqskaESSQSSVEENLLMKKELEEER----SRYQNLVKEYSQLEQRYENLRDEVTIL 1093
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEI------EELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLL 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1094 KQTPGhrknpSNQSSLESdsnypsiSTSEIGDTEDALQQVEEIgIEKAAMDMTvflKLQKRVRELEQERKKLQAQLEKGQ 1173
Cdd:TIGR02168  816 NEEAA-----NLRERLES-------LERRIAATERRLEDLEEQ-IEELSEDIE---SLAAEIEELEELIEELESELEALL 879

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 569003409  1174 QdsKKGQVEQQNNGLDVDQDADIAynslKRQELESENKKLKNDLNELRKAVAD 1226
Cdd:TIGR02168  880 N--ERASLEEALALLRSELEELSE----ELRELESKRSELRRELEELREKLAQ 926

PRK03918

DNA double-strand break repair ATPase Rad50;

901-1269

3.17e-10

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 3.17e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  901 RQELKALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTS------SHAVEVEKLKKELAHYQQNQ 974
Cdd:PRK03918  175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkeleELKEEIEELEKELESLEGSK 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  975 EAdtslqLQEEVQSLRTELQKAHSERRVLEDaHNKENGELRKRVADLEHENALLKDEKEYLNNQILCQSKAESSQSSVEE 1054
Cdd:PRK03918  255 RK-----LEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1055 NLL----MKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQsslesdsnypsistsEIGDTEDAL 1130
Cdd:PRK03918  329 RIKeleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL---------------TPEKLEKEL 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1131 QQVEE--IGIEKAamdmtvFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQV------EQQNNGLDVDQDADIAYNSLK 1202
Cdd:PRK03918  394 EELEKakEEIEEE------ISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgreltEEHRKELLEEYTAELKRIEKE 467

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569003409 1203 RQELESENKKLKNDLNELRKAVADQ---------AMQDNSTHSSPDSYSllLNQLKLANEELEVRKEEVLILRTQI 1269
Cdd:PRK03918  468 LKEIEEKERKLRKELRELEKVLKKEseliklkelAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEI 541

SMC_prok_A

TIGR02169

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

818-1235

4.19e-10

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

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 4.19e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   818 IVFQKQYRmlkarRAYRRVCRATVIIQSFTRAMFVRRNYRQVLME--------------HKATIIQKYARGWMARKRFLR 883
Cdd:TIGR02169  606 VEFDPKYE-----PAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEgelfeksgamtggsRAPRGGILFSRSEPAELQRLR 680

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   884 ERDAAIVIQCAF---RRLKARQELKALKIEARSAEhlkRLNVGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTsshaVEV 960
Cdd:TIGR02169  681 ERLEGLKRELSSlqsELRRIENRLDELSQELSDAS---RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE----QEI 753

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   961 EKLKKELAHYQ---QNQEADTSlQLQEEVQSLRTELqkAHSERRVLEDAHNKENGELRKRVADLEHENALLKD---EKEY 1034
Cdd:TIGR02169  754 ENVKSELKELEariEELEEDLH-KLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEY 830

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1035 L--------NNQILCQSKAESSQSSVEENLLMKKELEEERSRYQNLVKEysqLEQRYENLRDEVTILKQTPGHRKNPSNQ 1106
Cdd:TIGR02169  831 LekeiqelqEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD---LESRLGDLKKERDELEAQLRELERKIEE 907

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1107 SSLESDSNYPSIST---------SEIGDTEDALQQVEEIGIEKAAMDmtvflKLQKRVRELEQERKKLqaqlekgqqdsk 1177
Cdd:TIGR02169  908 LEAQIEKKRKRLSElkaklealeEELSEIEDPKGEDEEIPEEELSLE-----DVQAELQRVEEEIRAL------------ 970

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569003409  1178 kGQVeqqnNGLDVDQDADIA--YNSL--KRQELESENKKLK---NDLNELRKAVADQAMQDNSTH 1235
Cdd:TIGR02169  971 -EPV----NMLAIQEYEEVLkrLDELkeKRAKLEEERKAILeriEEYEKKKREVFMEAFEAINEN 1030

PRK02224

DNA double-strand break repair Rad50 ATPase;

852-1227

1.36e-09

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 1.36e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  852 VRRNYRQVLMEHKATIIQKYARGWMARKRFLRERDA---AIVIQCAFRRLKARQELKALK-IEARSAEHLKRLNVgMENK 927
Cdd:PRK02224  181 VLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAeldEEIERYEEQREQARETRDEADeVLEEHEERREELET-LEAE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  928 VVQLQRKIDDQNKEFKTLSEQLSavtsSHAVEVEKLKKELAHYQ-----QNQEADTSLQLQEEVQSLRTELQKAHSERRV 1002
Cdd:PRK02224  260 IEDLRETIAETEREREELAEEVR----DLRERLEELEEERDDLLaeaglDDADAEAVEARREELEDRDEELRDRLEECRV 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1003 LEDAHNKENGELRKRVADLEHENALLKDEKEYLNNQIL-CQSKAESSQSSVEEnllMKKELEEERSRYQNLVKEYSQLEQ 1081
Cdd:PRK02224  336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEeAREAVEDRREEIEE---LEEEIEELRERFGDAPVDLGNAED 412

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1082 RYENLRDEVTILKQTPGH--------RKNPSNQSSLESDSNYP----SISTSEIGDT-EDALQQVEEIGIEKAAMDMTVf 1148
Cdd:PRK02224  413 FLEELREERDELREREAEleatlrtaRERVEEAEALLEAGKCPecgqPVEGSPHVETiEEDRERVEELEAELEDLEEEV- 491

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003409 1149 LKLQKRVRELEqERKKLQAQLEKGQQdsKKGQVEQqnngLDVDQDADIAYNSLKRQELESENKKLKNDLNELRKAVADQ 1227
Cdd:PRK02224  492 EEVEERLERAE-DLVEAEDRIERLEE--RREDLEE----LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

887-1458

1.62e-09

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.06 E-value: 1.62e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   887 AAIVIQCAFRRLKARQELKALKIEaRSAEHLKRLNVgmenkvVQLQRKIDDQNKEFKTLSEQLSAVTSSHavEVEKLKKE 966
Cdd:TIGR00618  299 IKAVTQIEQQAQRIHTELQSKMRS-RAKLLMKRAAH------VKQQSSIEEQRRLLQTLHSQEIHIRDAH--EVATSIRE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   967 LAHyQQNQEADTSLQLQEEVQSLRTELQKAHSERRVL-EDAHNKENGELRKRV--ADLEHENALLKDEKEYLnnqilcQS 1043
Cdd:TIGR00618  370 ISC-QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILqREQATIDTRTSAFRDlqGQLAHAKKQQELQQRYA------EL 442

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1044 KAESSQSSVEENLLMKKELEEERSRYqnlvKEYSQLEQRYENLRDEVTILKQTPGHRKN--PSNQSSLESDSNYPSISTS 1121
Cdd:TIGR00618  443 CAAAITCTAQCEKLEKIHLQESAQSL----KEREQQLQTKEQIHLQETRKKAVVLARLLelQEEPCPLCGSCIHPNPARQ 518

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1122 EIGDTEdALQQVEEIGIEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQVEQQNNGLDVDQDADIAYNSL 1201
Cdd:TIGR00618  519 DIDNPG-PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1202 KRQELESENKKLKNDLN--ELRKAVADQAMQDNSTHSSPDSYSLLLNQLKLANEELEVRKEEV-----LILRTQIMNADQ 1274
Cdd:TIGR00618  598 DLTEKLSEAEDMLACEQhaLLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVrehalSIRVLPKELLAS 677

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1275 RRLSGKNMEPNINARTSWPNSEKHVD-----QEDAIEAYHGVCQTNSQTEDWGYLNEDGELGLAYQGLKQVARLLEAQLQ 1349
Cdd:TIGR00618  678 RQLALQKMQSEKEQLTYWKEMLAQCQtllreLETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK 757

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1350 AQSLEHEEEVEHLKAQVEALKEEMDKQQQTFCQTLLLSPEAQVEFGVQQEISRLTNENLDFKEL-VEKLEKNERKLKKQL 1428
Cdd:TIGR00618  758 ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLqCETLVQEEEQFLSRL 837

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 569003409  1429 KIYMKKV--------QDLEAAQALAQSDRRHHELTRQV 1458
Cdd:TIGR00618  838 EEKSATLgeithqllKYEECSKQLAQLTQEQAKIIQLS 875

PRK03918

DNA double-strand break repair ATPase Rad50;

899-1269

2.36e-09

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.36e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  899 KARQELKALKIEARSAEHLKRlnvGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTS--SHAVEVEKLKKELAHY-QQNQE 975
Cdd:PRK03918  235 ELKEEIEELEKELESLEGSKR---KLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYlDELRE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  976 ADTSL-QLQEEVQSLRTELQKAHSERRVLEDAHNKENgELRKRVADLEHENALLKDEKEYLNN-QILCQSKAESSQSSVE 1053
Cdd:PRK03918  312 IEKRLsRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKKEElERLKKRLTGLTPEKLE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1054 ENLLM----KKELEEERSryqNLVKEYSQLEQRYENLRDEVTILKQTPG------------HRKNPSNQSSLESD----- 1112
Cdd:PRK03918  391 KELEElekaKEEIEEEIS---KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteeHRKELLEEYTAELKrieke 467

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1113 ----------------------SNYPSISTSEigDTEDALQQVEE----IGIEKAAMDMTVFLKLQKRVRELEQERKKLQ 1166
Cdd:PRK03918  468 lkeieekerklrkelrelekvlKKESELIKLK--ELAEQLKELEEklkkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1167 AQLEKGQQ-DSKKGQVEQqnngldvdqdadiaynslKRQELESENKKLKNDLNELRKAVADqamQDNSTHSSPDSYSLLL 1245
Cdd:PRK03918  546 KELEKLEElKKKLAELEK------------------KLDELEEELAELLKELEELGFESVE---ELEERLKELEPFYNEY 604

                         410       420
                  ....*....|....*....|....
gi 569003409 1246 NQLKLANEELEVRKEEVLILRTQI 1269
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEEL 628

SMC_prok_A

TIGR02169

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

902-1174

4.94e-09

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 4.94e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   902 QELKALKIEARSAEHLKRLNV-------------GMENKVVQLQRKIDDQNKEF-------KTLSEQLSAVTSSHAV--- 958
Cdd:TIGR02169  214 QALLKEKREYEGYELLKEKEAlerqkeaierqlaSLEEELEKLTEEISELEKRLeeieqllEELNKKIKDLGEEEQLrvk 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   959 --------EVEKLKKELAHYQQNQEadtslQLQEEVQSLRTELQKAHSERRVLEdahnKENGELRKRVADLEHENALLKD 1030
Cdd:TIGR02169  294 ekigeleaEIASLERSIAEKERELE-----DAEERLAKLEAEIDKLLAEIEELE----REIEEERKRRDKLTEEYAELKE 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1031 EKEYLNNQIlcQSKAESSQSSVEENLLMKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQtpghrknpsnqssle 1110
Cdd:TIGR02169  365 ELEDLRAEL--EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA--------------- 427

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569003409  1111 sdsnypsistsEIGDTEDALQQVEEigiekaamdmtVFLKLQKRVRELEQERKKLQAQLEKGQQ 1174
Cdd:TIGR02169  428 -----------AIAGIEAKINELEE-----------EKEDKALEIKKQEWKLEQLAADLSKYEQ 469

Myo5p-like_CBD_Rasip1

cd15472

cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ...

