(data stored in ACNUC7421 zone)

HOGENOM: SHELP_1_PE1006

ID   SHELP_1_PE1006                       STANDARD;      PRT;   413 AA.
AC   SHELP_1_PE1006; A3QBN1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Multifunctional CCA protein;Includes: RecName:
DE   Full=CCA-adding enzyme; EC=2.7.7.72; AltName: Full=CCA tRNA
DE   nucleotidyltransferase; AltName: Full=tRNA CCA-pyrophosphorylase;
DE   AltName: Full=tRNA adenylyl-/cytidylyl-transferase; AltName: Full=tRNA
DE   nucleotidyltransferase; AltName: Full=tRNA-NT;Includes: RecName:
DE   Full=2'-nucleotidase; EC=3.1.3.-;Includes: RecName: Full=2',3'-cyclic
DE   phosphodiesterase; EC=3.1.4.-;Includes: RecName: Full=Phosphatase;
DE   EC=3.1.3 -; (SHELP_1.PE1006).
GN   Name=cca; OrderedLocusNames=Shew_1008;
OS   SHEWANELLA LOIHICA PV-4.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHELP_1.PE1006.
CC       Shewanella loihica PV-4, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:CCA_SHELP
CC   -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC       terminal CCA sequence in tRNAs without using a nucleic acid
CC       template. Adds these three nucleotides in the order of C, C, and A
CC       to the tRNA nucleotide-73, using CTP and ATP as substrates and
CC       producing inorganic pyrophosphate. Also shows phosphatase, 2'-
CC       nucleotidase and 2',3'-cyclic phosphodiesterase activities. These
CC       phosphohydrolase activities are probably involved in the repair of
CC       the tRNA 3'-CCA terminus degraded by intracellular RNases (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a
CC       3' CCA end + 3 diphosphate.
CC   -!- COFACTOR: Magnesium for nucleotidyltransferase activity (By
CC       similarity).
CC   -!- COFACTOR: Nickel for phosphatase activity (By similarity).
CC   -!- SUBUNIT: Monomer. Can also form homodimers and oligomers (By
CC       similarity).
CC   -!- DOMAIN: Comprises two domains: an N-terminal domain containing the
CC       nucleotidyltransferase activity and a C-terminal HD domain
CC       associated with both phosphodiesterase and phosphatase activities
CC       (By similarity).
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both
CC       ATP and CTP and is responsible for their addition (By similarity).
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
CC   -!- GENE_FAMILY: HOG000007368 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A3QBN1; -.
DR   EMBL; CP000606; ABO22879.1; -; Genomic_DNA.
DR   RefSeq; YP_001093138.1; NC_009092.1.
DR   ProteinModelPortal; A3QBN1; -.
DR   STRING; A3QBN1; -.
DR   GeneID; 4920857; -.
DR   GenomeReviews; CP000606_GR; Shew_1008.
DR   KEGG; slo:Shew_1008; -.
DR   eggNOG; COG0617; -.
DR   OMA; GHGQKGL; -.
DR   PhylomeDB; A3QBN1; -.
DR   BioCyc; SLOI323850:SHEW_1008-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:InterPro.
DR   HAMAP; MF_01261; CCA_bact_type1; 1; -.
DR   InterPro; IPR012006; CCA_bact.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR006674; Metal-dep_PHydrolase_HD_sub.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   PIRSF; PIRSF000813; CCA_bact; 1.
DR   SMART; SM00471; HDc; 1.
DR   HOGENOMDNA; SHELP_1.PE1006; -.
KW   metal dependent phosphohydrolase;
KW   ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nickel; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA repair; RNA-binding; Transferase;
KW   tRNA processing.
SQ   SEQUENCE   413 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKIYLVGGAV RDQLLNIPIK DRDYMVVGAT VQEMLDKGYR QVGKDFPVFL HPKTQQEYAL
     ARTERKTGVG YGGFSVYAAP DVTLEEDLLR RDLTINAIAQ DETGRVFDPY GGQADIEQRL
     LRHVSDAFVE DPLRVLRVAR FAARFQPLGF KVAPETMALM QRIAASGELE ALTPERVFQE
     LDKALSTEAP QVFFEVLREA GGLAILFPEI EALFGIPQPE QWHPEIDTGI HTLMVLEQAA
     RLSQDKQVRF AALVHDLGKA LSPKEHLPKH HGHGQKGLPL IRALCERFRV PNDYRDLALL
     VSDQHQNIHN AFELRAETMV KLFDKADLWR KPERLPQLLL ACEADCKGRT GLKERPYPQG
     AYVQHCFELA RNVAIKPIIE AGFKGAEIKA QLHKQRVEVI DQYKRKTAVN AKP
//

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