ADDA_DESAP
ID ADDA_DESAP Reviewed; 1230 AA.
AC B1I493;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Daud_1276;
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Candidatus Desulforudis.
OX NCBI_TaxID=477974;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent, dual-direction single-stranded exonuclease.
CC Recognizes the chi site generating a DNA molecule suitable for the
CC initiation of homologous recombination. The AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000255|HAMAP-Rule:MF_01451}.
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:0000255|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR EMBL; CP000860; ACA59787.1; -; Genomic_DNA.
DR AlphaFoldDB; B1I493; -.
DR SMR; B1I493; -.
DR STRING; 477974.Daud_1276; -.
DR EnsemblBacteria; ACA59787; ACA59787; Daud_1276.
DR KEGG; dau:Daud_1276; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000008544; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; DNA_helicase_suAddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1230
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379268"
FT DOMAIN 4..480
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 517..799
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 535..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1230 AA; 134543 MW; CE77062C2E970E49 CRC64;
MSSRNWTGPQ EAAIGCREKN LLVAAGAGSG KTAVLVERVI RRISDPAAPV DVDRLLVVTF
TNAAAAEMRK RVAEALEREL EKHPGMPLLE HQLRLLPQAD ITTIHSFCAE LLRRYHYLID
LDPEFRVADE TEAAILRQET LEEFFEEQYR VITGDPDLEF LVEAYGGERD DLKLQNLVSG
LHRFARSNPW PEAWLARAAA FGADPQGLDG DGPLAWGLRD LVGTGLEAAV FELRAALEAA
KAPGGPAVYA DALAAEVEGT ARLAGLVAGD WEPLRAAFLA FGFTPRLPAA RAGVDQELKD
LCSRCRKKAK ERIQNLKETF FARRPEELLS EMAALGPAMR RLAALAADFG EAYRTAKLAR
NLVDFADLEH YCLQILLAPG STPEAPVPSP VAAGLREYYV EVLVDEYQDI NAVQETILRL
VSRQDAAAPN LFMVGDVKQS IYRFRLAEPA LFLEKYRAFD TGEDAGGARR IDLSHNFRSR
ESIIHAVNAV FRRIMTPAVG ELAYDTAAEL VCGGTPAQLE GSGPPVEVHL LGAPTSVGRD
TAGTADDEPD RSDEADLTAV QREARLVAGI IRRLAGLGGE CTVPYRDIVV LMRATTGKAG
TYLEEFRRQN IPAYAKVGTG YFEAVEVETV LSLLKVIDNP HQDIPLAGVL RSPLVGLGAA
ELAAVRLADK EGDFFRAVVA AAGQGGRLGA VLAGFLERLE KWRSQARCGS LADLIWDVYR
TTGYYDYVGG LPGGAGRQAN LRALYDRARQ YEATAFRGLF RFLRFIELLQ EGGQDLGPAP
ALAESENVVR IMSIHQAKGL EFPVVILADM GRRFYMPDLN GEVLLHKDLG LGPYFVDPGA
RVSHPTAAWH VVRERLRREQ LAEEMRILYV AMTRARERLI LTGSAGRLEQ AVLRWSHAAA
GDGETLPVPV LAEAESFLDW VMPVLMAHPD GEPLRRLAVR SRPAAGTPKD RSRWEVHLHR
PEDLEEAAGA DPDTAAVLES LRRLAPIPAD GGLDEAVHRA LSWHYPWSAL ASCGAKISAT
EVKRRFAAAA AGEEEVPAVF PYRAPPARPA FLETARGLSP QAFGRAMHVV LQHLDLAGDL
SVDGIRAQVA GLEEREFLTA TEARAIDAEK LAGLFAGGLG RRLAGALWVR REWPFCLVVP
AHEIYPGLEG HPEERVMVQG IIDCLFAEPD GLVLVDYKTD RVGPGGEAAL ADRYRGQLDL
YARAVEAVLR RRVKERYLFL VMTGSAQIIQ
