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Protein

CCA-adding enzyme

Gene

cca

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271ATP or CTP; via amide nitrogen
Binding sitei30 – 301ATP or CTP
Metal bindingi40 – 401MagnesiumBy similarity
Metal bindingi42 – 421MagnesiumBy similarity
Binding sitei111 – 1111ATP or CTP
Sitei112 – 1121May assist in discriminating ATP from CTP
Sitei153 – 1531Involved in nucleotide selectionSequence analysis
Binding sitei154 – 1541ATP or CTP
Binding sitei157 – 1571ATP or CTP
Binding sitei160 – 1601ATP or CTP
Binding sitei163 – 1631ATP or CTP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

RNA repair, tRNA processing

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
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
Gene namesi
Name:cca
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404CCA-adding enzymePRO_0000139033Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1715Combined sources
Beta strandi22 – 265Combined sources
Helixi27 – 348Combined sources
Beta strandi42 – 476Combined sources
Helixi49 – 557Combined sources
Beta strandi57 – 637Combined sources
Helixi64 – 663Combined sources
Beta strandi68 – 736Combined sources
Beta strandi76 – 827Combined sources
Beta strandi84 – 863Combined sources
Beta strandi98 – 1003Combined sources
Helixi104 – 1096Combined sources
Beta strandi111 – 1144Combined sources
Helixi115 – 1173Combined sources
Beta strandi129 – 1313Combined sources
Helixi132 – 1387Combined sources
Beta strandi143 – 1453Combined sources
Helixi147 – 1537Combined sources
Helixi156 – 16813Combined sources
Helixi174 – 18310Combined sources
Helixi184 – 1896Combined sources
Helixi192 – 20312Combined sources
Beta strandi205 – 2073Combined sources
Helixi208 – 21710Combined sources
Turni219 – 2224Combined sources
Helixi231 – 2366Combined sources
Helixi237 – 2393Combined sources
Helixi242 – 2443Combined sources
Helixi248 – 25811Combined sources
Helixi264 – 2707Combined sources
Helixi275 – 29016Combined sources
Helixi294 – 2963Combined sources
Helixi299 – 32123Combined sources
Helixi326 – 33611Combined sources
Helixi344 – 3463Combined sources
Helixi351 – 3588Combined sources
Beta strandi362 – 3643Combined sources
Helixi365 – 37814Combined sources
Helixi386 – 39712Combined sources
Helixi399 – 4035Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MIVX-ray3.50A/B1-404[»]
1MIWX-ray3.00A/B1-404[»]
1MIYX-ray3.52A/B1-404[»]
ProteinModelPortaliQ7SIB1.
SMRiQ7SIB1. Positions 1-404.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIB1.

Family & Domainsi

Domaini

The crystal structure reveals a seahorse-shaped subunit consisting of four domains: head, neck, body, and tail. The head domain contains the nucleotidyltransferase activity. The neck domain provides a specific template for the incoming ATP or CTP, whereas the body and tail domains may be involved in tRNA binding.

Sequence similaritiesi

Family and domain databases

HAMAPiMF_01263. CCA_bact_type3. 1 hit.
InterProiIPR032810. CCA-adding_enz_C.
IPR023068. CCA-adding_enz_firmicutes.
IPR002646. PolA_pol_head_dom.
IPR032828. PolyA_RNA-bd.
[Graphical view]
PfamiPF01743. PolyA_pol. 1 hit.
PF12627. PolyA_pol_RNAbd. 1 hit.
PF13735. tRNA_NucTran2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7SIB1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPPFQEALG IIQQLKQHGY DAYFVGGAVR DLLLGRPIGD VDIATSALPE
60 70 80 90 100
DVMAIFPKTI DVGSKHGTVV VVHKGKAYEV TTFKTDGDYE DYRRPESVTF
110 120 130 140 150
VRSLEEDLKR RDFTMNAIAM DEYGTIIDPF GGREAIRRRI IRTVGEAEKR
160 170 180 190 200
FREDALRMMR AVRFVSELGF ALAPDTEQAI VQNAPLLAHI SVERMTMEME
210 220 230 240 250
KLLGGPFAAR ALPLLAETGL NAYLPGLAGK EKQLRLAAAY RWPWLAAREE
260 270 280 290 300
RWALLCHALG VQESRPFLRA WKLPNKVVDE AGAILTALAD IPRPEAWTNE
310 320 330 340 350
QLFSAGLERA LSVETVRAAF TGAPPGPWHE KLRRRFASLP IKTKGELAVN
360 370 380 390 400
GKDVIEWVGK PAGPWVKEAL DAIWRAVVNG EVENEKERIY AWLMERNRTR

EKNC
Length:404
Mass (Da):45,369
Last modified:December 15, 2003 - v1
Checksum:iDC0C8E4C47133940
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MIVX-ray3.50A/B1-404[»]
1MIWX-ray3.00A/B1-404[»]
1MIYX-ray3.52A/B1-404[»]
ProteinModelPortaliQ7SIB1.
SMRiQ7SIB1. Positions 1-404.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIB1.

Family and domain databases

HAMAPiMF_01263. CCA_bact_type3. 1 hit.
InterProiIPR032810. CCA-adding_enz_C.
IPR023068. CCA-adding_enz_firmicutes.
IPR002646. PolA_pol_head_dom.
IPR032828. PolyA_RNA-bd.
[Graphical view]
PfamiPF01743. PolyA_pol. 1 hit.
PF12627. PolyA_pol_RNAbd. 1 hit.
PF13735. tRNA_NucTran2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCCA_GEOSE
AccessioniPrimary (citable) accession number: Q7SIB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: December 15, 2003
Last modified: January 20, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.