ID A0A1M6RHG2_9CLOT Unreviewed; 987 AA.
AC A0A1M6RHG2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=SAMN02745883_01797 {ECO:0000313|EMBL:SHK31864.1};
OS Caminicella sporogenes DSM 14501.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caminicella.
OX NCBI_TaxID=1121266 {ECO:0000313|EMBL:SHK31864.1, ECO:0000313|Proteomes:UP000184082};
RN [1] {ECO:0000313|EMBL:SHK31864.1, ECO:0000313|Proteomes:UP000184082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14501 {ECO:0000313|EMBL:SHK31864.1,
RC ECO:0000313|Proteomes:UP000184082};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851};
CC -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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DR EMBL; FRAJ01000014; SHK31864.1; -; Genomic_DNA.
DR RefSeq; WP_072967744.1; NZ_FRAJ01000014.1.
DR AlphaFoldDB; A0A1M6RHG2; -.
DR STRING; 1121266.SAMN02745883_01797; -.
DR Proteomes; UP000184082; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR040980; SWI2_SNF2.
DR PANTHER; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000184082};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 288..481
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 987 AA; 112959 MW; E974582EC5D10DA7 CRC64;
MPTNTKESGL EALIVNYLVN KNGFEQGTNE DYNRDYAVDE TRLFRFLQET QPDEVEKIGI
LNSQHKKEQF LNRLQGEIAK RGIIDVLRKG ISFYPVNLIM FYMTPSEKNI KAKEMFEKNI
FSVTRQLMYS KNNTQLAIDL AIFINGLPII TCELKNRLTK QNVEDAVQQY KLDRDPRELL
FQFKRCMVHF AVDDNEVKFC TRLEGKKSWF LPFNKGYNGG AGNPPNPNGI KTDYLWKEIL
TKNELANIIE NYAQVVAEED EYTKKKKYKQ IFPRYHQLSV VKALLADVKE KGVGQKYLIQ
HSAGSGKSNS IAWTAHQLVG FEKDGKNIFD SVIVVTDRVN LDKQIKNTIK QFMQVSSTVG
HAENSGDLKK LIKEGKKIII TTVQKFPYIL DEIGTEHKGR NFAIIIDEAH SSQSGRMSAK
MNMALSGEYT NDEEETVEDK IIKMMEGRKM LKNASYFAFT ATPKNKTLEM FGIPVPNGDK
VQYKPFHIYT MKQAIEEGFI LDVLKYYTPI SSYYKIAKIV EDDPMFDKKK AQKKLKKYVE
SNSYAIEQKA DIMVTHFHEQ VIAKGKIGGK ARAMVVTSSI ERAIDYYYAI TKCLEKRKSP
YKAIVAFSGE KEYKGKVLTE ASINGFPSSQ IETEFKKDPY RFLIVANKFQ TGYDEPLLHT
MYVDKVLSGI KAVQTLSRLN RAYPGKTDTF VLDFANDTDT IKKAFETYYT TTILSEETDP
NKLYDLVTEM EQHQVYTDYH VNTLVELYLS GADRDRLDPI LDACVGIYEN LEEDEQVSFK
SSAKAFVRTY SFLGAILPYG NAEWEKLALF LNLLIPKLPS PVEEDLSKGI LDAIDLDSYR
AEIKQTMSII LEDQTEYSVG PVPTKSGGGI NEPEMDLLSN ILESFHDMWG NIDWKDEDQV
KRHIASIPAV VSKDVAYQNA MKNSDKQNAR IESERALNRA MINMMADNME LFKQFNDNPS
FKKWLSDMVF NLTYNTKGEV YTGEINI
//