1674-1782

1.85e-08

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: 58.44 E-value: 1.85e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1674 LDPEIILQVFKQLFYMINAVTLNNLLLRKDACS---WSTGMQLRYNISQLEEWLRGKNLHQSgAVQTMEPLIQAAQLLQL 1750
Cdd:cd15472   216 VHPEIASQMFAYLFFFSNASLFNQLMEKGSGGGffqWSRGVQIRANLDLLLDWLQGAGLGDL-AEEFFRKLSSTVNLLAT 294

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569003409 1751 KKKT--HEDAEAICSLCTSLSTQQIVKILNLYTP 1782
Cdd:cd15472   295 PKEQllQMSWSSLRAEFPALNPAQLHHLLRQYQL 328

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

915-1262

1.98e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 1.98e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   915 EHLKRLNVGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTSSHavevEKLKKELAHYQQ--NQEADTSLQLQEEVQSLRTE 992
Cdd:TIGR04523  221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ----NKIKKQLSEKQKelEQNNKKIKELEKQLNQLKSE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   993 LQKAHSERRvlEDAHNKENGELRKRVADLEH-ENALLKDEKEY--LNNQIlcQSKAESSQSSVEENLLMKKELEEERSRY 1069
Cdd:TIGR04523  297 ISDLNNQKE--QDWNKELKSELKNQEKKLEEiQNQISQNNKIIsqLNEQI--SQLKKELTNSESENSEKQRELEEKQNEI 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1070 QNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQ--SSLES-DSNYPSIStSEIGD-TEDALQQVEEIG--IEKAAM 1143
Cdd:TIGR04523  373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQkdEQIKKlQQEKELLE-KEIERlKETIIKNNSEIKdlTNQDSV 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1144 DMTVFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQVE------------QQNNGLD---VDQDADIAYNSLKRQELES 1208
Cdd:TIGR04523  452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekelkklnEEKKELEekvKDLTKKISSLKEKIEKLES 531

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003409  1209 ENKKLKNDLNELRKAVA--DQAMQDNSTHSSPDSYSLLLNQLKLANEELEVRKEEV 1262
Cdd:TIGR04523  532 EKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587

SCP-1

pfam05483

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

932-1375

2.40e-08

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.35 E-value: 2.40e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   932 QRKIDDQNKEFKTLS----------EQLSAVTSSHAVEVEKLKKELAhyqqnqEADTSLQLQEEVQSLRTELQKAHSERR 1001
Cdd:pfam05483  369 QQRLEKNEDQLKIITmelqkksselEEMTKFKNNKEVELEELKKILA------EDEKLLDEKKQFEKIAEELKGKEQELI 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1002 VLEDAHNKEngelrkrVADLEHENALLKDEKEYLNNQilcqskaessqssVEEnllMKKELEEERSRYQNLVKEYSQLEQ 1081
Cdd:pfam05483  443 FLLQAREKE-------IHDLEIQLTAIKTSEEHYLKE-------------VED---LKTELEKEKLKNIELTAHCDKLLL 499

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1082 RYENLRDEVT-ILKQTPGHRKNPSNQSSLEsdsnypsistseigdtEDALQQVEEIgiekAAMDMTVFLKLQKRVRELEQ 1160
Cdd:pfam05483  500 ENKELTQEASdMTLELKKHQEDIINCKKQE----------------ERMLKQIENL----EEKEMNLRDELESVREEFIQ 559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1161 ERKKLQAQLEKGQQDSKKGQVEQQNNGLDVDQDADIAyNSLKRQeLESENKKLKnDLNELRKAVADQAMQDNSthsSPDS 1240
Cdd:pfam05483  560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC-NNLKKQ-IENKNKNIE-ELHQENKALKKKGSAENK---QLNA 633

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1241 YSLLLNQLKLANEELEVRKEEvlILRTQIMNADQRRLSGKNMEPNINARTSWPNSEKHVDQEDAIEAYHGVCQTNSQTE- 1319
Cdd:pfam05483  634 YEIKVNKLELELASAKQKFEE--IIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEk 711

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569003409  1320 -----DWGYLNEDGELGLaYQGLKQVARLLEAQLQAQSLEHEEEVEHLKAQVEALKEEMDK 1375
Cdd:pfam05483  712 hkhqyDKIIEERDSELGL-YKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

937-1276

2.97e-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: 58.98 E-value: 2.97e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   937 DQNKEFKTLSEQLSAVTSSHAV--------EVEKLKkELAHYQQNQEADTSLQLQE-----EVQSLRTELQKAHSE---R 1000
Cdd:pfam17380  237 ERRKESFNLAEDVTTMTPEYTVryngqtmtENEFLN-QLLHIVQHQKAVSERQQQEkfekmEQERLRQEKEEKAREverR 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1001 RVLEDAHNKENGELRKRVADL-EHENALLKDEKEylnnqiLCQSKAESSQSSVEEnlLMKKELEEERSRYQNLvkEYSQL 1079
Cdd:pfam17380  316 RKLEEAEKARQAEMDRQAAIYaEQERMAMERERE------LERIRQEERKRELER--IRQEEIAMEISRMREL--ERLQM 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1080 EQRYENLRdevtILKQTPGHRKNPSNQSSLESDSNYPSISTSEI-GDTEDALQQVEEIGIEKAAMDMtvflklqKRVREL 1158
Cdd:pfam17380  386 ERQQKNER----VRQELEAARKVKILEEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREM-------ERVRLE 454

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1159 EQERKKLQAQLEKGQQDSKKGQV----EQQNNGLDVDQDADIAYNSL---KRQELESENKK--LKNDLNELRKAVADQ-- 1227
Cdd:pfam17380  455 EQERQQQVERLRQQEEERKRKKLelekEKRDRKRAEEQRRKILEKELeerKQAMIEEERKRklLEKEMEERQKAIYEEer 534

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 569003409  1228 ---AMQDNSTHSSPDSYSLLLNQLKLANEE---LEVRKEEVLILRTQIMNADQRR 1276
Cdd:pfam17380  535 rreAEEERRKQQEMEERRRIQEQMRKATEErsrLEAMEREREMMRQIVESEKARA 589

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

917-1303

1.85e-07

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 1.85e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   917 LKRLNVGMENKVVQLQRKIDDQNKEFKTLSEQLSA------VTSSHAVEVEKLKKELAHY--QQNQEADTSLQLQEEVQS 988
Cdd:TIGR04523  164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlelllsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   989 LRTELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKEYLNN-----QILCQSKAESSQSSVEENLL-MKKEL 1062
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlkseiSDLNNQKEQDWNKELKSELKnQEKKL 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1063 EEERSRYQNLVKEYSQLEQRYENLRDEVTIL-------------KQTPGHRKNPSNQSSLESDSNYpsisTSEIGDTEDA 1129
Cdd:TIGR04523  324 EEIQNQISQNNKIISQLNEQISQLKKELTNSesensekqreleeKQNEIEKLKKENQSYKQEIKNL----ESQINDLESK 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1130 LQQVEEIGIEKaamdmtvflklQKRVRELEQERKKLQAQLEKgqqdsKKGQVEQQNNGLD--VDQDA--DIAYNSLKR-- 1203
Cdd:TIGR04523  400 IQNQEKLNQQK-----------DEQIKKLQQEKELLEKEIER-----LKETIIKNNSEIKdlTNQDSvkELIIKNLDNtr 463

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1204 -------QELESENKKLKNDLNELRKAVADQAMQDNSTHSSPdsySLLLNQLKLANEELEVRKEEVLILRTQIMNADQRR 1276
Cdd:TIGR04523  464 esletqlKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK---KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540

                          410       420
                   ....*....|....*....|....*..
gi 569003409  1277 LSGKNMEPNINARTSWPNSEKHVDQED 1303
Cdd:TIGR04523  541 SDLEDELNKDDFELKKENLEKEIDEKN 567

SMC_prok_B

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

899-1088

2.17e-07

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 2.17e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   899 KARQELKALKIEARSAEHLKRlnvGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTSSHA---VEVEKLKKELAHY--QQN 973
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLE---SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEeleELIEELESELEALlnERA 883

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   974 QEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKEYLNNQ--------ILCQSKA 1045
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKI 963

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 569003409  1046 ESSQSSVEE---------------NLLMKKELEEERSRYQNLVKEYSQLEQRYENLRD 1088
Cdd:TIGR02168  964 EDDEEEARRrlkrlenkikelgpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021

HOOK

pfam05622

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...

902-1262

2.30e-07

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: 55.85 E-value: 2.30e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   902 QELKALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQNKEfktlSEQLSAVTSSHAVEVEKLKKELAHYQQNQEADTSL- 980
Cdd:pfam05622   35 QENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEE----NFRLETARDDYRIKCEELEKEVLELQHRNEELTSLa 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   981 ----QLQEEVQSLRTELQKA-------HSERRVLEDAhnkenGELRKRVADLEHENAllkdekEYLNNQILCQS---KAE 1046
Cdd:pfam05622  111 eeaqALKDEMDILRESSDKVkkleatvETYKKKLEDL-----GDLRRQVKLLEERNA------EYMQRTLQLEEelkKAN 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1047 SSQSSVEenlLMKKE-------LEEERSRYQNLVKEYSQLEQRY-------ENLRDEVTILKQTPGHRKNPSNQSSLESD 1112
Cdd:pfam05622  180 ALRGQLE---TYKRQvqelhgkLSEESKKADKLEFEYKKLEEKLealqkekERLIIERDTLRETNEELRCAQLQQAELSQ 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1113 SNYPSISTSEIGDTEDAlqqveEIgiekaamdmtVFLKLQKRVRELEQERKKLQAQLEkGQQDSKKGQVEQQnngLDvdq 1192
Cdd:pfam05622  257 ADALLSPSSDPGDNLAA-----EI----------MPAEIREKLIRLQHENKMLRLGQE-GSYRERLTELQQL---LE--- 314

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569003409  1193 DADiaynsLKRQELESENKKLKNDLNELRKAVADQAMQDNSTHSSPDSYSLL-------LNQLKLANEELEVRKEEV 1262
Cdd:pfam05622  315 DAN-----RRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLkqkleehLEKLHEAQSELQKKKEQI 386

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

915-1095

3.16e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.16e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  915 EHLKRLNvGMENKVVQLQRKID------DQNKEFKTLSEQLS---AVTSSHAVEVEKLKKELAHYQQNQEADTSLQLQEE 985
Cdd:COG4913   232 EHFDDLE-RAHEALEDAREQIEllepirELAERYAAARERLAeleYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  986 VQSLRTELQKAHSERRVLEDAHNKENGElrkRVADLEHENALLKDEKE-----YLNNQILCQS---KAESSQSSVEENLL 1057
Cdd:COG4913   311 LERLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEererrRARLEALLAAlglPLPASAEEFAALRA 387

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 569003409 1058 ----MKKELEEERSRYQN----LVKEYSQLEQRYENLRDEVTILKQ 1095
Cdd:COG4913   388 eaaaLLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLER 433

Smc

COG1196

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

940-1494

7.73e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 7.73e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  940 KEFKTLSEQLsavtsshavevEKLKKELAHYQQNQEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNK---ENGELRK 1016
Cdd:COG1196   213 ERYRELKEEL-----------KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEElrlELEELEL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1017 RVADLEHENALLKDEKEYLNNQIlcQSKAESSQSSVEENLLMKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKqt 1096
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDI--ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-- 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1097 pghrknpsnQSSLESDSNYPSISTSEIGDTEDALQQVEEigIEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKgQQDS 1176
Cdd:COG1196   358 ---------AELAEAEEALLEAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEE-ELEE 425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1177 KKGQVEQQNNGLDVDQDADIAyNSLKRQELESENKKLKNDLNELRKAVADQAMQDNSTHSSPDSYSLLLNQLKLANEELE 1256
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1257 VRKEEVLILRTqimNADQRRLSGKnmepnINARTSWPNSEkhvdqEDAIEAYHGVCQTNSQTEDWGYLnEDGELGLAYQG 1336
Cdd:COG1196   505 GFLEGVKAALL---LAGLRGLAGA-----VAVLIGVEAAY-----EAALEAALAAALQNIVVEDDEVA-AAAIEYLKAAK 570

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1337 LKQVARLLEAQLQAQSLEHEEEVEHLKAQVEALKEEMDKQQQTFCQTLLLSPEAQVEFGVQQEISRLTNENLDFKELVEK 1416
Cdd:COG1196   571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1417 LEK---NERKLKKQLKIYMKKVQDLEAAQALAQSDRRHHELTRQVTVQRKEKDFQGMLEYHKEDEALLIRNLVTDLKPQM 1493
Cdd:COG1196   651 LEGeggSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730


