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Database: UniProt
Entry: A0A0G4F1D2_VITBC
LinkDB: A0A0G4F1D2_VITBC
Original site: A0A0G4F1D2_VITBC 
ID   A0A0G4F1D2_VITBC        Unreviewed;       854 AA.
AC   A0A0G4F1D2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=Vbra_14156 {ECO:0000313|EMBL:CEM05190.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM05190.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM05190.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) 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       ECO:0000256|RuleBase:RU000394}.
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DR   EMBL; CDMY01000356; CEM05190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4F1D2; -.
DR   STRING; 1169540.A0A0G4F1D2; -.
DR   VEuPathDB; CryptoDB:Vbra_14156; -.
DR   InParanoid; A0A0G4F1D2; -.
DR   OMA; ETIPYEN; -.
DR   OrthoDB; 5481713at2759; -.
DR   PhylomeDB; A0A0G4F1D2; -.
DR   Proteomes; UP000041254; 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   CDD; cd01369; KISc_KHC_KIF5; 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:SF17; 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   ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000041254}.
FT   DOMAIN          5..332
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          392..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          337..371
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          602..669
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          709..750
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        402..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..821
FT                   /note="Basic and acidic 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   854 AA;  93846 MW;  D907B677F18C93BE CRC64;
     MSAENVKVVC RVRPLNDKEK GEGGIICVKV PEEKTIQLLD GGKKSAGDDR TFVFDRTFDW
     NCTQRQVYDF AARPIIESVL RGFNGTVLAY GQTSSGKTHT MQGVIEDQEQ RGIIPRMVNT
     IFEGVDAADE HIEFTVKVAI LEIYMEKIRD LLDPSKDNLK VHEDKVHGIY VGDITEEYVT
     CEQDVFDIMR IGQENRSVAA TNMNAHSSRS HLVFILSISQ RNLHDLSVKV GKLYLVDLAG
     SEKVAKTGAA GSTLDEAKMI NKSLSALGNV INALTDPKTS HVPYRDSKLT RILQESLGGN
     SKTCLIITAS PSSYNEAETL STLRFGWRAK QIKNVAKVNQ ERSVEELKML LEKAERTIEE
     QKGRIRLLEE TLRTNGITVP GGISKAPAAE AAAAASGMHH SKSEKTFSKP PKPEEEADEE
     SEFLQLMEEL YQKKAELKEQ SEAITELNRH VQSVNEQQKT VEAENQILVN RIADLSVTCE
     QLQYERQEQL DTIQQLEASR KAVESELKVL QDSQKNLLAQ ISEKDKEIDS MAKAGAVPTI
     PEDRVADMPK VAAAGSSEIA KIREQLLGQE GASASEELAG STDAAAAGGE LSKQMHELQK
     FKLSALAQME QLKKQNDDLR KGVYGKGDGA WAKEREAMLA DMQREQEQVA DLKVMLLEER
     KKAEDLKEML KDGERPLRRK VSQLDRNLEQ LTIMYHKLVS QNSGLKVECQ VNDKKIQRKE
     QRIAQLERNL KEAKAKYEKL LQQCANLTNT VEHMYRTGTI AGMAGMGAGG AAAAGAGSSA
     GGGAIAPGSA RRANIARPLK GGSHRVRRPT QAREMGEGGE GDESPFRGGI TTITEEGDAD
     GGDAADPEKR GAGA
//
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