ID L2FEG5_COLFN Unreviewed; 1712 AA.
AC L2FEG5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Kinesin-like protein unc-104 {ECO:0000256|ARBA:ARBA00020751};
GN ORFNames=CGGC5_14027 {ECO:0000313|EMBL:ELA24580.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA24580.1};
RN [1] {ECO:0000313|EMBL:ELA24580.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA24580.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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; KB021257; ELA24580.1; -; Genomic_DNA.
DR RefSeq; XP_007286360.1; XM_007286298.1.
DR STRING; 1213859.L2FEG5; -.
DR EnsemblFungi; ELA24580; ELA24580; CGGC5_14027.
DR HOGENOM; CLU_001485_20_2_1; -.
DR OrthoDB; 126886at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 CDD; cd22705; FHA_KIF1; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF5; -; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 8..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1533..1687
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 599..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1689..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 735..808
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1399..1424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1712 AA; 191157 MW; F399417F2B7A45CC CRC64;
MPPAGGGNIK VVVRVRPFNS REIDRGSKCI IEMKDNQTVL TPPSDAQQKG QKDSGQKVFA
FDRSYWSFDR KDNHYAGQDN LFDDLGQPLL DNAFGGYNNC IFAYGQTGSG KSYSMMGYGK
EVGIIPNICQ DMFRRISALQ EDKHLRCTVE VSYLEIYNER VRDLLNPSTK GNLKVREHPS
TGPYVEDLAK LVVGSFQEIE HLMDEGNKAR TVAATNMNET SSRSHAVFTL MLTQKRFDPD
TKMEMEKVAK ISLVDLAGSE RATSTGATGA RLKEGAEINR SLSSLGRVIS ALADISTGKK
KKGAGGQVPY RDSVLTWLLK DSLGGNSMTA MIAAISPADI NYDETLSTLR YADSAKRIKN
HAVVNEDANA RMIRELKEEL ALLRGQLGGG GTPLEKQFVS ITSSDGAVKK VSKAEIAEQL
NQSEKLLSDL NQTWEQKLQK TEEIHKEREA ALEELGISIE KGFIGLSTPK KMPHLVNLSD
DPLLAECLVY NLKPGLTTVG NMDTNAENQA NIRLNGTRIL HDHCAFENQQ DGTVMIIPRE
GASVMVNGKR IEEPKQLHSG YRVILGDFHI FRFNHPMEAQ KERADKSLLR QSVTASQLQG
LEGKAITPSA SPRPGHERNW SKAGSDFGDS RPDSPIPFRP GRDNDWSFAR REAAEAILGP
NQNLASLTDD ELNALFEGIQ RARAERVNGR DGDDDTESVT SYPIREKYMS TGTIDNFSLD
TALTMPSTPK PGEVDDKMRE VREEMQSQLD RQKEEYQEQL KTAEAANVEV EEIKKEKVRM
EETLKTIKED MQQQLEVQRR QFEEKLEKMD PLKRPKANPK LSDEELEIAR QVVKHWRTRR
YVRMAEAVLQ HASALKEAQI MSNELDEGVV FQFTVIDVGH SLCSSYDMVL NGLTGEGDDI
ALDEAQKPCI GVRVIDYKNS VVHLWSLEKL HDRVRQMRQM HQYLDQPEYA QHLSLDNPFV
ETCMPQYTLV GEVDVPLKAV FQSRVQDFAL DVLSPHTSHA IGMIKLSLEP SHARAPSNTL
KFNVVMHEMV GFAEREGTEV HAQLFIPGVS EEDGITTTQM IKDFDEGSIR FESVHSMSVP
LFSPQTVTLR AAIFAKVSAM HLDKLLSWDD MRDAVPLSRG KGKNARIAES QFFTEEKHDM
LARIQILELN EEGEYAPVEV AQTSEMDGGT FHLHQGLQRR IAINITHSSG DALPWDDAMN
LRVGKIQLLD QAGKSPDMGS TSPAITLKLA NKPTFRDNAN GTRSITLTGQ WDSSLHNSLL
LDRVTADKYR VQMTVAWEIS SSKFAEPMKF AMHVCCQIMS RSYVRQTSMF SALWQSVRFV
HATSAIFTLS MRPAPIKRIG DLWRMSSQHD YVKGEEQLTT WTPRGVSLVS DFILSRKKRR
RIAEIGSAQL LLKKIGLPEP RVKPAEEPQE EDIPPQPTFD HDDDDLLNDT PESSQVPEDD
LLNGDDQDSP QQDAETETET ATVQEPEEPK EPEMPEREKY LVERCLKLWN KYPDPLLQIL
SPANTDPPAD GAAPEPAAPM LIPTIIRVPK NPKVLKGGYL LVPNSSSTRW VKRFVELRRP
YLHIHSVTDG DEVAIVSLRN SRVDSQPGVI GLLSGEDDDT SSQANGSVEE FRPSHRRTAS
GRVISSIWTG TGTGGAQTGP NGGLQRLSER LQAGVFAIYG TNNTWLFAGR SERDKMDWIF
RIDQSYFSSS DSANGSGTGS PDRYDDSLIG GY
//
