GenomeNet

Database: UniProt
Entry: A0A0A8L638_9SACH
LinkDB: A0A0A8L638_9SACH
Original site: A0A0A8L638_9SACH 
ID   A0A0A8L638_9SACH        Unreviewed;       327 AA.
AC   A0A0A8L638;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=KLDO_g1987 {ECO:0000313|EMBL:CDO93695.1};
OS   Kluyveromyces dobzhanskii CBS 2104.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO93695.1, ECO:0000313|Proteomes:UP000031516};
RN   [1] {ECO:0000313|EMBL:CDO93695.1, ECO:0000313|Proteomes:UP000031516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA   Nystedt B., Astrom S.;
RT   "The genome of Kluyveromyces dobzhanskii.";
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}.
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:CDO93695.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CCBQ010000027; CDO93695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8L638; -.
DR   OrthoDB; 5489560at2759; -.
DR   Proteomes; UP000031516; 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; 5.
DR   SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR   PROSITE; PS51147; PFTA; 5.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW   ECO:0000256|RuleBase:RU367120}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU367120}.
FT   COILED          4..31
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   327 AA;  39450 MW;  9EF41691F8C8AACE CRC64;
     MHGIKRKEWT KELLRKKREE ERQKILDYQQ LTNDVLNSKR ERITDKNAFL KTTKLLDINP
     EFNAVWNYRR EIIKTLSLQL DENFWDSELN FTMEKLKVRP KVYWIWNHRL WCLQSYPNSP
     LKIWLKELAI VSKLLEMDSR NFHGWHYRRF IVKTVESLSG RSLNSDEFEY TTKKINQNIS
     NFSAWFQRTT IIESMLSKDQ ISDMDSFINN EFEYIKNAIF TDAEDQSVWT YLIWFIKESA
     MKNIMEPELY SNMVKALIEN IVLINDDELS FSGKDNGWCL KTLIVLESIQ KEYLKEDIQS
     KSQEYLDKLI TIDPLRKNRY LHQLKNL
//
DBGET integrated database retrieval system