ID C4IFX7_CLOBU Unreviewed; 975 AA.
AC C4IFX7;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=CLP_1884 {ECO:0000313|EMBL:EEP53849.1};
OS Clostridium butyricum E4 str. BoNT E BL5262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP53849.1, ECO:0000313|Proteomes:UP000003081};
RN [1] {ECO:0000313|EMBL:EEP53849.1, ECO:0000313|Proteomes:UP000003081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.;
RL Submitted (AUG-2009) 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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000256|ARBA:ARBA00038058}.
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:EEP53849.1}.
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DR EMBL; ACOM01000005; EEP53849.1; -; Genomic_DNA.
DR RefSeq; WP_003414892.1; NZ_ACOM01000005.1.
DR AlphaFoldDB; C4IFX7; -.
DR STRING; 1492.ATN24_10535; -.
DR eggNOG; COG1199; Bacteria.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_012117_1_0_9; -.
DR Proteomes; UP000003081; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; 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 InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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; PF13307; Helicase_C_2; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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};
KW Exonuclease {ECO:0000313|EMBL:EEP53849.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000313|EMBL:EEP53849.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003081}.
FT DOMAIN 250..528
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 975 AA; 113965 MW; 47E2B89C30ACA5DF CRC64;
MSEELKSILD NVIYLDIETT GLDETSSEII EIGAIKFKDN TITTFETLIR PRGRVPIGIY
NLCTGLSKEE LYSAPSLGNV RESLSQFLED LPLICHNGNF EKKFFRYHLP QIKNTIMDSM
ELAAILEPYH KEYNLNALMK TVTDMNKNEI HRGLDDSINT LKVVNSLLCR LWSSEEKKGK
KRTLYENINK YYPYLKNWSW NRHLLKPPFF IYDDYDYVSY KDKKENKAFL ENVKIDYGKY
EELLKDEKIW NNGGDFGYTY RKNQLEFSKK IRENYEKGER IFIEAPTGSG KTFAYVIIAA
IGTYLNSLKK RKDDASFIIS TNTKELQNQL IERDIPNILK KLCLYDKLKF GAMKGKANYI
CIERLNKCDR LEGDEEGNLA LLFLRRLAEK GEYGDIENIS YFIVKRFNLE RYFKDVTCDI
DSCNLEKCIK PCYLRKRYNE LPTENITVIN HSLLACWPYT EKKKINHLII DEGHNLMEKC
YDFFAEEFTS SEFLESLDMI DKGHPNIIGL LLNLNASFGF RETIEKDKIM YLVNEIIVNL
NILMNDFRSM RLVSGEYDFN TEFFIPRDDL KTMTKCLQPE ISALKESIYP LYKMLNTYVS
NIVLDDEVTG DNDYKNINDY IIKLKGTFDM LDKFLEASTF FAKILEIDKE YDEFRLKTVP
LNVGELVNEH MLKDVKSTTF LSATLRIENS FNRIKKHLGQ EKANDFLIPP VFDLKKQTKI
FALTDMGRYD DANYIKRISN FIYETSKKLS GHVLVLFNNN IRRNGVYEEL EMLTRGSKIE
VHTNKKSINI LNDKNRQAII LGTKGFFEGI DVPGDGLSCV MLDKLPNHSP EYPILRAVTT
YQHKMYQDFN YPQLCIKVKQ IYGRLVRSTF DYGYFIILDP GENQYTIRNL QRDLGGPVIE
STTSLKVLEG MESDYNNWKK RNLNIMIKKL QREKKDIGVE FEGESKKHKM FWELEGVENG
VYSFKNINYE LKGKL
//
