ID A0A1I1WR58_9PROT Unreviewed; 1157 AA.
AC A0A1I1WR58;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN ORFNames=SAMN05428977_100392 {ECO:0000313|EMBL:SFD95923.1};
OS Nitrosomonas sp. Nm166.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=1881054 {ECO:0000313|EMBL:SFD95923.1, ECO:0000313|Proteomes:UP000199102};
RN [1] {ECO:0000313|EMBL:SFD95923.1, ECO:0000313|Proteomes:UP000199102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm166 {ECO:0000313|EMBL:SFD95923.1,
RC ECO:0000313|Proteomes:UP000199102};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FONE01000003; SFD95923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1WR58; -.
DR STRING; 1881054.SAMN05428977_100392; -.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000199102; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:SFD95923.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000199102}.
FT DOMAIN 6..491
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 503..787
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 154..198
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1157 AA; 131309 MW; 413A81D865D83CF4 CRC64;
MADTELIPDA DERYRALDPA QSFIVQAPAG SGKTALLIQR YLKLLACVDA PEEIVAITFT
RKAAAEMRTR VLAALQVEKK PIDAETAYEK LNRELVAAFL QRDCQAGWHL IENPERLRIQ
TIDSLCAALT RQMPLLSKLG AQPETTEDAA DFYLEAARAT LEQVEQNHAI ALDVERLLEH
LDNDMARVET LLAEMLAQRD HWLRHIYGKT REELEASLQN SRRNALQFVF RLFPAAMHDE
LLALLRYAAA NLVAIGKSSI ISHCDQLDTL SASNVEHWCG IAELLLTKNG TWRERISANE
GFPPGNTKTE KDAAKAWKNR LEILINSLSS EETLRQALHA MRQLPPPYYS DKQWEILDAI
TRLLPHAVAQ LKIIFQSKGK VDFSEVAQRA LLALGDSESP TDLALALDYR IKHLMIDEFQ
DTSISQFKLI EKLIAGWEAG DGRSLFVVGD PMQSIYRFRE AEVGLFLQTR NVGIGNLVLQ
PIILRANFRS QQRIIDWVND TFSQILPTCE DIATGAVAYA PSIGIHPALT GDAVKIHPFF
EKDHAAEARQ VVEIIMQTRR DDPTATIAIL VRNRNHLSEI VKRIRAAGLC FRAIDIELLH
HKPVVQDLLA LTRVLVNPAD RLAWFALLRA PWCGLLLKDI AALAGIEQKE NDCGAITQET
TVWELMCDES RWHAISADAI VRIRRLREVL KLCMNHRQRQ SLRITVEAVW QVVGGPGCIN
PMAGDKDQII SSLDDARIYL DYLENREEAG NIQDLAAFER GLSELYASPD LQADDTLQIM
TIHKAKGLEF DTVIVPGLGR VSRKNDKQLL KWIEQPHNKA MNGENAPIAD LLLAPIQETG
TGADSIYRWL DKLEHDKEQF EADRLLYVAA TRAKKFLHLM GNVNLIPDTD GKLIPQKPLT
GSLLSRLWSR VQSIYRDAAE QNNAAGNCQS EDQSYEITIR NIKNQNIYRL RTEWVLPAAP
QSVTWQERQS NPHLREEIEF SWASEMARHV GNVAHRWLQQ IAEDEMRDWS PARLQGMRNQ
FRQNLFADGM SGNNKEMEYA VERVILTLTN ALNDKRGQWI LGPQRLAQNE LKISGIIDNT
PVSWVIDRTF CDSNGDRWIV DYKVSSHEGS DIQGFLDREQ MRYHHQLNCY AKLMQQIDSR
PVRLGIYFPL ICGWREW
//
