ID R7D570_9ACTN Unreviewed; 1127 AA.
AC R7D570;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=BN589_00757 {ECO:0000313|EMBL:CDD85744.1};
OS Collinsella sp. CAG:289.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=1262851 {ECO:0000313|EMBL:CDD85744.1, ECO:0000313|Proteomes:UP000017952};
RN [1] {ECO:0000313|EMBL:CDD85744.1, ECO:0000313|Proteomes:UP000017952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:289 {ECO:0000313|Proteomes:UP000017952};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CDD85744.1}.
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DR EMBL; CBHV010000078; CDD85744.1; -; Genomic_DNA.
DR AlphaFoldDB; R7D570; -.
DR Proteomes; UP000017952; 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; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000017952};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 365..525
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 154..188
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1127 AA; 129087 MW; 625FC11484ABD9DA CRC64;
MNFDFLKRED GYYGLFADAC IEAERVFPAS PAMCAVGCRK ALELAVKWVY AIDDSISMPY
RDNLSSLLHE RTFVEAVDER VWRKLVGINK LGNLSVHTER VVTPQDAVLA LRSLFEFTDW
IDYCYGPEYI ERSFDEKKIP KKGLQLTAAQ IRTIKSREAL LSQKDEEIKR LEEELKKMSS
WATQAKEENK QQRDFNPEEL SEFETRRRYV DWDLALAGWT LDKNAIRERK VQGMPIEPGN
NTGNGYVDYL LTGKDGKPLA IVEAKKTTYS EQKGLKQARL YADCLEREFG YRPPIFLTNG
FSTLFVDDEN GAPRQVSGIF SQDDLQRLLN RRGTTVKPTG LAVNEAIAGG GKRYYQVEAV
QHVCANIEEG HRKSLLVMAT GTGKTRVSAA LVDVLMRSGH VKNVLFLADR VALVRQAKHA
YQNYLPNASL CNLCSNKEER NARVVFSTYP TIMNAIDKER NEDGDRMFTP AHFDLIIVDE
AHRSIFKKYR AIFDYFDSLV VGLTATPANE VDRNTYDFFD VERGVPTYVY EYRTATEVDH
VLVPYYGIET HTDFIDDGIT YDDLSPEERE QFEDDFEEAG QEAPSEVGEE EINKWVYNEG
TIDSVLITLM EKGIHTQGGQ ELGKTVIFAQ NQKHARYIVE RFGELYPSLP GDYIQAVIHS
DDYAHAIIDD FELKNRPVIA VSVDMLDTGV DVPEIVNLVF FKKVRSKIKF WQMIGRGTRL
CEGLDVMDPL SGPSEDKERF FIFDWCRNFQ FFRENPKLVE GKLVVSVAEQ VFARQAELAM
LFQESTFADD EYQTWRAQLV ETMRSQVVAL NDELFTVRQH RREVEIYRRV ESYTVLSAVS
LAELKDPISM LIINDESDLG ALRFDNIMYG YMLALCKSQR VEVYKSRVVM MANKLCSLAS
VPQVNEQMSF IKRVADGQML DGASLLTLED IRKKLRSLVK FILGGQDRRD VITHLNDPVT
QITYGVVTDM SEDFEDYKLK VERYFKDYSD NLVIHKLRTN KPMTESEFAQ LEHIFTCELG
NAEDYATAYG NTPFGILVRS IVHLDRDAAN EAFAEFLNDQ SLNEQQINFV KRVVEYVVKL
GFMEPGDLNR PPFTRPRSFM QIFDERQQMA LVTVIKTIKE NAVSPAA
//
