ID A0A3N2DJM4_9GAMM Unreviewed; 1135 AA.
AC A0A3N2DJM4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EDC56_2637 {ECO:0000313|EMBL:ROS00003.1};
OS Sinobacterium caligoides.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Sinobacterium.
OX NCBI_TaxID=933926 {ECO:0000313|EMBL:ROS00003.1, ECO:0000313|Proteomes:UP000275394};
RN [1] {ECO:0000313|EMBL:ROS00003.1, ECO:0000313|Proteomes:UP000275394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100316 {ECO:0000313|EMBL:ROS00003.1,
RC ECO:0000313|Proteomes:UP000275394};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-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 -!- 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:ROS00003.1}.
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DR EMBL; RKHR01000005; ROS00003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2DJM4; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000275394; 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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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 4: Predicted;
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, ECO:0000313|EMBL:ROS00003.1};
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:UP000275394}.
FT DOMAIN 4..505
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 500..783
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1135 AA; 127276 MW; 6C738A4DBC120488 CRC64;
MSSLPVDYQQ RAEALDIRQS FCVSAPAGSG KTELLTQRIL RLLADCEKPE EVLAITFTRK
AASEMRSRIV KALEEAWRNE GEVAGHQLQT RELALKVLER DANLQWQLLH NPARLRIQTI
DGLCGALARQ LPVMTQFGTS PKITDDHQPL YERAIHRLLS SQGDESGEVG EAIETLLWHL
DNKLDKFFLL LTGLLAKRDQ WLGLVGAKLS GGIDVASLND FLEAWVAEQL EGALQLLAPY
GSDIARFGDY AASQLIEQNT TSRLTLLQGM AALPGQDIAA VECWQAVAEL LLTSGKWRKS
MTKKQGFPAK DKTLDEVTNL RRVETKAAML ALLESLRERD DIRSALAAVS YLPTSSYNQQ
QWHVLQAISV ILWQLNAHLQ IVFSEQGEVD YTAISMAALE AMGTEEEPTE LALLWDYTTR
HILVDEFQDT ANAQYALLVK LINGWYEDNE NNPARPKTLF LVGDGMQSIY AFREANVGLF
LQAREQGVGQ IALKPLDLSV NFRSKAGVVE WNNRVFARSF PPSSDRGRGA VCYSLAEAFD
QTDSDSAGRL LGCVDQEDRL LEAQQVVHLC AEARAKSTAG SLHSVAILVR NRSHLKQIIP
ALQEAGIPWQ ATDIHGLATQ MVVQDVMTLT LAMYDLSDRI SWLALLRSPL VGLSLNQFEQ
LSAIYLNTGC SVLSAYRQYA DEHIDVRIRD TAEQLVTAWD NRLRKPLRIW LQALWIALGG
AETMADSEQY GQVLRYFDLL EQLASNEVGL DTERLQQHVD KLYAEPLADS AAVQMMTIHK
SKGLEFDTVI LPGLDRQPRA DDKPLFNWQQ WTLNSGEQGI LVAPLAAEGA AEDSIFNLLQ
QESKQKLLLE KTRLLYVAAT RAVKQLYLVA NLKSDEKNGG YKRPASSSLL SSVWDAVVDE
VETVELPLSR SVNEQEGYAG IVRLPNDWQP EVVVAPSLLE RYRRDPMRGK QQNIPSFDEY
VVARHVGTVV HEYLQAICEQ GVSLWCEKII DQRRTAIRLR LKELGVAAVE LLKAEQWACL
LLNKTLASET GRWLLSSSHR DSQCEAELVT LKQGSQQRLI VDRSFIDEQG RRWIVDYKTA
SPSAGEEIEL FIQQESEAYR QQLATYRNCY KHMENLPTVC ALYFPSIDRL VKLTG
//
