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Database: UniProt
Entry: A0A364K169_9BACL
LinkDB: A0A364K169_9BACL
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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
//
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