ID A0A150GID9_GONPE Unreviewed; 972 AA.
AC A0A150GID9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=phytol kinase {ECO:0000256|ARBA:ARBA00039024};
DE EC=2.7.1.182 {ECO:0000256|ARBA:ARBA00039024};
GN ORFNames=GPECTOR_20g438 {ECO:0000313|EMBL:KXZ49582.1};
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:KXZ49582.1, 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:KXZ49582.1}.
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DR EMBL; LSYV01000021; KXZ49582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GID9; -.
DR OrthoDB; 5491403at2759; -.
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 Gene3D; 6.10.140.2220; -; 1.
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.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR PROSITE; PS50865; ZF_MYND_2; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 919..964
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 101300 MW; C08DAD92D4C865A8 CRC64;
MSSRRARTGG NGSSRSPANP DPLPPIVRDA LQRLPRAIEP LFSSRAQLEQ DVGGLGSPLA
RLRTAELRSI QQHVSVVRNF LSSAAGGAPS ASAAVLAHAT TRQALLCLLA ASLRLRRHDL
SGEGGSRQEL CAEIAEGVAV TVTFAMPSCP PPDHPGRGLR LPLLRSDALH AAARQLAELV
EPLEARAAAA VAGTAGTPPA GAGSPAPVVA GQGAMGRKTA VEECPTLTEP AAAYAAAVLS
LVYRIVIVAS DFDFEFKAPG GVQLLEALAA ALEGSQVLEH AGRALLLLRM HVRATRLSNQ
LDQAALWANT THCVLWQFIS LLHIQADEQG GSASADMRQL ADRLQAVLSG RCAQHAALCL
GLAVLCDTDG GPAYGLPPEL DAPLLPSEVR AYASGSRVMS AEAIRQLRGM LGMLQLRLRP
GVGAAAPPPG RRGALEVTMR VGWLAVASAR ALAAKTGGGG GGGGAGSSGE AGGSGGAVSV
DAKLAAQDVL PVALEALQCA RRHLLLGTRP EAEGAVAEAT RWWRLTAAVA ADVLPHARFA
PELTDFFDLL TVCWRDLLFG DGSLSLPPKA PPALAAALEG GVLRCLEGLI RCAGREPPRP
EASDIARAWV GLGTNMPLFL TLLLAYGEPR QAAALVGTLR KLLRIVGPPY GTMPAFMMRA
CDYVLDVVSN WDAAELMAAG MADQEGREGP SPASQQLVRL TFCAACEWLP RLSQMVLANR
TSGLTTLCTI CGWLPVLADC CDRAATVSDD GGWRALLLEE VGAVPLLDFA LHVVPRLDEL
DEQELVLVFL CQLVLGCCSV AAVYTGQGPT PAHAAVGAPE QSELEPLAAA AAGAVAEPFR
DAVGALPWRP ELLREAAARI RAYEPPELEL HEDADDLAAY LERGGRGAYD SPVDYASPLT
SVLLPPADVR RLLPGRCANP ACANLEGDSE ADLRLKACAG CGAVGYCCRP CQTAHWRAGH
KKACGRGRGG GA
//
