ID C5S0S1_9PAST Unreviewed; 444 AA.
AC C5S0S1;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Replication-associated recombination protein A {ECO:0000256|ARBA:ARBA00020776};
GN ORFNames=AM305_07483 {ECO:0000313|EMBL:EER47504.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER47504.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER47504.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER47504.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
CC -!- FUNCTION: DNA-dependent ATPase that plays important roles in cellular
CC responses to stalled DNA replication processes.
CC {ECO:0000256|ARBA:ARBA00002393}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00008959}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EER47504.1}.
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DR EMBL; ACQL01000069; EER47504.1; -; Genomic_DNA.
DR RefSeq; WP_005823298.1; NZ_ACQL01000069.1.
DR AlphaFoldDB; C5S0S1; -.
DR eggNOG; COG2256; Bacteria.
DR OrthoDB; 9778364at2; -.
DR Proteomes; UP000005532; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18139; HLD_clamp_RarA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 48..164
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 444 AA; 50203 MW; EFED89BBAC26DF9E CRC64;
MSSFSFDFAE DFRPLSARMR PRNLSEYIGQ HHLIGEGKPL RRAIESKHPH SMIFWGPPGT
GKTTLAEIIA YHFDADVERL SAVTSGIKEI REAIERAKLN RQTGRRTLLF VDEVHRFNKS
QQDAFLPYIE DGTIIFIGAT TENPSFELNN ALLSRARVYI LKPLQPADVL VVLQNALNDK
TRGLGAEKII LKDNVLNLLA DYVNGDARYA LNCLEQMSDM ATQTEAGKLF DLNLLTEILG
ERLARFDKGG DRYYDLISAL HKSIRGSSPD GALYWYARIL TAGGDPLYVA RRLLAIASED
IGNADPRAMQ VALSAWDCYT RVGAYEGERA IAQAVIYLAV APKSNAVYTA FNEAKRLAKE
AKDYDVPEHL RNAPTHLMKT LGYGEEYRYA HHEEHAYAAG ENYFPPELKD TQFYFPSERG
MEKQIKEKMV WLKALDAQSR IKRY
//
