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Database: UniProt
Entry: W1QGL6_OGAPD
LinkDB: W1QGL6_OGAPD
Original site: W1QGL6_OGAPD 
ID   W1QGL6_OGAPD            Unreviewed;       603 AA.
AC   W1QGL6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Kinesin heavy chain {ECO:0000313|EMBL:ESX01217.1};
GN   ORFNames=HPODL_00616 {ECO:0000313|EMBL:ESX01217.1};
OS   Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS   Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=871575 {ECO:0000313|EMBL:ESX01217.1, ECO:0000313|Proteomes:UP000008673};
RN   [1] {ECO:0000313|EMBL:ESX01217.1, ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RX   PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA   Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA   Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA   Skryabin K.G.;
RT   "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT   DL1.";
RL   BMC Genomics 14:837-837(2013).
RN   [2] {ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RA   Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA   Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT   "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL   Submitted (OCT-2013) 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:ESX01217.1}.
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DR   EMBL; AEOI02000005; ESX01217.1; -; Genomic_DNA.
DR   RefSeq; XP_013936051.1; XM_014080576.1.
DR   AlphaFoldDB; W1QGL6; -.
DR   STRING; 871575.W1QGL6; -.
DR   GeneID; 25770087; -.
DR   KEGG; opa:HPODL_00616; -.
DR   eggNOG; KOG0240; Eukaryota.
DR   HOGENOM; CLU_001485_2_1_1; -.
DR   OMA; SHIRVCI; -.
DR   OrthoDB; 5476186at2759; -.
DR   Proteomes; UP000008673; Chromosome III.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; 1.10.287.1490; -; 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   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF33; 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; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {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:UP000008673}.
FT   DOMAIN          39..363
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          389..426
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          478..540
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         121..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   603 AA;  68026 MW;  8804AD436B2E2B85 CRC64;
     MSHKASNARS RSPTKSPSKL QYKLLAPDLG GTEYVNNTNI KVIVRFRPEN EMEKASGATN
     IVEYHPDNQS VSVTVASNTT NFTFDRIFCE DTEQEEIFNY SVKQTTNDLA LGYNGTVLCY
     GQTGSGKSYT MMGDLHDERN KGQTPRIFEQ IFQGIEDSPK TLEYTVGVSY LEIYNENLRD
     LLNPKNNSKL AIHENKVDGV YVSNLETLYV SNLNDVYTIL DQGNKNRSVG STNMNEQSSR
     SHAIFQIRLS SKNLEDGIIK TGNLFLVDLA GSEKIDKTGA SGQLLEEAKK INSSLSALGN
     VINSLTDGKS THIPYRDSKL TRILQESLGG NSRTTLIINC SPSSLNDQET LSTLRFGSRA
     KYIKNSVHIN SELSNHELKK RYFDQAKINE ENVRKIQKLE TRNQELEEEN GQLKEELAKF
     KELMNMKTTS NEVTKLNDTI MMLKSSQLVM TRELEQKNAY IAELESKANE SVESTSKLEA
     LEKAIEHFSD HIEQIEGQNR QLKKDIQALQ QMSNQKTNKI KELEQQLKAQ EMLVEQDTQI
     FEQKLNHLKG RVSSHRSLKQ RTLSGEKENS GSSISSRTRP STKNRIGLNL RIVKPMRGGQ
     QGT
//
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