ID B7IG33_THEAB Unreviewed; 975 AA.
AC B7IG33;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Single-stranded-DNA-specific exonuclease RecJ {ECO:0000256|ARBA:ARBA00019841};
GN OrderedLocusNames=THA_559 {ECO:0000313|EMBL:ACJ75047.1};
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=484019 {ECO:0000313|EMBL:ACJ75047.1, ECO:0000313|Proteomes:UP000002453};
RN [1] {ECO:0000313|EMBL:ACJ75047.1, ECO:0000313|Proteomes:UP000002453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B {ECO:0000313|EMBL:ACJ75047.1,
RC ECO:0000313|Proteomes:UP000002453};
RX PubMed=19124572; DOI=10.1128/JB.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(2009).
CC -!- SIMILARITY: Belongs to the RecJ family.
CC {ECO:0000256|ARBA:ARBA00005915}.
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DR EMBL; CP001185; ACJ75047.1; -; Genomic_DNA.
DR RefSeq; WP_012579648.1; NC_011653.1.
DR AlphaFoldDB; B7IG33; -.
DR STRING; 484019.THA_559; -.
DR KEGG; taf:THA_559; -.
DR eggNOG; COG0608; Bacteria.
DR HOGENOM; CLU_009736_3_0_0; -.
DR OrthoDB; 9809852at2; -.
DR Proteomes; UP000002453; Chromosome.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 3.10.310.30; -; 1.
DR Gene3D; 3.90.1640.30; -; 1.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR041122; RecJ_OB.
DR PANTHER; PTHR30255; SINGLE-STRANDED-DNA-SPECIFIC EXONUCLEASE RECJ; 1.
DR PANTHER; PTHR30255:SF2; SINGLE-STRANDED-DNA-SPECIFIC EXONUCLEASE RECJ; 1.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF17768; RecJ_OB; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:ACJ75047.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:ACJ75047.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722}.
FT DOMAIN 78..227
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 315..434
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
FT DOMAIN 449..545
FT /note="RecJ OB"
FT /evidence="ECO:0000259|Pfam:PF17768"
SQ SEQUENCE 975 AA; 112642 MW; 38325CEFB8B116F6 CRC64;
MKWELKKFNK ELAQKISEEL SLPFLTSQLL VTRGYTDFEE IEKFLYPSKK HLRSPFLLKD
MDKAVRYLLE AREKKLPVFV YGDYDVDGIT GVATLVTFLS KYGWKVDYYI PNRLDEGYGI
QPQVVEEYFK KGYRVLLSVD CGITSFEAVE KARELGMYVI ITDHHTIKDK IPEAHAVVDP
KREDETYPFR DFAGVGVAYK LISAVAQELG IPGDEVDEVL DIVALGTIAD MVDLVDENRY
IVKEGLKRLN ATNRIGLLQL MKKLNITNIS SQDIGYRLAP KLNAAGRLYS AEDAYKLIMT
DNISSAEQLA EMLMGYNFTR QEIENKIFKE AIEKIEHSKI KDLPILIVSG DNWHAGVLGI
VATKLVQKYN KPSLVVSLEN GIGRGSGRSV DGVNILEVLS DFASYFEEFG GHPMAIGFSI
KNEKIPELIE AISEKFGNTF FEVDSKIEID SILEVDDIND EIIDSLRYLE PFGHGNPEPV
FLIKDSIVDR IRFFGNTNSN VRMILKGKNK QTVEGIGFGL RKNYYDIPAI QAFLTSLDVV
ANIRKNGVGP ILNILDFKIS SIHEEDYNDK YFIYSFTNDW KSQKEEEFKH FGVFDELSQR
YEKVEKYLHI QRPFVLQMDP MTRNAFLMLL MQKGRTLIVN PNNIEALHVD ESLSRHSPKD
LSFVNSLNRK ISNHVITNAV MIVEEQIPVD DFDFIVLNEI HILSALSTEM YEKLLEKLKK
EKLIITSLYK FDTNIPLYSE ERKLNFGLED RRNSKKTIDY DVDSIAFLFS NYNYVTKFYE
KLITKGYKFK DLVFYSPILE DFQKKAISTL IKKGRIKKLV SSTNSDGLPS MLPNGSEIRL
FDFPLSVKEL IDAVSGDSYT ILQLYYNEED AKKRMEHLKK LFPENLENAV KGFFENNIKN
KEEFLNFSNN VSISPKILNQ AIKDYKERKK ILRNIEREFE LRYFERYTMF LLNNSIKDIY
KMIEERDMYD TYLEI
//
