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Database: UniProt
Entry: A7IJM3_XANP2
LinkDB: A7IJM3_XANP2
Original site: A7IJM3_XANP2 
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};
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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
//
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