ID R7LZ00_9FIRM Unreviewed; 1128 AA.
AC R7LZ00;
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=BN701_01245 {ECO:0000313|EMBL:CDE93680.1};
OS Acidaminococcus sp. CAG:542.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=1262687 {ECO:0000313|EMBL:CDE93680.1, ECO:0000313|Proteomes:UP000018195};
RN [1] {ECO:0000313|EMBL:CDE93680.1, ECO:0000313|Proteomes:UP000018195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:542 {ECO:0000313|Proteomes:UP000018195};
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:CDE93680.1}.
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DR EMBL; CBJX010000083; CDE93680.1; -; Genomic_DNA.
DR AlphaFoldDB; R7LZ00; -.
DR STRING; 1262687.BN701_01245; -.
DR Proteomes; UP000018195; 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.
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 369..529
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 152..196
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1128 AA; 128704 MW; 70B62AC1F480542B CRC64;
MGNFDFLQQD PKFKPLYDVA SNAEKVLAID PAICAMTCRK AMETAVKWMY SIDRDLHIPY
QDNLITLLNT DEFKAIVDAK LQLRLEYIRR IGNTAAHAGP QSRKNVSQEQ AVLALESLYM
FLRFIAYSYS QIELPEEAFS AARISQPLKA DTGTLEKQAA ELAKAKAALE KKENELKAFQ
AKYAAAEAEA TALRKEKAQG FHLPPETMSE ADTRKAYIDV MLAEAGWVRG QNWVDEYPVD
QMPSPTGYGA ADYVLFGQDG KPLAVVEAKK TSRDVAAGRK QGKLYADSLE KRFGQRPIIF
LTNGFETRIV EDQKGGYPER TVSGIYSRSD LEKEFYKMGT KQPLINAQLD SHIAGRYYQL
AAVKAVCEAF DQRNRRKALL VMATGSGKTR TVISLVDVLL RHGWIRNFLF LADRNSLVLQ
AKKAFGNNLP NLTITNLTEK NANPSARGVF STYQTMIHCI DGIRDETGHR MFTCGHFDLI
IVDEAHRSLY NKYRAIFDYF DGLLVGLTAT PRDEIDRNTY SVFDLEDGVP TYNYDLQQAV
KDKFLVPYHV VDCKLKLMQE GIRYEDLTDE EKKAYEDTFT DEEGNLPQSI DGSALNQKIF
NKDTIKKALS VLMTDGIRIR YNSTIGKTII FARSHAHAEA ILKVWKEMYP ELSDDYCTVI
DNYIEYAQQA LDDFSDEKKL PQVAISVDML DTGVDVPSIL NLVFFKPVLS RAKFWQMIGR
GTRTCPKLLD GEDKKEFYIF DLCGNFDFFQ ENPNGIEASG VVSLAQGVFS LEVELIFRLQ
KLEQQTAELQ NVRNELVEKV ITKIQTLPRD NFAVQMQLQY VDGFQEKDRF TALAYQDVEN
LQKHLGPLMQ NEDKDFNAVR FDALLYQLEL ASAEGKAYPR GLTDLRKKLE ALTHLGTIPA
VQQKKEFITS LLHTDYLQKA GISQWEKIRK ELRDLMKLIP KGKAVIYETD FTDTLLQIKE
TGPDEQPVAP PVLDNYRKKV EFYLKQHEDI PAIRKLRNNE PMQKVDMDDL EDLLWNRLGT
EEQYHNEYQN QPLGEFVRSV VGMDKEALNQ AFAKYINQEN LNDNQIYFVK QLIDYLSVNG
FLKDNSILLK SPFTDRGTVN VLFGNDMDVW LQIRKVLEGI NQNVNVMQ
//
