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Database: UniProt
Entry: U2YUY2_9EURY
LinkDB: U2YUY2_9EURY
Original site: U2YUY2_9EURY 
ID   U2YUY2_9EURY            Unreviewed;       414 AA.
AC   U2YUY2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=DNA repair and recombination protein RadB {ECO:0000256|ARBA:ARBA00018143, ECO:0000256|HAMAP-Rule:MF_00350};
GN   Name=radB {ECO:0000256|HAMAP-Rule:MF_00350};
GN   ORFNames=MBEHAL_1575 {ECO:0000313|EMBL:GAD52815.1};
OS   Halarchaeum acidiphilum MH1-52-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae.
OX   NCBI_TaxID=1261545 {ECO:0000313|EMBL:GAD52815.1, ECO:0000313|Proteomes:UP000016986};
RN   [1] {ECO:0000313|EMBL:GAD52815.1, ECO:0000313|Proteomes:UP000016986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16109 {ECO:0000313|EMBL:GAD52815.1,
RC   ECO:0000313|Proteomes:UP000016986};
RA   Shimane Y., Minegishi H., Nishi S., Echigo A., Shuto A., Konishi M.,
RA   Ito T., Ohkuma M., Ohta Y., Nagano Y., Tsubouchi T., Mori K., Usui K.,
RA   Kamekura M., Usami R., Takaki Y., Hatada Y.;
RT   "Whole genome sequencing of Halarchaeum acidiphilum strain MH1-52-1.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in DNA repair and in homologous recombination. May
CC       regulate the cleavage reactions of the branch-structured DNA. Has a
CC       very weak ATPase activity that is not stimulated by DNA. Binds DNA but
CC       does not promote DNA strands exchange. {ECO:0000256|ARBA:ARBA00024641,
CC       ECO:0000256|HAMAP-Rule:MF_00350}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family. RadB
CC       subfamily. {ECO:0000256|ARBA:ARBA00006876, ECO:0000256|HAMAP-
CC       Rule:MF_00350}.
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:GAD52815.1}.
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DR   EMBL; BATA01000036; GAD52815.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2YUY2; -.
DR   eggNOG; arCOG00417; Archaea.
DR   Proteomes; UP000016986; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00350; RadB; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR   InterPro; IPR011939; DNA_repair_and_recomb_RadB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   NCBIfam; TIGR02237; recomb_radB; 1.
DR   PANTHER; PTHR22942:SF47; DNA REPAIR AND RECOMBINATION PROTEIN RADB; 1.
DR   PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1.
DR   Pfam; PF08423; Rad51; 1.
DR   PRINTS; PR01874; DNAREPAIRADA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00350};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00350};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00350};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00350};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00350}.
FT   DOMAIN          182..345
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   REGION          1..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  43819 MW;  5699CC66E8E2B101 CRC64;
     MIRVPWSRAP SPTRTMGSGA SRTSSSTTSA ASSTGTWKTA TTRSPERTAM PGRGPGSTPT
     TVRPPPRRTV KASSTAARGS SGSATTTSRG TSSSSSGPAM TTSASAGRGS PGSTVVNAAP
     RSRSSPTTSW YTSKSAVATT ITREGRASGE KKPSRARPAR RVGNGRARPS ARFSAAVRYW
     RPMEPLTTGC APLDDLLGGG VERGAVTQVY GPPAAGKTTV ALAAAAHVAA SGGTAVYVDT
     EGLSPDRFEQ VLSAVADDPD AAAERIVVSE ARDFDEQAEA VKDVEEFAER ADLVVLDSAT
     GFYRLRRTEA GSESGEALRE VARQITHLLS LARRHDLAVL VTNQVYTDPD ADRTRPLGGH
     TLEHWTATVV RLERFRGDVR RAVLEKHRAK PRGERTRFEI TERGIEAASE EVEF
//
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