ID A0A126V384_9RHOB Unreviewed; 170 AA.
AC A0A126V384;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|HAMAP-Rule:MF_00984, ECO:0000256|RuleBase:RU000524};
DE Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984};
GN ORFNames=RC74_17325 {ECO:0000313|EMBL:AML52782.1};
OS Falsihalocynthiibacter arcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Falsihalocynthiibacter.
OX NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML52782.1, ECO:0000313|Proteomes:UP000070371};
RN [1] {ECO:0000313|EMBL:AML52782.1, ECO:0000313|Proteomes:UP000070371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML52782.1};
RA Lee Y.M., Baek K., Lee H.K., Shin S.C.;
RT "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t from
RT arctic marine sediment.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in DNA replication, recombination and
CC repair. Binds to ssDNA and to an array of partner proteins to recruit
CC them to their sites of action during DNA metabolism.
CC {ECO:0000256|HAMAP-Rule:MF_00984}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00984}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00984}.
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DR EMBL; CP014327; AML52782.1; -; Genomic_DNA.
DR RefSeq; WP_039000655.1; NZ_CP014327.1.
DR AlphaFoldDB; A0A126V384; -.
DR STRING; 1579316.RC74_17325; -.
DR KEGG; hat:RC74_17325; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000070371; Chromosome.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd04496; SSB_OBF; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00984; SSB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR NCBIfam; TIGR00621; ssb; 1.
DR PANTHER; PTHR10302; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR PANTHER; PTHR10302:SF27; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR Pfam; PF00436; SSB; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50935; SSB; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00984};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_00984}; DNA repair {ECO:0000256|HAMAP-Rule:MF_00984};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00984};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00984}; Reference proteome {ECO:0000313|Proteomes:UP000070371}.
FT REGION 114..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 165..170
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 141..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 170 AA; 17827 MW; 3543A46DB6CB3B71 CRC64;
MAGSVNKVIL IGNLGRDPEV RSFPNGGKVC NLRIATSENW KDKNTGERRE KTEWHSVAIF
QEGLVRIAEQ YLKKGSKVYI EGQLQTRKYQ AQDGTDRYST EVVLQGFGGT LTMLDGRSEG
GGGGYDSGPS GGGYDSGPSG GGYSSGGNQG GGNQGGGNQG GGNIDDEIPF
//
