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Database: UniProt
Entry: A0A150GLF1_GONPE
LinkDB: A0A150GLF1_GONPE
Original site: A0A150GLF1_GONPE 
ID   A0A150GLF1_GONPE        Unreviewed;       787 AA.
AC   A0A150GLF1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=phytol kinase {ECO:0000256|ARBA:ARBA00039024};
DE            EC=2.7.1.182 {ECO:0000256|ARBA:ARBA00039024};
GN   ORFNames=GPECTOR_16g740 {ECO:0000313|EMBL:KXZ50565.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ50565.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + phytol = CDP + H(+) + phytyl phosphate;
CC         Xref=Rhea:RHEA:38055, ChEBI:CHEBI:15378, ChEBI:CHEBI:17327,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:58069, ChEBI:CHEBI:75483;
CC         EC=2.7.1.182; Evidence={ECO:0000256|ARBA:ARBA00036143};
CC   -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00024015}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid,
CC       chloroplast membrane {ECO:0000256|ARBA:ARBA00004508}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004508}.
CC   -!- SIMILARITY: Belongs to the polyprenol kinase family.
CC       {ECO:0000256|ARBA:ARBA00010794}.
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:KXZ50565.1}.
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DR   EMBL; LSYV01000017; KXZ50565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150GLF1; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR039606; Phytol/farnesol_kinase.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR32523; PHYTOL KINASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32523:SF8; PHYTOL KINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01753; zf-MYND; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          760..785
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|Pfam:PF01753"
FT   REGION          233..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   787 AA;  81047 MW;  4C031F84782F82EF CRC64;
     MQMALFVTGC AVHIQQAHAT ATALECYGGD TLGDSRAVAA AAQRVRDRSQ LLYQLLVSEL
     YGSQALEHSI RLLQLLTTLA AANTAGSSEH LSNQEAVDSR VLYVRSITTE MLSFLGGAYI
     RSAAAPMLAV PRTTDSRPDV PPPPWGPCAQ YLALANAVSA LAEAGFGGGD GEGGGMYGLP
     PELAAAMGLR RSQELRVGSG GSGSSSLLGR RPELLFETLL ALLEVQLDCG PGGNGSGEHG
     RNIDGGGVGV TATTSGGSGG GASGSTGLWS FIISPRAAHR LCMRITDLAI ASGQEAAGTA
     AAVGQRQQQA DTLCHLLPAG WAWHVAVRAL AVARGLLLGP MRRAGVADPE LVPQSLGSEP
     LLPVEYWRAV GRVLRMDAQL REANGRLHVT HVPLFPRLSC MLEIPDMCMA DSLASAEPSA
     SVAAALSSGL VAGLERCSRF FGRSEDPDDV GALYDNLLPA LVTQPSFFPH LLAFGPPGEV
     ASFLTTLAKL LHRCVDEAEE AADKAQPAAA GAGQPSLQWP GSASRGAMDG GREAVGHICK
     NMASLASNLT TVAVSVFCDP RVFPALALEG PATVRPQLRQ LLSLIVQRYL PPLARAVLLA
     PRLPRSYVEG LDLFDIALGS MDFGAMVLFN ATDPTRLPPL AAATASTTDS AASSTAAAAT
     PASESASAVS AAARAATVAT TVSGGPEARA AARAESWRSW LRGDGCGERL LQELRQRGAA
     LLPPAEAGAG LPLACANPRC INLACDSEAE LMAAAGGGGQ HCGGCGSARY CSAECQRTQG
     RAGHSAE
//
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