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Database: UniProt
Entry: G9ME75_HYPVG
LinkDB: G9ME75_HYPVG
Original site: G9ME75_HYPVG 
ID   G9ME75_HYPVG            Unreviewed;       545 AA.
AC   G9ME75;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=TRIVIDRAFT_35108 {ECO:0000313|EMBL:EHK27369.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK27369.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK27369.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC       ECO:0000256|RuleBase:RU000394}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK27369.1}.
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DR   EMBL; ABDF02000001; EHK27369.1; -; Genomic_DNA.
DR   RefSeq; XP_013961571.1; XM_014106096.1.
DR   AlphaFoldDB; G9ME75; -.
DR   STRING; 413071.G9ME75; -.
DR   EnsemblFungi; EHK27369; EHK27369; TRIVIDRAFT_35108.
DR   GeneID; 25793394; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_35108; -.
DR   eggNOG; KOG0245; Eukaryota.
DR   HOGENOM; CLU_001485_2_3_1; -.
DR   InParanoid; G9ME75; -.
DR   OMA; PRFYHHI; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000007115; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; cd01365; KISc_KIF1A_KIF1B; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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   PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT   DOMAIN          12..372
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          44..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          409..436
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        45..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..502
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         117..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   545 AA;  61860 MW;  EE7DDAB4A7AC38D2 CRC64;
     MPVISRVDRG GNVKVVVRLR AFLQRELQRR ARCLVEMDPV SQITTLRAPD EQDAPPSSSP
     SKSRKLADKS FTFDSSFWSH DPDDKDYATQ EDIYNSLGEE FLDHNFEGYH TCIFAYGQTG
     SGKSYTMMGT PENPGLIPRT CEDLFERIDA AHNEDSSVAY NVRVSYFEVY NEHVRDLLVP
     VVPNTAPNYL KIRESPTEGP YVKDLTEVPV RNIHEIMRYI KVGDASRTVA STKMNDTSSR
     SHAVFTIMLK QIHHDMETDE TTERSSRIRL VDLAGSERAK TTEATGARLR EGSNINKSLA
     TLGRVIAALA GPKQLRSGKR KDVVPYRDSI LTWLLKDSLG GNSKTAMIAC IAPSDYDETL
     STLRYADQAK RIRTRAKVNQ DHISSAERDA QIATMAQEIR MLQISVSDSR EREKNAQEAE
     ERLEEYQIRV GTMQRMMEER SMVAESKIKK LQMENEALKL HLKLAIDSLK NPIPPVQLES
     KESDEDEEDE YEYDSESTAA DDELQQEMER YLQDMGNLRK LIGGDLERFK DTDSVRMPLG
     VKQNV
//
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