ID A0A364K169_9BACL Unreviewed; 1318 AA.
AC A0A364K169;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN ORFNames=DL897_16395 {ECO:0000313|EMBL:RAL21424.1};
OS Thermoflavimicrobium daqui.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoflavimicrobium.
OX NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL21424.1, ECO:0000313|Proteomes:UP000251213};
RN [1] {ECO:0000313|EMBL:RAL21424.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL21424.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Wang X., Zhou H.;
RT "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT Moutai-flavour Daqu.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAL21424.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL21424.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Zhirakovskaya E.;
RL Submitted (JUN-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|ARBA:ARBA00011296,
CC 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:RAL21424.1}.
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DR EMBL; QJKK01000014; RAL21424.1; -; Genomic_DNA.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000251213; 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: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; 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 ENZYME HINDVIIP R PROTEIN-RELATED; 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:RAL21424.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000251213};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 286..468
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 1042..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1318 AA; 151083 MW; 8355C1824DD9847E CRC64;
MSNFYESELE KAVLEWFEEL HYEVQYGPNI APESDYRERD EYSDVILQGR LREALSRINP
RFSNEVIEEA IRKVSIPQSP DLLVNNQAFH QMVTDGIDVQ VRQEDGSFKT EKVWPIDLTR
PQNNDWLVVN QFRIKEGNTE KRLDVVVFVN GIPMSVFELK SMIDEQVDIT HAYEQMKTYQ
KALGTLFTYN AFNVISDGYH ARFGSLTADF DRYMWWRTVD GQEVAPTNVP QLDILIKGMF
AKERFVDLLR HFILFQTDGK NIYKIISAYH QYHATNKAVE RTFAATDEQG DRKVGVIWHT
QGSGKSLSMT FYTGKLVAEL NNPTVVVVTD RNDLDDQLFT TFSRSKQLLR QTPKQAGSRQ
ELRELLSVES GGIVFTTIQK FAPEVKGDQM PILTDRRNVV VIVDEAHRSQ YGFAAEVMGD
KQQAEIKFGL AKHMRDALPN ASYIGFTGTP VELADKNTPA VFGDYIDIYD MTRAVEDGTT
VKIFYESRLA ILNLPEKEKQ EIDRAYQQIA EYQEADESTQ SKLKAKFSRL EALVGSEKRL
KQIAQDIVTH FETRQKAIFG KAMIVTMSRQ IAVQLYDQII KLRPKWHHDE VSQGMIKVVM
TAGASDDEAM KKHHTTKRER EQLASRMKDL NDELKLVIVC DMWLTGFDVP CLHTIYIDKA
MKGHNLMQAI ARVNRVFKDK PGGLIVDYIG IAPSLKQALQ QYTQADRETT GIDTQLAIDL
MKEKLDLLQE MLYGHDYSAF ATGTPKERAQ TIVNTVDYVL SLGQEKKKQF IKWVTELAQA
YALCATTPEA QSLNVEIAFF KAVKAGIVKM VQPEKKRRPI RGMDSEINQL ISKSIITEGV
VDILAEVGLN KPNLAILSDE FLEEVKGLKQ KNLAVELLQR LLKDRIRIIS RRNLIQSKKF
SEMLEEAIEK YYNRLIDSTA MVLMLIEMAK EVNQSQKRGE DLGLSDAEVA FYDALSNSQD
AKELLGDHVL KQIARDLTAA LKKNLTIDWH LRESVRAQIR LFIKKLLKKY NYPPKQNQQI
VEMVVKQAEL MSQYDEDLLA DDTESEATEE HHEESPKVEP QEEITEANRI ESEATEEQQE
EINESAEEPE DKEPPLKPVA PIIEPTNEKA EAHSYSESQR SIDRVAEDSH KWLELIHPSY
QKVVEHMTKA GIPRPEVGYE FEENGEIIGE AELVWPESKI CLLTPAQSVD RDSIEKLGWR
VWDLPGDVTE EIDWLHLWKQ MQEPDTTEPK PSLEEGVKEQ IEVSLGNVTY RIEQHHNKSI
KVYRLNDYGK EKMLAKLILR KVIAEKKLDI SLYYATGTAK NTQTLGREVI RELRKQGK
//