ID E8LJ99_SUCHY Unreviewed; 1075 AA.
AC E8LJ99;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN Name=hsdR {ECO:0000313|EMBL:EFY07429.1};
GN ORFNames=HMPREF9444_00798 {ECO:0000313|EMBL:EFY07429.1};
OS Succinatimonas hippei (strain DSM 22608 / JCM 16073 / KCTC 15190 / YIT
OS 12066).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Succinivibrionaceae; Succinatimonas.
OX NCBI_TaxID=762983 {ECO:0000313|EMBL:EFY07429.1, ECO:0000313|Proteomes:UP000018458};
RN [1] {ECO:0000313|EMBL:EFY07429.1, ECO:0000313|Proteomes:UP000018458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22608 / JCM 16073 / KCTC 15190 / YIT 12066
RC {ECO:0000313|Proteomes:UP000018458};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2011) 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:EFY07429.1}.
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DR EMBL; AEVO01000036; EFY07429.1; -; Genomic_DNA.
DR RefSeq; WP_009143009.1; NZ_GL830973.1.
DR AlphaFoldDB; E8LJ99; -.
DR STRING; 762983.HMPREF9444_00798; -.
DR GeneID; 78339318; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_015458_1_0_6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000018458; 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; cd22332; HsdR_N; 1.
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; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 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; 2.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFY07429.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018458};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 319..495
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1075 AA; 125107 MW; 3E760D6B6A1B7EB9 CRC64;
MVVFNEDSRV KFPTIKYLME MGYEYISFKG VSYKGATLEK TLIDPLTNIL VERLKKAYLK
LNPTKSEPDF DSLLSKIQTS LNNKDLGKQF YNEILLNPDE RVIDLSSPEN FRVNNTFQLA
TELTCGNKDS DNFRPDITLF INGLPLAFIE VKKENNSKGI QAETERMKVR FKTSAFRRYL
NITQIMVFSN DMEYAEENRP PEQGAYYATI GKRDTKYSTF REDNQDSFPI KLYPHEVLKI
SEELMLKDNN VPQYINLSEY KENCKNAKTP TKRMCKSLFS FDRFHFLLKY GIAYADYSFG
NQKHIMRYPQ LFATKAIEKM LDKGGQKGII WHTQGSGKTA LAYYNVKYLT DYYHKQGVIP
QFFFIVDRLD LMDQAQMEFT ARGLKVVPVQ DKDDFKKIIS SPFATQNQEG KLEITVVNIQ
KFSDDSRVLS KSAYNLQVKR IYFIDEAHRN YNPKGSFLKN LISSDENAVM IALTGTPIIQ
RDINTKDIFG DYIHTYYYNE SISDGYTLRL LREKIDSNFS GVMKKTIADF QINPRFVKIK
DIYAHKNYVE PLLDYIVEDL KKFRAAQEDQ SLGGMIVCNS KEQAKTMYQI FLEKYTDRDE
VETTFEDGEK FIESVGPEVI EAKKCLPEKG RYRAALILCD VDGKDTRKAW IELYKEGLVD
FLIVYQMLQT GFDAPRLKKL YLNRNVRAHN LLQTLTRVNR PYKDQKYGYV VDFADIEEEY
EKTNGQYQHE LEDQNGKEFL DNSNKLFVTE DEAQEQIAQA VEALEPYNLQ SATSYSKQLN
MIDDTVLLNK LNNALNVILS VHNMLLTQGS DVDEIRNLFE EKCNFAEIKS FIKATKLRIA
SVNYMKHGEE AGSAREMLNI ALEDLTFNFE KNGEPQLLEL AEQYKQSVEY ARSQLLSSAD
PQDPEYISLR QAFLDEVAKH GMANLNDPET RHKLNMHDRV KVINDILNKI RRKNEEDNIL
AAKYKGDKKY VRIEKRMKEK AQNLERAHDS KASWFAFTKN QQKIDTILLN IKEDVDDFCL
DNDDIITVEG IFTKKIKSNV TRRFRQEEIN TDSELRSYVT NLIEKEYKNS VYERV
//
