ID A0A010SLT5_9PEZI Unreviewed; 1057 AA.
AC A0A010SLT5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Kinesin motor domain-containing protein {ECO:0000313|EMBL:EXF85843.1};
GN ORFNames=CFIO01_11719 {ECO:0000313|EMBL:EXF85843.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF85843.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF85843.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF85843.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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 -!- 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:EXF85843.1}.
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DR EMBL; JARH01000054; EXF85843.1; -; Genomic_DNA.
DR RefSeq; XP_007590499.1; XM_007590437.1.
DR AlphaFoldDB; A0A010SLT5; -.
DR STRING; 1445577.A0A010SLT5; -.
DR KEGG; cfj:CFIO01_11719; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_21_1_1; -.
DR OrthoDB; 239968at2759; -.
DR Proteomes; UP000020467; 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:UP000020467}.
FT DOMAIN 9..378
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 645..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1057 AA; 115657 MW; 68E56E55C2C7A35C CRC64;
MVVDPNAASI TVAVRVRPFT IREAAQLTRN EEGTVFLGDG SLAAAPPKLQ RGGIRPVIKV
VDDRCLVFDP PEDNPVHRFG RSVVPNGKKV KDQTFMFDRI FDDNATQNDV YEGTTKQLID
SVLDGYNATV FAYGATGCGK THTITGTSQH PGIIFMTMQE LFEKITERSQ EKTTEITLSY
LEIYNETIRD LLIPGGSKQG LMLREDSNQA VSVAGLTSHH PKNVQEVMDM IVQGNAWRTV
SPTEANATSS RSHAVLQINV SQKDRNASVN EPHTMATLSI IDLAGSERAS ATKNRGERLL
EGANINKSLL ALGSCINALC DPRKRNHVPY RNSKLTRLLK FSLGGNCKTV MIVCVSPSSV
HFDETQNTLR YANRAKNIQT KVTRNVFNVN RHVKDFLVKI DEQIALINEL KAQQKDAEKT
FYAKFRKQSE KRDAIAREGV QRLRVAYENS ANDRRDRINN MKKLRAFERR ISLLSAWVAS
FDTVCDQRGD EDAMPATLLA IRKTAQGIMV ELEHSRHHIH QKLENTNWER AIDTALHHSI
KQLPGGESDA AEIDTLTREA ELLKANFGRE ASHEVLEMDK GGDAAMMQVL LTAQFDILAS
LEDTLAMNEE DAVAHAKQII NRLLEAGFSA ASHVVKPDGA MIPVEKFSPR KQGTPKRKKA
VVNNTTSPIR QPAFVPPNEP APQPQASPIK LSPRRRKAAA PRSPRKGVSF TPVKRKSEAK
RGVRWRDDET ESGLADFEKT PKKFEATPEH TSPEKGLRMP ALPSYLRTAS PNPGNSGSDD
SPTLELPESS SIPPAKPNRF QAGFLTKGRI SSIGSGSPTV PIPTMSLPLG SSPSSDSGDR
VAPLRALDVH RSSNLSPPAF RSRIARASPP PRTSLSGNVS ADENNPPSPQ GPSGSESESP
SIDPRKIRSA LHSMKKVRGE HRRVSSIGGT AASNARRISS VNSIGSNHRA SASFSGPMAS
STNGISRSRR ASAERRLSPP MVCSPPDFRN DRAFTAGQAR RMHLGGSLRL EGGSPQAPQH
RMASADFKNR RITIGSLAAT GKIEKGHAPR PSVAGWR
//
