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PGTB2_DICDI
ID   PGTB2_DICDI             Reviewed;         339 AA.
AC   B0G172;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Probable geranylgeranyl transferase type-2 subunit beta;
DE            EC=2.5.1.60;
DE   AltName: Full=Geranylgeranyl transferase type II subunit beta;
DE            Short=GGTase-II-beta;
DE   AltName: Full=Rab geranyl-geranyltransferase subunit beta;
DE            Short=Rab GG transferase beta;
DE            Short=Rab GGTase beta;
DE   AltName: Full=Rab geranylgeranyltransferase subunit beta;
DE   AltName: Full=Type II protein geranyl-geranyltransferase subunit beta;
GN   Name=rabggtb; ORFNames=DDB_G0290671;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC       geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an
CC       -XXCC, -XCXC and -CCXX C-terminal. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; AAFI02000164; EDR41036.1; -; Genomic_DNA.
DR   RefSeq; XP_001733035.1; XM_001732983.1.
DR   AlphaFoldDB; B0G172; -.
DR   SMR; B0G172; -.
DR   STRING; 44689.DDB0233949; -.
DR   PaxDb; B0G172; -.
DR   EnsemblProtists; EDR41036; EDR41036; DDB_G0290671.
DR   GeneID; 8627741; -.
DR   KEGG; ddi:DDB_G0290671; -.
DR   dictyBase; DDB_G0290671; rabggtb.
DR   eggNOG; KOG0366; Eukaryota.
DR   HOGENOM; CLU_028946_3_0_1; -.
DR   InParanoid; B0G172; -.
DR   OMA; VKRCQCP; -.
DR   PhylomeDB; B0G172; -.
DR   Reactome; R-DDI-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR   Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR   PRO; PR:B0G172; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR   GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR   CDD; cd02894; GGTase-II; 1.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR026873; Ptb1.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11774; PTHR11774; 1.
DR   Pfam; PF00432; Prenyltrans; 5.
DR   SUPFAM; SSF48239; SSF48239; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW   Zinc.
FT   CHAIN           1..339
FT                   /note="Probable geranylgeranyl transferase type-2 subunit
FT                   beta"
FT                   /id="PRO_0000331291"
FT   REPEAT          24..65
FT                   /note="PFTB 1"
FT   REPEAT          72..113
FT                   /note="PFTB 2"
FT   REPEAT          120..161
FT                   /note="PFTB 3"
FT   REPEAT          168..209
FT                   /note="PFTB 4"
FT   REPEAT          216..257
FT                   /note="PFTB 5"
FT   REPEAT          264..306
FT                   /note="PFTB 6"
FT   BINDING         194..196
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250"
FT   BINDING         236..248
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  38012 MW;  C5741A1FB950F662 CRC64;
     MTDNINKEST TTTTTIDHTT NLLIDKHVEY IVKLGSKKDS FEYWVTEHIR MNGMYWGLSS
     LYLLKSLDKL DKNEVIQWLL SCQKSNGGFG GNTSHDDHLL STLSAVQILI QYDALDKIDI
     NSVVDYVVKL QREDGSFVGD QWGEVDTRFS YAAIMCLSLL KSLDKINCEK AVEYILSCQN
     FDGGFGSIPG AESHAGQIFT CVGALSILNE INKIDIDKLG WWLSERQLPN GGLNGRPEKS
     SDVCYSWWVL SALSAIDRLH WIDNDKLKSY ILKCQDNETG GIADKPGDIP DVFHTFFGIC
     GLSLMGYFKD QIESIDPVYA LGTKTLQKLG LNLPWNKNL
 
 
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