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Database: UniProt
Entry: A0A0F8X9F4_9EURO
LinkDB: A0A0F8X9F4_9EURO
Original site: A0A0F8X9F4_9EURO 
ID   A0A0F8X9F4_9EURO        Unreviewed;       359 AA.
AC   A0A0F8X9F4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=ARAM_000959 {ECO:0000313|EMBL:KKK26175.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26175.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK26175.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26175.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) 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}.
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:KKK26175.1}.
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DR   EMBL; JZBS01000568; KKK26175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8X9F4; -.
DR   STRING; 308745.A0A0F8X9F4; -.
DR   OrthoDB; 5489560at2759; -.
DR   Proteomes; UP000034291; 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   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; SSF48439; Protein prenylyltransferase; 1.
DR   PROSITE; PS51147; PFTA; 4.
PE   3: Inferred from homology;
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW   ECO:0000256|RuleBase:RU367120};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU367120}.
SQ   SEQUENCE   359 AA;  42124 MW;  E3E0D5FE82E139A8 CRC64;
     MASHGIPRVS AVERTEEAHM QELQKIEKYR SLEKVVGEKI TAQEYTPETL QKLSELLTKN
     PEYYTVWNYR RQVLQHEFSQ AASEDTNEAA VNRITSLIKT DLQFLIPLLR SFPKCYWIWN
     YRLWLLDQAK RLLPQATARK LWQEELALVG KMLSLDSRNF HGWGYRRFVV ETLETLSSEE
     ENEKSLAQAE FGYAKKMIST NLSNFSAWHY RTKLIQRLLN EKSADDEERK QMLDDELELI
     HRALCDPYDQ SLWFYHQNLM CTFDPETASH TMAPNLSGSE RLGYLQREIE EIQDMLDGAE
     DCKYIYQALI DCSLLAARVE GAIVDGDQQQ QILEWLSELK KLDPLRAGRW LELERSLCR
//
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