ID D7MIR1_ARALL Unreviewed; 675 AA.
AC D7MIR1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=ARALYDRAFT_493802 {ECO:0000313|EMBL:EFH46871.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348719; EFH46871.1; -; Genomic_DNA.
DR RefSeq; XP_002870612.1; XM_002870566.1.
DR AlphaFoldDB; D7MIR1; -.
DR STRING; 81972.D7MIR1; -.
DR EnsemblPlants; fgenesh2_kg.7__3235__AT5G41820.1; fgenesh2_kg.7__3235__AT5G41820.1; fgenesh2_kg.7__3235__AT5G41820.1.
DR GeneID; 9304649; -.
DR Gramene; fgenesh2_kg.7__3235__AT5G41820.1; fgenesh2_kg.7__3235__AT5G41820.1; fgenesh2_kg.7__3235__AT5G41820.1.
DR KEGG; aly:9304649; -.
DR eggNOG; KOG0529; Eukaryota.
DR HOGENOM; CLU_024090_0_0_1; -.
DR OrthoDB; 5489560at2759; -.
DR Proteomes; UP000008694; 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; 1.
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; 4.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS51147; PFTA; 3.
PE 3: Inferred from homology;
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW ECO:0000256|RuleBase:RU367120};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU367120}.
SQ SEQUENCE 675 AA; 77647 MW; A526FFD74238EED6 CRC64;
MHGRERNEAS KPEETAAKAL ELRSLQSQFM SNHHQKIYTQ EAIQLSAKLL GINPEAYTAW
NYRKLALESR IDEDSDPSLV DSIIDEELRV VQNALKRNPK SYGAWYHRKW VLSKKGHYYS
SLEKELQLLN DYQKQCLVND YQKQDDPKKQ DNARNFHAWN YRRFVVELTE TSEEDELQYT
NMINDICFSI YSAWHYRSVL VSSLVAKNAD GFMPKETIRR ELDYVHNAIF TDELGQSGWF
YYLWLLDQTL KMETPLRFSS WPSDGSIITT FCSESGSFPL ILYFDQAVSG VSSSTVTIDS
ELKANEDLVW EPVSDNKNSQ VDSCVWVAHL KFDSRGPCFS RKENKVKVSL GGIVSSMGCN
LSTPYEFVFT VLHTVGESSQ QGIVSWTDGF NNWDDAQSKD LNSFIALNAD AGFEWRKEAI
KIEIDHLRNL PDSKFGKLIL ARLLMAEETM ISDDAVKGFH YTEILQLYND LIALDSWHAQ
YYKDEHSVAL LHKVTSSTES MFRHLFRYRN MNNIVCLRLN NLTLSRIAAV EKLLFVQMLD
LSNNELHSAE GLEAMQLLCC LNLSHNRIMS FSALDSLRHL KQLRVLDVSH NLIGGEHPVD
TTRYLCSSPL SNSGEVGREV PCKYWDAYLV LRDLMKLKQL DIRGNDLIFS GEEFSSFVRQ
VVPKLVWLDG HKLTN
//
