ID K2BCL8_9BACT Unreviewed; 1009 AA.
AC K2BCL8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=ACD_49C00038G0057 {ECO:0000313|EMBL:EKD66523.1};
OS uncultured bacterium (gcode 4).
OC Bacteria; environmental samples.
OX NCBI_TaxID=1234023 {ECO:0000313|EMBL:EKD66523.1};
RN [1] {ECO:0000313|EMBL:EKD66523.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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 -!- 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|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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:EKD66523.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMFJ01021624; EKD66523.1; -; Genomic_DNA.
DR AlphaFoldDB; K2BCL8; -.
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; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
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; 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|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}.
FT DOMAIN 12..329
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 330..640
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1009 AA; 119478 MW; 260916C88562B0CF CRC64;
MQNTQNFEKA YSVLNTEQKN AVDSIYGPVM VVAWPGTGKT QIMALRAANI ILKTWVDPRN
ILITTFTEAG IISLKKRLFD FIGADSYKIN VSTIHSFCND VISDFPEKFL SFRAFKTIDD
IEQIEILEQI IDSGNYEALS SPYDKYHFLR SIKDSISKLK QEWIDNEQFK IIIEEQRKNY
EETLDLIDQK LKKYASEKEK SEKHILKLTE LNDIYAKYLQ ILNERWLYDF SDMIDFVLKK
FKEDQNLRLN YAEKYQFIMI DEYQDTNNAQ NEIIDLILSE SDDKNVMVVG DDDQSIYRFQ
WANLENMLYF SKKYEATKFV VLKQNYRSTQ GILDVASKSI NHNKSRISNF IPGLSKELVS
NKKFDSQPDL FICKNDIEEK AFILDQIKAL VETWEKYEDI AIIVRTNSEV ESFSDFLQTN
LIPVESKLKS NILKSRFVKL LISLIEIVVD PHKDDSKLAN ILRSPIADVN KLDILIILRK
LYNLNYKPEL KKKLFELISN FEFLTSISKP TDLQQAFFEQ EQSWIDQKIT QADKITNFVG
KILDCQAELS SNFYNFFKTI LEKFSFIEFV EKNWNFSDLE DIFTVLNYVK KLVELDKDIT
PEIFFKKISY FYKYNLTISR NILKSSIAGV QIMTAHQSKW LEFENVFLPS LLLWNWGSRK
VVDKIKLPFW IIGSTLTEDL AWAVENEEER RLFFVSLTRA KKKLTLSFPT WVDNKAKLQS
EFLQEIELTP RMVENIVLNN IVKNEFKIIS FDSLVNKEEE LYIQEFLKNY KLSASDLNKF
IEDPRIFLRD VIFKYPFEDN EFTIFGKVYH KTLEYFYLEF KKTGNPPDKN FLEKYFVWLL
NKEILSKPDF EKLKEKWITG LSGWYDNKRE FTLPLELEYN FRSKNIVFDW IPLTGKIDKI
EPANNDEVIL VDYKTGKTRS LNDIKWATQS WDGKYFRQLL FYKIMFSLDN TLASKYSVNS
LAIEFVEWKD GKYPFVNVDF REEDLDKVKE EIKEVWSKIN DLKFWRNLI
//
