ID N8SAX8_9GAMM Unreviewed; 1146 AA.
AC N8SAX8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-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 ORFNames=F985_03812 {ECO:0000313|EMBL:ENU42914.1};
OS Acinetobacter seifertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=1530123 {ECO:0000313|EMBL:ENU42914.1, ECO:0000313|Proteomes:UP000013065};
RN [1] {ECO:0000313|Proteomes:UP000013065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 973 {ECO:0000313|Proteomes:UP000013065};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 973.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ENU42914.1, ECO:0000313|Proteomes:UP000013065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 973 {ECO:0000313|EMBL:ENU42914.1,
RC ECO:0000313|Proteomes:UP000013065};
RX PubMed=25563912; DOI=10.1099/ijs.0.000043;
RA Nemec A., Krizova L., Maixnerova M., Sedo O., Brisse S., Higgins P.G.;
RT "Acinetobacter seifertii sp. nov., a member of the Acinetobacter
RT calcoaceticus-Acinetobacter baumannii complex isolated from human clinical
RT specimens.";
RL Int. J. Syst. Evol. Microbiol. 65:934-942(2015).
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:ENU42914.1}.
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DR EMBL; APOO01000022; ENU42914.1; -; Genomic_DNA.
DR RefSeq; WP_004703531.1; NZ_KB851200.1.
DR AlphaFoldDB; N8SAX8; -.
DR PATRIC; fig|520709.3.peg.3748; -.
DR HOGENOM; CLU_009326_0_0_6; -.
DR OrthoDB; 9804086at2; -.
DR Proteomes; UP000013065; 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; 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.
DR PROSITE; PS51194; HELICASE_CTER; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 387..545
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 619..781
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 149..218
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1146 AA; 130561 MW; FEA25E94642F1778 CRC64;
MSNFQFLEPE FKSLAATAKE AEKLVYISPQ FALAAARTSL ENLVLWLYQY DKKLTQPYDA
SLHNLLNDLK FKDLIPPYIW DKMDNIRMVG NSAVHGKKFK QLTTEETVKH ISHLFLMYVW
FERNYGSPSK DRSQSILFNP KLIPNADNTQ QITANKEQLQ KEKEAKEKQF AEQHKALRER
EQKLFELSAS LEEREKLLAN IDAELAQKRA DVEQAKIANS KIEDHTDYKE DETRKLKIDL
MLEEAGWEIG TSVREEVAVT GMPSPSGKGA VDYVLYDANG LPLAVVEAKR TSTDPDIGQQ
QAKLYADCLE QQTGQRPVIF YTNGYKTRIW NDVQGGPPRL VHGFYTQAEL KRLIERRKNN
PDLSSFPINA DIVERYYQTR AIKAMLAAYQ RKERAGLLIM ATGTGKTRTA IALVDVLMKA
NVVQKALFLA DRTSLVNQAH NAFKANLKDA SFVNLLEDKN QVGRVYFSTY QTMIGLIDEK
NADGTRQFGT GMFDLIIIDE AHRSVYQKFG EIFKYFDSLL VGLTATPRDE VDRDTYALFG
LESGVPTDYY DLDQAIADGY LVPPKAYSVP LKFMREGVKY DELSEEEKQH WDSLNWGDED
APEEVSASKI NKELFNTGTI DLMLKHLMEN GIKTEGGDRL GKTIIFAVNQ KHAQFIADRF
NENYPQYDGK FARVITHATK YPQSLIDDFS KKDLAEPQIA ISVDMLDTGI DVPEVVNLVF
FKAVRSKVKF MQMIGRGTRL CKELFSPEDD KKEFYIFDYC SNFEYFNENP DGAPVSTTEP
LGQRLFKARL NILSLLNAKD DDTEELKAVQ QDMRQSLQTE VKSMNNENFI VKSELEHVEH
FKNDDAWNNL DDLAIGTLRE HISKLPNQLE PETLEAKLFD MICYNLELAV LEKNNTAIQS
YANRVIEIAS KLESKENIPV VAEQIALIQD IQTVEYWKGI TLPMLEAMRK RIRGLVKLIE
KSTSTIVYSM LDDKIGDMQA VDIPVVSSGV NLAQYRKRVE SFIKANENHI TIAKLKRGLA
LTPTDLSELE RFVFEAQEVE SRDKFEECFG TEKSLPLFIR SLVGLERQAV QEAFSKYLQG
SSYNEKQIRF VEMLIEHLTQ NGVLDAAQLY EPPFNQIHYE GIDGVFGDAD ADNIFGVVEA
FNEAVA
//
