ID A0A1Y6ECF9_9GAMM Unreviewed; 181 AA.
AC A0A1Y6ECF9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|HAMAP-Rule:MF_00984, ECO:0000256|PIRNR:PIRNR002070};
DE Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984};
GN ORFNames=SAMN06297229_0379 {ECO:0000313|EMBL:SMQ60176.1};
OS Pseudidiomarina planktonica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1323738 {ECO:0000313|EMBL:SMQ60176.1, ECO:0000313|Proteomes:UP000194450};
RN [1] {ECO:0000313|Proteomes:UP000194450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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; FXWH01000001; SMQ60176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6ECF9; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000194450; Unassembled WGS sequence.
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 PIRSF; PIRSF002070; 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|HAMAP-Rule:MF_00984};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00984};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00984};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00984}; Reference proteome {ECO:0000313|Proteomes:UP000194450}.
FT REGION 111..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 176..181
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 117..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 181 AA; 20326 MW; B81FC58993484BE0 CRC64;
MASRGINKVI LIGNLGADPE IRYTQNSTAI ANLSIATSET WKDKQTGEQR EQTEWHRCVA
YRRLAEIAGE YLKKGSKIYV EGRLQTRKWQ GQDGVERYTT EIVINELQML DGRPGGQQGN
YGNQPSNQGQ GAPAQSRPQQ APAQQGGYQQ QPQQQPQQRP AQQPEPEPFS PDNDFDDDIP
F
//