ID A0A1C2HQQ5_9RHOB Unreviewed; 806 AA.
AC A0A1C2HQQ5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BFP70_07870 {ECO:0000313|EMBL:OCX66027.1};
OS Thioclava sp. SK-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX66027.1, ECO:0000313|Proteomes:UP000094269};
RN [1] {ECO:0000313|EMBL:OCX66027.1, ECO:0000313|Proteomes:UP000094269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-1 {ECO:0000313|EMBL:OCX66027.1,
RC ECO:0000313|Proteomes:UP000094269};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Thioclava sp. strain SK-1.";
RL Submitted (AUG-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:OCX66027.1}.
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DR EMBL; MDHA01000032; OCX66027.1; -; Genomic_DNA.
DR RefSeq; WP_066010793.1; NZ_MDHA01000032.1.
DR AlphaFoldDB; A0A1C2HQQ5; -.
DR STRING; 1889770.BFP70_07870; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000094269; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 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; 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; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000094269}.
FT DOMAIN 30..310
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 311..612
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 806 AA; 89699 MW; F06AF0128D85F008 CRC64;
MNSYDDDPYE AAMSLSQRAM MSARPTPYMD GLNSAQRDAV ETMDGPVLML AGAGTGKTKA
LTCRIAHLIH SAKARPNEIL AVTFTNKAAR EMKDRIGALL GGSIEGMPWL GTFHSVCVKL
LRRHAELAGL KSNFTILDTD DQIRLLKQLI IAANMDEKRW PARQLAGLID GWKNKALTPS
KVTGGETAAF DSRGSELYAL YQDRLRALNA VDFGDLLLHM VTIFQAHPDV LAQYQRWFRY
VMVDEYQDTN VAQYLWLRLL AQGHKNICCV GDDDQSIYGW RGAEVGNILR FEKDFPGAKV
VRLEQNYRST EHILGAASGL IAGNEGRLGK TLWTEQKGGE KLRLIGHWDG EEEARWIGEE
AEALSRGTRG LDPQRLNNQA ILVRASHQMR AFEDRFLTIG LPYRVIGGPR FYERMEIRDA
MAYFRLAIQP EDDLAFERII NTPKRGLGDK AQQKIQIAAR SNGLSLLDGA RLVLQAGDIG
GKGGNQLRAF VDNIDRWHAD ILGASSATAR SPADDEDELF EVMEDAVPPA NDHSHLRLAE
QILEDSGYVA MWQNDKTPEA PGRLENLKEL IKALEQFENL QGFLEHVALI MDNSSEETDD
KVTLMTLHGA KGLEFPVVFL PGWEDGLFPS QRSMDESGMQ GLEEERRLGY VGITRAEEIC
YISFAGNRRV YGQWQTQMPS RFIDELPAQH VDVMSPPGLG QKNYGSTMGN QIDERAAKAD
VYNSPGWKRL QSRGASQPKS PSRPGRYDVD AIAFEIGARV FHKKFGYGEV MGSEADKLIV
EFDKAGTKKL LASFVVSADA AGDVPF
//