ID A0A402CVX4_9BACT Unreviewed; 1100 AA.
AC A0A402CVX4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=CCAX7_25930 {ECO:0000313|EMBL:BDI30542.1}, CCAX7_25950
GN {ECO:0000313|EMBL:GCE54081.1};
OS Capsulimonas corticalis.
OC Bacteria; Armatimonadota; Armatimonadia; Capsulimonadales;
OC Capsulimonadaceae; Capsulimonas.
OX NCBI_TaxID=2219043 {ECO:0000313|EMBL:GCE54081.1};
RN [1] {ECO:0000313|EMBL:GCE54081.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:GCE54081.1};
RA Li J., Tonouchi A.;
RT "Draft Genome Sequence of Capsulimonas corticalis strain AX-7.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:BDI30542.1, ECO:0000313|Proteomes:UP000287394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI30542.1,
RC ECO:0000313|Proteomes:UP000287394};
RA Li J., Kudo C., Tonouchi A.;
RT "Capsulimonas corticalis gen. nov., sp. nov., an aerobic capsulated
RT bacterium, of a novel bacterial order, Capsulimonadales ord. nov., of the
RT class Armatimonadia of the phylum Armatimonadetes.";
RL Int. J. Syst. Evol. Microbiol. 69:220-226(2019).
RN [3] {ECO:0000313|EMBL:BDI30542.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI30542.1};
RA Li J., Tonouchi A.;
RL Submitted (MAY-2022) 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; AP025739; BDI30542.1; -; Genomic_DNA.
DR EMBL; BHFQ01000005; GCE54081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402CVX4; -.
DR REBASE; 621336; CcoAX7ORF25890P.
DR KEGG; ccot:CCAX7_25930; -.
DR InParanoid; A0A402CVX4; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000287394; Chromosome.
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 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 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:UP000287394};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 315..501
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1100 AA; 122840 MW; C8AB5013B7B45D48 CRC64;
MLTDFQEENY VERPFIAQLT AMQPLGWQHI EGDIYVPDVT ERPDFGAVLL EGRLRDAIKR
INRDESGQEW LDDVRATRMV GALSRLGQHK LMEANAVATN LLLLGYPVEG DPAQHGAGRS
VTARFIDFEN PANNDFLIIN QFRVDVPGGR NYIIPDLVMF VNGIPLVVIE CKSPSITNPI
EAGITQLLRY SNQRDSDDEG AERLFHYSQL LVSTFFDEAR VGTVGAGYEH FLEWKDTYPA
PTAQVVTDMG ISRLSSQQML GEGMLSPNNL LNIVKNFMVF SEAGGKVIKI APRYQQYRAV
EKAVHQLEHG QTRTQHGETD QRGGIVWHTQ GSGKSLTMVF LVRRMRAIPA LRRFKIVVVT
DRTDLEKQLK GTAQLTGENV RSARGVKAIE TLLSAPGADL VFAMIQKFRD TEGSDDQAAE
IDSDEADGRD DIETATALYP ELNPSEHIVV LIDEAHRSQT TSLHANLRRA LPNATFIGFT
GTPILMGLAK RTHEIFGPYI DRYTIRQSEQ DGATVRILYE GYDAGAFIKD DKTLDDLADE
LFGHLSTAER ERATARYARV ETVLEATNLI AAKADHALRH YVDTVLPNGF KAQIVAVSRL
AAVRFQHALV AAQRKLVSEI DGLSDDLLIL SETERSSLTD HVQQILRAHP HRNTIAGLEF
ASVISAGDQN DPKDWAEWTE AARQAQHIAR FKKPLRTATS DPAKTDPLAI LVVKSMLLTG
FDAPNEQALY LDRKMVGAEL LQAIARTNRT APRKKHGLIV DYRGIVEFLR RAVAVYSAED
MEDIRAGIVS IKDTLPTLAD RHRRVIAIFS ERNVSDISNV RAAVDVLADP RVRADFSVKY
KDFLESLDIV LPRPEALHFN ADARTLGVIN QMARNLYRDP QLMLVGAGQK VRDLIDQHVY
AMGIDPKVPP ISILDLGFDA AVAAQPSAKT QASEMEHAAR YHITSKYNED PSYYKRLSER
LEEILAHFGE NWDALVEALR QFTADVREGC PQDQSGLDPR TQAPFLGVLL EETGGSDGGD
DSIRRYAEPT VELVEVIRRH LRQAGFWRSE YAQRVLHGEI TVYLDDHELI PIDHQERVAD
RLVALSRTLH ARLVAEQSGD
//
