ID G9NBQ9_HYPVG Unreviewed; 1817 AA.
AC G9NBQ9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=TRIVIDRAFT_210991 {ECO:0000313|EMBL:EHK16263.1};
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:EHK16263.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK16263.1, 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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:EHK16263.1}.
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DR EMBL; ABDF02000091; EHK16263.1; -; Genomic_DNA.
DR RefSeq; XP_013950456.1; XM_014094981.1.
DR STRING; 413071.G9NBQ9; -.
DR EnsemblFungi; EHK16263; EHK16263; TRIVIDRAFT_210991.
DR GeneID; 25790595; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_210991; -.
DR eggNOG; KOG0244; Eukaryota.
DR HOGENOM; CLU_241013_0_0_1; -.
DR InParanoid; G9NBQ9; -.
DR OMA; WSLKATY; -.
DR OrthoDB; 1430657at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
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 Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF15; ZGC:66125; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 54..436
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1647..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 557..591
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 669..703
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1046..1094
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1151..1226
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1294..1355
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1395..1426
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1566..1646
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1686
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1817 AA; 204168 MW; CBA2531E3F401FC8 CRC64;
MATSPPDSPS PAHKLQRPLS AIATRPQPRS TSRLSMNSKQ GGESRASDED NRTAVRVAVR
VRPALNPEDP GYDLIPQRFQ RPMVHVTSNT SLSIDSPQGR KLFVFDRVFG PDVMQDGIWE
YLTDSINAFT QGYNVSLLAY GQSGAGKSYT MGTASAQQNP DDIGVIPRAA AALFEKLDVQ
RGGVNNGTMK SASSFRSPRG YGQQNNLGDR NWALTATYVE IYNETLRDLL VADSTPLNDR
TSVAIREDVK GNIILTGLHQ VDITCVDDLL NALAFGSSIR QTDATAINAK SSRSHAVFSL
NLVQRKSKFS NSDKRHSMPL EAMSGQDISV TTDSKLHFVD LAGSERLKNT GAQGERAKEG
ISINAGLAAL GKVISQLSSR NSGAHVSYRD SKLTRLLQDS LGGNAITYMI ACVTPPEFHL
SETLNTVQYA QRARAIQSKP RIQQVEEGDK NAIIERLKAE VAFLREQIRS ANGQGDLPPR
SANRSSERSE RQNEREAELQ NQLLDLQENY GTLNNRHARL IAEMAKARES EFQHHLQLDE
LQGENATDRL NRSNSFAQSV EQVVLEYEKT IQTLEQSLSK TRTTLSNTET NLLEKETKCA
YVETINTQLQ SRIQKLMDRE ASTESYLHDL EAKLDGHTSG EEKNSAIIVE LRKEISRIRE
NESASEDYIS TLEERLAEAD QDAELMQREI ERLEQVIERQ RSLGKLDALL HELDHVDESK
LRDSEDDTKE SSTDGHDHQT TQNNDQDTET EEAKAKLAPV VENDEDAVNA DEPVPRISED
QPVDDVAKNQ AFAQSKFVAD KLELVTRELF DLRTEHETTV HDYGRLHAKY EEAMRKLSEL
QDTIDEARYP DRLRHSIISV DAATETRPES FQSVQTSYAK DDLRSSAHRS LSSELSSVMD
SPITADTTHL DLESEDDTAT AKPAASVEDL TRELAEHVEL HEQHEQHEQI KLKEQTEHVE
QVEQVEQVQQ VEQKEPTEHV EPIEHVVEPE HVEQFELKEP VELKEHVEHV EQIQDTQQFE
FVVQQDDVEY QEPAEQPDQA DRSEQNEQLA LEIERLRVLA EEKEKAEREL AMKYAQLELK
HNETLDMVEE LKTEVTKART VDSGPRVIRR KSSQNLLGVD RAQRSFVSLR NLAAENFEGK
PETMQSFELN LNSAMHELQS RSERIQELES DIAAAKKEME SKMAIISGLA RERSSLKASP
VDMSMVATLR GQLEQSERQL YDLREAHAVR ERELTSEVEV LRKSVVSTPT REFMPSDEEE
ADIPYNERVS TLQAELAGWE SKHHTALVSM RSTEMEMQST IQQLEAQLEA ANTQLVESES
RAAAEKDAGE AKKEVAKQQE LIEFLRGEID EYKAVISSNA AKVAELEALH LSARAAMDDM
SKIHSSVTAE TTARHQELSA KLEELIASHE DATKAHQEEM DMLRQTHARE LADLRNHEQT
GYEKQVEVLM TEHSEAIFKL ESELAQSRDE LTRVATQIAA VFGAEMPLEK LGERIEALVA
GQNALELERK KMGELTSHVT ELSNINDSLV RDLEGVKTVI ASMLPGNTEA KVGPLVDQLA
AVKAKVEDLD GRNKKNSRLI EELEEQLQHN FDEVQVTNNR LSSLQSERNA QLDEALASRI
KLQSELETVR EEYAALQVKY NELANGDVKR SNSNSTIRKS SSHNSLPSPP PSVPLPPLPN
GAPSSPTSTR PPSKDNFNIS QVTEDQEARI RAIEKHLAAE RQLTQTLEEA LGDLEKQSKK
VKTDCDAWKK RAQELEAEVK ELKEKSVDQS QDNRYSMQAV EEERKKRQAA EAARKQLEER
MQAISKSKKK KGSLNCF
//
