ID G4ZFA6_PHYSP Unreviewed; 1304 AA.
AC G4ZFA6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
GN ORFNames=PHYSODRAFT_345966 {ECO:0000313|EMBL:EGZ16609.1};
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:EGZ16609.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ16609.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ16609.1,
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; EGZ16609.1; -; Genomic_DNA.
DR RefSeq; XP_009525667.1; XM_009527372.1.
DR STRING; 1094619.G4ZFA6; -.
DR EnsemblProtists; EGZ16609; EGZ16609; PHYSODRAFT_345966.
DR GeneID; 20648750; -.
DR KEGG; psoj:PHYSODRAFT_345966; -.
DR InParanoid; G4ZFA6; -.
DR OMA; VGAEDMC; -.
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 CDD; cd00124; MYSc; 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 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; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT DOMAIN 89..831
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 57..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..714
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 986..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1052..1139
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1188..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1304 AA; 147662 MW; 82DD56D2236A0047 CRC64;
MEGIRVFIPD EKLVWVPATV LSVDASGKVF CVRVQPLASS PSSSDYEADA PAEERTIDLN
DDGMPDSLPL QNGPHEGDEE DAKAKHAGVG AEDMCELGHL HEPAIVYNVR ERFFAKEPYT
YTGKIVVAVN PYQWIKENYS EELRDLYTQR PWDEMPPHVY ATSAEAFHHM KQHRIPQSIL
VSGESGAGKT ETVKIMMEHL ASISMGIAKR LHPAESGETI VVEKVLKSNP LLEAFGNAKT
IRNDNSSRFG KFTQLQFNSD YCLVGAECRH YLLEKSRVVA QAAGERNYHI FYQLVSAKED
VFGFTEDSSA KEFRYLQDEK LILDGQTDLE RYQVTRDALT TIGLSDKEQN ELFSALCGIL
RLGQLDFVPL ESNKDDASQA VAAASASDSV SAEQIDQQKI EIEQCAKLLG VEVAALSKQL
CSRTVKARQE VYCVPLSALH AGNNRDALAK EIYARVFGYL VRRVNHSISN SADRGASTPS
YLHIDLLDIF GFESFKHNSF EQFCINFANE KLQQKFTLDV FKTVQEEYQQ EGVAWEFVKY
RDNQDMLDLL ENSMGVMALL NEECVRPMGS DLSFVSKLVS LRESHPRLER ARLSQMHFML
HHYAGPVTYD AEGFVEKNKD SLQTDLLELL GTSSNGLMSM VFSDDDNTAF MTDADLAVRA
ATMMEGGRRS TVSRKTSTFM QETVSYKFKA QLSLLMSDIS STEVHYVRCI KPNSEKSPNS
YEIDAVVSQL RCAGVVEAIR ITRAAFPNKM AHEKFLRRFV MMRSKKNASA APASTTVTEA
CEQLAKELLS GDDFAKTQEG SEHSRTPTFV VGKSLVYFGK DVLEFLEHRR TTFVHERAIV
IQQTARRWMA RRRIKKVRTM ISNIQALHRC RMQRRSFLEK RRKCIVVQSV WRGVRSRQRV
YLLMKEKSAI KVQTAYRKYL SEKKYATFRN AVIKIQSTLK MKKQVGKYHK LLSERKEQDA
METEVELLKH RLEDEKRARM EIEAENSSLQ QELNQVRSSS VPSADSSIYE SEGPPNFRNS
SMRLSRIERE SMDDGKLLDD SERMIDYLRK EVTKGRELIQ LLSQENENLK AENKKIKDAY
TAAGASFAAL NQHNKQQSKA NLRLMSTHAA LIKSQEEKMK KYKKQVAELK EDLRMQRSVY
SAELKARVQQ QEVLVDIINL AESDGVSEDL LERMRAMAVD SKPSYENGRR SSEYTRPPTG
RRSSTASSRT GRESEYRDKR SDTATSLGTV PVSVAVGSNP TRNERRATLD TIMNNPVPQG
VSPQGEGISP PDRGSLNRSS VYSDDGHRKS RIGGMFKKMF KKDE
//
