ID D4VQT5_9BACE Unreviewed; 1603 AA.
AC D4VQT5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BN890_17020 {ECO:0000313|EMBL:CDM04128.1};
OS Bacteroides xylanisolvens SD CC 1b.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=702447 {ECO:0000313|EMBL:CDM04128.1, ECO:0000313|Proteomes:UP000019380};
RN [1] {ECO:0000313|EMBL:CDM04128.1, ECO:0000313|Proteomes:UP000019380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ramaraj T., Sundararajan A., Mudge J., Schilkey F.D., Delvecchio V.,
RA Donlon M., Ziemer C.;
RT "Improved hybrid genome assemblies of Bacteroides xylanisolvens SD CC 1b
RT and Bacteroides xylanisolvens SD CC 2a using Illumina and 454 Sequencing.";
RL Submitted (DEC-2013) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDM04128.1}.
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DR EMBL; CBXG010000019; CDM04128.1; -; Genomic_DNA.
DR RefSeq; WP_004316576.1; NZ_ADKP01000199.1.
DR Proteomes; UP000019380; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 274..454
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 484..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1049..1412
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT BINDING 1070..1077
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1603 AA; 184865 MW; 38AD1697D08799D6 CRC64;
MTNITFIDLE VNPVNRQISD MGAIRNDGAS FHANSPAQFI QFITQTEYIG GHNILNHDLK
YIIPLFQQTG YIQPKAIDTL YLSPLLFPAK PYHHLLKDDK LQTDSLNNPL NDSMKAHELF
LAEVEAFGRL DEDLKYIYYS LLHPTDEFKS FFDFIAYTIP FGKYDNPETV IRRRFAKEVC
EHAPLENYIS RAPIELAYCL ALINCRDRYS ITPPWVLHNF PKVESIMYVL RNTPCLTGCN
YCNKAFDIHR GLKHFFGFDA YRTYNNQPLQ ENAVQAAVEG KSILAVFPTG GGKSITFQVP
ALMSGEQVKG LTVVISPLQS LMKDQVDNLR KNDITSAVTI NGLLDPIERA KSFENVENGF
ASILYISPES LRSRSIERLL LGRKVVRFVI DEAHCFSSWG QDFRVDYLYI GDYLKQLQEK
KGLQQPIPVS CFTATAKQKV IEDISTYFKD KLNIRLELFR SDISRTNLQY QVFERNQENE
KYNSLRDIIE QKSCPTIVYV ARTRTATKLA ARLKQDGFSV AAFHGKMDIK DKTENQNDFI
AGNIQIMVAT SAFGMGVDKK DVGLVVHYEI SDSLENYVQE AGRAGRDEHI NASCYILFDE
EDLNKHFILL NQTKLHIGEI QQVWKSIKEI TRLRPKVSQS VLEIARKAGW DENVTNIETR
VTTAIAALEE SGYLHRGQNS PRVFADSILA KTAQEAIDKI NLSPRFNEKQ KMQATRIIKK
LISTKSRKHA NSEVPESRID YISDHLGISN EEVIQIITLL REEKILADSR DLTAYILRKE
QCNRSLEIIR FYNKLENFLL TVFEEEQKIV NLKELREEAE NAIQRNVSPD KLKALINFWA
EKNWIKRSYR DDNRNHISVY LRPQTGIPFE KRCENRHCLS EFIIDYLFNK IESDTESVTR
EEILVEFSIL ELKKAYENQN VLFQESVTLE EIEDTLFYLS RMGALQIEGG FLVIYNRMNI
ERLGATNIRY KQDDYRKLEQ FYTNKIQQIH IVGEYARKMV HDYQAALRLV DDYFSLNSTS
FIQKYFPGSR KDEINRRITP GKYRQLFGEL SKTQLEIVND NQPGHIVVAA GPGSGKTRLL
VHKLASLLLM EDVKHEQLLM LTFSRAAANE FRSRLHDLIG NAVGYIEIKT FHSYCFDLLG
RQGSIEKSKS VIKDAVEKIR NSEVEISRIT KSVLVIDEAQ DMTEDEFALI AALIEKNESL
KVIAVGDDDQ NIYAFRNSDS RHMQSLITNY QARHYELCEN FRSRSNLVAF ANAFVNLIPH
RMKHTPIQAH QLEKGSIRIT QYQSDNLIVP LIKDVLESPL AGTTGILTKT NEDAVFIACL
LQEQGMPVRL VQTNSGNFYL GDLDEIRYFN RALDLSQDTH LIDDERWETA KRCLKREFGH
AQSWEICRNI ILNFEQVYSR KYHSDWTNYL FESKLEDFYP VQGEAIVVST IHKAKGKEFD
NVFLLLTNIE SLSDEKKREV YVAITRAKQN LSIHTNGHYL SNIANGLAEY RINSNTYPAP
QSLCYTLTHR DLWLDFFIDS HCQAAINTLK SGMSLRLTEK GCTDFSNNEI LRFSKKFKDI
LNELIQKDYK LEKASVNFVV YWEKQEDKKE AKIVLPKVVF KKV
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