ID F0QS73_MYCSL Unreviewed; 1017 AA.
AC F0QS73;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=MSU_0822 {ECO:0000313|EMBL:ADX98343.1};
OS Mycoplasma suis (strain Illinois).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=768700 {ECO:0000313|EMBL:ADX98343.1, ECO:0000313|Proteomes:UP000007484};
RN [1] {ECO:0000313|EMBL:ADX98343.1, ECO:0000313|Proteomes:UP000007484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Illinois {ECO:0000313|EMBL:ADX98343.1,
RC ECO:0000313|Proteomes:UP000007484};
RX PubMed=21317328; DOI=10.1128/JB.00133-11;
RA Messick J.B., Santos A.P., Guimaraes A.M.;
RT "Complete genome sequences of two hemotropic Mycoplasmas, Mycoplasma
RT haemofelis strain Ohio2 and Mycoplasma suis strain Illinois.";
RL J. Bacteriol. 193:2068-2069(2011).
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; CP002525; ADX98343.1; -; Genomic_DNA.
DR RefSeq; WP_013610162.1; NC_015155.1.
DR AlphaFoldDB; F0QS73; -.
DR STRING; 768700.MSU_0822; -.
DR REBASE; 33776; MsuILORF822P.
DR KEGG; mss:MSU_0822; -.
DR HOGENOM; CLU_005762_1_1_14; -.
DR Proteomes; UP000007484; 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 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: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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000007484};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 285..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 874..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 725..759
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 874..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 119983 MW; 237A9C22EEAB6D30 CRC64;
MSESFFNKEE IKEQSIEKLK ELGWEIKNFS ELRWEDSRNP ILISELKLAL KKINSGIREE
QIQEVQKKLQ ESIKIKHFSL KNHEKKYKLI KNGFSYDGES QENIKIIDFE NPENNLFTVV
PDFEISSSNE EYFWEKYKPD LVCFVNGLPL IFFSIGESNH TPLKEIYLEN YKKIFFEKTP
QLFLFNAFSV ITNGKESKIG AVGNRFEFFH DWHRLDENCE GKRNILTLLK GICNKKNLLD
FFENFTIFQK EEDDEGERAE EKIVKIIARN HQFLGVNKAF ESFLKREENE GKIGTFWHTQ
GSGKSFSILF FAEKIIRKSE KGKIPLFLII TDRKDLERQI FRTFKSCGVL DGGVDGHVIS
NDMKLNSYEI KRAKKYLFCL VHKFNRNKAT SEIDTGGKEV VIIADEAHRT QYGDMASLMY
KSFPKSSRIG FTGTPLLVEN EKTARYFGNY VSKYDFGKAM DDGVTIPIVF ESRGCQIEEN
KNFQNVSDIS GASEEKIPKE WINNESNLRI LKKRLKNNAR DFVDYFSKRF IYKDPTIKDP
IIRKGMYICS YKETCILMHN FVSHYWQEKI KTLEEKKSTL TKKREIDRIE KIIFEMKRTE
MKVVISNWGD IDLDELKNLY GQQIEIPWNR EGERGVEERF KDRDDPFRVV FVVAMWLTGF
DVKPLTFLFI DKVLRDHTLM QAIARVNRVD KGKPKGFIVD YVGCIQHLKD SLKKYGGDFS
GERIIKEKKE IFEKIKLKIE ELEKSLRRIS ISIQEHLEKV KREGEVKTRE FLKEFKEKIC
ESIGKKRFNL EYSKIEEEIS GICEYELPLD VFDKWLVIKK IYKKINEGSF LEGEDSSLPK
IFGAQKHLDG KIDFKDNERH FQLEVHDFAE HIKKDSIEEN DEDNTKLERR EFNNSNYSSP
KSTNAFPNEQ QNNVDVFEKF SNLITKLNEG FEKPEGFEVR RQDDDLEEEN QWVEWNEEQL
EKDEDEETKI VFDEKNKEIS KSLEGGRKVN KEIEVNYVEK SSRKKIIFQK KRKLVKK
//
