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Database: UniProt
Entry: A0A2N4XEF8_9BACT
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ID   A0A2N4XEF8_9BACT        Unreviewed;       985 AA.
AC   A0A2N4XEF8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=C0V77_10250 {ECO:0000313|EMBL:PLK44811.1};
OS   Emticicia sp. TH156.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Emticicia.
OX   NCBI_TaxID=2067454 {ECO:0000313|EMBL:PLK44811.1, ECO:0000313|Proteomes:UP000234203};
RN   [1] {ECO:0000313|EMBL:PLK44811.1, ECO:0000313|Proteomes:UP000234203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH156 {ECO:0000313|EMBL:PLK44811.1,
RC   ECO:0000313|Proteomes:UP000234203};
RA   Cai h.;
RT   "genomes of bacteria within cyanobacterial aggregates.";
RL   Submitted (DEC-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}.
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:PLK44811.1}.
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DR   EMBL; PKRS01000004; PLK44811.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N4XEF8; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000234203; 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, ECO:0000313|EMBL:PLK44811.1};
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:UP000234203};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          293..490
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          619..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   985 AA;  114615 MW;  E3306783855C91F1 CRC64;
     MTEKRFEEYI EKYLTSTDDN GLVYTALHFS NYDRTLCLLP AEVLAFLQSS QPEAYQRWQV
     QFGEKADEKL LQRLSTQIEK DGLIKVLREG IRDRGVYFDM TYFEPKSGLN PEHQAKYLCN
     RLSIVRQLHY SKANEKSIDM VLFINGIPII GIELKNQLSG QDISHASRQY QFDRDPKNEP
     LLQFKRMLVH FIVDNDTVGM ASKLDGADTR FLPYNRDIVN PIVANDYKVS YLWKEVLSPN
     SVLDIIENFV LETTETEKEW DEKLGRVVEK KKDLLIFPRY HQLDVIRKLK TQIKAEGAGH
     YYLIQHTTGS GKSYSIGWLA HTLTSLYQNS SQKTRLFDTI VVVTDRKVLD KQLQKTLRDL
     EQTAGVVKAI DKNSEQLKEA LAKGNDIVVT TIQKFGVIAD AMSKLKGRTF GVIIDEVHSS
     QTGETAKKLK KSLSFNEFEE DEEEDYEDIM TKEILSRGRQ KHISFFGFTG TPKNKTLELF
     GRKNEFGQFV PFHSYSMKQS IFEGYTLDVL AHYMPYKRWF RLKQEDGKDD LELPEGKVKR
     ELMNFVDSHP ETIRQKVAII LNQFIHHTQK QIRGKARAMV VVRSRKHCVL YQQEMLKQMK
     ALRLPFSCLV AFSGSIQKDG KEHTEGSLNT ENGLQGGVSI PDGLKDPRFR ILIVSNKYQT
     GFDEPLIHTM FVDKRLGGVQ CVQTLSRLNR KATGKTDTFV LDFVNEPEEI IEAFQPFYTS
     TILTGETDSY KLYELDSEIK SFHLFTKYEL DEFCQLFFSE RKSDEAFQPY LNRAVEKWQE
     IEPTDKREEY RSLINAYCRL YSYISQIMDF QDAELEKLFI FLKYLKKKLP KRIGTTVDIT
     DAIDLESLRL QKQEEMKLKL DDKEGELDPM AESGAKGKDA EENSLLSEII RKVNEVHGVN
     LKEEDRIRLF NGLKNVYVRM SQSAEIRKVM EGDNSEANKW QYWNEMMSKI FLEYINDNFD
     FYKTVESPGI KPIIVDLMYR QYMRM
//
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