ID   A0A1Z4C2M0_9GAMM        Unreviewed;      1123 AA.
AC   A0A1Z4C2M0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=CEK71_17770 {ECO:0000313|EMBL:ASF47765.1};
OS   Methylovulum psychrotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylovulum.
OX   NCBI_TaxID=1704499 {ECO:0000313|EMBL:ASF47765.1, ECO:0000313|Proteomes:UP000197019};
RN   [1] {ECO:0000313|EMBL:ASF47765.1, ECO:0000313|Proteomes:UP000197019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HV10_M2 {ECO:0000313|EMBL:ASF47765.1,
RC   ECO:0000313|Proteomes:UP000197019};
RA   Mateos-Rivera A.;
RT   "Genome Sequencing of the methanotroph Methylovulum psychrotolerants str.
RT   HV10-M2 isolated from a high-altitude environment.";
RL   Submitted (JUN-2017) 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; CP022129; ASF47765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4C2M0; -.
DR   REBASE; 208538; MpsM2ORF17765P.
DR   KEGG; mpsy:CEK71_17770; -.
DR   OrthoDB; 9804086at2; -.
DR   Proteomes; UP000197019; Chromosome.
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   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   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
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; PF04313; HSDR_N; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:ASF47765.1};
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:UP000197019};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          373..506
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   COILED          144..202
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1123 AA;  127282 MW;  3BE2870CA0DC1B5C CRC64;
     MQSQNFEFLR EAWPELASLA GFAEQYAQVD PQSALTKLRN FAERSVAIVY MQLSLPKPPM
     AKFMELLSND AFKAITPQVV VDKLHTLRIY GNQAAHGEKV AGQNALSLLK EAFDIGRWLY
     VAYAQGDLRC LSDYQAPTPS SSAKADYKKE RKALLEQYAK QEARMQAMLA ELEAERDKSA
     QLERTAEELA TLKQQAANKG QQAANELHFN EAATRKHLID LQLAQVGWLI ANADSVTLEE
     KIFYQPTHSG EGYADYVLWD DNGKPLAVIE AKKAAADAEK GRHQAKHYAD GLEKMHGQRP
     VIFYTNGHDI WLWDDHPAQN YPPRHLYGFY AKSSLQYLVR QRAERKPLNS VTPKAEILGE
     RLYQHEALKR ICERFENKQR KALAVQATGT GKTRLSIALS DACMKAGWVK RVLFICDRRE
     LRKQAKNAYA EFLSTTITTL TSKSVEDTHH RIFVATYPGM VKIFQHFDTG FFDLIIADES
     HRSIYNIYGD IFNYFDALQV GLTATPVEMI SRSTCQLFGC DFKNPTSNYA LETAVEEGYL
     VPYQVVKHTT KFLRDGIKGK ALTAEEIAEL EDQGIDPNSL DFDGTDIDKA IYNKDTNRKI
     LQNLMENGIR QADGQTLGKT IIFARNHNHA KLLETLFNEL YPQYGGKFCQ VIDNYDPRAE
     SLIDDFKGQG SNSLLTIAVS VDMLDTGIDV PEIVNLVFAR PVKSPVKFWQ MVGRGTRLCK
     NLFGIGKHKT HFQIFDHWGV VEYHGMKTRE VTISQSKPLM QRLFETRLEL AKTSLHYAEP
     DFFGHLANWL HQTINSLDDK TMAVRDQWQN KHQMGDLQTL RQFNANTVTV LQNDIAPLMQ
     WLDVRGHADA YQWDLLLSQI QQAKIKQSAG FTDLAGEAIN QLWQLQMNLN QVKAKAATIK
     QCREQAWWQT ASLDDLEQVR IDLRSILQHR DKGAVPKPTP RVIDVQDSDE IREQQPTYLT
     AVDMASYRIK VEQALKPLFG QSPVLQKIRN GKAVTAVELA QLNALIHTQH PDIDLNTLKD
     FYSTAVPMEQ ILRTIVGMDS EAVNQHFADF IQHYPSLSAR QVQFLSLLKR QIAQSGAIEI
     NHLYEMPFAA IGEPDTVFTN AQQIDDLLAI VESFGKQPAT PTP
//