位置:首页 > 蛋白库 > CCA_SULAC
CCA_SULAC
ID   CCA_SULAC               Reviewed;         416 AA.
AC   Q4J9A0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01264};
DE            EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01264};
DE   AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01264};
GN   Name=cca {ECO:0000255|HAMAP-Rule:MF_01264}; OrderedLocusNames=Saci_1288;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC       terminal CCA sequence in tRNAs without using a nucleic acid template.
CC       Adds these three nucleotides in the order of C, C, and A to the tRNA
CC       nucleotide-73, using CTP and ATP as substrates and producing inorganic
CC       pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_01264}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3
CC         diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC         COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01264};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01264};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01264}.
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC       and CTP and is responsible for their addition. {ECO:0000255|HAMAP-
CC       Rule:MF_01264}.
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Archaeal CCA-adding enzyme subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01264}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000077; AAY80630.1; -; Genomic_DNA.
DR   RefSeq; WP_011278132.1; NC_007181.1.
DR   AlphaFoldDB; Q4J9A0; -.
DR   SMR; Q4J9A0; -.
DR   STRING; 330779.Saci_1288; -.
DR   EnsemblBacteria; AAY80630; AAY80630; Saci_1288.
DR   GeneID; 3473365; -.
DR   KEGG; sai:Saci_1288; -.
DR   PATRIC; fig|330779.12.peg.1246; -.
DR   eggNOG; arCOG04249; Archaea.
DR   HOGENOM; CLU_044679_1_0_2; -.
DR   OMA; DVDLVPC; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-UniRule.
DR   CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR   Gene3D; 1.10.1410.30; -; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   HAMAP; MF_01264; CCA_arch; 1.
DR   InterPro; IPR008229; CCA-adding_arc.
DR   InterPro; IPR042090; CCA_tRNA_nucleotrans_2.
DR   InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR011068; NuclTrfase_I-like_C.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   InterPro; IPR015329; tRNA_NucTransf2.
DR   PANTHER; PTHR39643; PTHR39643; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF09249; tRNA_NucTransf2; 1.
DR   PIRSF; PIRSF005335; CCA_arch; 1.
DR   SUPFAM; SSF55003; SSF55003; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   TIGRFAMs; TIGR03671; cca_archaeal; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding;
KW   Transferase; tRNA processing.
FT   CHAIN           1..416
FT                   /note="CCA-adding enzyme"
FT                   /id="PRO_0000139081"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         42
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         45
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         130
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         150
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         159
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         159
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
SQ   SEQUENCE   416 AA;  48307 MW;  DD668DAFA1470708 CRC64;
     MSVEEKVLEL IRPDDKDRER LEKVAEEVLS RLKGFDAQIQ GSFRKGTWLK GDTDIDIFVF
     YPKEVGKEYL REKSLKELIQ LFQDLNYEIA FAEHPYLILK INNVEVDVVP ALKIDSGEDV
     ITAADRTPFH TKFVTTHLDE KGKDEVRLLK QFMKGIGVYG AEIKVKGFSG YVAELLTIYY
     GNFRKVLESA KTWKPPIKLN LVEPKRDFDE PLQIPDPVDP KRNTASAVSL RNIAVFSLAS
     KIFIERPSIE FFFPTEIKAE EIIGDILLIK VEFKEKSVED IIWGQVWKNV EKLKNAIKTA
     GFSLIDIGAW GNSQTVKIAV QIEDKNISRY YLNQGPYFYV NGVDNFMRKN KYVWVGEDGR
     LYSLKKRRET NLEKIVLNNL SFKENFSVEM TWLSEINQDD KELHKFLRKR PTWMQT
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024