ID   PGTA2_ARATH             Reviewed;         687 AA.
AC   Q9FJ32;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Geranylgeranyl transferase type-2 subunit alpha 2 {ECO:0000305};
DE            EC=2.5.1.60 {ECO:0000305};
DE   AltName: Full=Geranylgeranyl transferase type II subunit alpha 2 {ECO:0000305};
DE   AltName: Full=Rab geranylgeranyl transferase alpha subunit 2 {ECO:0000303|PubMed:26589801};
DE            Short=AtRGTA2 {ECO:0000303|PubMed:26589801};
DE            Short=Rab-GGT alpha 2 {ECO:0000305};
GN   Name=RGTA2 {ECO:0000303|PubMed:26589801};
GN   OrderedLocusNames=At5g41820 {ECO:0000312|Araport:AT5G41820};
GN   ORFNames=K16L22.10 {ECO:0000312|EMBL:BAB10657.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=26589801; DOI=10.1074/jbc.m115.673491;
RA   Shi W., Zeng Q., Kunkel B.N., Running M.P.;
RT   "Arabidopsis Rab geranylgeranyltransferases demonstrate redundancy and
RT   broad substrate specificity in vitro.";
RL   J. Biol. Chem. 291:1398-1410(2016).
CC   -!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from
CC       geranylgeranyl diphosphate to both cysteines of Rab proteins with the
CC       C-terminal sequence -CCXX, CXXX, -XCCX and -XCXC, such as RABA1A,
CC       RABA2A, RABF2A and RABG2 (By similarity). Does not seem to be a
CC       functional Rab-GGT alpha subunit in vitro (PubMed:26589801).
CC       {ECO:0000250|UniProtKB:Q8VYB7, ECO:0000269|PubMed:26589801}.
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:0000250|UniProtKB:Q8VYB7};
CC   -!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of the Rab
CC       escort protein REP. {ECO:0000250|UniProtKB:Q8VYB7}.
CC   -!- SUBUNIT: Heterotrimer composed of the alpha subunit RGTA, the beta
CC       subunit RGTB and REP; within this trimer, RGTA and RGTB form the
CC       catalytic component, while REP mediates peptide substrate binding.
CC       {ECO:0000250|UniProtKB:Q8VYB7}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC       family. {ECO:0000305}.
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DR   EMBL; AB016871; BAB10657.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94733.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70211.1; -; Genomic_DNA.
DR   RefSeq; NP_001331841.1; NM_001344422.1.
DR   RefSeq; NP_198997.1; NM_123547.2.
DR   AlphaFoldDB; Q9FJ32; -.
DR   SMR; Q9FJ32; -.
DR   STRING; 3702.AT5G41820.1; -.
DR   iPTMnet; Q9FJ32; -.
DR   PaxDb; Q9FJ32; -.
DR   PRIDE; Q9FJ32; -.
DR   ProteomicsDB; 236723; -.
DR   EnsemblPlants; AT5G41820.1; AT5G41820.1; AT5G41820.
DR   EnsemblPlants; AT5G41820.2; AT5G41820.2; AT5G41820.
DR   GeneID; 834187; -.
DR   Gramene; AT5G41820.1; AT5G41820.1; AT5G41820.
DR   Gramene; AT5G41820.2; AT5G41820.2; AT5G41820.
DR   KEGG; ath:AT5G41820; -.
DR   Araport; AT5G41820; -.
DR   TAIR; locus:2153015; AT5G41820.
DR   eggNOG; KOG0529; Eukaryota.
DR   HOGENOM; CLU_024090_0_0_1; -.
DR   InParanoid; Q9FJ32; -.
DR   OMA; AWHYRSV; -.
DR   OrthoDB; 1527547at2759; -.
DR   PhylomeDB; Q9FJ32; -.
DR   BRENDA; 2.5.1.60; 399.
DR   PRO; PR:Q9FJ32; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJ32; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IBA:GO_Central.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018344; P:protein geranylgeranylation; IBA:GO_Central.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002088; Prenyl_trans_a.
DR   Pfam; PF01239; PPTA; 2.
DR   PROSITE; PS51450; LRR; 3.
DR   PROSITE; PS51147; PFTA; 5.
PE   3: Inferred from homology;
KW   Leucine-rich repeat; Prenyltransferase; Reference proteome; Repeat;
KW   Transferase.
FT   CHAIN           1..687
FT                   /note="Geranylgeranyl transferase type-2 subunit alpha 2"
FT                   /id="PRO_0000436610"
FT   REPEAT          38..72
FT                   /note="PFTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT   REPEAT          83..117
FT                   /note="PFTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT   REPEAT          132..167
FT                   /note="PFTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT   REPEAT          168..203
FT                   /note="PFTA 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT   REPEAT          214..248
FT                   /note="PFTA 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT   REPEAT          523..545
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          546..567
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          568..591
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          592..616
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          646..668
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   687 AA;  79141 MW;  89A26D1D4CF5F9F9 CRC64;
     MHGRKREEDP NPEETAAKAL ELRSLQSQFM SNHHQKIYTK EAIQLSAKLL ITNPEFYTAW
     NYPKLAFESR LDEDSDPSLV NSIIDEELGV VQNALERNVK SYGAWYHRKW VLSKKGHYYP
     SLENELQLLN DYQKQAHQKQ DDEKQDDPSR NFHAWNYRRF VVELTKTSEE DELQYTTDMI
     SDISFTIYSA WHYRSVLVSS LVAKKADGFM PKETIRRELD YVHSAIFTLE EKQSGWFYYL
     WLLDQTVKME IPLRFSSWPS DGSIIILSGP DCFNASSSTT KLTTFCSESG SFPLILYFDQ
     AVSGVSSSTV TIGSELKDLV WEPVSDKKNS QVDSCVWVAR LKFDCREPCF SRKETKVKVS
     LGGIVSSMGC NLTAPYEFVF TLRIHDTVEV ELSQQESIVS WTDGFDNWDD NALSNDLNSL
     TALNADTGFE WRKKAIKIEI ELFRTLPDSK IGKLILARLL MAEETMISNG VHYKEILQLY
     NDLMALDSWH NQYYKDEHSV ALIHKVTSRT ESMSRHLFRY RNMNNIICLR LNNLTLSRIA
     AVEKLLFVQM LDLSHNELHS AEGLEAMQLL CCLNLSHNRI RSFSALDSLR HLKQLRVLDV
     SHNHICGELP VDTTRYLCSS PLSNSGETGR EVPNKYQDAY LVLRDLMKLK QLDIRGNDLI
     FAGEEFSSFV RQVVPKLVWL DGHKLTS