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Database: UniProt
Entry: G4ZVF8_PHYSP
LinkDB: G4ZVF8_PHYSP
Original site: G4ZVF8_PHYSP 
ID   G4ZVF8_PHYSP            Unreviewed;      1911 AA.
AC   G4ZVF8;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Myosin-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHYSODRAFT_517698 {ECO:0000313|EMBL:EGZ11476.1};
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:EGZ11476.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ11476.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ11476.1,
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; JH159157; EGZ11476.1; -; Genomic_DNA.
DR   RefSeq; XP_009531809.1; XM_009533514.1.
DR   STRING; 1094619.G4ZVF8; -.
DR   EnsemblProtists; EGZ11476; EGZ11476; PHYSODRAFT_517698.
DR   GeneID; 20659963; -.
DR   KEGG; psoj:PHYSODRAFT_517698; -.
DR   InParanoid; G4ZVF8; -.
DR   OMA; NMHEAPL; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd14892; MYSc_Myo31; 1.
DR   CDD; cd00821; PH; 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; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 2.60.40.150; C2 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   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR025939; Aida_C.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR035892; C2_domain_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   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14186; Aida_C2; 1.
DR   Pfam; PF13637; Ank_4; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00015; IQ; 12.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51911; C2_AIDA; 1.
DR   PROSITE; PS50096; IQ; 6.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT   DOMAIN          114..919
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1408..1518
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REPEAT          1637..1669
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          1744..1911
FT                   /note="C2 Aida-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51911"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..782
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          864..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1353..1405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1353..1395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         222..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1911 AA;  214703 MW;  4129B64CC1B1DA07 CRC64;
     MLARRTPPTI STRPPSSKTL GKALESPSGN NQQHSNNANH AGRPAPLGQI DANHLQVGTK
     VWVADAKVLW RIGEVQSIAD DRKTAQVYLP DAADDQVQTL RMDQLVTFDA SHIVDHADVA
     LMNNMHEAPL LNVLRQRFER DEIYTFTADI LLSINPYKSI PLLYDVVGFM KSREEAATAT
     GDGSTSDSSA PPHLFSIAEK AYTGMKGVVP GSGTPQSIVI SGESGAGKTE ASKYIMKYLA
     TASKHAASSS TVAAGVHEQI EECVVLSNLI LESFGNAKTS RNDNSSRFGK YIQIHYSSEG
     RMAGVSIRHF LLEKTRLVRP EVNERNYHIF YQLLAGLDTL TTSSSDPSDS DRPLLLQNDV
     WNYTYLTRGD CVEVDGVDDA TEFEQLRRCL EQLGMDNASF QRPMFEVLAA ILHLGNVQFE
     SPTTQDDTNG DDSRENDPTH VVFPESDAGV NLEHVAMLLG VDAAEFANKM VTQTTVTGRG
     SILEIKLTPE QAKNAMDAFC KYLYGELFHH VITRINACAK QQTSLIPTTD KKTPKSRVQG
     GATAPTVAPF IGILDIFGFE VMKRNSLEQL CINFTNETLQ QQFNKHVFVL EQERYAREGI
     AVSPVEFQDN QRCLDLIQKP PLGLLPLLEE QMLLKRKTTD KQLLTIYHGN HLEKHPSYAK
     PRFECDEFII RHYAGDVVYD IHDFIAKNTD NLHDDLLDLL RRSSQPLLQA MFSAPVAASL
     GGAATKRGGP TTPTGAMHKR TQSASLTGTT TVSSRFRTQL AELMEVLWST TPSYIKCIKP
     NNLKFPGGFS CELVRDQLTY SGVLEVVRIR QEGFPIRKQY SVFYELFWSL AIAKYGVAAT
     RNNPGKMREA CEFIAREWLK DKELESEEPL KEDDESPETE KDETEPKPPR APARQIFAMG
     KNEIFLRYGQ VERLEGSLAT IRQESIVVLQ SKLVRARLAF KKFHKLRRAT VKWQALWRMR
     VQRAKYLKQH RAAIRIQAQF RCFQLTTLFQ KKKRAACIMT RVSRRYVTRC NFLRFLKATR
     AATEIQRHVR GFMLRTAAER ERKLRLRSTL KLQSWQRMHA HRRAFLAQRR AAIRIQTRYR
     ARTQRRRFLL EKKAEIVLAA FVRQFLQRRR FKKLKVCITK TQALVRKWEA RRRFVTLRSG
     VVCIQSQRRR HAARRVFVVR KAAVARLQHA MVGWIARCHY LALRRSTRTL QYCVTSWLLC
     RQFRRARKAS RRIQKTWRSH SRRVKWEAEV ASVFVSRSVN GTSTIAPGSG STSWTQHTRM
     EDSDRRMAKL RSQPDVYFVL QPRAFGYNSL FHEAAACGDF HVVKYMLQER SSEELLSLKN
     GRGFTAFHEA CANGQHTMVK YLVLQMTAMT ATGARENTPS TPKALEQSTK ANSTDGPEAK
     ETNATASSSD EVGNQQEEEP SSRIPERTIV YSGFLRKRRE TSRWMKRFVV LSVTADKQDH
     PQLEYYPNDR KLTLAGPSSL QIDLTTALLK TSVDLPFAFE LHSPQLLGGR NKEGRLYFAA
     SGALEIQCWL AHFRNIIPSS IESRVFAMHR SAQNSKLEFV DFKARQEACN LRSESSRQET
     PLHLVASCSS LVILAAIDDD TDNNKSSTTS EIQLDVTTAA ASSSSKSKSL LDAELELVKT
     AQWLLENGAD VNAMTTRQET PLQFALQAGH LMLAKLLLDR GALASNLSEP QLVFVRCLKA
     ELAKTAITSI SSAACTSVGI SHAPQPPSNP LLAAGSALLK RPNKLTRRLS ASEEELPMLF
     LVKQPGKVRH SSYVSLFVEL IALSDAALIG ARRPRIVISV MDGQRNLVEM RQQVSVQPVA
     SSNALLWGFT WHMQTPLENL PHGACVVLEF ATTSTSSVSP TNDGPTSPTL GASVLVPECW
     TYLQVDQRTA NSTALTAEMY KYPVDLSSHN TLHRADAFLS GEMLISQARA T
//
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