ID   U2I024_9SPHI            Unreviewed;      1120 AA.
AC   U2I024;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=M472_20510 {ECO:0000313|EMBL:ERJ61137.1};
OS   Sphingobacterium paucimobilis HER1398.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ61137.1, ECO:0000313|Proteomes:UP000016584};
RN   [1] {ECO:0000313|EMBL:ERJ61137.1, ECO:0000313|Proteomes:UP000016584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HER1398 {ECO:0000313|EMBL:ERJ61137.1,
RC   ECO:0000313|Proteomes:UP000016584};
RX   PubMed=23929486;
RA   White R.A.III., Suttle C.A.;
RT   "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398
RT   (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a
RT   Member of the Genus Sphingobacterium (Bacteroidetes).";
RL   Genome Announc. 1:e00598-13(2013).
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:ERJ61137.1}.
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DR   EMBL; ATDL01000003; ERJ61137.1; -; Genomic_DNA.
DR   RefSeq; WP_021068578.1; NZ_ATDL01000003.1.
DR   AlphaFoldDB; U2I024; -.
DR   STRING; 1346330.M472_20510; -.
DR   PATRIC; fig|1346330.5.peg.385; -.
DR   eggNOG; COG1074; Bacteria.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000016584; 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   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:SF64; ATP-DEPENDENT DNA HELICASE REP; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
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:UP000016584}.
FT   DOMAIN          1..486
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          530..795
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1120 AA;  128522 MW;  DAB6343C57F71709 CRC64;
     MNNVAPLKIL KASAGSGKTF SLTLHYLSLL LDNENNYREI LAVTFTNKAT AEMKERILSV
     LQGLAVDDSS PKIESFRELL LKQNPTWTAT IIQQKAHRAY RRILHDYSHF TISTIDGFSQ
     KVIRAFTYEL NLDAAYKIEM NTNKVKTDLT LMLNQLLDER PDLLNWIIGY AEKKINNNEN
     WNYRNQLTQL AGLIFSENFQ EFDAALTTAN TAEIFNLLNT EVIEKTQSYL DALSLAITSF
     QDTYRTVGVQ ADELKGKSRN KLVAASKVSS NVQKLSLSEL DKLMERFLLL IDNEEAFTDT
     EKNVRHDYIQ AFQPVLQQFV ELRKLTPIYI AYQAVQGNLY YLRLLKEMSD LLGTWRKENA
     AQLISDSQIL LNKLGLDNNN DPTFIWEKIG NRYNYFLFDE FQDTSRIQWK NYSPLLLNAL
     GNTAGGRNEH LIVGDVKQSI YRWRNGDWRI LLQQVEKQVV NTFHLSTGTQ SSFIENGVLE
     TNFRSLPNII RFNNYLYQQI PAHLQHVLNE KVSEELSDEG LQWWEHEGNH NMLIQAYENS
     SQSIPQQKAD NRVQQGSIEI DYFPVTDGRF RAKQTVDNAA EQLCQKIGQW ISTGRYEAKQ
     IGILVRSNAQ AMLIIQKLMD YKNRNSLTFD VISGDALSLA SNDAVNLLIE TLKAIVYTSD
     QHVIHHARIA YLYQLIQSNT SFDPALWLQF KANEIQAYRE ILPDELVTNW ELWQKLPLIH
     LIEKLIEIYG FTSPGNLHLP YILTFKDIVG SFTANGERGI TQFLEFWEQD GNKAALPSNG
     KVNAIEVTTI HKSKGLAYDV VMIPFCSWSI DGMLNGDFWI DTDNSPFAQL GKIPIKYNSN
     VARSIFYKQY YEEMLFNYMD SLNTLYVATT RAVEHLYITA PAFKETVDKK TGEITGMDIK
     NELISDALYQ VLAQPNSPFV LEDGQLHIDQ PISPLSDAKS THQDNQSIAL PFYPTSRAME
     SALNKSSHRS INTILMMEKA SQYGILAHEI MAEAAEESDI AKIIARYIDE GILAVENKDI
     LEKEINQIWH HPQIHPWLIG QHKIWNESAI ITSDGRTLRP DKVFTNDQET IVLDFKFTSD
     NYIEHKTQVD QYMKALQNLG YKQVKGYLYY AKVNELVEVR
//