ID W2W8C2_PHYPR Unreviewed; 1221 AA.
AC W2W8C2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
GN ORFNames=F441_16855 {ECO:0000313|EMBL:ETP06802.1};
OS Phytophthora parasitica CJ01A1.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP06802.1, ECO:0000313|Proteomes:UP000018958};
RN [1] {ECO:0000313|EMBL:ETP06802.1, ECO:0000313|Proteomes:UP000018958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP06802.1,
RC ECO:0000313|Proteomes:UP000018958};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ01A1.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP06802.1}.
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DR EMBL; ANIX01003402; ETP06802.1; -; Genomic_DNA.
DR AlphaFoldDB; W2W8C2; -.
DR EnsemblProtists; ETP06802; ETP06802; F441_16855.
DR Proteomes; UP000018958; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14895; MYSc_Myo34; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782}.
FT DOMAIN 62..788
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REPEAT 1117..1152
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 676..698
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 883..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 966..996
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 890..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1221 AA; 137300 MW; 8F6C33983F841F01 CRC64;
MQVYVRVHDA DYEWVRGRVL RRHESDASKL LVQLNNSDTT IEADEAQDVR MANELAAGLT
LADVENLDAL THLHEPAFVD YLAQRYGVDQ VYCRSGAVLI AVNPFKHISG LYDLHKYREE
MPGWTALPPH VFSIAEGAYR SLRRRLHEPG ASKKNQTILV SGESGAGKTE TTKFIMNYLA
QNSLDTTATT SSKRKRAIGG SELLSANPIL ESFGNARTLR NDNSSRFGKF VRMFFEGHEL
DASLKMAGTS VETYLLEKVR VVHQNDGERN FHVFYELLAG ACDDMKKELQ LESLSAQEFQ
YVSGGQCYQR NDGVRDDKQF QLVLQSMKAL GFTNVEQAAI WKILSALLHL GNVLFVASSE
DEGEEDNGAA SEPCRLASAS PSSLTVQEHL DIVSKLFAVD QEELVSALTT RKISVGGETF
HANLSLAQCG DARDAMARSL YAFLFQFLVS KVNSASPQVQ ERNPANKAAN KDTTPCIAVL
DIFGFEEFEV NQFEQFCINY ANEKLQYQFI QDILLTEQQA HIEEGIKWNA VDYEDNSVCL
EMIEQRPSGI FSLLDEECVV PKGSDAGFAR KMCQRLQDHS NFSASRTDQA DVAFQIHHYA
GKVRYQAEGF CDKNKDQPNA ELFSVLGKTS DSHLRELFEF FKASETAELS LGQPKLRRRS
SVLSAVGIGS QFKQQLASLL DVVQQTETHY IRCIKPNDES ASDQFDMAKV SSQLRYGGVL
KAVEIMRQSF PVRMSHSDFV RQYSLLTTSP SCTAGDLIET LKVDHAEVGR TRVFLRQQAF
DQLEKRREQV IADSAVKLQS SWRGRQQRRV YIRQLQVLWS IQVRWKAILE KKRRIARREE
AARTIQHSIH CWIQALQRRR HRSAILIQFV FRRWHQARVT LSRTAAEASA KTPRQEDKSE
DSVGYSGRES VLTIETLEDD VLSTATASVG TSAYSEDVEL SPMDAVRRAT LRGHMSELGG
ATDSDNAMLK KALREVERLR RRAEAAEAAL SHFAGRDVDV STEALSMVAT RADGPYYNRA
SDGGNALWRQ LNTSNLRIDR YGNTVLHQAV ESGNVELACA LLVNEASGAL DMLQQAETQR
GYSSLHLAVR GGNFEMVSLF FRPEVLPHLD LNFSDREGNT ALHLATQLQV KIASRVLELL
LCFGADANAV NFLKQTPLHL CSMIKRSGSA TCEIMETLLR HKADPQKVDF LKRSPLHYCM
EKGMYWCSES RRVRLVNRVM Y
//