                  .
gi 569003409 1494 L 1494
Cdd:COG1196   731 E 731

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

917-1297

8.46e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 8.46e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   917 LKRLNVGMENKVVQLQRKIDDQ----NKEFKTLSEQLSAVTSSHAVEVEKLKKeLAHYQQNQEADTSLQLQEEVQSLRTE 992
Cdd:pfam02463  125 LESQGISPEAYNFLVQGGKIEIiammKPERRLEIEEEAAGSRLKRKKKEALKK-LIEETENLAELIIDLEELKLQELKLK 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   993 LQ---------------------KAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKEYLNNQILCQSKAESSQSS 1051
Cdd:pfam02463  204 EQakkaleyyqlkekleleeeylLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1052 VEENLLMKKELEEErsryqnLVKEYSQLEQRYENLRDEVTILKQtpghrKNPSNQSSLEsdsnypsistSEIGDTEDALQ 1131
Cdd:pfam02463  284 QEEELKLLAKEEEE------LKSELLKLERRKVDDEEKLKESEK-----EKKKAEKELK----------KEKEEIEELEK 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1132 QVEEIGIEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKGQQ-DSKKGQVEQQNNGLDVDQDADIAYNSLKRQE---LE 1207
Cdd:pfam02463  343 ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlSSAAKLKEEELELKSEEEKEAQLLLELARQLedlLK 422

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1208 SENKKLKNDLNELRKAVADQAMQDNSTHSSPDSYSLLLNQLKLANEELEVRKEEvLILRTQIMNADQRRLSGKNMEPNIN 1287
Cdd:pfam02463  423 EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE-TQLVKLQEQLELLLSRQKLEERSQK 501

                          410
                   ....*....|
gi 569003409  1288 ARTSWPNSEK 1297
Cdd:pfam02463  502 ESKARSGLKV 511

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

924-1459

1.10e-06

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 1.10e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   924 MENKVVQLQRKIDDQNKEFKTLSEQLsavtsshavevekLKKElahyqqnqeadtslqlqEEVQSLRTELQKAHSERRVL 1003
Cdd:TIGR04523   38 LEKKLKTIKNELKNKEKELKNLDKNL-------------NKDE-----------------EKINNSNNKIKILEQQIKDL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1004 EDAHNKENGELRKRVADLEHENALLKDEKEYLNNQILCQSKAESSQSSVEENL-LMKKELEEERSRYQNLVKEYSQLEQR 1082
Cdd:TIGR04523   88 NDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIdKFLTEIKKKEKELEKLNNKYNDLKKQ 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1083 YENLRDEVTILKqtpghrKNPSNQSSLESDSNypsistSEIGDTEDALQQVEEIgIEKAAmdmtvflKLQKRVRELEQER 1162
Cdd:TIGR04523  168 KEELENELNLLE------KEKLNIQKNIDKIK------NKLLKLELLLSNLKKK-IQKNK-------SLESQISELKKQN 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1163 KKLQAQLEKGQQDSKKGQ-----VEQQNNGLDVDQDADIAYNSLKRQELESENKKLK---NDLNELRKAVADQAMQDNSt 1234
Cdd:TIGR04523  228 NQLKDNIEKKQQEINEKTteisnTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKeleKQLNQLKSEISDLNNQKEQ- 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1235 hsspdsyslllNQLKLANEELEVRKEEVLILRTQIMNADQRRLSGKNMEPNINARTSWPNSEKHVDQEDAIEAYHGVCQT 1314
Cdd:TIGR04523  307 -----------DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1315 NSQTEdwGYLNEdgelglaYQGLKQVARLLEAQLQAQSLEHEEEVEHLKaQVEALKEEMDKQQQTFCQTLLLSpeaqvef 1394
Cdd:TIGR04523  376 KKENQ--SYKQE-------IKNLESQINDLESKIQNQEKLNQQKDEQIK-KLQQEKELLEKEIERLKETIIKN------- 438

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1395 gvQQEISRLTNENLDFKELVEKLEKNERKLKKQLKIYMKKV----QDLEA-AQALAQSDRRHHELTRQVT 1459
Cdd:TIGR04523  439 --NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSInkikQNLEQkQKELKSKEKELKKLNEEKK 506

GumC

COG3206

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

901-1096

1.65e-06

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.65e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  901 RQELKALKIEARSAEH-LKRLNVgmENKVVQLQRKIDDQNKEFKTLSEQLSAVTSSHA---VEVEKLKKELAhyqQNQEA 976
Cdd:COG3206   181 EEQLPELRKELEEAEAaLEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAELAeaeARLAALRAQLG---SGPDA 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  977 DTSLQLQEEVQSLRTELQKAHSERRvledahnkengELRKRVADlEHENAL-LKDEKEYLNNQILCQSKA--ESSQSSVE 1053
Cdd:COG3206   256 LPELLQSPVIQQLRAQLAELEAELA-----------ELSARYTP-NHPDVIaLRAQIAALRAQLQQEAQRilASLEAELE 323

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 569003409 1054 ENLLMKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQT 1096
Cdd:COG3206   324 ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

899-1137

2.32e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.32e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  899 KARQELKALKIEARSAEH-LKRLNVGME---NKVVQLQRKIDDQNKEFKTLSEQLSAVTSSHAVEVEKLKKELAHYQQNQ 974
Cdd:COG3883    20 AKQKELSELQAELEAAQAeLDALQAELEelnEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  975 EADTSLQLQEEVQSLRTELQKAHSERRVLeDAHNKENGELRKRVADLEHENALLKDEKEYLNNQilcQSKAESsqssvee 1054
Cdd:COG3883   100 GSVSYLDVLLGSESFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEAL---KAELEA------- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1055 nllMKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQSSLESDSNYPSISTSEIGDTEDALQQVE 1134
Cdd:COG3883   169 ---AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245


                  ...
gi 569003409 1135 EIG 1137
Cdd:COG3883   246 AAG 248

Motor_domain

cd01363

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

637-661

3.40e-06

Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 49.27 E-value: 3.40e-06

                          10        20
                  ....*....|....*....|....*
gi 569003409  637 FRTSLNLLMETLNATTPHYVRCIKP 661
Cdd:cd01363   146 INESLNTLMNVLRATRPHFVRCISP 170

CCDC158

pfam15921

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

905-1283

5.69e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 5.69e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   905 KALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTSSHAVEVEKLKKELAHYQQNQEADTSL--QL 982
Cdd:pfam15921  391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLtaQL 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   983 QEEVQSLRTELQKAHSERRVLE--------------------DAHNKENGELRKRVaDLE-HENALLKDEKEYLNNqilC 1041
Cdd:pfam15921  471 ESTKEMLRKVVEELTAKKMTLEssertvsdltaslqekeraiEATNAEITKLRSRV-DLKlQELQHLKNEGDHLRN---V 546

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1042 QSKAESSQSSVEENllmKKELEEERSRYQNLVK--------------EYSQLEQRYENLR---DEVTILKQtpghrKNPS 1104
Cdd:pfam15921  547 QTECEALKLQMAEK---DKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRlelQEFKILKD-----KKDA 618

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1105 NQSSLE---SDSNYPSISTSEIGdtEDALQQVEEIGIEKAAM----------------DMTVFLK-LQKRVRELEQERKK 1164
Cdd:pfam15921  619 KIRELEarvSDLELEKVKLVNAG--SERLRAVKDIKQERDQLlnevktsrnelnslseDYEVLKRnFRNKSEEMETTTNK 696

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1165 LQAQLEKGQQdskkgQVEQQNNGLDVDQDADiAYNSLKRQELESENKKLKNDLNELRKAVadQAMQDNSTHSSPDSYSLL 1244
Cdd:pfam15921  697 LKMQLKSAQS-----ELEQTRNTLKSMEGSD-GHAMKVAMGMQKQITAKRGQIDALQSKI--QFLEEAMTNANKEKHFLK 768

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 569003409  1245 LNQLKLANEELEVRKE------EVLILRTQimnadQRRLSGK--NME 1283
Cdd:pfam15921  769 EEKNKLSQELSTVATEknkmagELEVLRSQ-----ERRLKEKvaNME 810

YhaN

COG4717

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

956-1185

5.76e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 5.76e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  956 HAVEVEKLKKELAHYQQNQEADTSLQLQEevqslrteLQKAHSERRVLEDAHnKENGELRKRVADLEHENALLKDEKEYL 1035
Cdd:COG4717    44 RAMLLERLEKEADELFKPQGRKPELNLKE--------LKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEEL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1036 NNQILCQSKAESSQSSVEENLLMKKELEEERSRYQNL---VKEYSQLEQRYENLRDEVTILKQtpghrknpsnqsSLESD 1112
Cdd:COG4717   115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQE------------ELEEL 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003409 1113 SNYPSISTSEigDTEDALQQVEEigiekaamdmtvflkLQKRVRELEQERKKLQAQLEKGQQDSKKGQVEQQN 1185
Cdd:COG4717   183 LEQLSLATEE--ELQDLAEELEE---------------LQQRLAELEEELEEAQEELEELEEELEQLENELEA 238

PTZ00121

MAEBL; Provisional

806-1427

1.12e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.12e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  806 RLAEHLRRTRAAIVFQKQYRMLKARR--------AYRRVCRATVIIQSFTRAMFVRRN-----YRQVLMEHKATIiQKYA 872
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKaedakkaeAVKKAEEAKKDAEEAKKAEEERNNeeirkFEEARMAHFARR-QAAI 1272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  873 RGWMARK----RFLRERDAAIVIQCAFRRLKArQELKALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQNK--EFKTLS 946
Cdd:PTZ00121 1273 KAEEARKadelKKAEEKKKADEAKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKaaEAAKAE 1351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  947 EQLSA---VTSSHAVEVEKLKKELAH---------YQQNQEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENgel 1014
Cdd:PTZ00121 1352 AEAAAdeaEAAEEKAEAAEKKKEEAKkkadaakkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE--- 1428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1015 RKRVADLEHENALLKDEKEYLNNQILCQSKAESSQSSVEEnllmKKELEEERSRYQNlVKEYSQLEQRYENLRDEVTILK 1094
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE----AKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAK 1503

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1095 QTPGHRKNPSNQSSLESDSNYPSISTSEIGDTEDALQQVEEIgieKAAMDmtvfLKLQKRVRELEQERKKLQAQLEKgqq 1174
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK---KKADE----LKKAEELKKAEEKKKAEEAKKAE--- 1573

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1175 dskkgqvEQQNNGLDVDQDADIAYNSLKRQELESENKKLKNDLNELRKAvaDQAMQDNSTHSSPDSYSLLLNQLKLANEE 1254
Cdd:PTZ00121 1574 -------EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1255 lEVRKEEVLILRTQIMNADQRRLSGKNMEPNINARTSWPNSEKHVDQEDAIEayhgvcqtnsqtedwgylNEDGELGLAY 1334
Cdd:PTZ00121 1645 -EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK------------------KEAEEAKKAE 1705

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1335 QGLKQVArllEAQLQAQSLEHEEEVEHLKAQVEALKEEMDKQQqtfcqtlllSPEAQVEFGVQQEISRLTNENLDFKELV 1414
Cdd:PTZ00121 1706 ELKKKEA---EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK---------AEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773

                         650
                  ....*....|....*
gi 569003409 1415 EKLEKN--ERKLKKQ 1427
Cdd:PTZ00121 1774 RKEKEAviEEELDEE 1788

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

880-1544

1.15e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 1.15e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   880 RFLRERDAAIVIQCAFRRLK-ARQELKALKIEARSAEHL------------KRLNVGMENKVVQLQRKIDDQNKEFKTLS 946
Cdd:pfam12128  235 GIMKIRPEFTKLQQEFNTLEsAELRLSHLHFGYKSDETLiasrqeerqetsAELNQLLRTLDDQWKEKRDELNGELSAAD 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   947 EQLSAVTSshavEVEKLKKELAHYQQnQEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKR--------- 1017
Cdd:pfam12128  315 AAVAKDRS----ELEALEDQHGAFLD-ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRrskikeqnn 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1018 --VADLEHENALLKDEK-----------EYLNNQILCQSKAESSQSSvEENLLMKKELEEERSRyQNLVKEYSQLEQRYE 1084
Cdd:pfam12128  390 rdIAGIKDKLAKIREARdrqlavaeddlQALESELREQLEAGKLEFN-EEEYRLKSRLGELKLR-LNQATATPELLLQLE 467

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1085 NLRDEVTILKQTPGHRKnpSNQSSLESD-----------SNYPSISTSEIGDTEDALQQVEEIGIEKAAmdmTVFLKLQK 1153
Cdd:pfam12128  468 NFDERIERAREEQEAAN--AEVERLQSElrqarkrrdqaSEALRQASRRLEERQSALDELELQLFPQAG---TLLHFLRK 542

