ID A0A093X8U6_9PEZI Unreviewed; 399 AA.
AC A0A093X8U6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=V490_07226 {ECO:0000313|EMBL:KFX89115.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX89115.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX89115.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX89115.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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:KFX89115.1}.
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DR EMBL; JPJS01002165; KFX89115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093X8U6; -.
DR STRING; 1437433.A0A093X8U6; -.
DR HOGENOM; CLU_031996_2_0_1; -.
DR Proteomes; UP000029320; 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; 3.
PE 3: Inferred from homology;
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW ECO:0000256|RuleBase:RU367120};
KW Reference proteome {ECO:0000313|Proteomes:UP000029320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU367120}.
FT REGION 81..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 46328 MW; 239D2ACBBEF04279 CRC64;
MTSHGVPRIA AATVRTEQQR QDEIDKIQKY QALVDLIETK VQERQYTPEV LALTSKLLTK
NPEYYTIWNV RRRLLISGLF SKSPDGQSPS TQQPSTSQAK TTNSPYEKSP SSTSTSNADS
SATPQSPPPQ NPGSNGTTLE LIKDDLTFLV PLLKQWPKCY WIWNHRIWLL QQATLRLDVP
VARRLWEEEL GLCNYMLVRD SRNFHGWGYR RMVVEKLESP SLNGKSLVEA EFAYTTKMVN
ANLSNFSAWH NRSQLIPRLL DERNASDEAR KEFLDEEFDT MRNALWTDAS DQSLWFYHQF
LMVTLLDRTA SILPNFTTEQ RVDYANSQID DLKEMLDGAE DRKWICNGLY EYTLAICRTC
ERKPTAEELQ DLKLWLDELK KLDPVRKGRW EEQEKSLDH
//