ID   A0A0N0XI33_9NEIS        Unreviewed;      1038 AA.
AC   A0A0N0XI33;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
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 {ECO:0000313|EMBL:KPC50189.1};
GN   ORFNames=WG78_18330 {ECO:0000313|EMBL:KPC50189.1};
OS   Amantichitinum ursilacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Amantichitinum.
OX   NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC50189.1, ECO:0000313|Proteomes:UP000037939};
RN   [1] {ECO:0000313|EMBL:KPC50189.1, ECO:0000313|Proteomes:UP000037939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGB-41 {ECO:0000313|EMBL:KPC50189.1,
RC   ECO:0000313|Proteomes:UP000037939};
RA   Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT   "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT   chitin-degrading bacterium.";
RL   Submitted (JUL-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}.
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:KPC50189.1}.
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DR   EMBL; LAQT01000031; KPC50189.1; -; Genomic_DNA.
DR   RefSeq; WP_053939256.1; NZ_LAQT01000031.1.
DR   AlphaFoldDB; A0A0N0XI33; -.
DR   STRING; 857265.WG78_18330; -.
DR   REBASE; 133389; Aur41ORF18310P.
DR   PATRIC; fig|857265.3.peg.3750; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000037939; 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, ECO:0000313|EMBL:KPC50189.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037939};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          295..501
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1038 AA;  115366 MW;  8EED7E0EE2EF7906 CRC64;
     MSQNLHQEHH FESAICEHLA AHGWLYAEGD ANRYDRQNGL FMPDLVAWLE QTQPEYWQGL
     NKTHGADLPG CLAERVRKRL NQVGTLDVLR RGIEMMGAPR PLDVVQFKPA LGLNPQIAAR
     YAANRLRVVR QVRHSLNNRS DAIDLVLFVN GIAVATAELK SDFTQSVGDA VDQYRLDRNP
     LPKGGVAEPL LSFMGGALVH FAVSQSEVMM TTRLAGTETR FLPFNRGNHG AAGNPINPDG
     YATAYLWEDV WAVESWLDIL GRYLIGRQNE KKQLTSVIFP RYHQLDVTRK LLADVATHGA
     GQRYLIQHSA GSGKTNSIAW SAHFLADLHD AAHRKVFDSV LVVSDRNVLD AQLQEAIFSF
     ERTTGVVETI TGARGSKNAQ LAQALKDDKK IIVCTIQTFP LALEAVEKLA ATKGKRFAVI
     ADEAHSSQTG DTAAMTRQML SGDEQAPSQE GDEEDAVDMM ARRMAARAGG EAGLTYVAFT
     ATPKSKTLEL FGRNDTDGKP QAFHVYSMRQ AIEEGFILDV LKNYITYSLA FRLAHNGVEL
     DERQVAKSEA VKGIMQWVRL HPYNIAQKVK VVVEHFRENV QPLLDGKAKA MIVVSSRKEA
     VRWQKATAAY IRAQNYPLGV LVAFSGEVDD PDSYPDGPVT EHSKALNPGL NGRDIREAFA
     EPGFHLLLVA DKFQTGFDQP LLCGMYVDKK LGGIQAVQTL SRLNRAHPGK DTTYILDFVN
     DAGDILAAFK TYYETAELEA TTDPHLVYDL RAKLDAAGYY DDFEVDRVAR VETDATAGQA
     ELIKAIASVA DRLLKRFKAA RDARVNAEIN KDAVAAQAAK DRMDALTLFK RDMGAFVRLY
     AFLSQIFDYG NTDIEKRFLF YKRLIPLLEF GRERDSVDLS RLQLTHHALR NKGKQPLTLD
     HGDAPKLQPV LASGSGSVQD EEKARLEEIV RALNEVFEGD LTNDDPLVYV NGVLKGKLLE
     NETLIRQADK NSKEQLTNSP DLDEGLLTAI MDGLDAHNRM SSQAMNSDRV RDQIKEVLLG
     PGQLYEALRM KARHQLRV
//