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1154 RVRELEQERKKLQAQLEKGQQD----SKKGQVEQQNN----GLDVDQdADIAYNSLKRQELESENKKLKNDLNELRKAVA 1225
Cdd:pfam12128  543 EAPDWEQSIGKVISPELLHRTDldpeVWDGSVGGELNlygvKLDLKR-IDVPEWAASEEELRERLDKAEEALQSAREKQA 621

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1226 DQAmqdnsthsspdsyslllNQLKLANEELEVRKEEVLILRTQIMNA--DQRRLSGKnMEPNINARTSWPNSEKHVDQED 1303
Cdd:pfam12128  622 AAE-----------------EQLVQANGELEKASREETFARTALKNArlDLRRLFDE-KQSEKDKKNKALAERKDSANER 683

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1304 AIEAYHGVCQTNSQTEDW-----GYLNEDGELGLAYqgLKQVARLLEAQLQAQSLEHEEEVEHLKAQVEALKEEMDKQQQ 1378
Cdd:pfam12128  684 LNSLEAQLKQLDKKHQAWleeqkEQKREARTEKQAY--WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLA 761

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1379 TfcqtllLSPEAQVEFGVQQEIsrltnenldfKELVEKLEKNERKLKKQLKIYmkkvqDLEAAQALAQSDRRhheLTRQV 1458
Cdd:pfam12128  762 S------LGVDPDVIAKLKREI----------RTLERKIERIAVRRQEVLRYF-----DWYQETWLQRRPRL---ATQLS 817

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1459 TVQRKEKDFQGMLEYHKEDEALLIRNLVTDLKPQ-----MLSGTVPCLPAYILYMCIRHADYTNDDLKvHSL-------- 1525
Cdd:pfam12128  818 NIERAISELQQQLARLIADTKLRRAKLEMERKASekqqvRLSENLRGLRCEMSKLATLKEDANSEQAQ-GSIgerlaqle 896

                          730       740
                   ....*....|....*....|
gi 569003409  1526 -LSSTINGIKKVLKKHNDDF 1544
Cdd:pfam12128  897 dLKLKRDYLSESVKKYVEHF 916

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

915-1268

1.45e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.45e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   915 EHLKRLNVGMENKVVQLQRKIDDqnkefktLSEQLSavtsSHAVEVEKLKKELAHYQQNQ-EADTSLQLQEE-------- 985
Cdd:pfam10174  383 RDLKDMLDVKERKINVLQKKIEN-------LQEQLR----DKDKQLAGLKERVKSLQTDSsNTDTALTTLEEalsekeri 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   986 VQSLRTELQKAHSERRVLEDAHNKENGELRKRV----ADLEHENALLKDEKEYLNNQILCQSKAESSQSSVEENLLMKKE 1061
Cdd:pfam10174  452 IERLKEQREREDRERLEELESLKKENKDLKEKVsalqPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKE 531

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1062 leeERSRYQNLVKEYSQLE---QRYENLRDEVTILKQTPGHRKNPSNQSSlesdsnypsistSEIGDTEDALQQVEEigi 1138
Cdd:pfam10174  532 ---ECSKLENQLKKAHNAEeavRTNPEINDRIRLLEQEVARYKEESGKAQ------------AEVERLLGILREVEN--- 593

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1139 EKAAMDmtvflklqKRVRELEQERKKLQAQLEKGQQDSKKGQVEQQNNGLDVDQDADIAYNSLKRQELESENKKLKNDLN 1218
Cdd:pfam10174  594 EKNDKD--------KKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALE 665

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 569003409  1219 ELRKAVADQAMQDNSTHSSPDSYSLLLNQLKlaneeLEVRK--EEVLILRTQ 1268
Cdd:pfam10174  666 KTRQELDATKARLSSTQQSLAEKDGHLTNLR-----AERRKqlEEILEMKQE 712

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

860-1227

1.74e-05

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 1.74e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   860 LMEHKATIIQKYARGWMARKRFLRERDAAIVIQCAFRRLKARQELKALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQN 939
Cdd:pfam02463  638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   940 KEFKTLSEQLSAVTSSHAVEVEKLKKELAHYQQNQEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRva 1019
Cdd:pfam02463  718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK-- 795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1020 dlehenaLLKDEKEYLNNQILCQSKAESSQSSVEENLLMKKELEEERSRYQ-----------------------NLVKEY 1076
Cdd:pfam02463  796 -------LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAlelkeeqkleklaeeelerleeeITKEEL 868

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1077 SQ--LEQRYENLRDEVTILKQTPGHRKNPSNQsslESDSNYPSISTSEIGDTEDALQQVEEIGIEKAAMDMTVFLKLQKR 1154
Cdd:pfam02463  869 LQelLLKEEELEEQKLKDELESKEEKEKEEKK---ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003409  1155 VRELEQERKKLQAQLEKGQQDSKKGQVEQQNNGldvdQDADIAYNSLKRQELESENKKLKNDLNELRKAVADQ 1227
Cdd:pfam02463  946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLM----AIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014

fMyo4p_CBD

cd15479

cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin ...

1662-1790

2.08e-05

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: 48.82 E-value: 2.08e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1662 MNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLRYNISQLEEWLRGKNlhqSGAVQTMEPL 1741
Cdd:cd15479   168 LNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPALNWKYGYEVDRNIERLVSWFEPRI---EDVRPNLIQI 244

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 569003409 1742 IQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERV 1790
Cdd:cd15479   245 IQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAILLKYKPANKGEAGV 293

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

899-1033

2.20e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.20e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  899 KARQELKALKIEARSAEHLKRLNvgmENKVVQLQRKIddqnkefKTLSEQLSAVTSSHavEVEKLKKELAHYQQNQEA-- 976
Cdd:COG1579    42 ALEARLEAAKTELEDLEKEIKRL---ELEIEEVEARI-------KKYEEQLGNVRNNK--EYEALQKEIESLKRRISDle 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569003409  977 DTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKE 1033
Cdd:COG1579   110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166

Golgin_A5

pfam09787

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...

927-1185

2.23e-05

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: 48.60 E-value: 2.23e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   927 KVVQLQRKIDDQNKEFKTLsEQLSAVTSSHAvEVEKLKKElahyqQNQEADTSLQLQEEVQSLRTELQKahserrvLEDA 1006
Cdd:pfam09787   18 RILQSKEKLIASLKEGSGV-EGLDSSTALTL-ELEELRQE-----RDLLREEIQKLRGQIQQLRTELQE-------LEAQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1007 HNKENGELRKRVADLEHENALLKDEKEYLNNQILCQSkaessqssvEENLLMKKELEEERSRYQNLVKEysqLEQRYENL 1086
Cdd:pfam09787   84 QQEEAESSREQLQELEEQLATERSARREAEAELERLQ---------EELRYLEEELRRSKATLQSRIKD---REAEIEKL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1087 RDEVTILKQtpghrkNPSNQSSLESdsnypsistseigdtedALQQVEEIGIEKAAMdmtvflklqkrVRELEQERKKLQ 1166
Cdd:pfam09787  152 RNQLTSKSQ------SSSSQSELEN-----------------RLHQLTETLIQKQTM-----------LEALSTEKNSLV 197

                          250
                   ....*....|....*....
gi 569003409  1167 AQLEKGQQDSKKGQVEQQN 1185
Cdd:pfam09787  198 LQLERMEQQIKELQGEGSN 216

PTZ00121

MAEBL; Provisional

896-1282

2.44e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 2.44e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  896 RRLKARQELKALKIE-ARSAEHLKRLNVGMENKVVQLQRKIDDQNK--EFKTLSEQLSAVTSSHAVEVEKLKKelAHYQQ 972
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKK--AEELK 1653

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  973 NQEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKEylnnqilcQSKAESSQSSV 1052
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE--------KKKAEELKKAE 1725

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1053 EENLL----MKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQSSLESDSNYPSISTSEIGDTED 1128
Cdd:PTZ00121 1726 EENKIkaeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1129 ALQQVEEIGIEKaamDMTVFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQVEQQNNGLDVDQDADIAYNSLKRQELES 1208
Cdd:PTZ00121 1806 NFANIIEGGKEG---NLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE 1882

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1209 E------NKKLKNdlNELRKAVADQAMQDNSTHSSPDsyslllnqlKLANEELevRKEEVLILRTQIMNadqrrLSGKNM 1282
Cdd:PTZ00121 1883 EieeadeIEKIDK--DDIEREIPNNNMAGKNNDIIDD---------KLDKDEY--IKRDAEETREEIIK-----ISKKDM 1944

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

933-1439

3.15e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 3.15e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   933 RKIDDQNKEFKTLSEQLSaVTSSHAVEVEKLKKELAHYQqnqeadtsLQLQEEVQSLRTELQKAHSERRVLE------DA 1006
Cdd:TIGR04523  138 KNIDKFLTEIKKKEKELE-KLNNKYNDLKKQKEELENEL--------NLLEKEKLNIQKNIDKIKNKLLKLElllsnlKK 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1007 HNKENGELRKRVADLEHENALLKDEKEYLNNQIlcqSKAESSQSSVEENLL--------MKKELEEERSRYQNLVKEYSQ 1078
Cdd:TIGR04523  209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQLNqlkdeqnkIKKQLSEKQKELEQNNKKIKE 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1079 LEQRYENLRDEVTILKQTPGHRKNPSNQSSLESDSNYPSISTSEIGDTEDALQQVEEigiekaamdmtVFLKLQKRVREL 1158
Cdd:TIGR04523  286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE-----------QISQLKKELTNS 354

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1159 EQERKKLQAQLEKgqqdsKKGQVEQQNNgldvdqdadiaynslKRQELESENKKLKNDLNELRKAVADQAMQDNsthssp 1238
Cdd:TIGR04523  355 ESENSEKQRELEE-----KQNEIEKLKK---------------ENQSYKQEIKNLESQINDLESKIQNQEKLNQ------ 408

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1239 dsysLLLNQLKLANEELEVRKEEVLILRTQImnadqrrlsgknmepninartswpnsekhVDQEDAIEAYHgvcqtnsqt 1318
Cdd:TIGR04523  409 ----QKDEQIKKLQQEKELLEKEIERLKETI-----------------------------IKNNSEIKDLT--------- 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1319 edwgylNEDGELGLAYQGLKQVARLLEAQLQAqsleheeevehLKAQVEALKEEMDKQQQTfcqtlLLSPEAQVEfGVQQ 1398
Cdd:TIGR04523  447 ------NQDSVKELIIKNLDNTRESLETQLKV-----------LSRSINKIKQNLEQKQKE-----LKSKEKELK-KLNE 503

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 569003409  1399 EISRLTNENLDFKELVEKLEKNERKLKKQLKIYMKKVQDLE 1439
Cdd:TIGR04523  504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

857-1092

3.60e-05

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: 48.58 E-value: 3.60e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   857 RQVLMEHKATIIQKYARGWMARKRFLrERdaaIVIQCAFRRL-KARQELKALKIEarSAEHLKRLNVGMENKVVQLQRKI 935
Cdd:pfam17380  325 RQAEMDRQAAIYAEQERMAMEREREL-ER---IRQEERKRELeRIRQEEIAMEIS--RMRELERLQMERQQKNERVRQEL 398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   936 DDQNKeFKTLSEQLSAVTSSHAVEVEKLKKElahyQQNQEadtslqlQEEVQslRTELQKAHSERRVLEDAHNKENGELR 1015
Cdd:pfam17380  399 EAARK-VKILEEERQRKIQQQKVEMEQIRAE----QEEAR-------QREVR--RLEEERAREMERVRLEEQERQQQVER 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1016 KRVADLEHENALLKDEKEY--------LNNQILCQSKAESSQSSVEENlLMKKELEEERSRYQNLVKEYSQLEQRYENLR 1087
Cdd:pfam17380  465 LRQQEEERKRKKLELEKEKrdrkraeeQRRKILEKELEERKQAMIEEE-RKRKLLEKEMEERQKAIYEEERRREAEEERR 543


                   ....*
gi 569003409  1088 DEVTI 1092
Cdd:pfam17380  544 KQQEM 548

PRK03918

DNA double-strand break repair ATPase Rad50;

