ID D7UY92_LISGR Unreviewed; 995 AA.
AC D7UY92;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, 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:EFI83879.1};
GN ORFNames=HMPREF0556_11467 {ECO:0000313|EMBL:EFI83879.1};
OS Listeria grayi DSM 20601.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI83879.1, ECO:0000313|Proteomes:UP000010119};
RN [1] {ECO:0000313|EMBL:EFI83879.1, ECO:0000313|Proteomes:UP000010119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI83879.1,
RC ECO:0000313|Proteomes:UP000010119};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2010) 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:EFI83879.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACCR02000004; EFI83879.1; -; Genomic_DNA.
DR RefSeq; WP_003759149.1; NZ_GL538354.1.
DR AlphaFoldDB; D7UY92; -.
DR STRING; 525367.HMPREF0556_11467; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_2_1_9; -.
DR Proteomes; UP000010119; 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:SF16; TYPE I RESTRICTION ENZYME 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFI83879.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010119};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 278..441
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 995 AA; 114192 MW; 4DF5F5F971F8438E CRC64;
MAEAKFEAAL IKKLEAEGWT YRKDLSNVSI KRIESHWREV LNETNAHKLN GTPLSDIEFG
LLLQELQRIR TPYDAQLLLV GAGGVGSIPV TRDDGSSLEV EIFYEDDVAG GRSRYEVVSQ
ITFDELPKGL TTKRIIDLAL LINGIPVCHI EEKDEHLQNQ WRAFEQLKGY HGDGLYQGLF
SFVQVQFILS QHSAHYFARP NALEHYNKSF VFGWRDEHNR DITDAFEFVH QVMGIPALHR
LITVNMIPDA SNDNLMVMRS YQIQATRQIL QRMKEMEASG LIQKEGGYIW HTTGSGKTVT
SFKVAQLLAS APRIRNVLFI VDRVDLIDQT LENFKDFAYI HFKKRIKKVN GYELKRELKH
KGASQILLIS VQGLTKAVKN GLVNDDWNVI IMDEAHRSAS GESVQLIKKA FKKTSWFGFT
GTPNFYSDEI NDIKTTREIS THDIFGKRLH TYSIKDAIGD GNVLGFDVTY FKPHWVIENP
IDDFTEKDYE KEIYQSDVYR QEVVQDILDN WQKTSSGVLI AGRRQENAFQ AMLAVSGKQA
VIHYYNILKE KAPHLNVAMT FSRDESNEYG TKEQNEALKK AIKDYTEKYN VPSILDAKDP
ARAYMLDITK RLARKKPYNQ GNEEDRLDLV IVSDQLLTGF DSKYINMIYM DKMLKEGMLI
QAMSRTNRTF DRNSKPHGKV RFYRQGDEMQ AFVENALLIY TKGGNDTLQE AEKDIAEQEP
KDLENDDILA KPQSHQILDL EEAVIRLKEL AGADFSQIPR GDNDLKEFVN LGLSTQNKIQ
RLVQQGYELG SEIEELDSSH QPTGEMVRLD VSSIEEFGAL QARLNDAREK LPEKERPDLT
EIKVGIQLYS HQIIDYDMLV GLLNAFIDDK SATNKAAIEK HITPMEEESR QEINEILDDI
ESGEITKHFT TESLQNMRKK YRTERRELKI RRWAANQNVN SNRIIEAYDA YLPGQTLIEN
PQLADIVRTI EKEEDIGFFE AAEFEDALLA FFETF
//