ID   M7NSL3_9BACT            Unreviewed;      1023 AA.
AC   M7NSL3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   Name=hsdR_1 {ECO:0000313|EMBL:EMR04680.1};
GN   ORFNames=ADICEAN_00132 {ECO:0000313|EMBL:EMR04680.1};
OS   Cesiribacter andamanensis AMV16.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC   Cesiribacter.
OX   NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR04680.1, ECO:0000313|Proteomes:UP000011910};
RN   [1] {ECO:0000313|EMBL:EMR04680.1, ECO:0000313|Proteomes:UP000011910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMV16 {ECO:0000313|EMBL:EMR04680.1,
RC   ECO:0000313|Proteomes:UP000011910};
RX   PubMed=23682146;
RA   Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT   from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL   Genome Announc. 1:E00240-13(2013).
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}.
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:EMR04680.1}.
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DR   EMBL; AODQ01000002; EMR04680.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7NSL3; -.
DR   STRING; 1279009.ADICEAN_00132; -.
DR   REBASE; 65432; Can16ORF135P.
DR   PATRIC; fig|1279009.4.peg.137; -.
DR   eggNOG; COG0610; Bacteria.
DR   Proteomes; UP000011910; 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   CDD; cd22332; HsdR_N; 1.
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, ECO:0000313|EMBL:EMR04680.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011910};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          306..524
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1023 AA;  116867 MW;  A59E1B9261C3EDBF CRC64;
     MYGSMPLNHT PMKHKEIEFE KAIEHCLLQP ESGYELGNPA AYNAEKGLFP QDIITFIRKS
     QPKRWAMLEQ FYGQQAGEAL ISDLEKELAA KGVLHVLRHG FKCFGKTFRL AYFTPNTRLN
     PKAWEDYGKN RLTVTRQLHQ SPKFPMQSVD VVLALNGLPV VTLELKNPLT GQTVAHAKKQ
     YRERDARDPL FRFKERALVH FAVDPDEVYM TTRLEGNSTF FLPFNRGFKN GAGNPPSNYD
     NYRTAYLWEQ VLQKDSLLDI IARFLHLEVT EKEIAVPEGI KTIKKEILIF PRYHQLDVVR
     SLVDSSREKG AGYNYLIQHS AGSGKSNSIA WLAHRLSSLH NEQDEKVFNT VIVITDRRVL
     DQQLQNTIYQ FEHKEGVVQK IEENTQQLAK ALSDNTPIII TTIQKFPFIA QALETLAKKG
     EGVKIETAGK RFAVIVDEAH SSQSGETATE LRKVLNKEGI QAAIASQMLE EEDEDLSEEA
     RENMYQEMLK RPKQPNISFF AFTATPKYRT KLNFNEPGPD GKSPFHLYSM RQAIEEGFIM
     DVLANYTTYK AYYGLIKKTE DDPEVPKKKA AKALARFMSL HPHNIRQKVE VIVEHFRLHT
     RHKIGGSAKA MVVTGSRLHA VRYKRAFDEY IKEKAYTGIR SLVAFSGTVQ DPDIPNSAYT
     EVGMNAGVKE SELPEKFATD AYQVLLVAEK YQTGFDQPLL HTMYVDKRLA GIQAVQTLSR
     LNRTARGKED TFVLDFVNTH EDIYEAFKPY YEATAIDAEP DPHQLSKLQH TLDQWQVYTY
     AEIVAFCEVW FSNKKDPSVS DHKKMNSILD KAVERFKEQS EAEQEEIKSQ MASFQRLYGF
     ISQIVPYQDS ALEKLYTYLR FLLTKLPHRN QEQFQLVGEV ALKYYRLQQI SAGSIELGTG
     EADPLKGPTE VGTGAPKDDK VNLSMLVDKL NDLFGTEFTK ADELFFDQVA ESAAAKDDII
     ATVRANTFEN FMHYFMTALD GLIFERLDGN EELVKKTMNN PDMYRTAAQH LGRDVYNRVS
     RRE
//