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Database: UniProt
Entry: D9RYR8_THEOJ
LinkDB: D9RYR8_THEOJ
Original site: D9RYR8_THEOJ 
ID   D9RYR8_THEOJ            Unreviewed;       731 AA.
AC   D9RYR8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE            EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN   OrderedLocusNames=Toce_1758 {ECO:0000313|EMBL:ADL08492.1};
OS   Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS   JW/IW-1228P).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermosediminibacter.
OX   NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL08492.1, ECO:0000313|Proteomes:UP000000272};
RN   [1] {ECO:0000313|EMBL:ADL08492.1, ECO:0000313|Proteomes:UP000000272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC   {ECO:0000313|Proteomes:UP000000272};
RX   PubMed=21304740;
RA   Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA   Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Thermosediminibacter oceani type strain
RT   (JW/IW-1228P).";
RL   Stand. Genomic Sci. 3:108-116(2010).
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         ECO:0000256|RuleBase:RU364053};
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, ECO:0000256|RuleBase:RU364053}.
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DR   EMBL; CP002131; ADL08492.1; -; Genomic_DNA.
DR   RefSeq; WP_013276514.1; NC_014377.1.
DR   AlphaFoldDB; D9RYR8; -.
DR   STRING; 555079.Toce_1758; -.
DR   KEGG; toc:Toce_1758; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_9; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000000272; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; 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; 2.
DR   InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
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   NCBIfam; TIGR01073; pcrA; 1.
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; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA-binding {ECO:0000256|RuleBase:RU364053};
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:UP000000272}.
FT   DOMAIN          5..283
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          284..557
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          640..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..661
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   731 AA;  84007 MW;  0981226630CEC97E CRC64;
     MNYLSDLNEE QRKAVTHPGG PLLILAGAGS GKTRVLTYRI AYLIEKMGVD PGSIMAITFT
     NKAAQEMKER IEKLLPWARG MLVSTFHSAC VRILRSDIDK LGYNKNFIIF DTQDQLVLIR
     DCIKALGLDE KKYAPTAVLN YIGRAKDRLQ TPEECHDRAK DIREKAMSRV YELYQKRLKE
     SNALDFDDLI MKTVELFRKN PEVLSYYQNR FRHILVDEYQ DTNRAQYVLV KLLAEKHRNL
     CVVGDDDQSI YGFRGADIRN ILDFEEDFPD ATVIRLEQNY RSTQNILDAA NSVISHNFDR
     KQKSLWTENG RGDKIYLATL GNEHEEAFFI AREIEKLVNM KNFRFRDFAV LYRTNAQSRV
     LEEMMVKMGL PYKIVGGVRF YQRREIKDIL AYLRVVANPS DNVSLLRIIN VPRRGIGEAT
     VETLKLLAEE REKSVYHIMK EELAELSSRV RSKLRDFVDM IDDFIKKAGE LSVPDLIAYI
     LDRSGYLKEL EAENTPDAQS RIENLKEMIG VAIEFEKKFP GAALQDFLAE IALVSDVDEF
     DEDRDAVILM TLHSAKGLEF PVVFLSGMDE GIFPHSRAMF DEEELEEERR LCYVGITRAK
     KRLYLTRAWS RNLYGNTSYY SASRFIDEIP ARLIKEIRPG DDTLEEEEKP REDKKAEQAV
     PVKPRTQKLK TGVKPQEPVK LNPGDRVKHS KWGEGVVTAV YGAGENTEIA VNFASEGTKR
     LMLKYAPLVK I
//
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