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Database: UniProt
Entry: A0A024G4N3_9STRA
LinkDB: A0A024G4N3_9STRA
Original site: A0A024G4N3_9STRA 
ID   A0A024G4N3_9STRA        Unreviewed;      1080 AA.
AC   A0A024G4N3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN   ORFNames=BN9_025050 {ECO:0000313|EMBL:CCI41721.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI41721.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI41721.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI41721.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-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}.
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:CCI41721.1}.
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DR   EMBL; CAIX01000024; CCI41721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024G4N3; -.
DR   STRING; 65357.A0A024G4N3; -.
DR   InParanoid; A0A024G4N3; -.
DR   OrthoDB; 48065at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
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; 2.60.200.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 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   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT   DOMAIN          35..298
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          684..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          436..494
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1015..1042
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         135..142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1080 AA;  122973 MW;  6D7886597EB81347 CRC64;
     MLFKHFPLGF YYYPSETPQK AFSSDKIGAS AMSVSIKVSV RCRPFTCDDK LGVFLTQSSE
     EQGEVQLINS TYSTTRFPFS YAWWSAYGYH RHVQGNLDQA QAMTLIDQAQ AYHSVGLKIK
     DDLLSGNAVV LFAYGLSGSG KTYTVFGPDA VDTPDAWFRH KTPHAQWGLF PRLAYEVFNE
     KQDGWKISMK YFQNVVDTVR DLMSPVAQEQ QYKAGIKKDS DGFTDIEWCQ SVVLKDWNDL
     RRTFMAANAR KAIAPTQFNH QSTRGHCIMT LEVEKPDPER EGIKQKGRVY VCDLAGTEPA
     GDIVYAEYKK ISFENGDQEY KYLGPHSDPS KSKELQDQGK KINLSLTEMA QFFMKMAEMV
     KANKLKPGIS IPGCNSYFLC KYLKDTMLQA RTYLFCAIRP EVKFHNYTFA TLGFAKNASV
     IKLQPKKACA VSSPAERKLM AELEQMKLLV KELRQENEKI AQVQDVSKIG DAEIQNEKLQ
     MEQLTEMVAQ KRLELENVLL GAATGASTAK NVQDELMQRQ REEYAKRGIH LYHFEADTTS
     PYLLNLDVDA YRSKRFMFLL NQPKVTIGPH GDIKPMSLNI VENHCFFQLE NGEIELHAGA
     GDVIHNGTEL RKNEKRILKQ YDRVAIATDL MLFVHPGKAS IDIEPTADDA AQEYQRALQS
     VDTTAMLELQ EEMKRFQEEK AKWELQKSQP VTHQPDHTST ESNMEKDLLA RQVNDQELRE
     VLPKIMETRQ IVRALNRGML DFETTLQSCT SCSSEQQAQN SMDRSSIPKV KIKVQNNDTE
     EIIFLDVFEF VKAHAMLKDE VAFLRNAIMN EREYASPPGH EPITLFFDHS FQIGSATIFP
     EYLLYNLETD SDDSQLNVKL AIPPFNTIGK LQVVWTPLSS PDSERHEEEH LLDIETPDDL
     LGNSWTYKLQ IQAISGLPLI TESAYCQYEF LGELFTTETV EQHTRNPVFG YEYVHHIESV
     TPNFIDFLQF QRIEFQVFVT PYIMNLPKDV ISTTNSVIVA NLGDREGSME ASVSRADLED
     WCMRLKTELQ DAREDILFLQ KAYQTATGRE APSRYGTTAI SCTPRKQLTS ALATDSQLNS
//
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