Reviewed, UniProtKB/Swiss-Prot Q9L7A3 (CCA_HAEDU)

Names and origin

Protein names

Recommended name:
    Multifunctional CCA protein
Including the following 4 domains:
    1- Recommended name:
            CCA-adding enzyme
              EC=2.7.7.25
              EC=2.7.7.21
        Alternative name(s):
            tRNA nucleotidyltransferase
            tRNA adenylyl-/cytidylyl-transferase
            tRNA CCA-pyrophosphorylase
            tRNA-NT
    2- Recommended name:
            2'-nucleotidase
              EC=3.1.3.-
    3- Recommended name:
            2',3'-cyclic phosphodiesterase
              EC=3.1.4.-
    4- Recommended name:
            Phosphatase
              EC=3.1.3.-

Gene names

Name:	cca
Ordered Locus Names:	HD_1091

Organism

Haemophilus ducreyi [Complete proteome] [HAMAP]

Taxonomic identifier

730 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.
Catalytic activity	ATP + tRNA(n) = diphosphate + tRNA(n+1). HAMAP MF_01261 CTP + tRNA(n) = diphosphate + tRNA(n+1). HAMAP MF_01261
Cofactor	Magnesium for nucleotidyltransferase activity By similarity. Nickel for phosphatase activity By similarity.
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.
Miscellaneous	A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity.
Sequence similarities	Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.

Ontologies

Keywords
Biological process	RNA repair tRNA processing
Ligand	ATP-binding Magnesium Metal-binding Nickel Nucleotide-binding RNA-binding
Molecular function	Hydrolase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	RNA repair Inferred from electronic annotation. Source: UniProtKB-KW tRNA 3'-terminal CCA addition Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP cyclic-nucleotide phosphodiesterase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatase activity Inferred from electronic annotation. Source: HAMAP tRNA adenylyltransferase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: HAMAP tRNA cytidylyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 412	412	Multifunctional CCA protein HAMAP MF_01261		PRO_0000138979
Sites
	Metal binding	21	1	Magnesium By similarity
	Metal binding	23	1	Magnesium By similarity
	Binding site	8	1	ATP or CTP; via amide nitrogen By similarity
	Binding site	11	1	ATP or CTP By similarity
	Binding site	91	1	ATP or CTP By similarity
	Binding site	138	1	ATP or CTP By similarity
	Binding site	141	1	ATP or CTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9L7A3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 4F5D348218E28066	FASTA	412	46,685
	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

References

	« Hide 'large scale' referencesShow '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
EMBLGenBankDDBJ	AF224467 Genomic DNA. Translation: AAF28362.1. AE017143 Genomic DNA. Translation: AAP95957.1.
RefSeq	NP_873568.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1491020.
GenomeReviews	Gene locus HD_1091 in contig AE017143_GR.
KEGG	hdu:HD1091.
NMPDR	fig|233412.1.peg.933.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9L7A3.
OMA	Q9L7A3. KHHGHGQ.
Enzyme and pathway databases
BioCyc	HDUC233412:HD_1091-MON.
BRENDA	2.7.7.21. 265031. 2.7.7.25. 265031.
Family and domain databases
HAMAP	MF_01261. [Tree]
InterPro	IPR012006. CCA_bact. IPR003607. Met-dep_phosphohydro_HD. IPR006674. Met-dep_phosphohydro_HD_sub. IPR002646. PolyA_pol_reg. [Graphical view]
Pfam	PF01966. HD. 1 hit. PF01743. PolyA_pol. 1 hit. [Graphical view]
PIRSF	PIRSF000813. CCA_bact. 1 hit.
SMART	SM00471. HDc. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CCA_HAEDU

Accession

Primary (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:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)