897-1226

4.76e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.76e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  897 RLKARQELKALKIEARSAEHLKRLNvGMENKVVQLQRKIDDQNK--EFKTLSEQLSAVTSS-HAVEVEKLKKElahyqqn 973
Cdd:PRK03918  452 ELLEEYTAELKRIEKELKEIEEKER-KLRKELRELEKVLKKESEliKLKELAEQLKELEEKlKKYNLEELEKK------- 523

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  974 qeadtslqlQEEVQSLRTELQKAHSERRVLEDAHNKENgELRKRVADLEHENALLKDEKEYLNNQILcqskaESSQSSVE 1053
Cdd:PRK03918  524 ---------AEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELE-----ELGFESVE 588

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1054 ENLLMKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQtpghrknpsnqsslesdsnypsiSTSEIGDTEDALQQV 1133
Cdd:PRK03918  589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK-----------------------AFEELAETEKRLEEL 645

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1134 E-EIGIEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEkgqqdSKKGQVEQQNNGLDvDQDADIAYNSLKRQELESENKK 1212
Cdd:PRK03918  646 RkELEELEKKYSEEEYEELREEYLELSRELAGLRAELE-----ELEKRREEIKKTLE-KLKEELEEREKAKKELEKLEKA 719

                         330
                  ....*....|....
gi 569003409 1213 LKnDLNELRKAVAD 1226
Cdd:PRK03918  720 LE-RVEELREKVKK 732

GumC

COG3206

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

930-1209

5.17e-05

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.17e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  930 QLQRKIDDQNKEFKTLSEQLSAVTSshavEVEKLKKELAHYQQNQEadtSLQLQEEVQSLRTELQkahserrvledahnk 1009
Cdd:COG3206   165 NLELRREEARKALEFLEEQLPELRK----ELEEAEAALEEFRQKNG---LVDLSEEAKLLLQQLS--------------- 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1010 engELRKRVADLEHENALLKDEKEYLNNQI--LCQSKAESSQSSVEENLlmkkeleeeRSRYQNLVKEYSQLEQRYenlr 1087
Cdd:COG3206   223 ---ELESQLAEARAELAEAEARLAALRAQLgsGPDALPELLQSPVIQQL---------RAQLAELEAELAELSARY---- 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1088 devtilkqTPGHrknpsnqsslesdsnyPSIstseigdtEDALQQVEEIGIEKAAMDMTVFLKLQKRVRELEQERKKLQA 1167
Cdd:COG3206   287 --------TPNH----------------PDV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 569003409 1168 QLEKGQQDSKK-GQVEQQNNGLdvDQDADIA---YNSL--KRQELESE 1209
Cdd:COG3206   335 QLAQLEARLAElPELEAELRRL--EREVEVArelYESLlqRLEEARLA 380

PRK03918

DNA double-strand break repair ATPase Rad50;

879-1172

7.58e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 7.58e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  879 KRFLRERDAAIVIQCAFRRLKaRQELKALKIEARSAEHLKRLNVGMENKVVQLQR---KIDDQNKEFKTLSEQLSavtss 955
Cdd:PRK03918  493 SELIKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKeleKLEELKKKLAELEKKLD----- 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  956 havEVEKLKKELAHYQQNQEADTSLQLQEEVQSLrtelqkahserrvlEDAHNKENgELRKRVADLEHENALLKDEKEYL 1035
Cdd:PRK03918  567 ---ELEEELAELLKELEELGFESVEELEERLKEL--------------EPFYNEYL-ELKDAEKELEREEKELKKLEEEL 628

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1036 nnqilcqSKAEssqssvEENLLMKKELEEERSRYQNLVKEYSqlEQRYENLRDEvtilkqtpgHRKNPSNQSSLESDSNY 1115
Cdd:PRK03918  629 -------DKAF------EELAETEKRLEELRKELEELEKKYS--EEEYEELREE---------YLELSRELAGLRAELEE 684

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569003409 1116 PSISTSEIGDTEDALQ-QVEEIgiEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKG 1172
Cdd:PRK03918  685 LEKRREEIKKTLEKLKeELEER--EKAKKELEKLEKALERVEELREKVKKYKALLKER 740

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

899-1230

1.16e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 1.16e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   899 KARQELKALK--IEARSA---EHLKRLNVGMENKVVQLQRKiDDQNKEFKTLSEQLSAVTSSHAVEVEKLKKELAHYQQN 973
Cdd:pfam01576  201 KGRQELEKAKrkLEGESTdlqEQIAELQAQIAELRAQLAKK-EEELQAALARLEEETAQKNNALKKIRELEAQISELQED 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   974 QEADTSLQ---------LQEEVQSLRTEL----------QKAHSER--------RVLED---AHNKENGELRKRvadleH 1023
Cdd:pfam01576  280 LESERAARnkaekqrrdLGEELEALKTELedtldttaaqQELRSKReqevtelkKALEEetrSHEAQLQEMRQK-----H 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1024 ENALlkdekEYLNNQIlcqSKAESSQSSVEENllmKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNP 1103
Cdd:pfam01576  355 TQAL-----EELTEQL---EQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1104 SN-------------QSSLESDSNYPSI-------STSEIGDTEDALQQVEEIGIEKAAMDmtvfLKLQKRVRELEQERK 1163
Cdd:pfam01576  424 SErqraelaeklsklQSELESVSSLLNEaegknikLSKDVSSLESQLQDTQELLQEETRQK----LNLSTRLRQLEDERN 499

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569003409  1164 KLQAQLEkgQQDSKKGQVEQQNngldvdQDADIAYNSLKRQ---------ELESENKKLKNDLNELRKAVADQAMQ 1230
Cdd:pfam01576  500 SLQEQLE--EEEEAKRNVERQL------STLQAQLSDMKKKleedagtleALEEGKKRLQRELEALTQQLEEKAAA 567

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

908-1205

1.57e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.57e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  908 KIEARSAEHLKRLNvGMENKVVQLQRKIDDQNKEFKTLSEQLSavtsSHAVEVEKLKKELAHYQQNQEadtslQLQEEVQ 987
Cdd:COG1340    19 ELREEIEELKEKRD-ELNEELKELAEKRDELNAQVKELREEAQ----ELREKRDELNEKVKELKEERD-----ELNEKLN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  988 SLRTELQKAHSERRVLEDAhNKENGELRKRVADLE--HENALLKDEKEylnNQILCQSKaessqsSVEENLLMKKELEEE 1065
Cdd:COG1340    89 ELREELDELRKELAELNKA-GGSIDKLRKEIERLEwrQQTEVLSPEEE---KELVEKIK------ELEKELEKAKKALEK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1066 RSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQSSLESDSNYPSIstseigdtEDALQQVEEIgIEKAAMDM 1145
Cdd:COG1340   159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA--------DELHKEIVEA-QEKADELH 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1146 TVFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQVEQQnngldvdqdADIAYNSLKRQE 1205
Cdd:COG1340   230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK---------AEEIFEKLKKGE 280

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

877-1496

1.70e-04

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.70e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   877 ARKRFLRERDAAIVIQCAFRRLKARQELKALK---------IEARSAEHLKRLNVGMEnKVVQLQRKIDDQNKEFKTLSE 947
Cdd:pfam12128  283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADaavakdrseLEALEDQHGAFLDADIE-TAAADQEQLPSWQSELENLEE 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   948 QLSAVTSSH------------------AVEVEKLKKELAHYQQN---QEADTSLQLQEEVQSLRTELQKAHSERRVLEDA 1006
Cdd:pfam12128  362 RLKALTGKHqdvtakynrrrskikeqnNRDIAGIKDKLAKIREArdrQLAVAEDDLQALESELREQLEAGKLEFNEEEYR 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1007 HNKENGELRKRVADLEHENALLKDEKeylNNQILCQSKAESSQSSVEENLLMKKELEEERSRYQNLVKEYSQLEQRYENL 1086
Cdd:pfam12128  442 LKSRLGELKLRLNQATATPELLLQLE---NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER 518

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1087 RDEVTILKQT---PGHR--KNPSNQSSLESDSNYPSISTSEIGDTE-----DALQQVEE-----IGIEKAAMDMTVFLKL 1151
Cdd:pfam12128  519 QSALDELELQlfpQAGTllHFLRKEAPDWEQSIGKVISPELLHRTDldpevWDGSVGGElnlygVKLDLKRIDVPEWAAS 598

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1152 QKRVR-ELEQERKKLQAQLEKGQQDSKK-----GQVEQQNNGLdvdQDADIAY--NSLKRQELESENKKLKNDLNELRKA 1223
Cdd:pfam12128  599 EEELReRLDKAEEALQSAREKQAAAEEQlvqanGELEKASREE---TFARTALknARLDLRRLFDEKQSEKDKKNKALAE 675

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1224 VADQAMQdnSTHSSPDSYSLLLNQLKLANEELevrKEEVLILRTQIMNADQRRLSGKNmepninartswpNSEKHVDQE- 1302
Cdd:pfam12128  676 RKDSANE--RLNSLEAQLKQLDKKHQAWLEEQ---KEQKREARTEKQAYWQVVEGALD------------AQLALLKAAi 738

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1303 DAIEAYHGVCQTNSQTEDWGYLNEDGELGLAYQGLKQVARLLEAQLQAQSLEHEEEVEHLKAQVEALKEEMDKQQQTFCQ 1382
Cdd:pfam12128  739 AARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSN 818

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1383 TLLLSPEAQVEFGVQQEISRLTNENLDfKEL--VEKLEKNERKLKKQLKIYMKKVQDLEAAQALAQSDRRHHELTRQVtv 1460
Cdd:pfam12128  819 IERAISELQQQLARLIADTKLRRAKLE-MERkaSEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQL-- 895

                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 569003409  1461 qrkeKDFQGMLEYHKEDEALLIRNLVTDLKPQMLSG 1496
Cdd:pfam12128  896 ----EDLKLKRDYLSESVKKYVEHFKNVIADHSGSG 927

YhaN

COG4717

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

871-1096

2.58e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.58e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  871 YARGWMARKRFLRERDAAIVIQCAFRRLKARQE----LKALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQNKEFKTLS 946
Cdd:COG4717   288 LLFLLLAREKASLGKEAEELQALPALEELEEEEleelLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  947 ---EQLSAVTSSHAVEVEKLKKELAHYQQNQEadtslqLQEEVQSLRTELQKAHSERRVLEDAHNKEngELRKRVADLEH 1023
Cdd:COG4717   368 leqEIAALLAEAGVEDEEELRAALEQAEEYQE------LKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEE 439

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003409 1024 ENALLKDEKEYLNNQIlcqSKAESSQSSVEENllmkKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQT 1096
Cdd:COG4717   440 ELEELEEELEELREEL---AELEAELEQLEED----GELAELLQELEELKAELRELAEEWAALKLALELLEEA 505

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

897-1167

2.69e-04

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: 45.88 E-value: 2.69e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   897 RLKARQELKALKIE----------ARSAEHLKRLNVGMENKVVQLQR-------KIDDQNKEFKTLSEQLSAVTSSHAVE 959
Cdd:pfam17380  300 RLRQEKEEKAREVErrrkleeaekARQAEMDRQAAIYAEQERMAMERereleriRQEERKRELERIRQEEIAMEISRMRE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   960 VEKLKKElaHYQQNQEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKR-VADLEHENA--LLKDEKEYLN 1036
Cdd:pfam17380  380 LERLQME--RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQReVRRLEEERAreMERVRLEEQE 457

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1037 NQ----ILCQSKAESSQSSVEENLLMKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQSSLESD 1112
Cdd:pfam17380  458 RQqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003409  1113 SNYPSISTSEIGDTEDALQQVEEIGIEKAAMD-MTVFLKLQKRVRELEQERKKLQA 1167
Cdd:pfam17380  538 AEEERRKQQEMEERRRIQEQMRKATEERSRLEaMEREREMMRQIVESEKARAEYEA 593

PLN03229

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

908-1216

2.96e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.62 E-value: 2.96e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  908 KIEARSAEHLKRLNVGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTsshaveVEKLKKELAhyQQNQEADTSLQLQEEVQ 987
Cdd:PLN03229  418 KVNMKKREAVKTPVRELEGEVEKLKEQILKAKESSSKPSELALNEM------IEKLKKEID--LEYTEAVIAMGLQERLE 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  988 SLRTELQKAHSE----RRVLEDAHNKENGELRKRVAD------LEHENALL------------KDEKEYLNNQI------ 1039
Cdd:PLN03229  490 NLREEFSKANSQdqlmHPVLMEKIEKLKDEFNKRLSRapnylsLKYKLDMLnefsrakalsekKSKAEKLKAEInkkfke 569

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1040 ----------LCQSKAESSQSSVEENLLMKKELEEERSRYQNLVKeySQLEQRYENLRDEVTILKQ----TPGHRKNPSN 1105
Cdd:PLN03229  570 vmdrpeikekMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIE--LELAGVLKSMGLEVIGVTKknkdTAEQTPPPNL 647

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1106 QSSLESDSNYPSISTSEIGDTEDALQQVEEIGIEKAAMDMTVFLKLQKRVRELEQE-RKKLQAQLEKGQQDSKKGQVeqq 1184
Cdd:PLN03229  648 QEKIESLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQiKQKIAEALNSSELKEKFEEL--- 724

                         330       340       350
                  ....*....|....*....|....*....|..
gi 569003409 1185 nngldvdqDADIAynsLKRQELESENKKLKND 1216
Cdd:PLN03229  725 --------EAELA---AARETAAESNGSLKND 745

PRK12704

phosphodiesterase; Provisional

960-1090

3.21e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.21e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  960 VEKLKKELAHYQQNQEadtsLQLQEEVQSLRTELQKAHSERRvlEDAHNKENgELRKRVADLEHENALLKDEKEYLNNQi 1039
Cdd:PRK12704   44 LEEAKKEAEAIKKEAL----LEAKEEIHKLRNEFEKELRERR--NELQKLEK-RLLQKEENLDRKLELLEKREEELEKK- 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 569003409 1040 lcQSKAESSQSSVEEnllMKKELEEERSRYQNLVKEYSQL--EQRYENLRDEV 1090
Cdd:PRK12704  116 --EKELEQKQQELEK---KEEELEELIEEQLQELERISGLtaEEAKEILLEKV 163

PRK01156

chromosome segregation protein; Provisional

922-1226

3.23e-04

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 3.23e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  922 VGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTSSHAVEVEKLKKELAHYQQN-QEADTSL-QLQEEVQSLRTELQKAHSE 999
Cdd:PRK01156  366 NSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKlQDISSKVsSLNQRIRALRENLDELSRN 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1000 ----------------------RRVLEDAHNKENG------ELRKRVADLEHENALLKDEKEYLNNQ-----ILCQSKAE 1046
Cdd:PRK01156  446 memlngqsvcpvcgttlgeeksNHIINHYNEKKSRleekirEIEIEVKDIDEKIVDLKKRKEYLESEeinksINEYNKIE 525

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1047 SSQSSVEENLLMKKELEEERSRYQNLVKEYSQ-----LEQRYEN------LRDEVTIlkQTPGHRKNPSNQS-------S 1108
Cdd:PRK01156  526 SARADLEDIKIKINELKDKHDKYEEIKNRYKSlkledLDSKRTSwlnalaVISLIDI--ETNRSRSNEIKKQlndlesrL 603

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1109 LESDSNYPSIST---SEIGDTEDALQ----QVEEIGIEKAAMDmtvflKLQKRVRELEQERKKLqaqleKGQQDSKK--- 1178
Cdd:PRK01156  604 QEIEIGFPDDKSyidKSIREIENEANnlnnKYNEIQENKILIE-----KLRGKIDNYKKQIAEI-----DSIIPDLKeit 673

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 569003409 1179 GQVEQQNNGLDVDQDADIAYNSlKRQELESENKKLKNDLNELRKAVAD 1226
Cdd:PRK01156  674 SRINDIEDNLKKSRKALDDAKA-NRARLESTIEILRTRINELSDRIND 720

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

861-881

3.83e-04

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

Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 39.23 E-value: 3.83e-04

                            10        20
                    ....*....|....*....|.
gi 569003409    861 MEHKATIIQKYARGWMARKRF 881
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRY 22

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

900-1428

3.89e-04

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 3.89e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   900 ARQELKALKIEARSaeHLKRlnvgMENKVVQLQRKIDDQNKEFKTLSEQLSAVTSSHAVEVEKLK--KELAHYQQNQEAD 977
Cdd:pfam01576  118 ARQKLQLEKVTTEA--KIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKslSKLKNKHEAMISD 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   978 TSLQLQEEVQSlRTELQKAhseRRVLEdahnKENGELRKRVADL-----EHENALLKDEKEylnnqiLCQSKAESSQSSV 1052
Cdd:pfam01576  192 LEERLKKEEKG-RQELEKA---KRKLE----GESTDLQEQIAELqaqiaELRAQLAKKEEE------LQAALARLEEETA 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1053 EENLLMKK-------------ELEEERSRYQNLVKEYSQLEQRYENLRDEVT-ILKQTPGHRKNPSN--------QSSLE 1110
Cdd:pfam01576  258 QKNNALKKireleaqiselqeDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTAAQQELRSKreqevtelKKALE 337

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1111 SDSNYPSISTSEIgdTEDALQQVEEIGiEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKGQQdsKKGQVEQQNNGLDV 1190
Cdd:pfam01576  338 EETRSHEAQLQEM--RQKHTQALEELT-EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ--AKQDSEHKRKKLEG 412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1191 D-QDADIAYNSLKRQELESENK--KLKNDLNELRKAVADqamQDNSTHSSPDSYSLLLNQLKLANEEL--EVRKEEVLIL 1265
Cdd:pfam01576  413 QlQELQARLSESERQRAELAEKlsKLQSELESVSSLLNE---AEGKNIKLSKDVSSLESQLQDTQELLqeETRQKLNLST 489

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1266 RTQIMNADQRRLSgKNMEPNINARTswpNSEKHVDqedaieayhgvcQTNSQTEDWGYLNED--GELGLAYQGLKQVARL 1343
Cdd:pfam01576  490 RLRQLEDERNSLQ-EQLEEEEEAKR---NVERQLS------------TLQAQLSDMKKKLEEdaGTLEALEEGKKRLQRE 553

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1344 LEAQLQaqsleheeevehlkaQVEALKEEMDKQQQTFCQtlllspeaqvefgVQQEISRLTNENLDFKELVEKLEKNERK 1423
Cdd:pfam01576  554 LEALTQ---------------QLEEKAAAYDKLEKTKNR-------------LQQELDDLLVDLDHQRQLVSNLEKKQKK 605


                   ....*
gi 569003409  1424 LKKQL 1428
Cdd:pfam01576  606 FDQML 610

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

926-1178

4.41e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 4.41e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   926 NKVVQLQRKIDDQNKEFKTLSEQLSAVTSshavevEKLKKELAHYQQNQEADTSLQLQEEVQSLRTELQKAHSERRVLED 1005
Cdd:TIGR00606  843 SKIELNRKLIQDQQEQIQHLKSKTNELKS------EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1006 AHNKENGELRKRVADLEHENALLKDE----KEYLNNQILCQSKAESSQSSVEENLLMKKELEeersrYQNLVKEYSQLEQ 1081
Cdd:TIGR00606  917 FLEKDQQEKEELISSKETSNKKAQDKvndiKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE-----LNTVNAQLEECEK 991

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1082 RYENLRDEVTILKQTPGHRKnpsNQSSLESDSNYPSISTSEIGDTEDALQQ-VEEIGIEKAAMDMTVFLKLQKRVRELEQ 1160
Cdd:TIGR00606  992 HQEKINEDMRLMRQDIDTQK---IQERWLQDNLTLRKRENELKEVEEELKQhLKEMGQMQVLQMKQEHQKLEENIDLIKR 1068

                          250
                   ....*....|....*...
gi 569003409  1161 ERKKLQAQlEKGQQDSKK 1178
Cdd:TIGR00606 1069 NHVLALGR-QKGYEKEIK 1085

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1202-1441

5.54e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 5.54e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1202 KRQELESENKKLKNDLNELRKAVADQAMQDNSthsspdsyslLLNQLKLANEELEVRKEEVLILRTQImNADQRRLSGKN 1281
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKA----------LLKQLAALERRIAALARRIRALEQEL-AALEAELAELE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1282 MEpnINArtswpNSEKHVDQEDAIEAYHGVCQTNSQTEDWGYL---NEDGELGLAYQGLKQVARLLEAQLQAQsleheee 1358
Cdd:COG4942    90 KE--IAE-----LRAELEAQKEELAELLRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEEL------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1359 vEHLKAQVEALKEEMDKQQQTFcqtlllspeAQVEFGVQQEISRLTNENLDFKELVEKLEKNERKLKKQLKIYMKKVQDL 1438
Cdd:COG4942   156 -RADLAELAALRAELEAERAEL---------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225


                  ...
gi 569003409 1439 EAA 1441
Cdd:COG4942   226 EAL 228

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

812-834

1.52e-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: 1.52e-03

                            10        20
                    ....*....|....*....|...
gi 569003409    812 RRTRAAIVFQKQYRMLKARRAYR 834
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23

SMC_prok_B

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

877-1451

1.56e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.56e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   877 ARKRFLRERDAAIVIQCAF----------RRLKARQELKALK---------IEARSAEH--LKRLNVGMENKVVQLQRKI 935
Cdd:TIGR02168  302 QQKQILRERLANLERQLEEleaqleelesKLDELAEELAELEekleelkeeLESLEAELeeLEAELEELESRLEELEEQL 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   936 DDQNKEFKTLSEQLSAVTSshavEVEKLKKELAHYQQNQEadtslQLQEEVQSLRTELQKAHSERRVLE-DAHNKENGEL 1014
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNN----EIERLEARLERLEDRRE-----RLQQEIEELLKKLEEAELKELQAElEELEEELEEL 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1015 RKRVADLEHENALLKDEKEyLNNQILCQSKAESSQSSVEENLLMK------------KELEEERSR---YQNLVKEYSQL 1079
Cdd:TIGR02168  453 QEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDSLERlqenlegfsegvKALLKNQSGlsgILGVLSELISV 531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1080 EQRYEN--------------------LRDEVTILKQT-------------PGHRKNPSNQSSLESDSNYPSI-------- 1118
Cdd:TIGR02168  532 DEGYEAaieaalggrlqavvvenlnaAKKAIAFLKQNelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVakdlvkfd 611

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1119 -----------STSEIGDT-EDALQQVEEI----------------------GIEKAAMDMtvfLKLQKRVRELEQERKK 1164
Cdd:TIGR02168  612 pklrkalsyllGGVLVVDDlDNALELAKKLrpgyrivtldgdlvrpggvitgGSAKTNSSI---LERRREIEELEEKIEE 688

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1165 LQAQLEKGQQDSKKGQVEQqnngldvdqdadiaynslkrQELESENKKLKNDLNELRKAVADQAMQDNSTHSSPDSYSLL 1244
Cdd:TIGR02168  689 LEEKIAELEKALAELRKEL--------------------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1245 LNQLKLANEELEVRKEEVLILRTQIMNADQRRLSG-KNMEPNINARtswpnSEKHVDQEDAIEAYHGVCQTnsqtedwgy 1323
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEQL-----KEELKALREALDELRAELTL--------- 814

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1324 LNED-GELGLAYQGLKQVARLLEAQ---LQAQSLEHEEEVEHLKAQVEALKEEMDKQQQTFcqtlllsPEAQVEFGVQQE 1399
Cdd:TIGR02168  815 LNEEaANLRERLESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEE 887

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|...
gi 569003409  1400 ISRLTNENLDFKEL-VEKLEKNERKLKKQLKIYMKKVQDLEAAQALAQSDRRH 1451
Cdd:TIGR02168  888 ALALLRSELEELSEeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940

DUF1690

pfam07956

Protein of Unknown function (DUF1690); Family of uncharacterized fungal proteins.

901-993

1.61e-03

Protein of Unknown function (DUF1690); Family of uncharacterized fungal proteins.

