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Database: UniProt
Entry: S2YE61_9ACTN
LinkDB: S2YE61_9ACTN
Original site: S2YE61_9ACTN 
ID   S2YE61_9ACTN            Unreviewed;      1078 AA.
AC   S2YE61;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=HMPREF1211_07652 {ECO:0000313|EMBL:EPD55687.1};
OS   Streptomyces sp. HGB0020.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD55687.1, ECO:0000313|Proteomes:UP000014410};
RN   [1] {ECO:0000313|EMBL:EPD55687.1, ECO:0000313|Proteomes:UP000014410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGB0020 {ECO:0000313|EMBL:EPD55687.1,
RC   ECO:0000313|Proteomes:UP000014410};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Streptomyces sp. HGB0020.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPD55687.1}.
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DR   EMBL; AGER01000031; EPD55687.1; -; Genomic_DNA.
DR   RefSeq; WP_016437503.1; NZ_KE150430.1.
DR   AlphaFoldDB; S2YE61; -.
DR   STRING; 1078086.HMPREF1211_07652; -.
DR   PATRIC; fig|1078086.3.peg.7704; -.
DR   HOGENOM; CLU_005762_1_0_11; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000014410; 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   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   InterPro; IPR021810; T1RH-like_C.
DR   NCBIfam; TIGR00348; hsdR; 1.
DR   PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENZYME HINDVIIP R PROTEIN-RELATED; 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   Pfam; PF11867; T1RH-like_C; 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, 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   Reference proteome {ECO:0000313|Proteomes:UP000014410};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW   ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN          304..483
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1078 AA;  121505 MW;  8946756EDF81A4E8 CRC64;
     MSAAVDEPLG EPSIDRLTEK ELELHALELL GEYGWQHIPG PELGPAHGVR ADWDDLVLRP
     RLLKAIRARH PRLPEHVAED AASELLRWHT RNDLRENHRF YERLTDGVSV PYDDPDSGKT
     RHVTIRPVDF TDPHGNDLVA ASQVRVRSTK NRTFVFDIVL YVNGLPLAAF ELKKADSNDS
     ARTAYDQLQG YRRELKETGT FATLLLTLVS DGITARLGTP FTPWQHMAPW HADEHDVMLR
     KEERQDGRAL ERMLYGAFEP VRFLDLIANF LSYSAPESGA VDTVKLAKAH QYIAVNAAVR
     ATESAVATDG RAGVVWHTQG AGKSEEMLFY VGKAARTPEL SNPTFVLLTD RIDLDTQLYD
     TFAASRTLEK ITGPPERADD TDQLRRLLQR PEGNGSVIFT TLQKFRLTQE EKGAGVRHPL
     ISPRRDVIVV VDEAHRSHYD FIDGYARNLR DALPNATFIA FTGTPIENGV GSTRGVFGEN
     IHTYDLTQAV DDGATVPVFY EPHLVRVDLP ADADLDELDA RAEGLIEGLS EEEKRKARRQ
     FGEYENLIGA PKRIEELAAT LLEHWDARRS EMIKITGYPG KGMVVCASRL IAARLFEAII
     RRRPEWAGEK DPGSQLFADD TGRVRVVFTG NAAKDRPEVA DYVRTPTQLK SIQKRVTEKD
     DELELVIVQS LWLTGFDAPP LHTLYLDKRM RGAALMQAIA RVNRTWPGKP SGLVVDFQGV
     IREIKEALAE YSERDRENPM LGADLRGAVQ LVRENHQRID ELLHGCPWRE IRDAGCPSAY
     REALTEVLEF LIVPEPKLEP GKATRRQRFM YHANLLRQAF SLCPTDQRVQ DLLPDIRFFE
     AVRTSREKYA MDEKEEQGLA TAADVRLLIA QLNESVVATE GVVDIYDAAG LTRPDLSHLD
     DRVLNDLKAS RHPNLAIAAL RRALMKEIKD AHPNNLTRQE TFTKKMKAAM NRYTNGLLTA
     AEFMEFLVNL AREVSADRGR AKKLGLTEDE LAFYDALAAD PSAVEEMEDT LLAKIAHELY
     DQIRKDVTVD WKVKEQARDK IMARVLRLLR KYGYPPDKQP AAIERVLKQA EEMAESLA
//
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