ID C9Z8J5_STRSW Unreviewed; 1028 AA.
AC C9Z8J5;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=SCAB_29211 {ECO:0000313|EMBL:CBG70023.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG70023.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG70023.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG70023.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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}.
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DR EMBL; FN554889; CBG70023.1; -; Genomic_DNA.
DR RefSeq; WP_013000701.1; NC_013929.1.
DR AlphaFoldDB; C9Z8J5; -.
DR STRING; 680198.SCAB_29211; -.
DR REBASE; 22874; Ssc87ORF29191P.
DR GeneID; 24309128; -.
DR KEGG; scb:SCAB_29211; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_1_11; -.
DR Proteomes; UP000001444; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 261..428
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1028 AA; 116367 MW; 65053434987A1406 CRC64;
MSNVGQPERK TQDRVIELFR DSLGYDYLGN WEYRAANSNI DVGLLTQNLR ARGYSDNLIN
KAIDKLKSDA SLGSSRDLYE ANRDVYGLLR YGVKVKPGVG EQTETVWLVD WARPEVNHFA
LAEEVTVLGQ HTKRPDIVLY VNGIAFGTIE LKRSKVAVSE GIRQSIGNQR PEFIRPFFTT
VQFVMAGNDV EGLRYSAIDT PEKYWLAWRE PSDIADPLDR SLTQLCSKER LLELVHDFMV
FDAGQKKTSR HNQYFGVKAA QERIAKREGG IIWHTQGSGK SLTMVWLAKW IRENQPDARV
LLITDRTELD DQIEKVFQGV NESIYRTKSG GDLLATLNVS EEWLVCSLVH KFRGSEDEAA
RDAAESEFIR ELKATIPKDF HAKGNIFVFV DEAHRTQSGK MHDAMKALMP GAMFIGFTGT
PLLKEDKATT EERFGSFIHT YQFDEGVADG VVLDLRYEAR NIDQDLTSPA KVDQWFEAKT
RGMTDLSRAE LKKRWGTMQK VVSSEPRARQ IVNDILLDME IKPRLSNGRG NAILVSQSIY
QACKFYELFT QAGFKGKCAI ITSYTPQASD ISKEDSGHGA TERLRQYEIY RQMLADHFNE
PADKAMGKVE QFEKDVKERF VNDPGQMRLL IVVDKLLTGF DAPSATYLYI DKKMQDHGLF
QAICRVNRLD GEDKDYGYIV DYRDLFNSLE SAITDYTGGA LEGYETKDIE GLLSDRIDKA
RDDLDEALEK IRALCEPVAP PKDTLQYQQY FCAREQGNAE QLKANEPKRV ELYKSVAAVT
RAYGNLANDM QAAGYSDAEA TAIKDEIAHY ANVRDEVKLG AGEDVDFKQY EAGMRHLLDT
YISAKPSEVV SDFQEAGLIQ LIVEMGAGAL DKLPAGIKKD PEAMAETIAN NMRKVIIDER
PMNPKYYDKM SELLDAILEE RRQGALDYKE YLEKLLEHAS NLGKGESDTE YPEWADNGAR
RALIDFFDQA PELAAVVDTT ILHTKPDSWV GNAMKEKKVK RALAQTLPAD FDRLDELLEL
LKARHEYR
//
