ID A0A1W5D244_9LECA Unreviewed; 588 AA.
AC A0A1W5D244;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM37204.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) 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; FWEW01001429; SLM37204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5D244; -.
DR OrthoDB; 5489560at2759; -.
DR Proteomes; UP000192927; 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; 3.10.290.30; MM3350-like; 1.
DR Gene3D; 1.25.40.120; Protein prenylyltransferase; 1.
DR InterPro; IPR024047; MM3350-like_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; 5.
DR SUPFAM; SSF159941; MM3350-like; 1.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR PROSITE; PS51147; PFTA; 5.
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, ECO:0000313|EMBL:SLM37204.1}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 67450 MW; 672512AA7987B641 CRC64;
MTSHGIPRPG ASEPRTEQGR KRELQKIEEY QNLVNQVNKA IRERQYTNEV LRLTSKLLTL
NPEYYTIWNH RRIILQYYFR EQRDVKRGQD GGASTVPSGH NTIIDIISDD LQFLVPLLRK
FPKCYWIWKY RLWLLEQSTT LLPIPSARQL WQEELGLVGK MLSLDSRNFL GWGYRRTVVA
ALESDSLNTG EDNNSMVEQE FRYTTKMIET NLSNFSAWHS RSKLIPRLLD ERAADETTRQ
GFLDDELVLI QEALYTDPYD QSLWFYHHYL MCTFDPHSCQ NTMASRLTPD QRLEYIIREI
DKTMEMLDGA EDCKWIYQAL IQLSTMYKAS SGAWPGQAAG MGDWVSELRK LDPLRAGRWT
DLDRELRSED LASSLTIAES NRQGHYGLPI STARQRKLHS NMTLESSTSI YLMNYLVQVT
VVRTSNPAVT RLLLIPATAT FEALHLAIEA AFGWKGQDYD PGNYNFKVIE ENTLTENVLL
GISGYDSEDR GYHSIGYAPN VYLYQVFDNF ELRGQGLQYV SDGGLGGPIH TVQILGHNAS
TTIGEAVCLG GQGHTFLRLW LTAQESKKPV LSTWALDLNR VNERMAEL
//
