ID A0A1Y2URL6_9PEZI Unreviewed; 1044 AA.
AC A0A1Y2URL6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=M434DRAFT_399820 {ECO:0000313|EMBL:OTA86680.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA86680.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA86680.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA86680.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112568; OTA86680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2URL6; -.
DR STRING; 1001938.A0A1Y2URL6; -.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0005819; C:spindle; IEA:UniProt.
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 GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01370; KISc_KIP3_like; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF13; KINESIN-LIKE PROTEIN; 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 Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000194361}.
FT DOMAIN 10..380
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 647..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1044 AA; 114182 MW; C6322220A0CA3714 CRC64;
MASKDPGASS ITVAVRVRPF TIREAAQLQR NDDGTLFLGD GSLAAAPTPK LKQSGIRSVI
KVVDDRCLVF DPPEDNPVQK FSRSVVPNGK KVKDQVFAFD RIFDENTSQT EVYEATTKNL
LDSVLDGYNA TVFAYGATGC GKTHTITGTS QMPGIIFLTM QELFEKIAER SDEKHTEISL
SYLEIYNETI RDLLVPGGSK QGLMLREDSN QAVTVAGLTS HHPKDVQEVM DMIVQGNEYR
TVSPTEANAT SSRSHAVLQI NVAQKDRNAS VNEPHTMATL SIIDLAGSER ASATKNRGER
LIEGANINKS LLALGSCINA LCDPRKRNHV PYRNSKLTRL LKFSLGGNCK TVMIVCVSPS
SAHFDETQNT LRYANRAKNI QTKVTRNVFN VNRHVKDFLV KIDEQMALIN ELKAQQKDAE
RIFFAKFQKQ LEKKNWSVKE GVQRIKTAYE NSQSERQEKV NLMKKQRGIE RRIGLLSSWI
AAFDAVCDMR EDEDSMPPNL TAMRKTAIGI QLELEDSRQH IHQKLSKMNW ERAIDGALQH
SISQLPSGEG HSVDNGEIES LTREAELWKA KFAREADREV LEQDRAGDAG IMQVLLTAQF
EILASLSETM NMSEEEAVAH AKSIIHRLLE TGYTAAAQVV KPDGAKMPVE AFPPTKRGTP
KRKKMSMGKD AVKPIPNPAL AAIAASQPQQ MFGSPVRGSP RRRKALNARK GVSFTPVKKK
SRVVRWRDDD GESGTLADFE KTPQKFDSSP ERNSPEKAIP KITAIPLNFN KDSSADESSP
SLTIPEVSSL SVSKPNRFQA GFLSKARSSD ALGSLSPPTI SINATSSSSD GEEKPSPLRN
LDVSRTANIS SPKTRLSSLS PSSIPAPRVT STFSSDENQP PSSDSDTSAI IDASNLRSAI
HASKRPKRLS SLAGGINGPV ATSRRVSSIG SLGGHKQTNS YTGPLASSTN GISRLRRGSA
ERHRSPPISC SPPDISVRES RSFTPGQARR MNLSNSVRGA GGLTSPSERR ERLEASGRNR
RITIGGSAMA GNGARRERGS LAWR
//
