ID I1XKP8_METNJ Unreviewed; 1287 AA.
AC I1XKP8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 OrderedLocusNames=Q7A_2153 {ECO:0000313|EMBL:AFI84967.1};
OS Methylophaga nitratireducenticrescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI84967.1, ECO:0000313|Proteomes:UP000009144};
RN [1] {ECO:0000313|EMBL:AFI84967.1, ECO:0000313|Proteomes:UP000009144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI84967.1,
RC ECO:0000313|Proteomes:UP000009144};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
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; CP003390; AFI84967.1; -; Genomic_DNA.
DR RefSeq; WP_014707335.1; NC_017857.3.
DR STRING; 754476.Q7A_2153; -.
DR REBASE; 48171; MspJAM1ORF2154P.
DR KEGG; mej:Q7A_2153; -.
DR PATRIC; fig|754476.3.peg.2130; -.
DR eggNOG; COG0610; Bacteria.
DR eggNOG; COG1708; Bacteria.
DR HOGENOM; CLU_004848_1_0_6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000009144; 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; cd05403; NT_KNTase_like; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 1.20.58.910; -; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041633; Polbeta.
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; PF18765; Polbeta; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 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 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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 381..546
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1287 AA; 148147 MW; 3EBB00AE95755B0C CRC64;
MTNSVENSYG LSAQTISAIH AALATFPSIQ SAVLYGSRAK GDYRPNSDID LTLHVDASAS
EHLLFEVMGA MEELDTPYSF DISLYQHIDN DNLKDHIQRV GVEFYNAAKY QQQTQLVKQQ
LGTKDKGAQS EAQLEAGLVN RLVSLGYERI VIESAQALKA NLKRQLEIHN YDALNGQPLS
EAEFTKVLNH LDKGNVFQRA KTLRDRFQFT RDDGSSCYLQ FMNTAHWCQN QYQVTHQVTQ
IGKYENRYDV TLLINGLPLV QIELKRRGIE LKEAFNQINR YQRHSFWTDS GLFNYVQLFV
ISNGVNTKYY ANNRKQDFKQ TFYWADEQNN LITQLDAFAD VFLEKCHVSK MISKYIVLHE
SDKILMVLRP YQYYAVEAIE NQVKNGRKHG YIWHTTGSGK TLTSFKAAQI LTKLPKVYKV
VFVVDRADLD YQTTREFNFF SEGSVDGTDN TASLVKQMAG ENKLIVTTIQ KLNTAISKPR
HEAAMEALRD KRVIFIFDEC HRSQFGETHK NIVKFFTKAQ MFGFTGTPIF VENATSNEHG
KRTTKDLFGE CLHKYVITNA IADENVLKFS VEYWGKLKRK DGSLIDEQVD KINKKQFFES
DARIEGVVDW IIANHNRKTH NKQFSAMLCV SNKDMLIKYY ETFKRKKAAG EHDLRVVTIF
TYAANEEDED ANGLIGEPDF DIKTDDPKTR HTREKLESYV ADYNAMYHTQ HSVKDSKAFY
IYYKDIAKRI KERDKESFQD KDRADILLVV NMFLTGFDAK KLNTLYVDKN LKYHGLIQAF
SRTNRILGEL KSQGNIVCFR NLKDNTDEAI KLFCDTNANE DILMEPYPFY VERFNHELEQ
VLALANTPDA VNDLKSEDAQ FAFVQAFRQL LRTLNKLKPF TDFTWSDLQL DEQTFEDFKS
KYLDIYDRSH DNEPGASILE EVDFELELIH RDEVNVAYIL KLLGDIQASK TKSGNQADAD
KARQDVMSLL DKEVQLRSKR ELIEKFMQEY MPQITPEQDL TEIFAGFWHK EKRQAVHALC
EREQLNKDAV YRMIDDYNFT GKDPLRDQVF SALNYQPKLM ERKRIYTRIL KEFKDIIEAF
EDHTGSIGVG EDSADYDATT LRSLAHPIGD QVIFFTDEVK TARQATELAR FVIHTDQPYE
QGIASLSIYP EGGELLGRGV INQAILTEYF QLTSEFQMLL TQYELDFSQP ENAQQGTLFW
SLSEARQGST ILEFVLNVWG YSTAVGEAIF EFLNACGGAA AGLYVLRETI REKYSTTQKG
TDAEAETSII ISENIEAELA KIKRDRE
//
