ID A0A1I1AAZ1_9BACL Unreviewed; 1441 AA.
AC A0A1I1AAZ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000256|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000256|HAMAP-Rule:MF_01451};
GN ORFNames=SAMN05216312_106184 {ECO:0000313|EMBL:SFB35161.1};
OS Cohnella sp. OV330.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFB35161.1, ECO:0000313|Proteomes:UP000198686};
RN [1] {ECO:0000313|EMBL:SFB35161.1, ECO:0000313|Proteomes:UP000198686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV330 {ECO:0000313|EMBL:SFB35161.1,
RC ECO:0000313|Proteomes:UP000198686};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC Rule:MF_01451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000256|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01451}.
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DR EMBL; FOKE01000006; SFB35161.1; -; Genomic_DNA.
DR Proteomes; UP000198686; Unassembled WGS sequence.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
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:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01451};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01451};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01451}; Reference proteome {ECO:0000313|Proteomes:UP000198686}.
FT DOMAIN 73..571
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 635..933
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 651..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1441 AA; 156359 MW; 43C3A7637434E777 CRC64;
MSESRGNGND EQLAFDWGGL FDDVGRRDEA DDRTASGDGA AEDGMAEAAN VGGLASFAGG
DGLAATYARP EGSRWTAEQW AAIAAGGRHL LVAAAAGSGK TAVLVERIIS RIADERDPLD
VDALLVATFT KAAAAEMKER IRTALELKLE QSPGSAHLRR QLALLPRASI TTLHSFCMEA
VQRYAPLIGL DPGFRIANET EAELLRMDTL DELFETRYEE ELALGEDGTL ATLADMYGGQ
RSDEPLHRLV LELFDFSRSH PWPDAWLRAT AASFDIRGEA ELASSPWVQS MRADVLLALS
GAAGLLRGAW ELASAPGGPE PYASTLAEDA ALVAALTETV ADRPWTAWRE PFASASFGRL
KACRGDGYDP ELQERVKRMR DEAKKTVTRL AEEWFVRSPA QYAEELAALA PRMREIAELV
IAFGDKYEAA KREKGLLDFG DLEHYALRIL RATDSSPHAV RPSDAALAYR ERFREILLDE
YQDTNEVQEA IVSLIARTDP GNVFMVGDVK QSIYGFRLAE PGLFLAKYKT YDVWTPQGPE
SAGGGAAANG EGASGGGDGL RIDLARNFRS RSRVLDAVNH VFRLIMREPV GEMDYDRRAE
LIYGEGYPAE EAGAEVLGKE EMPSYAVEML LIDTGAGSGG ARRVEVAAAD PGADSAGAAG
GSEEGADADE EELESAQLEA RCIAAGIAKL TGTDGSGRPP FAVYDGRSGL HRPLAYRDII
ILLRAATSLA PVVLEELRSA GIPAYADLAT GYFAAVEVDV MLSLLHIIDN PDQDIPLAGV
LRSPIVGLSA DELAAVRIAD RAGSFWSAVR TAAVDAEDES LRERIAAFVQ SLEGWRTFAR
REPLGELLHA LYRDTGYFDF VGGLPGGGQR QANLRALIDR ARQYERNSSY RGLFRFLRFL
GRMRDTGGDL GAARAVGEQE DVVRVVSIHK SKGLEFPVVF VAGLGRRFNR QDLSGMFLRH
KKLGFGPRMV ERVTRVSYPT LPQLAIRRRM KAELLAEEMR VLYVALTRPK EKLILVGTTK
DALSDLDHWR RTAADATDRL QDHAVAAAGR YLDWLGPASI LTGADWLAGG SSGAAGPNEA
AAQAAAGGEA AAFRTSRSPA PAAWTCRVLP SRALLSPKAQ ELTAMEGEPL WNLATRLEPL
PGPVSPAGEA AYAALSWQDP HAAASRAAAK TSITAMKSAR DFDGAGRPAA GSAAGERTPT
LEAVQEFAAL QNGSDAEGFM EPQDSAQMPD LEEMRHPAWN PEEVPDSGYW TYRLRRPKFM
AARRMSAAER GTAVHLVMQH LPIGLSPNRA EAEVAALLER LIAQLILTQE QREAAERVDI
ASFFRTELYA RMGRAARLWR EWPFSAGIPA AEAHPSADAD DLKGETVLIQ GVLDCLFDDG
ERLVLVDYKT DAVPDRDWQA AAEKHRFQME MYARAVEGIM GRKVDEGHIY FVEGGVGVQL
Y
//
