ID Q7RLT7_PLAYO Unreviewed; 706 AA.
AC Q7RLT7;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit alpha {ECO:0000256|RuleBase:RU367120};
DE EC=2.5.1.60 {ECO:0000256|RuleBase:RU367120};
DE AltName: Full=Geranylgeranyl transferase type II subunit alpha {ECO:0000256|RuleBase:RU367120};
GN ORFNames=PY02453 {ECO:0000313|EMBL:EAA21899.1};
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA21899.1, ECO:0000313|Proteomes:UP000008553};
RN [1] {ECO:0000313|EMBL:EAA21899.1, ECO:0000313|Proteomes:UP000008553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL {ECO:0000313|EMBL:EAA21899.1,
RC ECO:0000313|Proteomes:UP000008553};
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E.,
RA Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B.,
RA van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to cysteines occuring in specific C-
CC terminal amino acid sequences. {ECO:0000256|RuleBase:RU367120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC ChEBI:CHEBI:86021; EC=2.5.1.60;
CC Evidence={ECO:0000256|ARBA:ARBA00001577,
CC ECO:0000256|RuleBase:RU367120};
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000256|ARBA:ARBA00006734, ECO:0000256|RuleBase:RU367120}.
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:EAA21899.1}.
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DR EMBL; AABL01000673; EAA21899.1; -; Genomic_DNA.
DR STRING; 73239.Q7RLT7; -.
DR PaxDb; 73239-Q7RLT7; -.
DR EnsemblProtists; EAA21899; EAA21899; EAA21899.
DR InParanoid; Q7RLT7; -.
DR OMA; WEFYRWF; -.
DR Proteomes; UP000008553; Unassembled WGS sequence.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0097354; P:prenylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.40.120; Protein prenylyltransferase; 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002088; Prenyl_trans_a.
DR PANTHER; PTHR11129:SF2; GERANYLGERANYL TRANSFERASE TYPE-2 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1.
DR Pfam; PF01239; PPTA; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS51147; PFTA; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW ECO:0000256|RuleBase:RU367120};
KW Reference proteome {ECO:0000313|Proteomes:UP000008553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU367120}.
FT COILED 119..150
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 706 AA; 85368 MW; DEB1C526EC666DC3 CRC64;
MHGRKANNYK EEYGKLEKVK ELIPVVNDLI IKKKTSKYEK KYIQMSSTIL RKCPYIQTLW
NYRKEYFEFI KDEYLNRNEK IHNDPKVTLI THLAIDVIRL FVYIYQYIYF YFFPFHKAGD
IEEKKSEEFK NELKEMMENE NSMIEDILVK FSKCNELWFH KLWIIKYCIK NDLINLEHLL
NELEYCKKSL YIDDRNYHCW NYRSYIISCI NIYKKKTNEN LPTNMGSVEI NEDDKNKHVE
QNVNNFNVQT SNCELSKLLI ERNFSNFSAW FLKYSLKEEL ININEELELI KNAIFTDPSD
QSLWEYYRWF LFKKGKYEEE IFFITLENNS LYIFFQNIVK INTDKSKCYD SQNEEICGEW
DRQFIINNSG NKNLESYIYI FKVNENINLS NFSYLKLSIC YYKYNIHTPQ NINYEENVLQ
DLLIGYDHLI PNEKNQYNII YEINFXNFSK NSHFKLLLNY SKENNKEDQT LCKNNCVKPY
TNLYKYINDT NIRLNLAKNV NFHLLNFELE QINELLCLES DCKYALFTKY EILKKLERFD
ELFEVIDKLK EIDNIRIEYY NDKESELRIQ QKVYDYYRSS KIEDNDEILD LSGLNIENII
YPSLIEAFYI QKINLSNNIL FESWSGKCTI NFLYNLKELH LCNNKIKQLS TLMKNLYNLK
LLEMLDVSNN ELVKLDEELD KYEFDTPPLL NNLHVTFKGV EVVLLK
//
