ID A7IJM3_XANP2 Unreviewed; 1131 AA.
AC A7IJM3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Xaut_2985 {ECO:0000313|EMBL:ABS68216.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS68216.1, ECO:0000313|Proteomes:UP000002417};
RN [1] {ECO:0000313|EMBL:ABS68216.1, ECO:0000313|Proteomes:UP000002417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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 ---------------------------------------------------------------------------
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; CP000781; ABS68216.1; -; Genomic_DNA.
DR AlphaFoldDB; A7IJM3; -.
DR STRING; 78245.Xaut_2985; -.
DR KEGG; xau:Xaut_2985; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_1_1_5; -.
DR PhylomeDB; A7IJM3; -.
DR Proteomes; UP000002417; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; 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; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 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 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 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:UP000002417}.
FT DOMAIN 9..476
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 496..782
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1131 AA; 122033 MW; A10CFED2833F8094 CRC64;
MMSRVSTVLK DDGARRDAIS LHDRSILVEA GAGSGKTAVM AGRIAAMLAE GVSPRAIAAV
TFTELAASEL LSRVREFVAD LSDGKIATEL RVALPHGLSQ AHRDNLAAAS TAIDEITCST
IHGFCQRLIK PYPAEADIDP GAGVMDRNQA DLTFLEIVDG WLRERLSGGQ GGILAEMVLH
SPGETVALVH KIAENLRRRR TLAAPPISPL DGRLTAFRQA AADFAGFMHG TGTTEPETVV
IVERLVEMAT ALANGSDPAT PAGLVQLLTS RPHPDLCTKA GTFASYRKKG KWAAAAKQAG
LSKADGDRLN DDADAHYTAC CDAWISLLQA AASQALAALI EEARPVLQRY RDHKRASAQL
DFDDLIFAAR DMLRDHDEVR RALGQRFAHV LVDEFQDTDP LQTEIFWRLC GEPVEGNDDW
TRFRIRPGAL FLVGDPKQAI YRFRGADVGA YVQARDAFRV QDPDSLLSIS TNFRSCASIL
TFVNERFEAV LSADGQPGFT ALDPFHSDRG GLCVAALDIA VADENGKASA EQQRDAEADA
IAELCARLIE SHPIIDRRSG AERPCQPGDI ALLAPTGAEL WRYEEALERR GIPVATQAGK
GLFRRQEIQD LIALTRVLAD RRDTLALGAL LRGPLVGLTE EDLLDIVWGL PRSKEQPDRI
PRLDLSIDPA VITHSLARAV IERLQSLSRR GNSTTPHELL SQAVDVMRVR PLLLERHRGQ
AERALANIDL YLSLSTGYAV RGLRAFAEAM TAAWSDEARA VEGRPDAQEE AVALFTMHAA
KGLEWPIVIP VNTMTGVMAP ESAVIDRQTE TFYCSVLGVA PEGYETARQA EKEELDRERI
RLWYVAATRA RELLVLPRLD TTPSKSAWIG LVDLSLADLP GLDASHLPAG LTAAGAGTDN
TQTRATFAAE AETITAAQTR LTWLAPSRDE NAAGIVLREE EAAIWTGLAD DQPPELEAAA
LVQGGRERGL ILHKLMEEVL TGETSEAEAA LTDRAADLIH ALGRSPVSAP ATGLSAEELA
ACVVQTLALP DIAILRPDLL AEFPVYAAQA SDGVETATAG ITDALTIGED GRPVVVVDWK
SDVNPEAQTL DHYRAQVRAY LDMTGAERGL IVLMTRGMVI AVSPSPQTVA T
//