Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9L7A3 (CCA_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multifunctional CCA protein

Including the following 4 domains:

  1. CCA-adding enzyme
    EC=2.7.7.72
    Alternative name(s):
    CCA tRNA nucleotidyltransferase
    tRNA CCA-pyrophosphorylase
    tRNA adenylyl-/cytidylyl-transferase
    tRNA nucleotidyltransferase
    tRNA-NT
  2. 2'-nucleotidase
    EC=3.1.3.-
  3. 2',3'-cyclic phosphodiesterase
    EC=3.1.4.-
  4. Phosphatase
    EC=3.1.3.-
Gene names
Name:cca
Ordered Locus Names:HD_1091
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases By similarity. HAMAP MF_01261

Catalytic activity

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate. HAMAP MF_01261

Cofactor

Magnesium for nucleotidyltransferase activity By similarity.

Nickel for phosphatase activity By similarity. HAMAP MF_01261

Subunit structure

Monomer. Can also form homodimers and oligomers By similarity.

Domain

Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities By similarity. HAMAP MF_01261

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity. HAMAP MF_01261

Sequence similarities

Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Multifunctional CCA protein HAMAP MF_01261
PRO_0000138979

Sites

Metal binding211Magnesium By similarity
Metal binding231Magnesium By similarity
Binding site81ATP or CTP; via amide nitrogen By similarity
Binding site111ATP or CTP By similarity
Binding site911ATP or CTP By similarity
Binding site1381ATP or CTP By similarity
Binding site1411ATP or CTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9L7A3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4F5D348218E28066

FASTA41246,685
        10         20         30         40         50         60 
MQIYLVGGAV RDQLLNLPIK DRDFLVVGAT AKELINQGYQ QVGADFPVFL HPVTQQEYAL 

        70         80         90        100        110        120 
ARQERKSGTG YTGFVCDFSP NVTLEQDLIR RDLTINAMAQ DLTSGQIFDP FGGKTDLANR 

       130        140        150        160        170        180 
LLRHISDAFA EDPLRVLRVA RFAARFHHLG FSIAEQTLEL MQKMTACGEL NHLTAERIWR 

       190        200        210        220        230        240 
ETEKALHTES PHIYFQVLRK VNALAILFPE IDQLFGQIQS VKYHLETDRG QHTLLALQQA 

       250        260        270        280        290        300 
KLLVKQAHNP TALLWAVLCH DLGKDLISAE MLPHHYQPNV TGIQLTHQLA DRLKVPTAVK 

       310        320        330        340        350        360 
ELALLVNKYH TNCHKIAELD SERVLELFNQ LDVWRKPQRL DDFLLACEAD ARARLGAEYC 

       370        380        390        400        410 
SYPQATLAID YFNAANAVNV QAIIADGFKK QAIRDELNNR RINIIKQIKN AI

« Hide

References

« Hide 'large scale' references
[1]Wang J., Hanson E., Munson R.S. Jr.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF224467 Genomic DNA. Translation: AAF28362.1.
AE017143 Genomic DNA. Translation: AAP95957.1.
RefSeqNP_873568.1. NC_002940.2.

3D structure databases

ProteinModelPortalQ9L7A3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1491020.
GenomeReviewsGene locus HD_1091 in contig AE017143_GR.
KEGGhdu:HD1091.
NMPDRfig|233412.1.peg.933.
PATRIC20178529. VBIHaeDuc133973_0904.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG635063.
OMARWACLLH.
ProtClustDBPRK10885.

Enzyme and pathway databases

BioCycHDUC233412:HD_1091-MONOMER.

Family and domain databases

HAMAPMF_01261. CCA_bact_type1.
[Tree]
InterProIPR012006. CCA_bact.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR006674. Metal-dep_PHydrolase_HD_sub.
IPR002646. PolA_pol_head_dom.
[Graphical view]
KOK00974.
PfamPF01966. HD. 1 hit.
PF01743. PolyA_pol. 1 hit.
[Graphical view]
PIRSFPIRSF000813. CCA_bact. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCCA_HAEDU
AccessionPrimary (citable) accession number: Q9L7A3
Secondary accession number(s): Q7BY46
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents