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Database: UniProt
Entry: A0A168GDI3_MUCCL
LinkDB: A0A168GDI3_MUCCL
Original site: A0A168GDI3_MUCCL 
ID   A0A168GDI3_MUCCL        Unreviewed;       326 AA.
AC   A0A168GDI3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, 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};
DE   Flags: Fragment;
GN   ORFNames=MUCCIDRAFT_131632 {ECO:0000313|EMBL:OAC97579.1};
OS   Mucor lusitanicus CBS 277.49.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=747725 {ECO:0000313|EMBL:OAC97579.1, ECO:0000313|Proteomes:UP000077051};
RN   [1] {ECO:0000313|EMBL:OAC97579.1, ECO:0000313|Proteomes:UP000077051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAC97579.1,
RC   ECO:0000313|Proteomes:UP000077051};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-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:OAC97579.1}.
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DR   EMBL; AMYB01000015; OAC97579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168GDI3; -.
DR   STRING; 747725.A0A168GDI3; -.
DR   VEuPathDB; FungiDB:QYA_131632; -.
DR   OrthoDB; 5489560at2759; -.
DR   Proteomes; UP000077051; 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   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW   ECO:0000256|RuleBase:RU367120};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077051};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU367120}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OAC97579.1"
FT   NON_TER         326
FT                   /evidence="ECO:0000313|EMBL:OAC97579.1"
SQ   SEQUENCE   326 AA;  39046 MW;  BC83A0DCFBA6ECD8 CRC64;
     HGRKREKTTE EVVKARKAKE AVKIKEYNQL VDECREKMKN KEYNQDTFKL TSQLVEWNLD
     YYTIWNYRRI LLQEFVLKEL DAEEQQKVYN KELMLFLQLI KKNPKSYWMW NHRIWCLQHM
     PKPDWQQELG LVDKMLTMDA RNFHGWDYRR FVVGHLRREA GNDPQALAHI VQQEYKFTTQ
     KINQSFSNYS AWHQRSKLLP EIVVSMTTEE KNQVALNELD LVKNAIYTDP EDQSAWLYYW
     WLLGRAPDHV TLLGAYQMES DPECCTVSQW ILSHVCIGAL QTLVHFLTQL AAYEKQDQPS
     IYAEIVDLLD KLCDIDSDRR LRYKDL
//
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