ID A0A2K3UXV4_9DEIO Unreviewed; 301 AA.
AC A0A2K3UXV4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CVO96_08205 {ECO:0000313|EMBL:PNY81370.1};
OS Deinococcus koreensis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2054903 {ECO:0000313|EMBL:PNY81370.1, ECO:0000313|Proteomes:UP000236379};
RN [1] {ECO:0000313|EMBL:PNY81370.1, ECO:0000313|Proteomes:UP000236379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJW1-2 {ECO:0000313|EMBL:PNY81370.1,
RC ECO:0000313|Proteomes:UP000236379};
RA Choi A.;
RT "Deinococcus koreensis sp. nov., a radiation-resistant bacterium isolated
RT from river water.";
RL Submitted (JAN-2018) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00984}.
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:PNY81370.1}.
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DR EMBL; PPPD01000001; PNY81370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3UXV4; -.
DR OrthoDB; 9809878at2; -.
DR Proteomes; UP000236379; 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; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
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; 2.
DR PANTHER; PTHR10302; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR PANTHER; PTHR10302:SF27; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR Pfam; PF00436; SSB; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR PROSITE; PS50935; SSB; 2.
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:UP000236379}.
FT REGION 232..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 296..301
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT COMPBIAS 244..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 32600 MW; EFF80489F120593B CRC64;
MARGMNHVYL MGALARDPEL RYTPNGTAVF EATVAGEDHI VGMDGKERKL PWYHRVSILG
KPAEWQAERN LKGGDAVMVE GSLEYSQWEA PEGGKRSMVR VKALRMEQLG YQPELVQDAG
GGVRMGSGMN EVIMIGNVTR DPDLRYTPAG DAVLGIGLAV NESWTDRQGQ KQEKTHWIDV
TLWRELAEAM KDLKKGDPVV VQGRLVNEAW TDKDGNKRNS TKVEATRVEA LSRGAAAGQS
GYAASPATPR TQTASSAARP QASRAQPARA ATASAGGNRS GGLDIDQGLD DFPPEEEDLP
F
//