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Database: UniProt
Entry: M7UN95_BOTF1
LinkDB: M7UN95_BOTF1
Original site: M7UN95_BOTF1 
ID   M7UN95_BOTF1            Unreviewed;      1846 AA.
AC   M7UN95;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Putative kinesin heavy chain protein {ECO:0000313|EMBL:EMR88348.1};
GN   ORFNames=BcDW1_2971 {ECO:0000313|EMBL:EMR88348.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR88348.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; KB707787; EMR88348.1; -; Genomic_DNA.
DR   STRING; 1290391.M7UN95; -.
DR   HOGENOM; CLU_001485_20_2_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd22705; FHA_KIF1; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd22249; UDM1_RNF168_RNF169-like; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}.
FT   DOMAIN          8..365
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1628..1801
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1496..1517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1545..1613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1692..1716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1804..1846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          436..474
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          758..835
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1499..1517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1557..1605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1696..1716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         111..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1846 AA;  204235 MW;  7A5D30C882E6FB96 CRC64;
     MAPGGGGNIK VVVRCRPFNS REIDRGAKCI VQMKDAQTVI TPPEGHEAKS RDAKGGKADT
     GQKVFAFDRS YWSFDKNDPS YAGQDNLHTD LGKPLLDNAF QGYNNCIFAY GQTGSGKSYS
     MMGYGKDAGV IPKICQDMFE RIGELQQDKH LKCTVEVSYL EIYNERVRDL LNPSTKGNLK
     VREHPSTGPY VEDLAKLVVS SFQEIENLMD EGNKARTVAA TNMNETSSRS HAVFTLTLTQ
     KRLDVETKMA MEKVAKISLV DLAGSERANS TGATGARLKE GAEINRSLST LGRVIAALAD
     LSEGKKKKVG KGNQVPYRDS VLTWLLKDSL GGNSMTAMIA AISPADINFD ETLSTLRYAD
     SAKRIKNHAV VNEDANARMI RELKEELAQL RGKLTGGGGG GGGGGPADEI YAEGTPLEKQ
     MVTIVSSDGA VKKVSKAEIT EQLNQSEKLY SDLNQTWEEK LQKTEEIHKE REAALEELGI
     SIEKGFVGLH TPKKMPHLVN LSDDPLLAEC LVYNLKPGST SVGNVDTNAA HAAEIRLNGT
     RILHEHCTFE NVDNVVTLTP TEGAAVMVNG QRVEKPTRLR SGFRVILGDF HIFRFNNPTE
     ARAERAEQSL LRHSVTANQL ENFKDWDKFS PSSTPRPAHD RTFSKAISDL DFDGSSRADS
     PVPGRGLSDW SLARREAAGA ILGTDQKIAG LSDEELNVLF EDVQRARAER ATANLEDDLD
     SVTSYPMREK YLSNGTLDNF SLDTALTMPS TPKQGEVEDR MREVKEEMQV QLEKQREEFQ
     EQLEIAKTSN VEVEEIKKEK VRMEETLREV KEEMLKQLEV QRKEYEEKLQ ELSPVKSGPD
     GPPPLSEKEI VVAEKVAKHW QGRRYVRMAE AVFQNAAILK EAQIMSHEMD ENVVFQFAVV
     DIGHALCSSY DMVLNDIEGD DFHLEDATKP CIGVRVIDYR NNVAHLWSLD KLQDRIRKMR
     QMHQYLDRPE YLQHFRLDNP FMETCMPQYT HVGDVDVPLS AVFESRVQDF TLDVLSPFTM
     HAIGIIKLSL EPSSAKAPSN TLKFNVVMHE MIGFAEREGT EVHGQLFIPP ASNEGGVTTT
     QMIKDFDEGP IRFESVHSMS VPMFGPTDVS LRVAIFAKVS SMHLDKLLSW DDMRDNIPQP
     KKKRKGARIA ESQFYSEEKH DVFAKVQILE LAESGDYPAV EVIQTSELDQ GTFQLHQGLQ
     RRIAVTLTHN SGDALPWSDV TGLRVGRIQL VDHIGKSPDL SSPSTPPLYL KLLSKPIVKA
     NANGTSNVCI VGKWDSSAHE SLLLDRVTAD KYKVQMSLSW DVKSEKLSRL MTFNMDVCSQ
     IMSRNYVRST SMFASLFQSV RIVHSMTSIY SISVRPVAVK RAGDLWRMNT SEDYVKGEEA
     LTNWTPRGIS LVKDFISARR KRQRLAEIDA AQPLLRRIAS SPVPITIPAP SIPQVVELDP
     ADIPLPVSPP ATTENFPSPL SIDEALPSSV DGNALGIHRD GQFNNEITEK IESAIDTGSI
     PHDPSQEQEK PQNQSEYNPH QTALLQKFTK YFHLCRDPST TILTPTNIEP PINGSPAPSL
     FHTTSFTSNT SRSNSPRPSN FSNSLHPSTA NSRQTSRSRQ TSPIPHAHPK PSIPQHLATI
     SQIKKNPSVL KAGMLLVPSA DSTKWIRRFV ELRRPYLHIH AVAGPNSGEE VNVVGLRNAR
     VDHSPEIAKL LRNERQGGSG NASRNSSPAS AGAQQSWSNN GIGGIYGYGG RGRSGSGMGM
     GIMGYGGRGN GNANGNGNGE SRREIEETVF AVYGTNNTWL FRARSEREKV EWIWKIDQGY
     FSGGGGRAGN GSGNNSRGRR DDGSGDSDDV DAEVDVDVDR EDYLAD
//
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