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Database: UniProt
Entry: G4ZCI9_PHYSP
LinkDB: G4ZCI9_PHYSP
Original site: G4ZCI9_PHYSP 
ID   G4ZCI9_PHYSP            Unreviewed;      1477 AA.
AC   G4ZCI9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Myosin-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHYSODRAFT_559706 {ECO:0000313|EMBL:EGZ16878.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ16878.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ16878.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ16878.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; JH159154; EGZ16878.1; -; Genomic_DNA.
DR   RefSeq; XP_009525936.1; XM_009527641.1.
DR   EnsemblProtists; EGZ16878; EGZ16878; PHYSODRAFT_559706.
DR   GeneID; 20663430; -.
DR   KEGG; psoj:PHYSODRAFT_559706; -.
DR   InParanoid; G4ZCI9; -.
DR   OMA; MIDHEFE; -.
DR   Proteomes; UP000002640; 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   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   CDD; cd14891; MYSc_Myo30; 1.
DR   CDD; cd06093; PX_domain; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 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   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00787; PX; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT   DOMAIN          24..75
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          76..781
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1175..1306
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          657..679
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1453..1477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          878..1007
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1463..1477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1477 AA;  164539 MW;  7B6A5FAFFCA31AF4 CRC64;
     MSTPPPIARQ ASKSDADVEL LPVEVGQPVW VPATAAERVW DKATVMAIGG LKVTVRTQAG
     KIQQVDRGLA VPLNPREADD MTSLYYIHEA GVLHNLEERC KLDGGDGTGQ KPYTFMANVL
     IAVNPLRELP NPSVSEVVNT AGSAPHPYSI AEMAYQQMVY NSGTDQPTNQ SVVISGESGA
     GKTESSKIVL RHLTTRGLYG KKARGDDIEN MSKTRQQHGT SLDHRLIEQN PILEAFGNAK
     TLRNYNSSRF GKFMKLQFTA DGEFKLAGAL VETYLLEKSR LVYQVDGERN FHIFYQLLAG
     ASPQARKEFE LTQAEDFCYL NQSGCYIAEE TDDRACFEAV VRGLSCVGID EQVQHVIFSV
     VAGLLHLGNI EFDEEDTPEG EAAVIEKDSA KRAIVAASRL LGVNEQDLRK VIMTRDIVTR
     EETYTVRRNE QAAVYARDAI AKALYSRMFD WVIKQVNSSL GHDPNPLPYI GVLDIFGFES
     FQRNDFEQLL INYTNEVLQA TFNNQVFIAE MELYKREGIT VGRIKWPDNR ECVDLIASKP
     NGILSLLDAE AMNPQPSDAK FLRTLHSKHS KHPYFPRPHP KDMEHMFIVR HFAGAVSYTI
     GSFIDKNNDS IPPDMSNLFS GSSNKLVPAF FKQEVDTSRP GKRKLTKSVA AKFSNQMQEL
     VDTLDATRCN FIRCIKPNAL MRVGMFDPRY VVGQLRCQGI MQTAQVLKVG LPTRVSYSEL
     VGAYKKFMPA DAQRLFANQS DPTLITAILW AFQVPMDAYK LGITKLFFKA GKIAVLDSIL
     KINWATEGPH IVSRMKLWLA RRRWRVGLAK VIAQNRFAKL LRRIQFRRNS LVRIQRWWRA
     YSVRREFQKK RTAAVVVQAL FRGMTARRLF KSKKQEMLAL AAARAAEAKR QAEEAKRREE
     EARMAAEIAR RESIARAAAE EDRLRMEAEA RAAEEEAIRL AKEAAAAVAE AEAAAAEATA
     AVEHERQAEL RAIAEAKELE ERMEREREEA ERRKEQALLE AASVSASLLS GLAQVNSVQT
     PAGQVHVVEI PDDVSQENRE QLQQLNDLLL SGAIAQAEYD ELVPFLLEKP EEAPSGAALT
     AEQEESLSRL YTTGVYGIQI RCPACGATNN TANGNHCDEC GSLLTTSDES SAAAADPAYY
     GYRGQSRQQR SLSTLTAPLG TFSTENGRIV IHDGYFEAQM HRTQVLQDDN YTEYTVYVLR
     CQWQPKDSHE STTWLVSHRF SVFEKLHKDL KRKIPTAVAT IPLFPRKHVL GGVFKGKTGN
     SSAIVEERKQ GLERYVAQVL ELCARLPENL NVPELDRFLN VSRQVEQFRR QVLSNGSDES
     GAAPAGFGRA LNVNAGGAEG MAAREQARLP TELPTPLDEE ELSHTEQAVA LLNASIRCAR
     GDLRRDASVQ HHLKVCVQLL PRLQISANLD NPFANVDLIP RAMQCQEDLE TTMGLYNDSL
     LAVTETYALS AQEGGGVQAP PPFVPGQQNS YQPSYGV
//
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