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Database: UniProt
Entry: W7MJD0_GIBM7
LinkDB: W7MJD0_GIBM7
Original site: W7MJD0_GIBM7 
ID   W7MJD0_GIBM7            Unreviewed;      1585 AA.
AC   W7MJD0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Myosin MYO2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FVEG_07789 {ECO:0000313|EMBL:EWG47745.1};
OS   Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS   fungus) (Fusarium verticillioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG47745.1, ECO:0000313|Proteomes:UP000009096};
RN   [1] {ECO:0000313|EMBL:EWG47745.1, ECO:0000313|Proteomes:UP000009096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
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; DS022251; EWG47745.1; -; Genomic_DNA.
DR   RefSeq; XP_018753936.1; XM_018896462.1.
DR   STRING; 334819.W7MJD0; -.
DR   EnsemblFungi; FVEG_07789T0; FVEG_07789T0; FVEG_07789.
DR   GeneID; 30065561; -.
DR   KEGG; fvr:FVEG_07789; -.
DR   VEuPathDB; FungiDB:FVEG_07789; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   HOGENOM; CLU_000192_3_1_1; -.
DR   OMA; EIMFDDR; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000009096; Chromosome 3.
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:0006996; P:organelle organization; IEA:UniProt.
DR   CDD; cd15480; fMyo2p_CBD; 1.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 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; IPR002710; Dilute_dom.
DR   InterPro; IPR046943; Fungal_Myo2/2A_CBD.
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; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 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};
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:UP000009096}.
FT   DOMAIN          6..61
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          74..781
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1228..1497
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          188..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..678
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1030..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1559..1585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1585 AA;  180545 MW;  8464F90FAE6B4728 CRC64;
     MASAYEVGTR AWQPDTAEGW VASELINKTV DGSKVKLTFQ LENGDTKDIE VTAEALQSGN
     DPSLPPLMNP TMLEASDDLT NLSHLNEPAV LQAIRLRYLQ KEIYTYSGIV LIATNPFARV
     DSLYVPGMVQ VYAGRQRATQ APHLFAIAEE AFMDMVRDKK NQTVVVSGES GAGKTVSAKY
     IMRYFATRES PDNPGGRSKR GAESMSETEE QILATNPIME AFGNAKTTRN DNSSRFGKYI
     EIMFDEHTNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ LVAGASEQQR EELNLLPIEE
     FEYLNQGNCP TIDGVDDKAE FEATKKSLST IGVTDAQQAD IFKLLAGLLH LGNVKITASR
     NDSVLAPNEP SLERACAILG VKAEEFARWI VKKQLVTRGE KITSNLSQAQ AIVVRDSVAK
     FIYSSLFDWL VDIINHSLAA EEVLNRVVSF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
     QEFNQHVFKL EQEEYLREEI DWTFIDFSDN QPCIDLIEGR MGILSLLDEE SRLPMGSDEQ
     FVTKLHHNFT PDKHKFYKKP RFGKSAFTVC HYAIDVTYES EGFIEKNRDT VPDEHMAVLR
     ATSNEFLKTV LDAASAVREK DAASSSSSSV KPAAGRKIGV AVNRKPTLGG IFRSSLIELM
     STINNTDVHY IRCIKPNEAK EAWKFEGPMV LSQLRACGVL ETVRISCAGY PTRWTYEEFA
     LRYYMLVKSD QWTSEIREMA DAILKKALGT SSSKGMDKYQ LGLTKIFFRA GMLAFLENLR
     TTRLNDCAIM IQKNLRAKYY RRRYLDAREA IVMTQSAIRS WKARKQVQEL RTIRAATTIQ
     RVWKGSKQRK AYQQIRKDMV LFESAAKGYL RRKNIMEERL GNAALKIQRS WRSRRQLRAW
     RQYRNKVVLI QSLWRGRSAR KDYKKIREEA RDLKQISYKL ENKVVELTQS LGSMKEKNKG
     LASQVENYEG QIKSWKKRHN DLEARTKELQ TEANQAGIAV ARLQAMEDEM KKLQIAFDES
     TANIKRMQEE ERELRESLRA TNSELETARR SSTQHEKDNM SLRQELESLR DALELARRNA
     PINGELANGT TPAAAAPSGL INLVSSKKPK RRSAGAEPRE LDRFSGTYNP RPVSMAVTGT
     AHRQNLSGST FLPGVDNIEM ELETLLADED GLNEEVTMGL IRNLKIPSPS STPPPSDKEV
     LFPSYLINLV TSEMWNNGFV KESERFLANV MQSIQQEVMQ HDGDEAINPG AFWLSNVHEM
     LSFVFLAEDW YEAQKSDNYE YDRLLEIVKH DLESLEFNIY HTWMKVLKKK LHKMIIPAII
     ESQSLPGFVT NESSRFLGKL LQSNSTPAYS MDNLLSLLNS VFRAMKAYYL EDSIITQTIT
     ELLRLVGVTA FNDLLMRRNF LSWKRGLQIN YNITRIEEWC KSHDMPEGTL QLEHLMQATK
     LLQLKKATLN DIEIIQDICW MLSPNQIQKL LNQYLVADYE QPINGEIMKA VASRVTEKSD
     VLLLQAVDMD DSGPYEIAEP RVITALETYT PSWLQTPRLK RLAEIVSAQA IAQQEKFDYT
     DGEDYEDGQP QHHELAGVDE VETES
//
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