ID A0A223CYH0_9BACL Unreviewed; 745 AA. AC A0A223CYH0; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 22-FEB-2023, entry version 20. DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053}; DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364053}; GN Name=pcrA {ECO:0000313|EMBL:ASS74173.1}; GN ORFNames=CIG75_03680 {ECO:0000313|EMBL:ASS74173.1}; OS Tumebacillus algifaecis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Tumebacillus. OX NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS74173.1, ECO:0000313|Proteomes:UP000214688}; RN [1] {ECO:0000313|EMBL:ASS74173.1, ECO:0000313|Proteomes:UP000214688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=THMBR28 {ECO:0000313|EMBL:ASS74173.1, RC ECO:0000313|Proteomes:UP000214688}; RX PubMed=25858243; DOI=10.1099/ijs.0.000240; RA Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.; RT "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum."; RL Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015). 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=3.6.4.12; CC Evidence={ECO:0000256|ARBA:ARBA00001665, CC ECO:0000256|RuleBase:RU364053}; CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|RuleBase:RU364053}. 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; CP022657; ASS74173.1; -; Genomic_DNA. DR AlphaFoldDB; A0A223CYH0; -. DR KEGG; tab:CIG75_03680; -. DR OrthoDB; 9810135at2; -. DR Proteomes; UP000214688; 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 PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1. DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR01073; pcrA; 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}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, 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:UP000214688}. FT DOMAIN 12..293 FT /note="UvrD-like helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51198" FT DOMAIN 294..572 FT /note="UvrD-like helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51217" FT BINDING 33..40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560" SQ SEQUENCE 745 AA; 84268 MW; 573E561B2BC5EE46 CRC64; MFSIQGGEKM LENLNPQQKE AVLHSAGPLL IIAGAGSGKT SVLTRRIAYL IEERRVAPWQ ILAITFTNKA AREMRERVEN LIGPTAHDIW ISTFHSMCVR VLRRDADKLG YTNSFTILDA GDQLTAVKQC LKELNLDPKK FDPRGLLATI SNAKNDLLTH ERFASTVRDG DVFGGVAAQV YEAYQKKLKS NNALDFDDLI MKTVYLFQHH EDVLSLYQNR LHYIHVDEYQ DTNKAQYKLV QMLAKKKRNI CVVGDSDQSI YAWRGADITN ILNFEKDYPE TTVIKLEQNY RSTGRILEAA NHVIANNRER KEKNLWSTKA EGELVKLYKA YDEHSEAQFV IQQTLEHLKG GGRHSDIAVL YRTNAQSRVI EEALLKSTVP YTIYGGVKFY ERKEIKDILA YLRLIANLND DLSLTRVINV PKRGIGDTTV GKILDYAATH GISAFQALME IENVGIRGKA NGAIKEFVLL LRNFATQMPY LSVTDLAEEV MKLTGYRKEL ELEKTLEADA RLENLDEFLS VTAEFDNKHE MTEENRLVEF LSDVALIADS EQSEGETGPE SIKLMTLHAA KGLEFPVVFL VGLEEGMFPS NRTLTQGDER DVEEERRLMY VGITRAEEKL FISHAGSRMM YGQIKANPPS RFIREIPPSL LEEVGIIRRQ PAQERVRSDI PGLQNGTRVP SGFGADPNLT WEVGEWVAHR KWGLGEIVKS EGVGDNLELY IQFEDLAIGM KKLLARFAPI VKVED //