ID Q7NAH2_MYCGA Unreviewed; 1051 AA.
AC Q7NAH2;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 126.
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 Name=hsdR {ECO:0000313|EMBL:AAP57035.1};
GN ORFNames=MGA_0541 {ECO:0000313|EMBL:AAP57035.1};
OS Mycoplasmoides gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasma gallisepticum).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=710127 {ECO:0000313|EMBL:AAP57035.1, ECO:0000313|Proteomes:UP000001418};
RN [1] {ECO:0000313|EMBL:AAP57035.1, ECO:0000313|Proteomes:UP000001418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2)
RC {ECO:0000313|Proteomes:UP000001418};
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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; AE015450; AAP57035.1; -; Genomic_DNA.
DR RefSeq; WP_011113946.1; NC_004829.2.
DR AlphaFoldDB; Q7NAH2; -.
DR REBASE; 7181; MgaRORF537P.
DR KEGG; mga:MGA_0541; -.
DR PATRIC; fig|233150.7.peg.765; -.
DR HOGENOM; CLU_004848_2_1_14; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000001418; 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; cd22332; HsdR_N; 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:SF16; TYPE I RESTRICTION ENZYME 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001418};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 299..470
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1051 AA; 123711 MW; E8799CBC23FA76F5 CRC64;
MSKYINEGEH EFENLLVKKL TEQYGWKLGN FKLDEKDAII KYPDEKRLIN NWRDILNKLN
KGQDRLNGRD LDDDEMNKIY NEFKSRTPYE INLLFNGGSI NITRTDGSNV SLILFHKNDI
GGGSTVYQIV RQPQFKGHNG DRGDLQLLIN GIPLIHIELK DVRRGENEND KLSKAFYQIK
NYYENDNFNG LFKCIQIFVT MTPNKTRYFA NPGSARNFEK KFWFKWTDAQ NKEITDWKEI
AKEFLSIPIA HNLIAHYTIP DKGSESLKIV RPYQYHAIKK VLDKVIRVKK NGLWDKKLED
DFKSEKSCHV WHTTGSGKTL TSYKLAELIY QWNKDGSLAD KVVFVADRIE LVKQTLIEYK
SFSPTTKTVQ GTYNTDDLFK KLISSSRELI VTSIYKLSKL SNLNEFQLPK KILDKRIVFV
VDECHRSTFD KMFKQIRQVF NKAIFIGFTG TPILNENKKN DLTTYQIFGE EIHNYKISNA
IADESVLKID TYSVYTINYE DIISKIKRFD PNYQFPDEKK ERYEKVEKFL VSNKDESPFD
HQHRKVVVSD IRENWKSRSD ERKFHAILTV PDIDQAIEYY KLFIQENNDD LNLNVTAIFD
PNFDTTEEDD KYDYHGNKIA YESKVKNKED AIKLILANYH KMFSSCDEIF RYLQHEGECS
LDEWDKFKED VQLRLAHKDR YKYLTNDDSK IDLVIVVNQL LTGYDSKYIN TLYLDRRFSS
PEQYVQAISR TNRVLNDQKQ MGQVVYYRLC QSVKEHIEKA FDIYSNENIA QKIFISDIEN
NIAQMNEIFS EIKKVFESTN IKNFSSAPQN KSGKRKFVNE FNKLAKLYRI ISLQLFNWDT
WKNKDKKQLD FDQEQYLTLE QRYKEIADEV INDPDEFYVP IELSLVYKGS SSRETTINLK
FLFDNKNTLT KQDAYNMLSK NITRLSVEDQ EIAKVVFNKN WDDANNNLLI ENTVDFWSKF
EAEKNARNDA YLVQQAKSLG CSYEALKALV DKYKFIATED INVNNNMEIE AFIKTYVNTY
MQIHNILQVF AEAEMNAKIL DIIARVNKKE F
//
