ID A0A109QXQ1_9MICO Unreviewed; 1098 AA.
AC A0A109QXQ1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=AWU67_03035 {ECO:0000313|EMBL:AMB60302.1};
OS Microterricola viridarii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microterricola.
OX NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB60302.1, ECO:0000313|Proteomes:UP000058305};
RN [1] {ECO:0000313|EMBL:AMB60302.1, ECO:0000313|Proteomes:UP000058305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB60302.1,
RC ECO:0000313|Proteomes:UP000058305};
RX PubMed=26854947; DOI=10.1016/j.jbiotec.2016.02.011;
RA Himanshu, Swarnkar M.K., Singh D., Kumar R.;
RT "First complete genome sequence of a species in the genus Microterricola,
RT an extremophilic cold active enzyme producing bacterial strain ERGS5:02
RT isolated from Sikkim Himalaya.";
RL J. Biotechnol. 222:17-18(2016).
RN [2] {ECO:0000313|Proteomes:UP000058305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS5:02 {ECO:0000313|Proteomes:UP000058305};
RA Kumar R., Singh D., Swarnkar M.K.;
RT "First complete genome sequence of a species in the genus Microterricola,
RT an extremophilic cold active enzyme producing strain ERGS5:02 isolated from
RT Sikkim Himalaya.";
RL Submitted (JAN-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; CP014145; AMB60302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109QXQ1; -.
DR KEGG; mvd:AWU67_03035; -.
DR Proteomes; UP000058305; Chromosome.
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:0016787; F:hydrolase activity; 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; 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:SF55; DNA HELICASE; 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}; 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};
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:UP000058305}.
FT DOMAIN 14..347
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 348..673
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1098 AA; 118809 MW; A71C3B5B4E4BCC50 CRC64;
MGAAALALAL ELPPPTPEQI AVIEAPPGGQ AIVVAGAGSG KTETMANRVV WLLANGHAAV
PEVLGLTFTR KAAGELAVRI RERVEQLVQA GIADVKIDIF ETASVSTYNS FASAIYRENA
MLIGREPDAV VLGEASAWQL ARQVVSDTAD PRLVEIDKRL DAVTGGVLTL SRSLAENVVD
VRDVHAMVRD FTDMADLPIG GTGRKKTPHA SFTSALEAVG GLPPLLDLAE RFQAEKRRRG
FVEFSDQVAL ALEVCERNPA VTAGYRERYK AVLLDEYQDT SVVQTRLLAA LFGGHGVMAV
GDPDQSIYGW RGASAANLAR FSRDFRGSGD DAAEAERFEL SISWRNPRAV LAAANEIVRP
FTIQEGEAQP GDTPPKSPLT APSFASDGLL DVSFTETVED EAAAVAEWFA QRLGQGTGKA
DGTKRSAAML CRSLGKISVF TEALRERGVP FHVLGLAGLL DQPVIVDLVS ALRVLHDPSR
GSELLRVLAG ARWNIGPKDL HALGKLAGEL AQRDHSLAKL SDEVRARLRG SVADDEGRSI
VDALDFLVTA REGHGLVRGF SEVGLARLKE AGDQLIGLRR RAGLELLDLV TLVQQELLLD
IEVAANGIRP LGGASLEAFD ELVSGFLAAS EHSSLGAFLG WLEEAEQRDR LAPRQEEPEP
GTVQILTIHG SKGLEWDVVA VPRMVVDEMP GKPRSTLGWL AFAELPFEFK GDAAELPELA
WRGVHDQTQF DESVTDFKEQ NAAHFAAEQR RLAYVAVTRT KSELLLSGSW WWGQKGARGP
SMFLRELAVA GLIDPELLPG SPEEAENPRS EHSVPPEWPL HPLGVRGQAV LNAAALTQTA
VDSGSGAPIP ERLRAEIDAL LEERRRRMQG RAALALPTRI PASRFKDFIA DPAAVAEQLR
RPMPQRPYRA TRLGTLFHSW VEQRSSAVPS GDTLDAGLFE LEGIDLDSFG DDAAGDSLFE
SELVGSELEG TEAEQFARLR ATFEASPWAG LAPEDVEVEI HLVLDAQVFI CKLDAVYRTA
QGYQIVDWKT GKAPKNAADL ALKQTQLALY RLAYSRWKGV PVEQIDAVFY FVADDVVIAP
EHLAGEHELL ELWAGVTA
//