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Database: UniProt
Entry: A0A2T3Z656_9HYPO
LinkDB: A0A2T3Z656_9HYPO
Original site: A0A2T3Z656_9HYPO 
ID   A0A2T3Z656_9HYPO        Unreviewed;      1415 AA.
AC   A0A2T3Z656;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN   ORFNames=M441DRAFT_430318 {ECO:0000313|EMBL:PTB40282.1};
OS   Trichoderma asperellum CBS 433.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB40282.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB40282.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB40282.1,
RC   ECO:0000313|Proteomes:UP000240493};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KZ679263; PTB40282.1; -; Genomic_DNA.
DR   STRING; 1042311.A0A2T3Z656; -.
DR   OrthoDB; 1430657at2759; -.
DR   Proteomes; UP000240493; 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; 1.10.287.1490; -; 1.
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; KINESIN-LIKE PROTEIN KIN-4A; 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:UP000240493}.
FT   DOMAIN          54..440
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          186..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          528..581
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          673..707
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1137..1219
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1273..1341
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1381..1412
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        23..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        998..1012
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   1415 AA;  158335 MW;  B36575374107CB5E CRC64;
     MASSPPGSPS PAHKLQRPLS AIATRPQPRS TSRLSMNSKQ GGESRASDED NRTAVRVAVR
     VRPQLRPEDP GYDLIPQRFQ RPMVHVTSNT SLSIDSPQGR KLFVFDRVFG PEVTQSGIWD
     YLSDSINAFT QGYNVSLLAY GQSGAGKSHT MGTSSPDAQS NPEDMGVIPR AAAALFEHLD
     VQRGGANNNG STMKSASSFR SPRGYGQQNN LGDRNWAMTA TYVEIYNETL RDLLVADSTG
     FNDRTSVAIR EDVKGNIILT GLHQVDITCV DDILNALDFG SSIRQTDATA INAKSSRSHA
     VFSLNLVQRK SKYSNSDKRH SMPLEAMSGQ DVSVTTDSKL HFVDLAGSER LKNTGAQGER
     AKEGISINAG LAALGKVISQ LSSRNSGAHV SYRDSKLTRL LQDSLGGNAI TYMIACVTPP
     EFHLSETLNT VQYAQRARAI QSKPRIQQIE EGDKNAIIER LKAEVAFLRE QIRSANTGLT
     EQPRSANRSS ERSERQNERE LELQNQLLDS QENYNTLSQR HAHLISEMAK AQESESEHHR
     QLDELQGENA TDRLNRSNSF AKAVEQVVLE YEKTIQTLEQ SLSSTRTTLS NTETNLLEKE
     TKCAYVETIN SQLQSRLQKL TDREAHTANY LHDLETKLDG HTNGEEKNAT IIVELRKEIS
     RIRENESASE DYISTLEERL AEADQDAELM QREIERLEQV IERQRSLGKL DALLHELDHV
     DESKTSDFEG GTNDETAERQ SNQSVDSKAQ GYDDDENATP TLAPVVENDE DAANAAKPVS
     KAAEEQSNGD VAQNQATAQT KFVSDKLELV TRELFDLRTE HESTVHDYGR LHAKYEEAMK
     KLSELQDTID EARYPSRARH SIISVDAATE TRPESFQSAA TSDVKDDVRS SVPRSLSSEL
     SSVIDSPITA DTTHMDLESE DDTATAKPAT SVEDLTRELV EHVELHEQDE LKEKHEHVEH
     VELAEPIEQQ EVEHYDVEPR EFEQQEVEQQ EVEQQEVEQQ EVEQHAEQVE VEPVKAVEQN
     AKSEQNEHSE QNERLIAELE RLRVLAEEKE TAEQELALKY AQLELKHHET LDMVEELKTE
     VSKARTVEAG PRVIRRKSSQ NLLGVDRAQR SFASLRNLAA ENFEGKPETM QSFELSLNSA
     IHELQSRSER IQELESDVAA AKKEMESKMA IISGLARERS SLKASPVDMS MVATLRGQLE
     QSERQLSDLR SAHAARERDL TSEVEILRKS VASTPTREFT PSDEEETDIP YNERVSTLQA
     ELAGWENKHH NALVSMRSTE REMQETIQQL EAQVEAANAQ LAESQSLVAA GRDAEEAKKE
     VRKQQDLIEF LRGEIDEYKA VISSNATKVT ELEALHRSAR AAMDDMSKMH SEVTAETTAR
     HQELSTKLEQ LIASHEDATK AHQEEMEALK DREIN
//
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