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Database: UniProt
Entry: A0A087YFP4_POEFO
LinkDB: A0A087YFP4_POEFO
Original site: A0A087YFP4_POEFO 
ID   A0A087YFP4_POEFO        Unreviewed;       585 AA.
AC   A0A087YFP4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Geranylgeranyl transferase type-2 subunit alpha {ECO:0000256|ARBA:ARBA00014772, ECO:0000256|RuleBase:RU367120};
DE            EC=2.5.1.60 {ECO:0000256|ARBA:ARBA00012656, ECO:0000256|RuleBase:RU367120};
DE   AltName: Full=Geranylgeranyl transferase type II subunit alpha {ECO:0000256|RuleBase:RU367120};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016847.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000016847.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   -!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from
CC       geranylgeranyl diphosphate to both cysteines of Rab proteins with the
CC       C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A
CC       and RAB7A. {ECO:0000256|ARBA:ARBA00002902}.
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; AYCK01004053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007550708.1; XM_007550646.2.
DR   AlphaFoldDB; A0A087YFP4; -.
DR   STRING; 48698.ENSPFOP00000016847; -.
DR   Ensembl; ENSPFOT00000016869.2; ENSPFOP00000016847.2; ENSPFOG00000016750.2.
DR   GeneID; 103137094; -.
DR   CTD; 5875; -.
DR   eggNOG; KOG0529; Eukaryota.
DR   GeneTree; ENSGT00550000075121; -.
DR   OMA; PKSYNAW; -.
DR   OrthoDB; 5489560at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0097354; P:prenylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.120; Protein prenylyltransferase; 1.
DR   Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002088; Prenyl_trans_a.
DR   InterPro; IPR036254; RabGGT_asu_insert-dom_sf.
DR   InterPro; IPR009087; RabGGT_asu_insert-domain.
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; PF14580; LRR_9; 1.
DR   Pfam; PF01239; PPTA; 5.
DR   Pfam; PF07711; RabGGT_insert; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR   SUPFAM; SSF49594; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   PROSITE; PS51450; LRR; 1.
DR   PROSITE; PS51147; PFTA; 5.
PE   3: Inferred from homology;
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW   ECO:0000256|RuleBase:RU367120};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU367120}.
FT   DOMAIN          264..364
FT                   /note="Rab geranylgeranyltransferase alpha subunit insert-
FT                   domain"
FT                   /evidence="ECO:0000259|Pfam:PF07711"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..214
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  67734 MW;  E891DB0D65B48DBD CRC64;
     MHGRVKVKTT AQQEEEKRKE REKKLKVYVA ARDACFSKRK DGVFDDEALQ LTQQLLSANP
     DFATLWNYRR EILTHLETVK DEDEAQKIYE AELSFLESCL KVNPKSYGSW HHRGWVSARL
     PRPDWARELR LCDRCLSLDD RNFHCWDYRR MVVKMSSVPV KQELEFTDRL IGSNFSNYSS
     WHYRSTLLPL LHPGSPEPPP SRCDGDPPHS CSPPSPQTHF HRVCEEQLLK EYELVQNAFF
     TDPNDQSAWF YYRWLLGRAE REEMISCAYV SREQERVAVA FSRPVNAQSG SLLLVLDGQP
     QRVEWRSVHP HFKHSPVWIC DLPPGTISDI ANEHNLTVHW TEKHTHRDCA LYTGRSESWC
     RDTATDLELF RSELSVEKTS VLQSELQSVN QLQELEPLNK WCLLTIILLM RALDPLGYEK
     ETLAHFQTLK EVDSMRSAYY SDLCSKFMIE NTILKMEYAE VRVFSISDRN LTTLCHLDQL
     LLVTHINLSS NQLRRLPPQF AMLQCLEVVE ADNNSIENLE GVYHLPKLEE VSLKNNKIST
     LADLQPLASC PKLRRLDLRG NPVTQTANVE SELAELLPSV ADLLL
//
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