ID A0A0Q4KZ97_9SPHN Unreviewed; 436 AA.
AC A0A0Q4KZ97;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Replication-associated recombination protein A {ECO:0000256|ARBA:ARBA00020776};
GN ORFNames=ASE86_10770 {ECO:0000313|EMBL:KQN26981.1};
OS Sphingomonas sp. Leaf33.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN26981.1, ECO:0000313|Proteomes:UP000051455};
RN [1] {ECO:0000313|EMBL:KQN26981.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26981.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN26981.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26981.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQN26981.1}.
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DR EMBL; LMLB01000001; KQN26981.1; -; Genomic_DNA.
DR RefSeq; WP_056427028.1; NZ_LMLB01000001.1.
DR AlphaFoldDB; A0A0Q4KZ97; -.
DR STRING; 1736215.ASE86_10770; -.
DR OrthoDB; 9778364at2; -.
DR Proteomes; UP000051455; 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; 1.20.272.10; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051455}.
FT DOMAIN 54..172
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 47173 MW; E6EDA1CF6F8D8FFC CRC64;
MADLLAGLEP PADPLPDSAP LADRLRPQAL DEVVGQEHVT GAEGAIGRMV AAGRLSSLIL
WGPPGTGKTT IARLLADAVG LRFAPISAVF SGVADLKKVF AEAKLAARTG QRTLLFVDEI
HRFNRAQQDG FLPYVEDGTV TLVGATTENP SFELNAALLS RAQVLILHRL GATALNKLLD
RAEALMERAL PVTPAARDAL VASADGDGRF LLNQAETLWS VDIAEPLDPA GLGAFLQRRV
AVYDKDREGH YNLISALHKS IRGSDPQAAL YYLARMLTAG EDPLFVLRRL IRAAVEDIGL
ADPNAVVQCV AAKDTYDFLG SPEGELAIVQ ACLYLATAPK SNAAYKAQKA AWRAAKETGS
LMPPANILNA PTKLMKQIGY GADYAYDHDA ADGFSGANYW PDEMEPQAFY QPTDRGFEKR
LSERLAWWDE RRKGRE
//
