ID A0A0P1J026_9RHOB Unreviewed; 884 AA.
AC A0A0P1J026;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Name=uvrD {ECO:0000313|EMBL:CUK26518.1};
GN ORFNames=TA5114_02333 {ECO:0000313|EMBL:CUK26518.1};
OS Cognatishimia activa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatishimia.
OX NCBI_TaxID=1715691 {ECO:0000313|EMBL:CUK26518.1, ECO:0000313|Proteomes:UP000051184};
RN [1] {ECO:0000313|Proteomes:UP000051184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5114 {ECO:0000313|Proteomes:UP000051184};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-2015) 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}.
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DR EMBL; CYUE01000020; CUK26518.1; -; Genomic_DNA.
DR RefSeq; WP_058315398.1; NZ_CYUE01000020.1.
DR AlphaFoldDB; A0A0P1J026; -.
DR STRING; 1715691.TA5113_01159; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000051184; 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; 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; 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; PF21196; PcrA_UvrD_tudor; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 3.
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:UP000051184}.
FT DOMAIN 32..312
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 313..686
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 884 AA; 98976 MW; 29D0F0820288893F CRC64;
MSSFDESDAF EGASQQSLAS RAMAARPTPY LDELNPAQRE AVEKLDGPVL MLAGAGTGKT
KALTSRIVHL LNTGRARPNE ILAVTFTNKA AREMKDRVGR TLGQTIEGMP WLGTFHSVCV
KLLRRHAELV GLKSNFTILD TDDQIRLLKQ LIQAANIDEK RWPPRQLASL IDGWKNKALT
PDRLPSADAG AFNNKGGELY AQYQTRLREL NAVDFGDLLL HVVVIFQNNP DVLEQYQRWF
RYVLVDEYQD TNVAQYLWLR LLAKEHQNIC CVGDDDQSIY GWRGAEVGNI LKFEKDFPGA
HVVRLEQNYR STPHILAAAS AVISGNENRL GKTLWTAAQR GEQVKLIGHW DGDEEARWIG
EKVDGLLSGS APEAKRRENA RSEQMVEEVD RLHDLNLQRG YNSRAQLVDA LKESEVFKEN
VENEDLLWEL ATRKEEGRSV EVCFQKFDLE DMAILVRASH QMRAFEDRFL TIGLPYRVIG
GPRFYERMEI RDAMAYFRVV TSPEDDLAFE RIVNTPKRGL GNVAVQKIQA AARENGVSLV
EGARILLDNK GIGGKGAKEL RILVDNIDRW RGLGVQREVE IPLNDDEVID DGTTQSAMRF
APAGDNMPHT ELAEIILDES GYTSMWQNDK TPEAPGRLEN LKELVGQLAN FDNLQGFLEH
VSLVMDNDND DADAKISIMT LHAAKGLEFP VVFLPGWEDG LFPSQRSMDE SGLKGLEEER
RLAYVGITRA EEVCTISFAG NRRVFGQWQS QMPSRFIDEL SEEDVEVLTA PGIYGGGHSG
ATGDFGSGIQ DRVQSANTYN SPGWKRMQDR AGQRGLSQPK ESKHTIIDLE AVSSHSVGDR
VFHQKFGYGE IMEIEGDKLV IEFDKAGEKK VVAKFVTAST DIPF
//
