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Database: UniProt
Entry: V9VNC3_9RHOB
LinkDB: V9VNC3_9RHOB
Original site: V9VNC3_9RHOB 
ID   V9VNC3_9RHOB            Unreviewed;       440 AA.
AC   V9VNC3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Replication-associated recombination protein A {ECO:0000256|ARBA:ARBA00020776};
GN   ORFNames=METH_01225 {ECO:0000313|EMBL:AHC99507.1};
OS   Leisingera methylohalidivorans DSM 14336.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=999552 {ECO:0000313|EMBL:AHC99507.1, ECO:0000313|Proteomes:UP000018780};
RN   [1] {ECO:0000313|EMBL:AHC99507.1, ECO:0000313|Proteomes:UP000018780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14336 {ECO:0000313|EMBL:AHC99507.1,
RC   ECO:0000313|Proteomes:UP000018780};
RG   DOE Joint Genome Institute;
RA   Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (SEP-2013) 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}.
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DR   EMBL; CP006773; AHC99507.1; -; Genomic_DNA.
DR   RefSeq; WP_024088567.1; NC_023135.1.
DR   AlphaFoldDB; V9VNC3; -.
DR   STRING; 999552.METH_01225; -.
DR   KEGG; lmd:METH_01225; -.
DR   PATRIC; fig|999552.6.peg.240; -.
DR   HOGENOM; CLU_017985_1_1_5; -.
DR   OrthoDB; 9778364at2; -.
DR   Proteomes; UP000018780; Chromosome.
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          57..175
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  48161 MW;  D06D388DFF2C2D7D CRC64;
     MADLFGSPAS ADGDPQQPSV NRPLADRLRP QSLAEVIGQQ QVLGPEAPLG VMLASGSLSS
     LIFWGPPGVG KTTIARLLAQ ETDLHFVQIS AIFTGVPELR KVFESAKIRR QNGQGTLLFV
     DEIHRFNKAQ QDGFLPHMED GTILLVGATT ENPSFELNAA VLSRSQVLVL ERLSLADLEH
     LTQRAEKELG RALPLSGDAR DALHEMADGD GRALLNLIEQ VAAWKAAAPL GREALASRLM
     RRAAKFDKSG DEHYNLISAL HKSIRGSDPD AALYWLARML EGGEDPRFLA RRLTMMSTED
     IGMADPQANT VCLNAWQTYE RLGSPEGELA LANAAVYLAL APKSNAVYVG IKAARRLAKT
     TGSAPPPKHI LNAPTKLMSE QGYGDGYAYD HDAEDGFSGQ NYFPDGVKRP VLYQPVERGF
     ERELKRRTDY FANLRLKRNK
//
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