RECJ_THET8
ID RECJ_THET8 Reviewed; 666 AA.
AC Q5SJ47;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Single-stranded-DNA-specific exonuclease RecJ;
DE EC=3.1.-.-;
GN Name=recJ; OrderedLocusNames=TTHA1167;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION AS AN EXONUCLEASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP COFACTOR.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=21087930; DOI=10.1074/jbc.m110.161596;
RA Wakamatsu T., Kim K., Uemura Y., Nakagawa N., Kuramitsu S., Masui R.;
RT "Role of RecJ-like protein with 5'-3' exonuclease activity in
RT oligo(deoxy)nucleotide degradation.";
RL J. Biol. Chem. 286:2807-2816(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH MANGANESE, AND
RP DNA-BINDING.
RX PubMed=20129927; DOI=10.1074/jbc.m109.096487;
RA Wakamatsu T., Kitamura Y., Kotera Y., Nakagawa N., Kuramitsu S., Masui R.;
RT "Structure of RecJ exonuclease defines its specificity for single-stranded
RT DNA.";
RL J. Biol. Chem. 285:9762-9769(2010).
CC -!- FUNCTION: Single-stranded-DNA-specific exonuclease acting in a 5' to 3'
CC direction; has no detectable activity on ssRNA.
CC {ECO:0000269|PubMed:21087930}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21087930};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21087930};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21087930};
CC Note=Requires a divalent cation; Mg(2+) > Mn(2+) > Co(2+). Structures
CC with 1 Mg(2+), or 1 or 2 Mn(2+) were determined; the authors conclude 2
CC metal ions are required for activity. {ECO:0000269|PubMed:21087930};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 uM for ssDNA 6-mers {ECO:0000269|PubMed:21087930};
CC KM=0.084 uM for ssDNA 11-mers {ECO:0000269|PubMed:21087930};
CC KM=0.037 uM for ssDNA 21-mers {ECO:0000269|PubMed:21087930};
CC Note=kcat for ssDNA remains unchanged as chain length increases from
CC 6-mers to 21-mers.;
CC -!- SUBUNIT: Monomer. Intact protein binds ss- but not dsDNA.
CC {ECO:0000269|PubMed:20129927, ECO:0000269|PubMed:21087930}.
CC -!- SIMILARITY: Belongs to the RecJ family. {ECO:0000305}.
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DR EMBL; AP008226; BAD70990.1; -; Genomic_DNA.
DR RefSeq; WP_011228485.1; NC_006461.1.
DR RefSeq; YP_144433.1; NC_006461.1.
DR PDB; 1IR6; X-ray; 2.90 A; A=40-463.
DR PDB; 2ZXO; X-ray; 2.50 A; A=1-666.
DR PDB; 2ZXP; X-ray; 2.30 A; A=1-666.
DR PDB; 2ZXR; X-ray; 2.15 A; A=1-666.
DR PDBsum; 1IR6; -.
DR PDBsum; 2ZXO; -.
DR PDBsum; 2ZXP; -.
DR PDBsum; 2ZXR; -.
DR AlphaFoldDB; Q5SJ47; -.
DR SMR; Q5SJ47; -.
DR STRING; 300852.55772549; -.
DR EnsemblBacteria; BAD70990; BAD70990; BAD70990.
DR GeneID; 3168814; -.
DR KEGG; ttj:TTHA1167; -.
DR PATRIC; fig|300852.9.peg.1147; -.
DR eggNOG; COG0608; Bacteria.
DR HOGENOM; CLU_009736_5_2_0; -.
DR OMA; FIICDHH; -.
DR PhylomeDB; Q5SJ47; -.
DR SABIO-RK; Q5SJ47; -.
DR EvolutionaryTrace; Q5SJ47; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR041122; RecJ_OB.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF17768; RecJ_OB; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Exonuclease; Hydrolase; Manganese;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..666
FT /note="Single-stranded-DNA-specific exonuclease RecJ"
FT /id="PRO_0000419756"
FT BINDING 80
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20129927"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20129927"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20129927"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20129927"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20129927"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20129927"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20129927"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2ZXR"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1IR6"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1IR6"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:2ZXP"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2ZXP"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:2ZXP"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2ZXP"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2ZXP"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 293..321
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1IR6"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 377..383
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 407..419
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 440..447
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 469..484
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:2ZXP"
FT STRAND 501..514
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 517..529
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 546..554
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 566..573
FT /evidence="ECO:0007829|PDB:2ZXR"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:2ZXR"
FT TURN 582..584
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 586..590
FT /evidence="ECO:0007829|PDB:2ZXR"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:2ZXR"
FT TURN 611..614
FT /evidence="ECO:0007829|PDB:2ZXP"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:2ZXO"
FT HELIX 624..639
FT /evidence="ECO:0007829|PDB:2ZXR"
FT HELIX 643..655
FT /evidence="ECO:0007829|PDB:2ZXR"
SQ SEQUENCE 666 AA; 72865 MW; B5EDA4031A6CAA68 CRC64;
MRDRVRWRVL SLPPLAQWRE VMAALEVGPE AALAYWHRGF RRKEDLDPPL ALLPLKGLRE
AAALLEEALR QGKRIRVHGD YDADGLTGTA ILVRGLAALG ADVHPFIPHR LEEGYGVLME
RVPEHLEASD LFLTVDCGIT NHAELRELLE NGVEVIVTDH HTPGKTPPPG LVVHPALTPD
LKEKPTGAGV AFLLLWALHE RLGLPPPLEY ADLAAVGTIA DVAPLWGWNR ALVKEGLARI
PASSWVGLRL LAEAVGYTGK AVEVAFRIAP RINAASRLGE AEKALRLLLT DDAAEAQALV
GELHRLNARR QTLEEAMLRK LLPQADPEAK AIVLLDPEGH PGVMGIVASR ILEATLRPVF
LVAQGKGTVR SLAPISAVEA LRSAEDLLLR YGGHKEAAGF AMDEALFPAF KARVEAYAAR
FPDPVREVAL LDLLPEPGLL PQVFRELALL EPYGEGNPEP LFLLFGAPEE ARRLGEGRHL
AFRLKGVRVL AWKQGDLALP PEVEVAGLLS ENAWNGHLAY EVQAVDLRKP EALEGGIAPF
AYPLPLLEAL ARARLGEGVY VPEDNPEGLD YAWKAGFRLL PPEEAGLWLG LPPRPVLGRR
VEVALGREAR ARLSAPPVLH TPEARLKALV HRRLLFAYER RHPGLFSEAL LAYWEVNRVQ
EPAGSP
