ID A0A2K8NTQ6_9MOLU Unreviewed; 1000 AA.
AC A0A2K8NTQ6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 Name=hsdR {ECO:0000313|EMBL:ATZ17147.1};
GN ORFNames=ELUMI_v1c04230 {ECO:0000313|EMBL:ATZ17147.1};
OS Williamsoniiplasma luminosum.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Williamsoniiplasma.
OX NCBI_TaxID=214888 {ECO:0000313|EMBL:ATZ17147.1, ECO:0000313|Proteomes:UP000232063};
RN [1] {ECO:0000313|EMBL:ATZ17147.1, ECO:0000313|Proteomes:UP000232063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PIMN-1 {ECO:0000313|EMBL:ATZ17147.1,
RC ECO:0000313|Proteomes:UP000232063};
RA Lo W.-S., Gasparich G.E., Kuo C.-H.;
RT "Genome sequence of Entomoplasma luminosum PIMN-1 (ATCC 49195).";
RL Submitted (NOV-2017) 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}.
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DR EMBL; CP024963; ATZ17147.1; -; Genomic_DNA.
DR RefSeq; WP_025734377.1; NZ_CP024963.1.
DR AlphaFoldDB; A0A2K8NTQ6; -.
DR REBASE; 225938; EluPIMN1ORF4190P.
DR KEGG; elj:ELUMI_v1c04230; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000232063; 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; 1.20.58.2040; -; 1.
DR Gene3D; 3.90.1570.50; -; 2.
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; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME R PROTEIN; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF12008; EcoR124_C; 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:UP000232063};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 308..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1000 AA; 117051 MW; 56E5346A9C6A9364 CRC64;
MNKDIKIIME TTFNTVVNEY VSKKQNYNYY ESEAQLEDTF IKDLINQGYQ YLALNTDQDL
ILNLRKQLEK LNNIEFTEKE WKDFYNNVIA NKAEGLIEKT RKIQEDYKQY IKRESDGSPK
NIYLIDKTNV HNNTVQVINQ FEENEGNYKG RYDVTILVNG LPMVHIELKR RGVNIREAFN
QIQRYARDNF WAGSGLFEYV QLFVISNGTN TKYYSNTTRK EQVEKTLNHK QLQSKAFEFT
SNWTDEKNNL ITDLKDFTST FFNKRTLLNI LTRYCVFTVD ENLLVMRPYQ ITATEKIINK
ITISSHYKKE GTKDAGGYIW HTTGSGKTLT SFKTAKLATE LDFVDKVLFV VDRKDLDYQT
IKEYDKFEKG SANGNKSTEE LKKNLEDPLK KIVITTIQKL SNFVKKYKKH DIYNKHLVLI
FDECHRSQFG DMNKAITKSF KKYHLFGFTG TPIFAENTND NVGFQTTEAT FGEKLHAYTI
VNAINDGNVL PWRVEYLTTF HEKDEIVNKK VKAIDKQSAL NNVKRIREIV KYIIDRFDTK
TLLTPPASIK NPNPNLTKKK YNSILAVSSI EAAKAYYLEF KKTISEENLN LKVATIFSFN
PNEDMNEIDE DFDVSNLDSS SKDFLASAIN DYNEVFKTNF SVNGDSFQNY YKDLSEKTKQ
TQIDILIVVN MFLTGFDAPN LNTLWVDKEL KYHNLIQAFS RTNRILNNVK KFGNIICFRN
IEQKAKEAIA LFGDENANSI VLIKTYEEYY NGYIDKKGEK NPGYKKLIEQ LLEQFPLNEQ
IIGELQKNNF VGLYGKILQY SRWLKPFDEF ENNQILTPRQ IQDYQSLYLD FYEEKRGKSS
DVENINDDLV FEIELVRQVD INVDYILQLI KANWRKNSNL DPDIISKLDS SPDLRNKKDL
ILEFVKHYDG QDDIEGEFSI FIKESRFNDL KTIIDNNNLN EKATLKFIEL CFDFGYLKTI
GEEIDKILPP ISRFDTNNIR PKIKEKVTNL LQDFFEKYYF
//