ID A5HZM5_CLOBH Unreviewed; 1115 AA.
AC A5HZM5; A7G1I1;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Type I restriction enzyme R subunit {ECO:0000313|EMBL:CAL82234.1};
DE EC=3.1.21.3 {ECO:0000313|EMBL:CAL82234.1};
GN Name=hsdR {ECO:0000313|EMBL:CAL82234.1};
GN OrderedLocusNames=CBO0682 {ECO:0000313|EMBL:CAL82234.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82234.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL82234.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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; AM412317; CAL82234.1; -; Genomic_DNA.
DR RefSeq; WP_011948403.1; NC_009698.1.
DR RefSeq; YP_001253223.1; NC_009495.1.
DR RefSeq; YP_001386615.1; NC_009698.1.
DR AlphaFoldDB; A5HZM5; -.
DR REBASE; 15279; CboHORF678P.
DR REBASE; 15843; CboAHORF732P.
DR GeneID; 5184937; -.
DR KEGG; cbh:CLC_0736; -.
DR KEGG; cbo:CBO0682; -.
DR PATRIC; fig|413999.7.peg.678; -.
DR HOGENOM; CLU_009326_0_0_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006304; P:DNA modification; IEA:InterPro.
DR CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025285; DUF4145.
DR InterPro; IPR013670; EcoEI_R_C_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF13643; DUF4145; 1.
DR Pfam; PF08463; EcoEI_R_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CAL82234.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 358..519
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 600..762
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 160..187
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1115 AA; 130508 MW; 44021108D9E167C8 CRC64;
MCTNFEFLKF KKEFTSFSDA CIEAEKSILV SPSTTAILSR RALELAVKWV YSFDEDLEIP
YRDNISSLIH SGSFLELIDS EMFPLLKFII SLGNVAVHTN KSITREEAIL SLHNLYQFIN
WIDYCYGDDY KEKKFDENSL LQGEEKRVRP EELKDLYDKL SSKDKKLEEI IKGNEELRKE
ITQKRKDNTE NYDFDIDEIS EFDTRKIYID VELKLAGWDF NKDIGEEIEL FGMPNNAEKG
YADYVLYGDN GKPLAVVEAK KTSKDPKIGR EQAKLYADCL EKQYDVRPVI FYTNGLETYI
WDDYNGYSER RIYGFFKKDE LQLMIYRRTQ KKTLRNINIK DEISNRYYQK EAITACCEEL
ERRKRKLLLV MATGTGKTRT AISLVDVLTR HNWVKNILFL ADRTALVKQA KKNFSNLLPD
LSLCNLLDSK DNPEESRMIF STYPTMMNAI DDTKAKDGKR LFTCGHFDLI IVDESHRSIY
KKYKAIFDYF DAYLIGLTAT PKDEVDKNTY GIFDMENGVP TYAYEFDKAV EDEFLVEYET
IEVKSKIMED GIKYDELSDE DKEEYEDKFD KDENIGEEIY SSAINQWLFN ANTIDLVLNK
LMENGLKIEG NEKLGKTIIF AKSHKHAEAI KERFDILYPE LGSNYAKVID NQINYVESVI
DDFSDKDKLP QIAISVDMLD TGIDIPEILN LVFFKKIRSK TKFWQMIGRG TRLCEDLLGV
GQDKDKFLIF DFCNNFEFFR MNPKGFKGNL GQTLSERIFN LKLDLVKELQ DLRYSDEEYV
SHRNELLKDL IEDVNNLNED NFMVKINLKY VEKYKNKNEW QSLGAISTQD IKEHISPLIS
KLKDDEFAKR FDILMYTIEL ANLQGNNATR PIKSVIETAE SLSKLGTIPQ IQQQKYIIDK
VRTTEFWEDV DLFELDEVRS ALRELLKYLE KITQTTYYTH FEDMIINEES HGAMYNANDL
KNYRKKVEYY LKEHENELAI YKLKNNKQLT KQDLETLESI MWQELGTKAD YEKEFGDMPV
NKLVRKMVGL DRNIANELFS EFLNNENLNT KQIHFVKLII DYVVKYGFID DNKILTEDPF
RTVGNISILF KDNRNEVISI ISKVAEIKNN AEIII
//
