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
//