ID   A0A2C9CH68_KUEST        Unreviewed;       927 AA.
AC   A0A2C9CH68;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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_4 {ECO:0000313|EMBL:SOH05031.1};
GN   ORFNames=KSMBR1_2544 {ECO:0000313|EMBL:SOH05031.1};
OS   Kuenenia stuttgartiensis.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Kuenenia.
OX   NCBI_TaxID=174633 {ECO:0000313|EMBL:SOH05031.1, ECO:0000313|Proteomes:UP000221734};
RN   [1] {ECO:0000313|Proteomes:UP000221734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Frank J.;
RL   Submitted (OCT-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; LT934425; SOH05031.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9CH68; -.
DR   REBASE; 223648; KstMBR1ORF2552P.
DR   KEGG; kst:KSMBR1_2544; -.
DR   Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
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; 1.20.58.910; -; 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; IPR022625; TypeI_RM_Rsu_C.
DR   NCBIfam; TIGR00348; hsdR; 1.
DR   PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 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; 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:UP000221734};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW   ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN          189..370
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   927 AA;  107144 MW;  8DFA10AF99F0C02B CRC64;
     MREINTFRRD DDTPLQYTLV NIKDWCKNEF EVINQLRINT ENSHHRYDVI LLINGVPAVQ
     IELKTLQVKP KRAMEQIVEY KNDPGNGFTN SLLCFMQLFI VSNENNTYYF ANNHKDHFAF
     NADERFLPIY QLADEANKKI THLHDFAERF LAKCTLGQMI SRYMVLVVSE QKLMIMRPYQ
     IYAVKAIVDC IHQNRGNGYI WHTTGSGKTL TSFKASTLLK DNPDIEKCLF VVDCKDLDKQ
     TRDEFNKFQE GCVEENTNTE TLVQRLLSED YADKVIVTTI QKLGLALDEN SKRNQNSKQK
     GRLTFKERLM PLRDKRIVII FDECHRAQFG DNHKAIKEFF PKAQLFGFTG TPIFEENATY
     KQVDGTVGSY KTTKDIFEKQ LHVYTITHAI DDGNVLRFHV DYFKPDSKKK VKTADTISKK
     AVVDSILDKH DSATNARRFN ALLATGSIND AIEYHELFKE IQKKRVQENE DFTPLNVACV
     FSPPAEGNKD VQQIQEDLPQ EKADNEQEPD KKKEALKAII VDYNKQYGTN HRIYDFDLYY
     QDVQKRIKDH KYSNADYPHK NKIDLVIVVD MLLTGFDSKY LNTLYVDKNL KQHGLIQVFS
     RTNRVLNDTK PYGNILDFRM QTKEVDEAIA LFCGQGTERA KEIWLVDPAP EVIEKYKKAV
     AALGDFMQAS DLVCEPQEVY NLKGDTARIN FINRFKEIQR VKTQLDQYTD LTPEQKAHIE
     TLIPEDQLRS FRSSYLETAK QLKERQQKEG INADPSVQQL DFEFVLFASA VIDYDYIMKL
     ISRFTQNKPG KQKMTREQLI DLLSSSANLI DEREDIVAYI NSLEVGKGLD EKEIKEGYQK
     FKTENAEKDM AEAACKHGLE PEALQSFVDA IIDRMVFDGE KLSDLMEPLG LSWKDRTKNE
     LELMEDLIPL LKKLAGGREI AGLTAYE
//