ID A0A0D9QL01_PLAFR Unreviewed; 699 AA.
AC A0A0D9QL01;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=AK88_02625 {ECO:0000313|EMBL:KJP87730.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP87730.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP87730.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KQ001670; KJP87730.1; -; Genomic_DNA.
DR RefSeq; XP_012335673.1; XM_012480250.1.
DR AlphaFoldDB; A0A0D9QL01; -.
DR EnsemblProtists; KJP87730; KJP87730; AK88_02625.
DR GeneID; 24267939; -.
DR VEuPathDB; PlasmoDB:AK88_02625; -.
DR OMA; WEFYRWF; -.
DR OrthoDB; 5489560at2759; -.
DR Proteomes; UP000054561; 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; 2.
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; SSF52075; Outer arm dynein light chain 1; 1.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS51147; PFTA; 2.
PE 3: Inferred from homology;
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW ECO:0000256|RuleBase:RU367120}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU367120}.
FT REGION 190..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 82462 MW; 46E6CCE9D9627BD2 CRC64;
MHGRKSSNSK EDKAKLEKVK ELVHLGNNLI KKKNEKTYDK KYIESTSVIL RKCPYLETLW
NFRKEYFEFV QNVGTPVGDV GKGDEEADCA KHPPSEDLKT LMKNENTMVE EIVSKFNKCN
ELWFHKLWII KFCLKNDLMD FSDLMNELEF CKSALYRDDR NYHCWNYRSY IIACVHIYLK
SGKHGKAQNG EAQIAKGSSD ERDPASTQHG NQFDVHKSNY ELSKTLIERN FSNFSAWFLK
YTIHESLIST ENELDLIKNA IFTDPFDQSL WEFYRWFLFQ KGNDKEEIFF TLLQNNCVYF
FFQNLVMANL SKSKCYDENG KEITGEWGQH FVPPNNPQDS FESYVYFFKI TDKHILLSDQ
PTCLKFCIFY YKYNLYEPEE VHYEKNVLSD LMVCHDFLRE ENKYEHNIVY LIDFRKFSQN
EHFKILLDYD TLSRGDAKMD SKSSCLNTFT PLYKYINRSN ILLNTAKHIN FASLNLELEN
INELLLLERN CKFALFTKLE ILRRLEQFDE LFHLLELLKL VDSIRVEYYK DLETELRIQK
KIHEYYEDSE MGDKGALDLS GLNIDSITYP FMIEAFFIPS INLSSNLISE SYNGKCTINF
LYNLKELNLN HNKIKSLVVL MKNLYNLKLL EKLDVSSNAL ANLDEDLDNY SFVLLPNLKQ
INISDSNLSA LLNQRYKHKS VLNTYNVMQD GWRVILSKG
//
