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Database: UniProt
Entry: A0A2K8NTQ6_9MOLU
LinkDB: A0A2K8NTQ6_9MOLU
Original site: A0A2K8NTQ6_9MOLU 
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
//
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