ID A0A430FM84_9BIFI Unreviewed; 1033 AA.
AC A0A430FM84;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=D2E25_0331 {ECO:0000313|EMBL:RSX54025.1};
OS Bifidobacterium goeldii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2306975 {ECO:0000313|EMBL:RSX54025.1, ECO:0000313|Proteomes:UP000287533};
RN [1] {ECO:0000313|EMBL:RSX54025.1, ECO:0000313|Proteomes:UP000287533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2034B {ECO:0000313|EMBL:RSX54025.1,
RC ECO:0000313|Proteomes:UP000287533};
RA Lugli G.A., Duranti S., Milani C.;
RT "Characterization of the phylogenetic diversity of five novel species
RT belonging to the genus Bifidobacterium.";
RL Submitted (SEP-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSX54025.1}.
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DR EMBL; QXGL01000001; RSX54025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430FM84; -.
DR REBASE; 385105; Bgo2034BORF330P.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000287533; Unassembled WGS sequence.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000287533};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 293..468
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 492..519
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1033 AA; 117875 MW; 2A100C57CBBCD621 CRC64;
MGEGRLTDVN GSQSISILDE FAFEQAIISH LVGMGYEYFY GPEVSRTNDS YRDALMPGVL
EEALRRINPH AHPAAIEEAL RKVSDIEGID LLSRNIAFTD YMQSGVEVSY FDGEKTRPDN
IKIIDFDHPE RNTFAVINQW TYVEYEEKRP DLIIFVNGMP LVIFELKSPA RENVDSSDAY
LQLRNYMKVI PTLFTYNAFC VMTDMADTRV GTITASEDRF MQWKTADGDY SRIDTGKPIR
WTTMLDGMLS KERLIDILRN FICFSKSENG TVKILAAYHQ YFGVHKAVES TLRAMNGDGK
AGVFWHTQGS GKSLSMVFYA HLLAEQVNSP TIVVTTDRTD LDGQLYGQFV KCADFLRQQP
QQAVSRDNLV ELLNNRQANG IVFTTMQKFS ESDEPLSERR NIVVMADEAH RSQYGLEIKL
HADGTHSVGD ALKVRQALPN ASYIGFTGTP IETQDKSTRE IFGDYVDVYD MTQSVEDGAT
RPVFYESRVV SLKLDENILR ELDKQYENIS DDADEMAIDR SKRDLSTMDS VLGAPETIDS
LCRDIVNHYE ENRADELTGK ALVVAYSRPI AMRMYKKFLE LCPQWKDKVH VVMTSSNQDP
EEWHKVIGNK AHKDELAKEF KDDDSPFKIA IVVDMWLTGF DVPSLSTMYV YKPMKGHNLM
QAVARVNRVY KGKEGGLIVD YIGIAGALKR AMHDYTKRDR ERYGDMNVAD TAYPLFLDKL
SACRDFLHGL DYQNRIHTNS AEQMAEAIAD GADYLLDPER EKDRKDFIKC AKEMAQAFGL
CRSMVADELK IEEAYIDVLR TQMLKVLNVN PGNPRMSLKE INKQIAAIME QGVHNEGVID
LFEDRTVEVS LFDESFLAEI AQMEQKNLAV ELLRKLLDDQ VKAYRKKSVV MAGKFSEMLQ
QSVNAYLNGM LTNAEVIQQL LDMAKEIMAA RQEGKTLGLD DEELAFYDAL TKPQAIKDFY
ENDELVAITR ELTDTLRKNR TIDWQKKDDA RARMRMSIKR LLRKHKYPPD EVPEAIETVM
QQCELWVDYE EGN
//
