ID   HERA_PYRFU              Reviewed;         551 AA.
AC   Q8U1P0;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=DNA double-strand break repair helicase HerA {ECO:0000305};
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:F2Z5Z6};
GN   Name=herA {ECO:0000303|PubMed:18957200};
GN   OrderedLocusNames=PF1165 {ECO:0000312|EMBL:AAL81289.1};
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH NURA.
RX   PubMed=18957200; DOI=10.1016/j.cell.2008.09.054;
RA   Hopkins B.B., Paull T.T.;
RT   "The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA
RT   double-strand break.";
RL   Cell 135:250-260(2008).
CC   -!- FUNCTION: Involved in DNA double-strand break (DSB) repair
CC       (PubMed:18957200). Acts probably with NurA to stimulate resection of
CC       the 5' strand and produce the long 3' single-strand that is required
CC       for RadA loading (PubMed:18957200). Exhibits DNA-dependent ATPase
CC       activity and DNA helicase activity (By similarity) (PubMed:18957200).
CC       {ECO:0000250|UniProtKB:F2Z5Z6, ECO:0000269|PubMed:18957200}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:F2Z5Z6};
CC   -!- ACTIVITY REGULATION: Helicase activity is stimulated in the presence of
CC       NurA. {ECO:0000269|PubMed:18957200}.
CC   -!- SUBUNIT: Homohexamer (PubMed:18957200). Interacts with NurA
CC       (PubMed:18957200). {ECO:0000269|PubMed:18957200}.
CC   -!- SIMILARITY: Belongs to the HerA family. {ECO:0000305}.
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DR   EMBL; AE009950; AAL81289.1; -; Genomic_DNA.
DR   RefSeq; WP_011012305.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U1P0; -.
DR   SMR; Q8U1P0; -.
DR   STRING; 186497.PF1165; -.
DR   EnsemblBacteria; AAL81289; AAL81289; PF1165.
DR   GeneID; 41712973; -.
DR   KEGG; pfu:PF1165; -.
DR   PATRIC; fig|186497.12.peg.1225; -.
DR   eggNOG; arCOG00280; Archaea.
DR   HOGENOM; CLU_023842_2_0_2; -.
DR   OMA; EPNDQRY; -.
DR   OrthoDB; 33242at2157; -.
DR   PhylomeDB; Q8U1P0; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR008571; HerA-like.
DR   InterPro; IPR018538; HerA_barrel_dom.
DR   InterPro; IPR033186; HerA_C.
DR   InterPro; IPR002789; HerA_central.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42957; PTHR42957; 1.
DR   Pfam; PF05872; DUF853; 1.
DR   Pfam; PF01935; DUF87; 1.
DR   Pfam; PF09378; HAS-barrel; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA repair; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..551
FT                   /note="DNA double-strand break repair helicase HerA"
FT                   /id="PRO_0000434023"
FT   BINDING         152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT   BINDING         161..166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT   BINDING         507..508
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97WG8"
SQ   SEQUENCE   551 AA;  61823 MW;  6E2042F7FA1ED2E2 CRC64;
     MEEFVGIVRG EASFTSYEFS INPSANVSFG EFVVTKNRDG DLVLGTVRHV KNVNWLLSSV
     KSNFNSLALD IEEYGESLGE NEEVVATVRI LGKIEGNELV PNRVPIRNGE YVYKASDDLL
     QMIYGNDGIE IGTLLLRPNV RIKLDVNELV SRHFAVLAVT GAGKSNAVAV IIKGIVEDVG
     GTVVVLDPHG DYVNLRLPET GIDLVNIIDG KIRIEDLDPE ELADLIGISS SAQIQRHFLS
     LAWETVKHKN QSLGGESLLE ALLDLLNEWI SRKTIKYWSE KEGRMKSEDL KSERIETIRG
     IIFRIRRFLR NYGNIVTSEN LVAAIKPGMV NVIDLSPLDE NQMKVVVGKF LEAVFEKRVE
     YEMARKRFEK ETSKKKRDEY EEIMTEIESK YPALAYPILV IVEEAHIFAP QGEENDAMRI
     MGRIAREGRK FGVGLGVVSQ RPSKLNEDIL SQMNTKIILR IVNPRDQDYV LKASEQLSKD
     LMDDIAGLGK GEAVIVGQAI KLPALVRIYN FKELRGKAGT GQYGGEDIGI LDRWNKMKRN
     MVNSLDIDID F