ID A0A1I1HA81_9CLOT Unreviewed; 1069 AA.
AC A0A1I1HA81;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN ORFNames=SAMN05421842_101227 {ECO:0000313|EMBL:SFC20512.1};
OS Clostridium uliginosum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=119641 {ECO:0000313|EMBL:SFC20512.1, ECO:0000313|Proteomes:UP000199263};
RN [1] {ECO:0000313|EMBL:SFC20512.1, ECO:0000313|Proteomes:UP000199263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12992 {ECO:0000313|EMBL:SFC20512.1,
RC ECO:0000313|Proteomes:UP000199263};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|ARBA:ARBA00011296,
CC 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; FOMG01000001; SFC20512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1HA81; -.
DR STRING; 119641.SAMN05421842_101227; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000199263; 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; 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; 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:UP000199263};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 302..452
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1069 AA; 122936 MW; A3220F86F42F1E93 CRC64;
MTEDKFETEL IQYITTGAIT KPEHLEGLGG FVIAEDNVDY VVKSKLWTYE PEIKTTEQLW
NNFKKILERN NQNTLDNPLS VVEFNQVKKA ISDIKTPYEA GQFLYGLNGV SQIEIDLDDG
RHVFLTVFDQ KQVGAGDTVY QVVNQIKRLA IINGKQDRRF DTTLLINGLP IIQIEEKRDT
HDVNEALNQM HQYCDENQYG DIFSTLQILV AITPNNVKYM ANTTADKFNK DFAFNWQRKS
DSSIVRNWKE FADSMLSIPM AHQMATNYMI LDGTKNKQTL KVMRPYQVYA TQNVIEKIKK
VDFEFGTNKV GYIWHTTGSG KTITSFKTAW LASRMPKVDK VVFVVDRIAL TKQTNENYRA
YDPDSSEDMI GSVQNTNNTT DLSRKLKSKD NNIIVTSVQK LDTLVKRKSF QPPDKNIVFI
VDEAHRSTGS ENFEKIQKAF KKSAWIGYTG TPMFDETTTG LRTEDIFGRL LHAYTIREAI
ADKNVLGFKV DFETTIDEEQ MKREYLPAFY RERYPNWTEQ QIQEKINNLN QEDMDDAIEP
SFYDENIDHV KLVVEDIFTN WRNRSNEGKY NALFTTHVGA GKASTPMAMM YFREFKKVND
ENRKNGGQVL KVAVTFSLNS SNNNNMLETN KGLFEAINIY NKEFGTSFGM DDVAGYTQDV
TSRLNKSAVD KNYLDIVIVV DQLLTGFDAP ELNTLYVDRT LKGAGLIQAY SRTNRIADMQ
DKPWGRIVNY RWPAYNEKLM NKALAIYANK DSAILSDEEQ RKANEKDGIV AKPFEDIFNE
VKETVEKLSD LTKEFEQLPS SEKKKEEMLE LLRDYNAGMA KLKQYNSEEV DGNIVGFNYD
NPDELVEMLG MTSEQEVMLT TVLTNELKQH IAKEKNIPLH QIELKMTHVK YVRINYDYLT
ELVERLLNEV HEGKKEEAKE TKDKIDQFAN GLDDRNYANK IMNAANAIIK GHYPPAGAIV
KYPIKLQSSD VIIEQANNVS LDRTFLDFRV KWGITDIITS AEMRELFSTH HYGSQDLDDN
GKIRDIVAKA TLDYVRLAHD EEIQNLPKMK YRNGLRNAIY KLADEQVEN
//
