ID L1MDB1_9CORY Unreviewed; 1011 AA.
AC L1MDB1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=HMPREF9997_02025 {ECO:0000313|EMBL:EKX89020.1};
OS Corynebacterium durum F0235.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1035195 {ECO:0000313|EMBL:EKX89020.1, ECO:0000313|Proteomes:UP000010445};
RN [1] {ECO:0000313|EMBL:EKX89020.1, ECO:0000313|Proteomes:UP000010445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0235 {ECO:0000313|EMBL:EKX89020.1,
RC ECO:0000313|Proteomes:UP000010445};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKX89020.1}.
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DR EMBL; AMEM01000030; EKX89020.1; -; Genomic_DNA.
DR AlphaFoldDB; L1MDB1; -.
DR STRING; 1035195.HMPREF9997_02025; -.
DR PATRIC; fig|1035195.3.peg.1819; -.
DR eggNOG; COG4096; Bacteria.
DR HOGENOM; CLU_009326_0_0_11; -.
DR Proteomes; UP000010445; 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 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; 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; 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; 1.
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 Helicase {ECO:0000313|EMBL:EKX89020.1};
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:UP000010445};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 259..416
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 503..654
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 8..92
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1011 AA; 114020 MW; 532D65D428B725F9 CRC64;
MINAPKQRNQ TQRELTNLNR KLKEAIEEQN ATKLLLSEQE EKWRKERERH LKQIAAFQGE
NEELEKRLTE ERTALEAELE QMRAEIAALQ AVDTSANFAI SEAETRRDLI DPALGEAGFS
VERGNLLTEF PIDNGRVDYV LLGDGGTPYA LVEAKKTSKS IDAGRQQAEF YADALEKRYG
TRPIIYYTNG YEIRLLDDGA QLPGVGGYQP RAVEGYATKD ELYAMIRKRS QRQALDAVGV
DKHIAGRAYQ TIMLQAVAER FGAGHRRSLL VMATGTGKTR TAIALVKKLM QAGWAKNVLF
LADRKSLVKQ AAESFNQHLE NVPVVNLLDN PRGDGQIYFS TYQTMINMLG GEHGAARSFS
PYHFDLVIVD EAHRTIYRRY SRIFDYFDSL LLGLTATPRQ EVDRNTYRMF NLEDGSPTAD
YPLNQAIDDG YLVPFKSFQC SSVILREGVV YANLSPEEQL EWENQNWGID ENGDPIEAPE
EANSDEINAK LYNKDTIRQV VGQVLKHGIK VAGADRIGKT IFFTRNKKHA ELVYEILIET
NPQVKAAVIT HDAYNSLELI DHFKSSGKDA IDIAISVDML DTGVDVPSVV NLVFFKPVYS
NTKFWQMIGR GTRLAENLFG EGLDKKEFFI FDYCDNLRRF NGTDGIPPTE GSPQRSLSER
TFLHRVELVS LLPAGDEVRE TVVDKLRSQL ESVPRRSVLV RPEDRAGLER FTGADAWQEV
DIDVNALNEL AYLPFADGPE DEEHAKRFDY LLLSLQLDIA HGDALTERNR DKLTGIAEHL
LTKTNVPRVA EAAETLERYS ADMWWEGITI LELEAARREL RTLVQFMDRG SRNAVVMDVK
DELVEPEEFA LLTESAGGFR SSVEDRIRDV LEKHQNELAI QRIRKLKPLT AQDVDSLEGI
IATAGEETVE EFRDKIDGQS VVGFVRGLIG LDESAVEEAF ADLLERSQLS AMQMEFLRRI
IRVLSKTGSL TMNQLYDEPF NELGNVVDVF DGNMAIVLDL KTRLEQVNAV G
//
