ID C0ZCH4_BREBN Unreviewed; 967 AA.
AC C0ZCH4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=3'-5' exonuclease DinG {ECO:0000256|HAMAP-Rule:MF_02206, ECO:0000256|RuleBase:RU364106};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_02206, ECO:0000256|RuleBase:RU364106};
GN Name=dinG {ECO:0000256|HAMAP-Rule:MF_02206,
GN ECO:0000256|RuleBase:RU364106, ECO:0000313|EMBL:BAH43483.1};
GN OrderedLocusNames=BBR47_25060 {ECO:0000313|EMBL:BAH43483.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH43483.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH43483.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exonuclease. {ECO:0000256|HAMAP-Rule:MF_02206,
CC ECO:0000256|RuleBase:RU364106}.
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 -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 2 sub-
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02206,
CC ECO:0000256|RuleBase:RU364106}.
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DR EMBL; AP008955; BAH43483.1; -; Genomic_DNA.
DR RefSeq; WP_012686188.1; NC_012491.1.
DR AlphaFoldDB; C0ZCH4; -.
DR STRING; 358681.BBR47_25060; -.
DR KEGG; bbe:BBR47_25060; -.
DR eggNOG; COG0847; Bacteria.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_1_0_9; -.
DR Proteomes; UP000001877; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd06127; DEDDh; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_02206; DinG_exonucl; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR006310; DinG.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR01407; dinG_rel; 1.
DR NCBIfam; TIGR00573; dnaq; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02206};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_02206,
KW ECO:0000256|RuleBase:RU364106};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:BAH43483.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02206};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_02206, ECO:0000256|RuleBase:RU364106};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02206}; Reference proteome {ECO:0000313|Proteomes:UP000001877}.
FT DOMAIN 266..549
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT MOTIF 482..485
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 301..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 967 AA; 109274 MW; C15DDC94CA8ED4FF CRC64;
MNRLLVVDFE TTGSHPRQGD SIIQIGAVAI DDGQITESFS TLIHPGQDIP PFITQLTGIT
NEMVADAPSL EEVFPDFLRL LDGRAFVAHN ASFDLQFLQE ALLSQGYYAF DGYVLDTVEL
SRVLLPMQNS YRLGELASEL EIEHDNPHQA DSDALATAQL FLHLLDILKK LPLVTIQRLQ
MLVSSFRSDI EVLLRQIEME KLIELPELDG TPTKTDSSDM WDIYRQLALR KREEKLTASL
KHPPVDVTVT KAFAEQLEDV LGENGYMQAK MSGYQRRDAQ EAMMHAVYEA MEDGVHLLVE
AGTGTGKSLA YLLPGIIWAH HNQQQLVVST NTIQLQEQLF HKEIATLQES LPFSFTASTL
KGRGNYLCLR KFEQAVDEPV EGSSQEMRLV KGQMLTWLTQ TVTGDVEELS MPPSGQLLWQ
QVKSDTGSCL NRACPWFSRC YYFQAKERAR DVDVLIVNHA LFISDLQAEN RILPAYEVAI
VDEAHHLEDA ATQHLGKQFS TTQLLFLLDR ASVEESGSIA RFAEELQSWM PAVQEEVVAK
LLELRKQSAT LREKAQQWTQ LLYAWASDRA EETTDAGRET VRYRIESFVG KHEKIRKVTK
KLIEGMTAYA AGIEQLLRTT PQEEKPPFAV RSLLTDLFGL IKDWQNTVEL LHFFLLEQDA
EYVYWMEVES RTARKQVHLS AALLKVADSL AEPLFAQKRS LILTSATLTV KNSFSYIKSQ
FGLDQLPEER VRTLSLPSPF HYEEQGLLLI PSDFPAPGKE SDHTYLEAVI QGCVDVVLAS
KGRTLILFTS HSMLRLVYQA MKERLAEAPE PYTLFGHGID SNNRSKLVRL FRSMERSVLL
GTSSFWEGVD IQGEWLSSLV IVRLPFAPPN HPVYQGRAEL LKAEGKNAFM SLSLPQAVLQ
FKQGVGRLIR HHLDRGVVIV LDTRVVEARY GRSFLQSLPP FQIESGPWPT LRERIEPFLS
MQSLSDS
//
