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Database: UniProt
Entry: F4NSU5_BATDJ
LinkDB: F4NSU5_BATDJ
Original site: F4NSU5_BATDJ 
ID   F4NSU5_BATDJ            Unreviewed;       227 AA.
AC   F4NSU5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
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};
DE   Flags: Fragment;
GN   ORFNames=BATDEDRAFT_8821 {ECO:0000313|EMBL:EGF83855.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF83855.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF83855.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) 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; GL882879; EGF83855.1; -; Genomic_DNA.
DR   RefSeq; XP_006675050.1; XM_006674987.1.
DR   AlphaFoldDB; F4NSU5; -.
DR   STRING; 684364.F4NSU5; -.
DR   GeneID; 18243067; -.
DR   HOGENOM; CLU_031996_3_1_1; -.
DR   InParanoid; F4NSU5; -.
DR   OMA; TNAMFTD; -.
DR   OrthoDB; 5489560at2759; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
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-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; 4.
PE   3: Inferred from homology;
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW   ECO:0000256|RuleBase:RU367120};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU367120}.
FT   NON_TER         227
FT                   /evidence="ECO:0000313|EMBL:EGF83855.1"
SQ   SEQUENCE   227 AA;  27447 MW;  B5175443E40FD9D4 CRC64;
     RAHSKLDNES LQVTTTLLTQ NPEFYTIWNF RRDILVHMHK EIEPDQVQTD CEIELRLTEQ
     LLQGAPKSYW VWNHRRWTLQ HMPNPSWERE LKLLDYMLDL DARNFHGWDY RRYVVAEIKT
     RKPQQEFEYT LNKINQNFSN YSAWHYRSKL FPWIFIDPKS CNTAISQDLE IVRNAVFTEP
     ADQSAWLYQR WLLGKVSTQM MQSNSVWQEE LSFIEQLSEI EPDSKCK
//
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