ID A0A066WZE9_COLSU Unreviewed; 1716 AA.
AC A0A066WZE9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative kinesin motor domain-containing protein {ECO:0000313|EMBL:KDN62258.1};
GN ORFNames=CSUB01_05681 {ECO:0000313|EMBL:KDN62258.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN62258.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN62258.1}.
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DR EMBL; JMSE01001344; KDN62258.1; -; Genomic_DNA.
DR STRING; 1173701.A0A066WZE9; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_20_2_1; -.
DR OMA; RIDKPKR; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
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:SF3; KINESIN FAMILY MEMBER 14-LIKE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT DOMAIN 1..344
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1537..1691
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 605..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1591..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 743..816
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 605..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1716 AA; 190849 MW; 46556661E7AC3DD5 CRC64;
MLTDGIAEID RGSKCIIEMK DNQTILTPPS DAHVKNAKDA GQKVFAFDRS YWSFDRNDSH
YAGQENLFDD LGHPLLENAF AGYNNCIFAY GQTGSGKSYS MMGYGKEFGI IPKICQDMFR
RISALQEDKT LRCTVEVSYL EIYNERVRDL LNPSTKGNLK VREHPSTGPY VEDLAKLVVG
SFQEIEHLMD EGNKARTVAA TNMNETSSRS HAVFTLMLTQ KKFDPETKME MEKVAKISLV
DLAGSERATS TGATGARLKE GAEINRSLSS LGRVISALAD ISTGKKKKGP GGQVPYRDSV
LTWLLKDSLG GNSMTAMIAA ISPADINYDE TLSTLRYADS AKRIKNHAVV NEDANARMIR
ELKEELALLR NQLGGGVTSG ATGGAAGGVG TSEEVYPEGT PLEKQFVTIT SSDGAVKKVS
KAEIAEQLNQ SEKLLTDLNQ TWEQKLAKTE EIHKEREAAL EELGISIEKG FIGLSTPKKM
PHLVNLSDDP LLAECLVYNL KPGLTTVGNM DTNADNQANI RLNGTRILHD HCAFENGPDG
TVMVIPKEGA SVMVNGKRIE EPKQLHSGYR VILGDFHIFR FNHPMEAQKE RADKSLLRQS
VTASQLQNLE KSTSTPAVSP RPGHERNWSR AGSDFGDSRP DSPIPFRPGR DNDWSFARRE
AAEAILGPNQ NLASLTDEEL NALFEGIQRA RAERVNGREG DDDSESVTSY PIREKYMSTG
TLDNFSLDTA LTMPSTPKQG EVDDKLREVR EEMQSQLDRQ KEEYQDQLKT AEAANVEVEE
IKKEKVRMQE TLQALKKDMQ QQLEVQRRQF EEKIEKMDPL KRPKANPKLS DEEVEIAKRV
IKHWRTRRFV RMAEAVLQHA STLKEAQIMS NELDEGVVFQ FTVVDLGHSL CSTYDMVLNG
LTGEGDDIAL DEAQKPCIGV RVVDYKNSVV HLWSLEKLHD RVRQMRQMHQ YLDQPEYAQH
LSLDNPFIET CMPQYTLVGE VDVPLKAVFE SRVQDFALDV LSPHTSHAIG MIKLSLEPSH
ARAPSNTLKF NVVMHEMVGF AEREGTEVHA QLFIPGVSEE DGITTTQMVK DFDEGPIRFE
SVHSMSVPLF SPQNVTLRAA IFAKVSAMHL DKLLSWDDMR DAVPVSQGKP KGARIAESQF
YTEEKHDLLA RLQILELNEE GEYAPVEVAQ TSEMDGGTFQ LHQGLQRRIA INITHSSGDA
LPWDDAMNLR VGRIQLLDQA GKSPDMTSTS PTITLKLANK PAFRDNVNGT RSITLTGQWD
SSLHSSLLLD RVTADKYRVQ MTVAWEISSS KFAEPMKFAM RVCCQIMSRS WVRQTSMFSS
LWQSVRFVHA TSGIFTLSMR PAPIKRIGDL WRMSSQHDYV KGEEQLTTWT PRGVSLVSDF
ILARKKRSRI AEIGAAQTLI KKIGPPQPRV LPAEEETLEE DLPPQPTYHN DDDELLNDTP
ESSQVPEDEE LVHGDSQDTP QPEGETEAAQ TTQEPEIPQR EKQILEKCIN LWHKYPDPLL
RILSPSNTDP PADGSVPEAS APPSLIPTII RVPKNPKVLK GGYLLIPNSS STRWVKRFVE
LRRPYLHIHS VTDGDEVAIV SLRNSRVDSQ PGVIGLLSGD DDDGGSQTNG GSEEFRPSHR
RTASGRVIST IWTGTGHGGA ANGASGGLQK LSERLQAGVF AIYGTDNTWL FAARSERDKM
DWIFRIDQSY FSGSDSTTGS GAGSPDRYDD SLIGGY
//
