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Protein

Protein RecA

Gene

recA

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (By similarity). Probably involved in base excision repair (PubMed:19303848).UniRule annotation1 Publication
Following severe irradiation (7 kGy of gamma irradiation) genomic DNA is fragmented. DNA is progressively degraded for the first 1.5 hours after IR, in a step promoted by RecA and counterbalanced by DNA Pol I and Pol III, followed by massive DNA synthesis and genome reassembly in the next hour. Optimal priming of DNA synthesis requires both RecA and RadA, Pol III initiates DNA synthesis while both Pol I and Pol III are required for its contination. In the absence of RecA the majority of the chromosome is still reconstituted, via either single-strand annealing or non-homologous end joining (PubMed:19303848).1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi78 – 858ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • DNA recombinase assembly Source: GO_Central
  • double-strand break repair Source: CACAO
  • mitotic recombination Source: GO_Central
  • response to ionizing radiation Source: GO_Central
  • SOS response Source: UniProtKB-HAMAP
  • strand invasion Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, SOS response

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2389-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RecAUniRule annotation
Alternative name(s):
Recombinase AUniRule annotation
Gene namesi
Name:recAUniRule annotation
Ordered Locus Names:DR_2340
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Reduced DNA synthesis rate even in the absence of ionizing radiation (IR) (PubMed:19303848). Cells lacking this gene have a reduced capacity to survive IR (from 90% survival to <10(-7)), DNA repair following IR is slow (PubMed:20451472, PubMed:19303848). Single recA mutants rarely reconstitutes the whole genome following IR, and their DNA is not degraded post-IR (PubMed:19303848). A double recA-ddrB disruption shows no signs of DNA repair 24 hours after IR (PubMed:20451472). Double recA-radA deletion mutants have a more severe effect than either mutation alone after IR (PubMed:19303848).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Protein RecAPRO_0000122700Add
BLAST

Proteomic databases

PRIDEiP42443.

Interactioni

Protein-protein interaction databases

STRINGi243230.DR_2340.

Structurei

Secondary structure

1
363
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 3317Combined sources
Helixi57 – 626Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 798Combined sources
Helixi84 – 9714Combined sources
Beta strandi102 – 1087Combined sources
Helixi113 – 1186Combined sources
Helixi123 – 1253Combined sources
Beta strandi127 – 1293Combined sources
Helixi134 – 14512Combined sources
Turni146 – 1483Combined sources
Beta strandi151 – 1566Combined sources
Turni158 – 1603Combined sources
Helixi178 – 19417Combined sources
Turni195 – 1973Combined sources
Beta strandi200 – 2067Combined sources
Helixi224 – 2307Combined sources
Beta strandi232 – 24110Combined sources
Beta strandi252 – 26514Combined sources
Beta strandi270 – 2767Combined sources
Turni277 – 2793Combined sources
Helixi283 – 29311Combined sources
Beta strandi296 – 3005Combined sources
Beta strandi303 – 31412Combined sources
Helixi315 – 3228Combined sources
Helixi326 – 34015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XP8X-ray2.50A1-363[»]
ProteinModelPortaliP42443.
SMRiP42443. Positions 15-341.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42443.

Family & Domainsi

Sequence similaritiesi

Belongs to the RecA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C68. Bacteria.
COG0468. LUCA.
HOGENOMiHOG000264120.
InParanoidiP42443.
KOiK03553.
OMAiPPFKEAH.
OrthoDBiPOG091H01OP.

Family and domain databases

CDDicd00983. recA. 1 hit.
Gene3Di3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00268. RecA. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR013765. DNA_recomb/repair_RecA.
IPR020584. DNA_recomb/repair_RecA_CS.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR023400. RecA_C.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERiPTHR22942:SF1. PTHR22942:SF1. 1 hit.
PfamiPF00154. RecA. 1 hit.
[Graphical view]
PRINTSiPR00142. RECA.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
TIGRFAMsiTIGR02012. tigrfam_recA. 1 hit.
PROSITEiPS00321. RECA_1. 1 hit.
PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42443-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKDATKEIS APTDAKERSK AIETAMSQIE KAFGKGSIMK LGAESKLDVQ
60 70 80 90 100
VVSTGSLSLD LALGVGGIPR GRITEIYGPE SGGKTTLALA IVAQAQKAGG
110 120 130 140 150
TCAFIDAEHA LDPVYARALG VNTDELLVSQ PDNGEQALEI MELLVRSGAI
160 170 180 190 200
DVVVVDSVAA LTPRAEIEGD MGDSLPGLQA RLMSQALRKL TAILSKTGTA
210 220 230 240 250
AIFINQVREK IGVMYGNPET TTGGRALKFY ASVRLDVRKI GQPTKVGNDA
260 270 280 290 300
VANTVKIKTV KNKVAAPFKE VELALVYGKG FDQLSDLVGL AADMDIIKKA
310 320 330 340 350
GSFYSYGDER IGQGKEKTIA YIAERPEMEQ EIRDRVMAAI RAGNAGEAPA
360
LAPAPAAPEA AEA
Length:363
Mass (Da):38,145
Last modified:May 30, 2000 - v2
Checksum:iDEF379CF0EF59D74
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241G → S in rec30; DNA-repair deficient.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01876 Genomic DNA. Translation: AAC33148.1.
AB005471 Genomic DNA. Translation: BAA21330.1.
AE000513 Genomic DNA. Translation: AAF11887.1.
PIRiC75285.
RefSeqiNP_296061.1. NC_001263.1.
WP_010888966.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF11887; AAF11887; DR_2340.
GeneIDi1798669.
KEGGidra:DR_2340.
PATRICi21632388. VBIDeiRad64572_2571.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01876 Genomic DNA. Translation: AAC33148.1.
AB005471 Genomic DNA. Translation: BAA21330.1.
AE000513 Genomic DNA. Translation: AAF11887.1.
PIRiC75285.
RefSeqiNP_296061.1. NC_001263.1.
WP_010888966.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XP8X-ray2.50A1-363[»]
ProteinModelPortaliP42443.
SMRiP42443. Positions 15-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_2340.

Proteomic databases

PRIDEiP42443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF11887; AAF11887; DR_2340.
GeneIDi1798669.
KEGGidra:DR_2340.
PATRICi21632388. VBIDeiRad64572_2571.

Phylogenomic databases

eggNOGiENOG4105C68. Bacteria.
COG0468. LUCA.
HOGENOMiHOG000264120.
InParanoidiP42443.
KOiK03553.
OMAiPPFKEAH.
OrthoDBiPOG091H01OP.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2389-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP42443.

Family and domain databases

CDDicd00983. recA. 1 hit.
Gene3Di3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00268. RecA. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR013765. DNA_recomb/repair_RecA.
IPR020584. DNA_recomb/repair_RecA_CS.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR023400. RecA_C.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERiPTHR22942:SF1. PTHR22942:SF1. 1 hit.
PfamiPF00154. RecA. 1 hit.
[Graphical view]
PRINTSiPR00142. RECA.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
TIGRFAMsiTIGR02012. tigrfam_recA. 1 hit.
PROSITEiPS00321. RECA_1. 1 hit.
PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRECA_DEIRA
AccessioniPrimary (citable) accession number: P42443
Secondary accession number(s): O32510
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 30, 2000
Last modified: September 7, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.