ID A0A1V1RGZ1_9ACTN Unreviewed; 955 AA.
AC A0A1V1RGZ1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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};
GN Name=uvrD {ECO:0000313|EMBL:GAV31784.1};
GN ORFNames=emb_1d0614 {ECO:0000313|EMBL:GAV31784.1};
OS Coriobacteriaceae bacterium EMTCatB1.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae.
OX NCBI_TaxID=1927122 {ECO:0000313|EMBL:GAV31784.1, ECO:0000313|Proteomes:UP000191049};
RN [1] {ECO:0000313|EMBL:GAV31784.1, ECO:0000313|Proteomes:UP000191049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EMTCatB1 {ECO:0000313|EMBL:GAV31784.1};
RA Kobayashi H., Fu Q., Maeda H., Sato K.;
RT "Draft genome sequence of a novel Coriobacteriaceae sp. strain EMTCatB1
RT reconstructed from the metagenome of a thermophilic electromethanogenic
RT biocathode.";
RL Submitted (DEC-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};
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:GAV31784.1}.
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DR EMBL; BDLO01000001; GAV31784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1RGZ1; -.
DR STRING; 1927122.emb_1d0614; -.
DR Proteomes; UP000191049; 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: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; 3.
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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000191049}.
FT DOMAIN 14..307
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 316..594
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 955 AA; 109810 MW; 27F148E86E47169B CRC64;
MQLELHQAIE EHFPTLNDDQ RRVVGTLEGP LLVIAGPGSG KTLCLVLRTL NALLLGKAEP
SEIILCTFTE KAALELRDRL AEAASLCGYQ SDLTSLRTGT IHSICNALIQ EYRHHTPLGA
GFETLDDLTQ LLFIYENFTE LLGEGAEPPY LGKWGSKWDT IRRLTERFNK LTEELVDPAA
LIADPDPYIA ELGRVFDRYG QLLLERNRVD FSHQQKVAWQ LMQEPLVREQ VAGRIRYVMV
DEYQDTNYVQ EQLMLDLSSL AGNLCVVGDE DQALYRFRGA TVRNILEFAK RFPECPVVKL
QTNYRSHRDI IAAYDRWMAS AQWQDRSGQR YRYDKTIAPP KGEKFAHYPA VFQIWGTSAR
DEAERFADLV VFLKDNEVIE DYNQVALLMY SVQKKYSSPF IEALKRRGIP AFCPRARTYF
ENEEVRLMVA CLATVLGFYE DGQGEGGGRN AESMRAYVDE CLVELAAAVQ GSPGLQRRLQ
EFSAQVEALR DRDSLDVRLA DVFYRLLGEE PFVSFVKDEN RARNLAMFSS MLSTLQAYYH
LNVITGRNKQ YMKFALFGSM LPVIFGAGMN EFEDKDAPFP SGYVQIMTIH QSKGLEFPVV
AVDSLTATAG VAKQVDQELS RFYHREPYEP AGMITEFDNM RLFYVAFSRA QNLLVLSSHE
RPHARFAPIW DDLQQWPHVD RETLAKQRWN ARERKGPKRR FSFTGDLKIY ETCPRQYEFF
RHYDFTPSRS ATIFFGLLVH QTIEEIHRLV LEGRLGELDD ARITQLFEKT YGLLTLQDVR
PVGEEAKQAA LEQVKRYVRL NRDTMARVEE TEVDVSVEKN GYILHGVVDL LLGADGKLEV
LDFKASKRPD DGDPILRDYE RQLCTYAHIL ERRHGRRPDR LLLYWTGEES RERALMEFPY
REELVAEAAE HFDEVVRRIL ARDFCVSERP DSSICKECDV RPVCVADCLM ERVEA
//
