GenomeNet

Database: UniProt
Entry: W9J204_FUSOX
LinkDB: W9J204_FUSOX
Original site: W9J204_FUSOX 
ID   W9J204_FUSOX            Unreviewed;      1585 AA.
AC   W9J204;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Myosin MYO2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOYG_03612 {ECO:0000313|EMBL:EWY99620.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY99620.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY99620.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; JH717840; EWY99620.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000192_3_1_1; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000030753; 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: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:UP000030753}.
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          1035..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..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   COMPBIAS        1084..1102
FT                   /note="Polar residues"
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;  180570 MW;  C91D99C4D3F9FA8F 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 LVAGASDQQR 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 RRRYLEAREA IVMTQAAIRS 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
     PLNGELANGT TPAASAPSGL INLVSSKKPK RRSAGAEPRE LDRFSGTYNP RPVSMAVTGT
     AHRQNLSGST FLPGVDNIEM ELETLLADED GLNEEVTMGL IRNLKIPSPS STPPPSDKEV
     LFPSYLINLV TSEMWNNGFV KESERFLANV MQSIQQEVMQ HDGDEAVNPG 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 VEVEQ
//
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