ID A0A2T6B0V4_9RHOB Unreviewed; 792 AA.
AC A0A2T6B0V4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=C8N44_10692 {ECO:0000313|EMBL:PTX49714.1};
OS Allosediminivita pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Allosediminivita.
OX NCBI_TaxID=1267769 {ECO:0000313|EMBL:PTX49714.1, ECO:0000313|Proteomes:UP000244069};
RN [1] {ECO:0000313|EMBL:PTX49714.1, ECO:0000313|Proteomes:UP000244069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29329 {ECO:0000313|EMBL:PTX49714.1,
RC ECO:0000313|Proteomes:UP000244069};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTX49714.1}.
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; QBKN01000006; PTX49714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6B0V4; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000244069; 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:UP000244069}.
FT DOMAIN 29..309
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 310..584
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 792 AA; 88318 MW; EAD662B06F70A7F4 CRC64;
MSSFDDMDAF EAASLSARAM AARPAPYLDS LNPAQREAVE HLDGPVLMLA GAGTGKTKAL
TTRIVHLLNT GRARPNEILS VTFTNKAARE MKSRVSATLG QTVEGMPWLG TFHAICVKLL
RRHAELVELK SNFTILDRDD QIRLLKQLIQ AAGIDEKRWP ARQLSSIIDD WKNRALTPDK
VPAADAGAYN HKGPQLYAQY QARLRELNAC DFGDLLLHMV TIFQTHPDVL EQYQRWFRYI
LVDEYQDTNV AQYLWLRLLA QGHRNICCVG DDDQSIYGWR GAEVGNILRF EKDFPGAHVV
RLEQNYRSTP HILAAASNVI RGNSSRLGKE LWTEADSGEK VRLIGHWDGE EEARWIGEEV
ESMQAGTRGM APRGLDDMAI LVRASHQMRA FEDRFLTIGL PYRVIGGPRF YERLEIRDAM
AYFRLVVSPE DDLAFERIVN TPKRGLGDKA QQTIQRIARD NGLPLVEGAR RAVEDGAIKG
KGGAALRELL DGLVRWGRMT GDPDMTHMEL AEVILDESGY TGMWQADKTP EAPGRLENLK
ELVKALEGFE NLQGFLEHVS LVMDNESDDG GEKVSIMTLH AAKGLEFPVV FLPGWEDGLF
PSQRSMDESG VKGLEEERRL AYVGITRAEE VCTISFAGNR RVFGQWQSQM PSRFIDELPE
DHVEVLTPPG LYGGGYGAAG MSASASPQIM AGQASGLHDR ASRADVYNSP GWKRMQARSQ
ERPVSQPRES RAQVIDLDAV SSFETGQRVF HQKFGYGEII GIEGDKLEVA FEKAGTKKVV
AKFVHAEDDV PF
//