Pssm-ID: 429752 Cd Length: 138 Bit Score: 40.66 E-value: 1.61e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   901 RQELKALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQNKEfktlSEQLSAVTSSHAV--EVEKLKKELahyQQNQEADt 978
Cdd:pfam07956   27 RAQLLELYIQARVAEELKRLQAEEEEALKKFEDKLEKSLLD----DDDAGDGLSSAALneKIEELRKKL---EEFRKRV- 98

                           90
                   ....*....|....*
gi 569003409   979 SLQLQEEVQSLRTEL 993
Cdd:pfam07956   99 RLKLPEEVEAAREAV 113

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

908-1091

1.68e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.68e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  908 KIEARSAEhLKRLnvgmENKVVQLQRKIDDQNKEFKTLSEQLSAV------------TSSHAVEVEKLKKELAHYQQNQe 975
Cdd:COG4913   611 KLAALEAE-LAEL----EEELAEAEERLEALEAELDALQERREALqrlaeyswdeidVASAEREIAELEAELERLDASS- 684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  976 aDTSLQLQEEVQSLRTELQKAHSERRVLedahNKENGELRKRVADLEHENALLKDEKEylnnqilcqsKAESSQSSVEEN 1055
Cdd:COG4913   685 -DDLAALEEQLEELEAELEELEEELDEL----KGEIGRLEKELEQAEEELDELQDRLE----------AAEDLARLELRA 749

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 569003409 1056 LL--MKKELEEERSRYQ---NLVKEYSQLEQRYENLRDEVT 1091
Cdd:COG4913   750 LLeeRFAAALGDAVERElreNLEERIDALRARLNRAEEELE 790

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

992-1209

1.87e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.87e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  992 ELQKAHSERRVLEdahnKENGELRKRVADLEHENALLKDEKEYLNNQIlcqskaessqssveenllmkKELEEERSRYQN 1071
Cdd:COG1579    11 DLQELDSELDRLE----HRLKELPAELAELEDELAALEARLEAAKTEL--------------------EDLEKEIKRLEL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1072 LVKEYSQLEQRYENLRDEVtilkqtpghrKNPSNQSSLESDSnypSISTSEIGDTEDALQQVEEIgIEkaamdmtvflKL 1151
Cdd:COG1579    67 EIEEVEARIKKYEEQLGNV----------RNNKEYEALQKEI---ESLKRRISDLEDEILELMER-IE----------EL 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569003409 1152 QKRVRELEQERKKLQAQLEkgqqdSKKGQVEQQNNGLDVDQDADIAynslKRQELESE 1209
Cdd:COG1579   123 EEELAELEAELAELEAELE-----EKKAELDEELAELEAELEELEA----EREELAAK 171

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

979-1449

1.91e-03

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.91e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   979 SLQLQEEVQSLRTELQKAHSERRVLEDAHNKENgeLRKRVADLEHENALLKDEKEYLNNQILCQSKAESSQSSVEENLLM 1058
Cdd:TIGR00618  191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQV--LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1059 KKELEEERSRYQNLVKEYS--------------------QLEQRYENLRDEVTILKQTPGHRKNPSNQSSlesdsnypsi 1118
Cdd:TIGR00618  269 IEELRAQEAVLEETQERINrarkaaplaahikavtqieqQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS---------- 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1119 STSEIGDTEDALQQvEEIGIEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKGQQDSK--KGQVEQQNNGLDVDQDADI 1196
Cdd:TIGR00618  339 SIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQslCKELDILQREQATIDTRTS 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1197 AYNSLKRQ--ELESENKKLKNDLNELRKAVADQAMQD--NSTHSSPDSYSLLLNQLKLANEEL----EVRKEEVLILRTQ 1268
Cdd:TIGR00618  418 AFRDLQGQlaHAKKQQELQQRYAELCAAAITCTAQCEklEKIHLQESAQSLKEREQQLQTKEQihlqETRKKAVVLARLL 497

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1269 IMNADQRRLSGKNMEPNInartswpnsekHVDQEDAIEAYHGVCQTNSQTedwgylnedgelglaYQGLKQVARLLEAQL 1348
Cdd:TIGR00618  498 ELQEEPCPLCGSCIHPNP-----------ARQDIDNPGPLTRRMQRGEQT---------------YAQLETSEEDVYHQL 551

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1349 QAQsleheeevehlKAQVEALKEEMDKQQQTFcqtlllSPEAQVEFGVQQEISRLTNENLDFKELVEKLEKNERKLKKQL 1428
Cdd:TIGR00618  552 TSE-----------RKQRASLKEQMQEIQQSF------SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ 614

                          490       500
                   ....*....|....*....|.
gi 569003409  1429 KIYMKKVQDLEAAQALAQSDR 1449
Cdd:TIGR00618  615 HALLRKLQPEQDLQDVRLHLQ 635

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

899-1216

1.94e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.94e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  899 KARQELKALKIEARSAEH-LKRLNVGMEnkvvQLQRKIDDQNKEFKTLSEQLSAVTSshavEVEKLKKELAHYQQNQEad 977
Cdd:COG4372    35 KALFELDKLQEELEQLREeLEQAREELE----QLEEELEQARSELEQLEEELEELNE----QLQAAQAELAQAQEELE-- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  978 tslQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKEYLNNQILCQSKAESSQSSVEENLL 1057
Cdd:COG4372   105 ---SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1058 mKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQSSLESDSNYPSISTSEIGDTEDALQQVEEIG 1137
Cdd:COG4372   182 -EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003409 1138 IEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQVEQQNNGLDVDQDADIAYNSLKRQELESENKKLKND 1216
Cdd:COG4372   261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

896-1282

2.08e-03

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 2.08e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   896 RRLKARQELKALKIEARSAE---------HLKRLNVGMENKVVQLQRKIDDQNKEFKTL--SEQLSAVTSSHAVEVEKLK 964
Cdd:TIGR00606  719 KKKEKRRDEMLGLAPGRQSIidlkekeipELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQ 798

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   965 KELA----HYQQNQEADTSLQLQEEVQSLRTELQKAHSERRVLedahNKENGELRKRVADLEHENALLKDEKEYLNNQIL 1040
Cdd:TIGR00606  799 MELKdverKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV----VSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1041 CQSKAESSQSSVEENLLMK-KELEEERSRYQNLVKEYSQLEQRYENLRDEvtilKQTPGHRKNPSNQsslesdsnypsIS 1119
Cdd:TIGR00606  875 QIGTNLQRRQQFEEQLVELsTEVQSLIREIKDAKEQDSPLETFLEKDQQE----KEELISSKETSNK-----------KA 939

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1120 TSEIGDTEDALQQV--EEIGIEKAAMDMTVFLKLQKrvrelEQERKKLQAQLEKGQQDSKKGQVEQQNNGLDVD---QDA 1194
Cdd:TIGR00606  940 QDKVNDIKEKVKNIhgYMKDIENKIQDGKDDYLKQK-----ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQE 1014

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1195 DIAYNSLKRQELESENKKLKNDLNELRKAVA-DQAMQDNSTHSspdsyslllnqlKLANEELEVRKEEVLILRTQIMNAD 1273
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEVEEELKQHLKEMGqMQVLQMKQEHQ------------KLEENIDLIKRNHVLALGRQKGYEK 1082


                   ....*....
gi 569003409  1274 QRRLSGKNM 1282
Cdd:TIGR00606 1083 EIKHFKKEL 1091

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

897-1228

2.23e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 2.23e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   897 RLKAR-QELKAL--KIEARSAEHLKRlNVGMENKVVQLQRKIDDqnkefktLSEQLsavtsshaveveklkkelahyqqN 973
Cdd:pfam01576   65 RLAARkQELEEIlhELESRLEEEEER-SQQLQNEKKKMQQHIQD-------LEEQL-----------------------D 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   974 QEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGE---LRKRVADLEHEnalLKDEKEYLNNQILCQSKAESSQS 1050
Cdd:pfam01576  114 EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKErklLEERISEFTSN---LAEEEEKAKSLSKLKNKHEAMIS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1051 SVEENLlmKKeleEERSRyQNLVKEYSQLEQRYENLRDEVTILKQTPGHRKNPSNQSSLEsdsnypsistseigdTEDAL 1130
Cdd:pfam01576  191 DLEERL--KK---EEKGR-QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE---------------LQAAL 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1131 QQVEEIGIEKAAmdmtvflkLQKRVRELEQERKKLQAQLEkgQQDSKKGQVEQQNNGLDVDQDA------DIAYNSLKRQ 1204
Cdd:pfam01576  250 ARLEEETAQKNN--------ALKKIRELEAQISELQEDLE--SERAARNKAEKQRRDLGEELEAlkteleDTLDTTAAQQ 319

                          330       340
                   ....*....|....*....|....
gi 569003409  1205 ELESenkKLKNDLNELRKAVADQA 1228
Cdd:pfam01576  320 ELRS---KREQEVTELKKALEEET 340

PLN02939

transferase, transferring glycosyl groups

959-1220

2.32e-03

transferase, transferring glycosyl groups

Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 2.32e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  959 EVEKLKKELAHYQQN-QEADTSLQLQEEVQSlRTELQKAHSERRVLEDAHNKENG-----ELRKRVADLEHENALLKDEK 1032
Cdd:PLN02939  164 EKEALQGKINILEMRlSETDARIKLAAQEKI-HVEILEEQLEKLRNELLIRGATEglcvhSLSKELDVLKEENMLLKDDI 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1033 EYLNNQILCQSKAESSQSSVE-ENLLMKKELEEERSRYQNLVKEYSQLEQR-YENLRDEVTILKQTPGHRKNPSNQSSLE 1110
Cdd:PLN02939  243 QFLKAELIEVAETEERVFKLEkERSLLDASLRELESKFIVAQEDVSKLSPLqYDCWWEKVENLQDLLDRATNQVEKAALV 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1111 SDSNypsistseigdtEDALQQVEEIgieKAAMDMTVFLKLQKRVRELEQER-KKLQAQLEKGQQDSKKgQVEQQNNGLD 1189
Cdd:PLN02939  323 LDQN------------QDLRDKVDKL---EASLKEANVSKFSSYKVELLQQKlKLLEERLQASDHEIHS-YIQLYQESIK 386

                         250       260       270
                  ....*....|....*....|....*....|.
gi 569003409 1190 VDQDadiaynSLKRQELESENKKLKNDLNEL 1220
Cdd:PLN02939  387 EFQD------TLSKLKEESKKRSLEHPADDM 411

DUF4686

pfam15742

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...

930-1166

2.69e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.

Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 42.36 E-value: 2.69e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   930 QLQRKIDDQNKEfkTLSEQlsaVTSSHAVEveklkkelahyqqNQEADTSLQLQEEVQSLRTELQKAHSERRvLEDAHNK 1009
Cdd:pfam15742  178 QQKRKLLDQNVN--ELQQQ---VRSLQDKE-------------AQLEMTNSQQQLRIQQQEAQLKQLENEKR-KSDEHLK 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1010 ENGELRKRVADLEHENALLKDEkeylNNQILCQSKAESSQSSvEENLLMKKELEEERSRYqnlVKEYSQLEQRYENLRDE 1089
Cdd:pfam15742  239 SNQELSEKLSSLQQEKEALQEE----LQQVLKQLDVHVRKYN-EKHHHHKAKLRRAKDRL---VHEVEQRDERIKQLENE 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1090 VTILKQtpghrknpsnQSSLESDSNYPSISTSEIGDTE--DALQQV---EEIGiekaAMDMTVFLKLQKRVRELEQERKK 1164
Cdd:pfam15742  311 IGILQQ----------QSEKEKAFQKQVTAQNEILLLEkrKLLEQLteqEELI----KNNKRTISSVQNRVNFLDEENKQ 376


                   ..
gi 569003409  1165 LQ 1166
Cdd:pfam15742  377 LQ 378

CBD_MYO6-like

cd21759

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

856-972

2.81e-03

Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 40.18 E-value: 2.81e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  856 YRQvlmeHKATIIQKYARGWMARKRFlRERdaaivIQCaFRRLKA-RQELKALKieaRSAEHLKRLNVGMENKVVQLQRK 934
Cdd:cd21759    43 YRR----EALIKIQKTVRGYLARKKH-RPR-----IKG-LRKIRAlEKQLKEME---EIASQLKKDKDKWTKQVKELKKE 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 569003409  935 IDDQNKEFKTlSEQLSAVTSSHAVE--VEKLKKELAHYQQ 972
Cdd:cd21759   109 IDALIKKIKT-NDMITRKEIDKLYNalVKKVDKQLAELQK 147

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

1119-1336

2.85e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.85e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1119 STSEIGDTEDALQQVEEigiEKAAMDMTV------FLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQVE-------QQN 1185
Cdd:COG3883    21 KQKELSELQAELEAAQA---ELDALQAELeelneeYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLYR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1186 NGLDV--------------------------DQDADI--AYNSLKrQELESENKKLKNDLNELRKAVADQAMQDNSTHSS 1237
Cdd:COG3883    98 SGGSVsyldvllgsesfsdfldrlsalskiaDADADLleELKADK-AELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409 1238 PDSYSLLLNQLKLANEELEVRKEEVLILRTQIMNADQRRLSGKNMEPNINARTSWPNSEKHVDQEDAIEAYHGVCQTNSQ 1317
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256

                         250
                  ....*....|....*....
gi 569003409 1318 TEDWGYLNEDGELGLAYQG 1336
Cdd:COG3883   257 AAAGSAGAAGAAAGAAGAG 275

COG2433

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

943-1094

3.00e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.00e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  943 KTLSEQLSAVTSSHAVEVEKLKKELAHYQQNQEADtslqLQEEVQSLRTELQKAHSERRVLEDahnkENGELRKRVADLE 1022
Cdd:COG2433   376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTE----EEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLE 447

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003409 1023 HEnalLKDEKEYLNNQILCQSKAESSQssvEENLLMKKELEEERSRYQNLVKEYSQLEQ-RYENLRDEVTILK 1094
Cdd:COG2433   448 RE---LSEARSEERREIRKDREISRLD---REIERLERELEEERERIEELKRKLERLKElWKLEHSGELVPVK 514

CAGE1

pfam15066

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...

