ID A0A222XC42_9CELL Unreviewed; 1060 AA.
AC A0A222XC42;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CBP52_11320 {ECO:0000313|EMBL:ASR55584.1};
OS Cellulomonas sp. PSBB021.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2003551 {ECO:0000313|EMBL:ASR55584.1, ECO:0000313|Proteomes:UP000214627};
RN [1] {ECO:0000313|EMBL:ASR55584.1, ECO:0000313|Proteomes:UP000214627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB021 {ECO:0000313|EMBL:ASR55584.1,
RC ECO:0000313|Proteomes:UP000214627};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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; CP021430; ASR55584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222XC42; -.
DR REBASE; 214170; CspBB021ORF11320P.
DR KEGG; cez:CBP52_11320; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000214627; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; 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 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 Pfam; PF11867; T1RH-like_C; 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 Helicase {ECO:0000313|EMBL:ASR55584.1};
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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 287..462
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1060 AA; 117860 MW; DF8A3CE7963EF815 CRC64;
MTMSEDAWEQ LALETLAEPL MWRVARGPQI APGSGERESW DDLVIPSRLR RALRDLNPSV
PVGYLEQAMA EILAPSSQDA LTENYRIHRF LTEGYRGLTY IDDEGREQTP TIRLVDVDPD
RNDWLAANQV TVVRGDVERR FDVVLYLNGM PVVLIELKRA GSANAGLASA HAQIETYVRE
LPLVFRFAVL AVISDGITAR YGTPFTPLHH WTPWNVDDVG AVVGAEHTAD GMSALDVLLD
GLAYQPRFLQ LLNGYVAFDG GDDGLTKRIA KPHQYFAVDK AIAATIAAVG SNGKAGVVWH
TQGSGKSMEM ELYANQVLRH PRLANPTIVV VTDRTELDGQ LYQGFARSLL LPEKPQQVVR
REELRAELRG RMSGGIYFTT LQKFSRTKDE RDAGAAHPLL SDRSNIVVIV DEAHRSHYDD
LDGYAWHLRN ALPRATLIAF TGTPVAFAER DTREVFGDYI DIHDLTRAVE DGATVPVHFE
SRLVKVRWAD EVDEDTIDRA ADEVTSGLDD TERERIEKSV AVVNAVYGAP ARIAMLADDL
VAHWEDRRAS MGAALGTPET PFISGKALVV CATREICARL YSALVERRPD WHSDELEKGR
VKVVYSGSAS DTMPVAQHVR RDSANAVVKQ RLKNPDDELE IVIVKDMMLT GFDSPPLHTL
YLDRPLKGAL LMQTLARVNR TFRGKQDGLL VAYAPLADNL HAALAEYTVS DQETRPVGRP
VDEAVDLVGQ LLDRLDTLLD GYDWRARLRQ GDRRAYVAAV LGAVDYLRRP DTPPVTSSDG
EESRVAAYRR EAGRLARAWA IAGRADALHA RRPDAQFFEE VRVWIGKFDA EDRQARGEPV
PDDVQRLLNQ LLAGVVQSTE VLDIYTAAGM PRPALSDLTP EFLAQAQASE RPHLAIEALR
ALIEAESRTA TRHNLVRRCA FSERLAELMN SYTNAQLTSA EVIAAMIELA RDVAREASRG
AHFSPPLDED ELAFYDAVAS NESAVELQGE DVLAQIAREL VTIMRRDVKT DWTVRDDVKA
KLRSSIKRLL VKHDYPPDKQ PAAIRLVLEQ MESMAPRLTA
//
