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
//