ID A0A1T0AR57_9PAST Unreviewed; 1004 AA.
AC A0A1T0AR57;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=B0187_07815 {ECO:0000313|EMBL:OOR98772.1};
OS Haemophilus paracuniculus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=734 {ECO:0000313|EMBL:OOR98772.1, ECO:0000313|Proteomes:UP000190867};
RN [1] {ECO:0000313|EMBL:OOR98772.1, ECO:0000313|Proteomes:UP000190867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 43573 {ECO:0000313|EMBL:OOR98772.1,
RC ECO:0000313|Proteomes:UP000190867};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Haemophilus paracuniculus CCUG 43573 type
RT strain.";
RL Submitted (FEB-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:OOR98772.1}.
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DR EMBL; MUYA01000009; OOR98772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0AR57; -.
DR STRING; 734.B0187_07815; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000190867; 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:0004386; F:helicase activity; 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 Helicase {ECO:0000313|EMBL:OOR98772.1};
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:UP000190867};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 306..506
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 883..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 115908 MW; F6B2CAAF1514B27B CRC64;
MVTSTKEKDL EIAIERALTG ACREQVVNQT NEPAASYLTK DHGFQLGFSH DFDPHFALDM
SLFWTFLQTS QKDELARFQQ LNPNDWDRKI LERLDRNLKK YGVLQLLKKG LDIDNTHFDL
LYPVPLASSG EKVKQRFEQN IFSCMRQVPY SRISNETIDM VLFINGLPII TLELKNHWTG
QTARYDGQKQ YCNRDLSQTL LQFGRCLVHF SLDTEEAFMT TKLAGANTFF LPFNKGHNQG
KGNPPNPNGH RTAYLWQEIF TKQSLANIIQ HFVRLDGSSK DPLEKRSLFF PRYHQLEVVR
RLIEHVGQNG VGKRYLIQHS AGSGKSNSIT WLAYQLIETY PQNQTAANTR ALDRPMFDSV
IVVTDRRLLD KQLRDNIKEF SEVKNIIAPA MNSAELRESL ESGKKIIITT IQKFPFIVDG
IADLSDKQFA VIIDEAHSSQ SGSAHDNMNK AMGKESDELE DAQDLILKTM QARKMRGNAS
YFAFTATPKN TTLEKFGEKQ ADGKFKPFHL YSMKQAIEEG FILDVLANYT TYRSFYEIQK
SIEDNPEFES NKAQKRLKAY VERSQQTIDI KAEVMLDHFI TQVFNRKKLK GKAKGMVITQ
NIETAIRYFK ALNRLLDERG NPFSIAIAFS GSKVVDGLEY TESEMNGFAE SDTKDYFDRD
EYRLLVVANK YLTGFDQPKL CSMYVDKKLT GVLCVQALSR LNRSANKLGK RTEDLFVLDF
FNDTEEIKAA FDPFYTSTTL SQATDANVLY ELKTQLDEVG VYEQEEVNRF TEGYFTNLDI
QQLSSMIDLA VNRFDLELGL EQAEKIDFKV KAKQFLKIYG QMAAIIPFEQ MIWEKLFWFL
KFLVPKLKVQ DPIDELDEIL NAVDLSSYGL AKTKLNHRID LEDEETELDP QNANPRSAHQ
DDKTPIDEII HNFNEKWFQG WGATPEEQRV KFLNIIDRIR SHKDYEQKYK NNPDIHTRGL
AFEQILRDVM SERHRDELEL YKLFAKDPSF KMAWTQSLQR ALGI
//
