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Database: UniProt
Entry: G5QC83_SALMO
LinkDB: G5QC83_SALMO
Original site: G5QC83_SALMO 
ID   G5QC83_SALMO            Unreviewed;      1022 AA.
AC   G5QC83;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE            Short=R protein {ECO:0000256|RuleBase:RU364115};
DE            EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN   ORFNames=LTSEMON_6219 {ECO:0000313|EMBL:EHC71745.1};
OS   Salmonella enterica subsp. enterica serovar Montevideo str. S5-403.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913242 {ECO:0000313|EMBL:EHC71745.1, ECO:0000313|Proteomes:UP000003221};
RN   [1] {ECO:0000313|EMBL:EHC71745.1, ECO:0000313|Proteomes:UP000003221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-403 {ECO:0000313|EMBL:EHC71745.1,
RC   ECO:0000313|Proteomes:UP000003221};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
CC   -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC       activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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         ECO:0000256|RuleBase:RU364115};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC       ECO:0000256|RuleBase:RU364115}.
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:EHC71745.1}.
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DR   EMBL; AFCS01001381; EHC71745.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5QC83; -.
DR   REBASE; 44036; Sen403ORF6218P.
DR   PATRIC; fig|913242.3.peg.5416; -.
DR   Proteomes; UP000003221; 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; cd18030; DEXHc_RE_I_HsdR; 1.
DR   CDD; cd22332; HsdR_N; 1.
DR   CDD; cd18800; SF2_C_EcoR124I-like; 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; IPR004473; Restrct_endonuc_typeI_HsdR.
DR   InterPro; IPR040980; SWI2_SNF2.
DR   NCBIfam; TIGR00348; hsdR; 1.
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, ECO:0000256|RuleBase:RU364115};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364115};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW   ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN          254..431
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1022 AA;  117151 MW;  48F1B7A0BA207970 CRC64;
     MTQKRVIQLF TEHLGYHYLG NWHKREDNRN IEPGLVSAWL TKRGVSEVLI ARAIRQLDRA
     ASLGEGRILY DANKEVYRLL RYGVKDKEGA GEQNQTVWLV DWENPDANEF AIAEEVTYNG
     ENKKRPDLVL YVNGIALGVI ELKRSTVSVS EGIRQNLDNQ QKAFIRNFFT TIQLVMAGND
     LEGLRYGVIE TPEKYYLQWK EAAESPHTNM LDRHLAQICN KQRLLELIHD FIVFDAGVKK
     TCRHNQYFGV TATKPFIQRN EGGIIWHTQG SGKSLTMVWL AKWIRENITD SRVLIITDRT
     ELDEQIEKVF NGVEEDILRT RSGADLVARL NQTKPWLICS LVHKFGRQEE DDKDADTDDF
     IEQMKRNIPA DFSPKGKLFV FVDECHRTQS GKLHSAMTSI LPDAQFIGFT GTPLMKKDKK
     KSVEVFGPYI HTYKFDEAVN DGVVLDLRYE ARDIDQRVKS QKKVDQWFDA KTSKLSRLGQ
     QQLKQKWASM QKLLSSRSRL EQIVADILLD FEQKPRLADG RGNAMLVCSS VYQACKCYEM
     FSDAGFAGKC AIVTSYQPNA SEIKGEESGE GLTEKLAKYN IYRKMLAEYF EQPEAEAAKR
     VSDFEKEVKQ RFIKEPGQMR LLIVVDKLLT GFDAPSATYL YIDKKMADHN LFQAICRVNR
     LDGEDKEYGY IVDYKDLFRS LEKTVQDYTA EAFDGYDKED VAGLLKDRLQ QAKIDLDGAL
     DAVRTLCEPV KMPRNQLDYQ HYFCGESGAS IEQLSEKEAL RLTLYQSVAK LIRAFTNLAG
     ELTDAGYSEQ QANQIRIDVE FYTKVRDEIK IASGDFVDMK QFEPGMRQML DLWVDADPSE
     TLMDFEELGL LELIIERGEE ALDGLPADMR GNQEAMAEAI ENNVRRTIVD ENPVNPKYYE
     KMSVLLDELI ALRRQQAISY QDYLERVREL AKQVKHPQSG SKSTYPASID TLAKKALYDN
     LGQDEVLVIK IDTAVRHTKK ADWYGDRFKE REISFAIAEE IKGYSVTVAD VMALVKVQKE
     YR
//
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