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Database: UniProt
Entry: G9NEQ3_HYPAI
LinkDB: G9NEQ3_HYPAI
Original site: G9NEQ3_HYPAI 
ID   G9NEQ3_HYPAI            Unreviewed;       361 AA.
AC   G9NEQ3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=TRIATDRAFT_296919 {ECO:0000313|EMBL:EHK50948.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK50948.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK50948.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(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}.
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:EHK50948.1}.
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DR   EMBL; ABDG02000012; EHK50948.1; -; Genomic_DNA.
DR   RefSeq; XP_013949103.1; XM_014093628.1.
DR   AlphaFoldDB; G9NEQ3; -.
DR   STRING; 452589.G9NEQ3; -.
DR   GeneID; 25780609; -.
DR   eggNOG; KOG0529; Eukaryota.
DR   HOGENOM; CLU_031996_2_0_1; -.
DR   OMA; RKFPKCY; -.
DR   OrthoDB; 5489560at2759; -.
DR   Proteomes; UP000005426; 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; 4.
PE   3: Inferred from homology;
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW   ECO:0000256|RuleBase:RU367120};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU367120}.
FT   REGION          82..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   361 AA;  41825 MW;  6AD8F6E4BCBEB640 CRC64;
     MASHNVARTT RVRTEEQRLQ EIEKINKYRG LEDQIRSQAA LGTYTLQLYD LTTKLLRLNP
     EYYTVWNVRR RCLLSCLLST TTDQPASDTQ DATPGAKNQQ SDGDVLQSEV AFTMPLLMEF
     PKCYWIWNFR QWLLSQAILR LPLPAARKIW ETELGLVSKM LNRDQRNYHA WGYRRYVVAQ
     LESPELDGKS MAEDEFAYTT TMIQANLSNF SAWHNRSLLI PKVLEQRGSD DKARAAFLAE
     ELDLVRDGLN VGPEDQSLWY YHQFLVSQIV GDGNGQSITP ALTVDEKITY LKREIDEITD
     LLEDYDDIKW IYEALLEYNL ALNRLEDKSG GAGNLQTWLT KLRALDPMRM GRWKDVEQQA
     K
//
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