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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//