2QLC


Conserved Protein Domain Family
RadC

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pfam04002: RadC 
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RadC-like JAB domain
A family of proteins present widely across the bacteria. This family was named initially with reference to the E. coli radC102 mutation which suggested that RadC was involved in repair of DNA lesions. However the relevant mutation has subsequently been shown to be in recG, where radC is in fact an allele of recG. In addition, a personal communication from Claverys, J-P, et al, indicates a total failure of all attempts to characterize a radiation-related function for RadC in Streptococcus pneumoniae, suggesting that it is not involved in repair of DNA lesions, in recombination during transformation, in gene conversion, nor in mismatch repair. Computational analysis, however, provides a possible function. The RadC-like family belong to the JAB superfamily of metalloproteins. The domain shows fusions to an N-terminal Helix-hairpin-Helix (HhH) domain in most instances. Other domain combinations include fusions to the anti-restriction module ArdC, the DinG/RAD3-like superfamily II helicases and the DNAG-like primase. In some bacteria, closely related DinG/Rad3- like superfamily II helicases are fused to a 3'-5' exonuclease in the same position as the RadC-like JAB domain. These conserved domain associations lead to the hypothesis that the RadC-like JAB domains might function as a nuclease.
Statistics
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PSSM-Id: 397899
Aligned: 844 rows
Threshold Bit Score: 72.4361
Threshold Setting Gi: 524315599
Created: 20-May-2020
Updated: 7-Aug-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
2QLC_F                   5 V-KGA----RDVFEYmkgripdE-T----K--EHLFVLFLSTKNQILRHETI----TIGTLTASLIHPREIFKAAIRESA 68  Chlor...
Q5FNC5                 112 TlSNW----EQLMAY-------LdQalegGipGQFRLLYLDNRNRLLADEAA----PEAD--SLAERNRAIAIRALALHA 174 Gluco...
CAP55930               115 LtRTPmrdwDAVLAY-------CdTvltgAppGQLRILFLDSSNHIIADEALdaalDTGELD---LVQRHILLRALDLHA 184 Gluco...
PRJNA213647:NX02_00285 116 L-SNW----QALLDYlhvdmahS-A----I--ERVRVLHLNAKNMLIRDELM----SEGSIDQAAVHVREVIRRAIELGS 179 Sphin...
Q5NPS3                 106 L-SGW----QALIDYlhadmafR-L----T--ERCRLLHLDNHNRLIRDEIL----SEGSVDQAPVYVREVIRRAIELCS 169 Zymom...
WP_015457963           113 L-ASW----QALLDYlradmahR-T----I--ERVRVLHLNSKNMLIRDELT----SEGSVDQAAVYVREIIRRAIDLGS 176 Sphin...
WP_014076616           114 L-SSW----QALLDYlradmafM-S----V--ERVRVLHLNSRNMLLRDDHM----RDGTIDQAAVYVREVVKRAVELGS 177 Sphin...
Q2LSS5                 185 I-SCT----GELLDFcktalggL-K----D--ENFCVLYLDTQNRIIAFETI----QKGIVNQAVVYPRQVIERALSHKS 248 Syntr...
WP_013707266           112 L-PV-------LIDYcrtsmggL-K----D--EQFRVIFLNSQNEVIAEETI----QEGTVDQTVVYPRKVLEAALKHKA 172 Desul...
WP_013045538           126 L-TNW----VQVQEYcinrlahQ-P----I--EHFLILCLDNQNRLIAEETL----SKGTVDQTPVYVREVVNAALKHHA 189 Candi...
2QLC_F                  69 HSIILVHNHPS--GDVQPSNADKQVTSILKKAGDLLQIELLDHVIVGNNDW 117 Chlorobaculum tepidum TLS
Q5FNC5                 175 TALIGFHIRPK-----ERPADLSQSARQLDFAMRPLSITLHDVLITN-EGr 219 Gluconobacter oxydans
CAP55930               185 TAFVGIRIAPVwpPPAALVERDAVLMQAISYHAQNLSLTVQDHLILHhgqw 235 Gluconacetobacter diazotrophicus P...
PRJNA213647:NX02_00285 180 SALILVHNHPS--GDPQPSRADITLTRDIIEAGRRMDIQVHDHVIIGAHGH 228 Sphingomonas sanxanigenens DSM 196...
Q5NPS3                 170 VGLILVHNHPS--GDASPSEADIQLTRSIVAAARPLKIYLHDHVIISSSGA 218 Zymomonas mobilis
WP_015457963           177 AALILVHNHPS--GDPTPSRQDIALTRDLATAAKPLGIAIHDHVIIAGEGH 225 Sphingomonas sp. MM-1
WP_014076616           178 ASLILVHNHPS--GSPEPSRQDVEFTREIINALRPIGVSVHDHIIIGTDGH 226 Sphingobium sp. SYK-6
Q2LSS5                 249 SALILVHNHPS--GFVKPSDADIRLTRTITDTAKLLDIMVHDHLIIGENRF 297 Syntrophus aciditrophicus SB
WP_013707266           173 TGLILVHNHPS--GRLTPSTADRELTRAIIQAAQPLAITVHDHLIISKQGH 221 Desulfobacca acetoxidans
WP_013045538           190 QSSILVHNHPS--GEAEPSRADIEMTLAIQDALNIMSINLHDHLIVAGKQC 238 Candidatus Puniceispirillum marinum
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