ID   A0A1L3MFV2_9MICO        Unreviewed;       995 AA.
AC   A0A1L3MFV2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=ASJ30_06220 {ECO:0000313|EMBL:APH01188.1};
OS   Janibacter indicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=857417 {ECO:0000313|EMBL:APH01188.1, ECO:0000313|Proteomes:UP000182938};
RN   [1] {ECO:0000313|EMBL:APH01188.1, ECO:0000313|Proteomes:UP000182938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YFY001 {ECO:0000313|EMBL:APH01188.1,
RC   ECO:0000313|Proteomes:UP000182938};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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; CP013290; APH01188.1; -; Genomic_DNA.
DR   RefSeq; WP_072624348.1; NZ_CP013290.1.
DR   AlphaFoldDB; A0A1L3MFV2; -.
DR   REBASE; 174178; JteJYFY1ORF6230P.
DR   KEGG; jte:ASJ30_06220; -.
DR   Proteomes; UP000182938; 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   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.
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, ECO:0000313|EMBL:APH01188.1};
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:UP000182938};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          263..505
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
SQ   SEQUENCE   995 AA;  109332 MW;  A5CE6912ED4660AE CRC64;
     MANTTEATFE ANIEAHLTNH GWSSLAPNSY DRDLGLFADE LIAYVEASQP QAWDKLVKHH
     GGESNARHKF VAAAAKAIDH QGTIAALRGW IKDTGVKVRL CSFKPAHSLS PELTHAYESN
     RTAVVRQLHH SESNTHDSLD LVLVVNGIPV ATAELKNQFT GQGVEHAMAQ YRADRNPHDK
     IFAQRTLVHF AVDPHQVTMT TKLAGDATRF LPFNQGSAGP GRSGTAGNPS STGYQTAYLW
     EDVWQRDAWL QMLETFIHVE GGRVLFPRFH QWHAVRSLLA ATRADGVGVD RLIQHSAGSG
     KSNTIAWTAH SLSRLHGEDD KPIFDKVVVI TDRKVLDKQL QDTVAGLDHT PGTIVRIDQK
     SNQLKDALQG SAARVIITTL QKFPVVADLA AEEAAKGAAQ GVAGKHFAVI VDEAHSSTSG
     ESMSKLKQVL GSGQDALAVA EAAEAAAEAE ADEQDILLTS AQSHGKQSNL SYFAFTATPK
     PKTLEIFGQL NSEGVKVPFH TYSMRQAIDE GFIHDVLTNY TTYDVFYKLS TSRPDKDPEV
     DAAKAKVEMA QFASLHPHMM EAKAKIIVEH FRDKTAHKIN GQAKAMVVTR SRLHAIKTKQ
     AIDAYIAAQG YDNGPHPLRT LVAFSGTVTD KDNDVTYTEA GLNGFPESQL PKEFHDNYQV
     LVVAEKYQTG FSEALLHTMY VDKKLGGVKA VQTLSRLNRT TTGKDDTFVL DFANSAEEIQ
     ESFAPFYETT LAQPTDPNVL HTMEVDIMSA PVFAQEEMTA AVTALLSGDP AQQPAIYTNV
     APAVGRYLNL DEAEQDSYRS KVGQFCRMYS FMSQVIQWHD AELELLFLFG KLFLADLPKS
     TQDPMPQISK LVQLTHLALR QNSSGAITLN ATEEPGVALP GQGKGSSSEP LMDRLSALVA
     AMNEKFGISL DSSDIRWIDQ QWNTVLGDVE LATVAKHNDH SQFDLVLEEK VDDLVLDRHA
     KNGELFNQFF GNPEFKKMLV SHLSSTYNEF RKQSA
//