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Database: UniProt
Entry: A0A1I8B980_MELHA
LinkDB: A0A1I8B980_MELHA
Original site: A0A1I8B980_MELHA 
ID   A0A1I8B980_MELHA        Unreviewed;       502 AA.
AC   A0A1I8B980;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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};
OS   Meloidogyne hapla (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig1606.frz3.gene5};
RN   [1] {ECO:0000313|WBParaSite:MhA1_Contig1606.frz3.gene5}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   AlphaFoldDB; A0A1I8B980; -.
DR   WBParaSite; MhA1_Contig1606.frz3.gene5; MhA1_Contig1606.frz3.gene5; MhA1_Contig1606.frz3.gene5.
DR   OMA; VIELAMN; -.
DR   Proteomes; UP000095281; Unplaced.
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; 2.
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; 3.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU367120}.
SQ   SEQUENCE   502 AA;  58225 MW;  F5954B050F479DA5 CRC64;
     MMHFVKKSQV SEGEKTAYEK KRAAKLERFV QMKERIFEKR KIGEYDEEIM ELTAELLGKH
     ADIYTFWNIR REAIERICVK LEGESEKENI ERKSKLLDKE LKLTQECLMK NPKSYSSWHH
     RFLVVSQRPK INFQEELALC DNALALDCRN FHCWGKFFSD RLIGKNPSNY SAWHYRGTLL
     PRLEENRKEI SEGRLLTDEC LKGEFEKVLH VCGVNSEDQT AWTYCRWLVE LATNGLPNSP
     QIVAARFLDS TTVLVVFSEA VNKQVVKNSF NLFDYSKIMK FESFSPFKTS DFVSEFKYSH
     VWLLSNVSSP LLICPLNQEG KDEAEIKQIE IDKIFVDGFY FQKNFTSSAI NVRELPRKCL
     DDLIKLCNDL IPVEDNPWAL AALTRAMFYL KGINKQTFEL AKDNCEKLKK IDFQRSEMYE
     ELMDKYRLIK SLNEESSPAG GTLLSKLIEG NRQLNLKEIG LKSLDNIPLL SAFVSTDNLI
     NDNLMALKNL TLDGNPTKEE SK
//
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