959-1171

3.04e-03

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.

Pssm-ID: 464481 Cd Length: 528 Bit Score: 42.13 E-value: 3.04e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   959 EVEKLKKELAHYQQNQEAD---TSLQLQEEVQslrtELQKAHSERRVLEDAHNKengeLRKRVADLEHENALLKDEKEYL 1035
Cdd:pfam15066  318 EVLQKLKHTNRKQQMQIQDlqcSNLYLEKKVK----ELQMKITKQQVFVDIINK----LKENVEELIEDKYNVILEKNDI 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1036 NNQIlcqskaessQSSVEENLLMKKELEEERSRYQNLVKE-------YSQLEQRYenlrdeVTILKQtpghrKNPSNQSS 1108
Cdd:pfam15066  390 NKTL---------QNLQEILANTQKHLQESRKEKETLQLElkkikvnYVHLQERY------ITEMQQ-----KNKSVSQC 449

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003409  1109 LESDSNYpSISTSEIGdtedALQQVEEiGIEKAAMDMTVFLKLQKRVRELE----------------QERKKLQAQLEK 1171
Cdd:pfam15066  450 LEMDKTL-SKKEEEVE----RLQQLKG-ELEKATTSALDLLKREKETREQEflslqeefqkhekenlEERQKLKSRLEK 522

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

842-1464

3.73e-03

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 3.73e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   842 IIQSFTRAMFVRRNYRQVLMEHKATIIQKYARGWMARKRFLRERDAAIVIQCafRRLKARQELKALKIEAR--------- 912
Cdd:pfam12128   99 IAGGYRLDDFIKANNDFVKCETVAELGRFMKNAGIQRTNLLNTREYRSIIQN--DRTLLGRERVELRSLARqfalcdses 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   913 SAEHLKRLNVGMENKvvqlqrkiddqNKEFKTLSEQLSAVTSSHAV----------EVEKLKKELAHYQQNQ-EADTSLQ 981
Cdd:pfam12128  177 PLRHIDKIAKAMHSK-----------EGKFRDVKSMIVAILEDDGVvppksrlnrqQVEHWIRDIQAIAGIMkIRPEFTK 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   982 LQEEVQSLRT---ELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEkeylnnqiLCQSKAESSQS-SVEENLL 1057
Cdd:pfam12128  246 LQQEFNTLESaelRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQ--------WKEKRDELNGElSAADAAV 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1058 MKKELEEERSRYQNLVKEYSQLEQRYENLRDEvtilkqtpghrknPSNQSSLESDSNYPSISTSEIGDTEDALQQVEEIG 1137
Cdd:pfam12128  318 AKDRSELEALEDQHGAFLDADIETAAADQEQL-------------PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI 384

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1138 IEKAAMDMTVFLKLQKRVRE------------LEQERKKLQAQLEKGQQDSKKGQVEQQNN--GLDVDQDADIAYNSLK- 1202
Cdd:pfam12128  385 KEQNNRDIAGIKDKLAKIREardrqlavaeddLQALESELREQLEAGKLEFNEEEYRLKSRlgELKLRLNQATATPELLl 464

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1203 ------------RQELESENKKLKNDLNELRKAvadQAMQDNSTHSSPDSySLLLNQLKLANEELevrkEEVLI------ 1264
Cdd:pfam12128  465 qlenfderieraREEQEAANAEVERLQSELRQA---RKRRDQASEALRQA-SRRLEERQSALDEL----ELQLFpqagtl 536

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1265 ---LRTQImnADQRRLSGKNMEPNINARTSWPNSEKHVDQEDAIEAYhGVCQTNSQTE--DWGYLNEDgelglayqgLKQ 1339
Cdd:pfam12128  537 lhfLRKEA--PDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLY-GVKLDLKRIDvpEWAASEEE---------LRE 604

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1340 VARLLEAQLQAQSLEHEEEVE---HLKAQVEALKEEMDKQQQTFCQTLLlspEAQVEFGVQQEISRLTNENLdfKELVEK 1416
Cdd:pfam12128  605 RLDKAEEALQSAREKQAAAEEqlvQANGELEKASREETFARTALKNARL---DLRRLFDEKQSEKDKKNKAL--AERKDS 679

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 569003409  1417 LEKNERKLKKQLKIYMKKVQdleaaQALAQSDRRHHELTRQVTVQRKE 1464
Cdd:pfam12128  680 ANERLNSLEAQLKQLDKKHQ-----AWLEEQKEQKREARTEKQAYWQV 722

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

877-1181

4.06e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.06e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   877 ARKRFLRERDAAIVIQCAFRRLKA--RQELKALKIEARsaeHLKRLNVGMENKVVQLQRKIDDQNKEFKTLSEQlSAVTS 954
Cdd:pfam07888   53 ANRQREKEKERYKRDREQWERQRRelESRVAELKEELR---QSREKHEELEEKYKELSASSEELSEEKDALLAQ-RAAHE 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   955 SHAVEVEKLKKELAhyQQNQEADTSLQ-LQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRVADL-EHENALLKDEK 1032
Cdd:pfam07888  129 ARIRELEEDIKTLT--QRVLERETELErMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFqELRNSLAQRDT 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1033 EYLNNQ---ILCQSKAESSQSSVEENLLMKKELEEERSRYqnlvkeySQLEQRYENLRDEVTILKQTPGHRKNPSNQSSL 1109
Cdd:pfam07888  207 QVLQLQdtiTTLTQKLTTAHRKEAENEALLEELRSLQERL-------NASERKVEGLGEELSSMAAQRDRTQAELHQARL 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1110 ESDSNYPSISTSEIGDTED---------ALQQVEEIGIEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKgQQDSKKGQ 1180
Cdd:pfam07888  280 QAAQLTLQLADASLALREGrarwaqereTLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR-EKDCNRVQ 358


                   .
gi 569003409  1181 V 1181
Cdd:pfam07888  359 L 359

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

1044-1279

4.09e-03

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.09e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1044 KAESSQSSVEENLLMKKEL-----------EEERSRYQnlvKEYSQLEQRYENLRDEVTILKQTPGHRKNpsNQSSLESD 1112
Cdd:pfam07888   28 RAELLQNRLEECLQERAELlqaqeaanrqrEKEKERYK---RDREQWERQRRELESRVAELKEELRQSRE--KHEELEEK 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1113 SNYPSISTSEIGDTEDALQQVEEigiekaamdmtvflKLQKRVRELEQERKKL--QAQLEKGQQDSKKGQVEQQNNGLDV 1190
Cdd:pfam07888  103 YKELSASSEELSEEKDALLAQRA--------------AHEARIRELEEDIKTLtqRVLERETELERMKERAKKAGAQRKE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1191 DQDADIAYNSlKRQELESENKKLKNDLNELRKAVADQAMQDNSTHSSPDSYSLLLNQLKLANEELEVRKEEVLILRtQIM 1270
Cdd:pfam07888  169 EEAERKQLQA-KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ-ERL 246


                   ....*....
gi 569003409  1271 NADQRRLSG 1279
Cdd:pfam07888  247 NASERKVEG 255

Smc

COG1196

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

801-1088

4.92e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 4.92e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  801 GYLARRLAEHLRRTRAAIVFqkqyrmLKARRAYRrvcrATVIIQSFTRAMFVRRNYRQVLMEHKATIIQKYARgwmarkR 880
Cdd:COG1196   546 AALQNIVVEDDEVAAAAIEY------LKAAKAGR----ATFLPLDKIRARAALAAALARGAIGAAVDLVASDL------R 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  881 FLRERDAAIVIQCAFRRLKARQELKALKIEARSAEHLKRLNVGMEnKVVQLQRKIDDQNKEfktLSEQLSAVTSSHAVEV 960
Cdd:COG1196   610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE-GGSAGGSLTGGSRRE---LLAALLEAEAELEELA 685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  961 EKLKKELAHYQQNQEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKEYLNNQIL 1040
Cdd:COG1196   686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569003409 1041 cQSKAESSQSSVEE----NLLMKKELEEERSRYQNLVKEYSQLEQRYENLRD 1088
Cdd:COG1196   766 -ERELERLEREIEAlgpvNLLAIEEYEELEERYDFLSEQREDLEEARETLEE 816

SMC_prok_A

TIGR02169

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

896-1453

5.34e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 5.34e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   896 RRLKAR-QELKALKIEARSAEHLKRLNV-GMENKVVQLQRKIDDQNKEFKTLSEQLSAVtsshAVEVEKLKKELAH---- 969
Cdd:TIGR02169  290 LRVKEKiGELEAEIASLERSIAEKERELeDAEERLAKLEAEIDKLLAEIEELEREIEEE----RKRRDKLTEEYAElkee 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409   970 ----YQQNQEADTSLQ-LQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKEYLNNqilCQSK 1044
Cdd:TIGR02169  366 ledlRAELEEVDKEFAeTRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE---LEEE 442

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1045 AESSQSSV---EENLL-MKKELEEERSRYQNLVKEYSQLEQRYENLRDEVTILKQTpghrknpsnQSSLESDSNYPSIST 1120
Cdd:TIGR02169  443 KEDKALEIkkqEWKLEqLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ---------ARASEERVRGGRAVE 513

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1121 SEIGDTEDA-------LQQVEE---IGIEKAAMDMTVFLKLQ-----KRVRELEQERK----------KLQAQLEKGQQD 1175
Cdd:TIGR02169  514 EVLKASIQGvhgtvaqLGSVGEryaTAIEVAAGNRLNNVVVEddavaKEAIELLKRRKagratflplnKMRDERRDLSIL 593

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1176 SKKGQVEQQNNGLDVDQ----------------------------------DADI---------------------AYNS 1200
Cdd:TIGR02169  594 SEDGVIGFAVDLVEFDPkyepafkyvfgdtlvvedieaarrlmgkyrmvtlEGELfeksgamtggsraprggilfsRSEP 673

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1201 LKRQELESENKKLKNDLNELRKAV---------ADQAMQDNSthsspDSYSLLLNQLKLANEELEVRKEEVLILRTQIMN 1271
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELrrienrldeLSQELSDAS-----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1272 ADQRRLSGKNMEPNINARTSwPNSEKHVDQEDAIEayhgvcqtnsqtedwgylneDGELGLAYQGLKQVARLLEAQlqaq 1351
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIE-ELEEDLHKLEEALN--------------------DLEARLSHSRIPEIQAELSKL---- 803

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003409  1352 slehEEEVEHLKAQVEALKEEMDKQQQtfcQTLLLSPEAQvefGVQQEISRLTNENLDFKELVEKLEKNERKLKKQLKIY 1431
Cdd:TIGR02169  804 ----EEEVSRIEARLREIEQKLNRLTL---EKEYLEKEIQ---ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873

                          650       660
                   ....*....|....*....|..
gi 569003409  1432 MKKVQDLEAAQALAQSDRRHHE 1453
Cdd:TIGR02169  874 EAALRDLESRLGDLKKERDELE 895