ID W9X3R7_9EURO Unreviewed; 981 AA.
AC W9X3R7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 28-JUN-2023, entry version 43.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=A1O7_01474 {ECO:0000313|EMBL:EXJ65134.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ65134.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ65134.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ65134.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-2013) 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,
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:EXJ65134.1}.
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DR EMBL; AMGW01000001; EXJ65134.1; -; Genomic_DNA.
DR RefSeq; XP_007753701.1; XM_007755511.1.
DR AlphaFoldDB; W9X3R7; -.
DR STRING; 1182544.W9X3R7; -.
DR GeneID; 19176086; -.
DR VEuPathDB; FungiDB:A1O7_01474; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_24_0_1; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000019473; 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 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:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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};
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:UP000019473}.
FT DOMAIN 222..578
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 303..310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 981 AA; 105713 MW; 95A05F3A62046DB9 CRC64;
MSLPVLSRPV ADPPTGALPP IPMNKPPRKS LGQTPSRLKL PSRPSALQTS QPVQSAPNLS
PERASGASVT RGVRKVVSIG SFPQPPTVNS RPPTSASMAS STSIKKRTSD GGHSIQAPSG
RSKKSPRNST APSFRTSQTP SLLNSAGDGM TVSARYNKRT SDAQSSVHSP PQSRSSSANG
SYSTSATTFE EGDEDSRGRT KELEDGSADP KTLSKGKEVK GNVIVSVRVR PDVGNQNNTQ
TEGEWMVDGR RGLVAFRGKE GGDYHLDNVF TTHDDNAKVY DSAAKRLVRR VMEGYHGTVF
AYGMTGTGKT FSMQGTMSSP GVIPLAITDI FSYIRETPHR EFLLRVSYLE IYNEKIHDLL
ALPAGGVVGQ QQEEIKLRED SKRGVYASPL KEEIVQSPTQ LLRVIHRGDQ ARRTGSTQFN
SRSSRSHAVV QIVVESRERI PGSGSLQENG KRVAMLPGGV RVSTLSLIDL AGSERAAEDK
ERRAEGAHIN KSLLTLGTVI AKLSGTRDKN GNLLDKDGKH LPYRDSKLTR LLQPALSGNS
LVSILCTIQI GAGLASAGSN HIGETLNTLK FAARAKNNIV SHAKKAVEEL GSVNSGLLER
YRSEIASLRA QLEGQQKSAA EKEERQLERE AEQRHEEQML EMQLARTALK ERIEHLNRLI
LCSKSTGVNS GTVSAMGMHS RLSNGTEFGA PRSVRSSASQ STLGVGPSLG RHPSVASLSG
AASASAHLSF QGIPDEDEEA GGDFGDGRAS LQAQVRALQA DLQDKTRYIS TLEKRLLQAR
RSSHSRVSMA FNKPTGDDTE MQRRLEEKDA MISDLQKTVS ALRSAVRKRE IAELTPEMSS
SEFKQNRAQG HQSNSSNGSS HTGSQLSGPT HQILPGGPRS PLTASPLTIL SPQKAMDKKR
KTVDEMSRML DEMIQDKVAS GKLNNRRSSS VRVASRGSSA PRRHSRRMSV AANSPTTGPG
LGTMVASLRE RDSVVEPSSP S
//
