ID A0A0P0USU8_9GAMM Unreviewed; 1018 AA.
AC A0A0P0USU8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=BSEPE_1189 {ECO:0000313|EMBL:BAS68177.1};
OS endosymbiont of Bathymodiolus septemdierum str. Myojin knoll.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1303921 {ECO:0000313|EMBL:BAS68177.1, ECO:0000313|Proteomes:UP000067399};
RN [1] {ECO:0000313|EMBL:BAS68177.1, ECO:0000313|Proteomes:UP000067399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS68177.1,
RC ECO:0000313|Proteomes:UP000067399};
RA Fujiwara Y., Takai K., Uematsu K., Tsuchida S., Hunt J.C., Hashimoto J.;
RT "Phylogenetic characterization of endosymbionts in three hydrothermal vent
RT mussels: influence on host distributions.";
RL Mar. Ecol. Prog. Ser. 208:147-155(2000).
RN [2] {ECO:0000313|EMBL:BAS68177.1, ECO:0000313|Proteomes:UP000067399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS68177.1,
RC ECO:0000313|Proteomes:UP000067399};
RX PubMed=26418631; DOI=10.1038/ismej.2015.176;
RA Ikuta T., Takaki Y., Nagai Y., Shimamura S., Tsuda M., Kawagucci S.,
RA Aoki Y., Inoue K., Teruya M., Satou K., Teruya K., Shimoji M., Tamotsu H.,
RA Hirano T., Maruyama T., Yoshida T.;
RT "Heterogeneous composition of key metabolic gene clusters in a vent mussel
RT symbiont population.";
RL ISME J. 10:990-1001(2016).
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; AP013042; BAS68177.1; -; Genomic_DNA.
DR RefSeq; WP_066045136.1; NZ_AP013042.1.
DR AlphaFoldDB; A0A0P0USU8; -.
DR STRING; 1303921.BSEPE_1189; -.
DR REBASE; 127734; EbaMkORF1193P.
DR KEGG; ebh:BSEPE_1189; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000067399; 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; 1.20.58.910; -; 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; 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; 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:UP000067399};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 261..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 483..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 117104 MW; EC4D6A4D57A1C987 CRC64;
MTIREQQIED ALITKLKDLK YTYREDIRDR TALEQNFREK FEALNRVNLT DAEFARLRDE
IVNPDVFTAA KTLRERNTFQ REDGTPLQYT LVNIKDWCKN EFEVINQLRI NTDNSNHRYD
VILLINGVPV VQIELKTLDV SPRRAMEQIV EYKNESGNGY TNTLMCFMQL FIVSNENKTR
YFANNHNQHF SFNADERFLP VYELASEDNK KINHLHDFAD HFLAKCTLGQ MISRYMVLVA
SEQKLMIMRP YQIYAVKAIV DCIHQNRGNG YIWHTTGSGK TLTSFKASTL LKDNPDIDKC
LFVVDRKDLD RQTREEFNKF QDGCVEENTN TETLVRRMLS EDYADKVIVT TIQKLGLALD
ETSKRNQANK QKGKQTYKQR LEPLRNQRMV FIFDECHRSQ FGDNHQAIKS FFPNAQLFGF
TGTPIFEENA TYKTIDGTQA SYKTTKDIFQ KELHHYTITN AIEDRNVLRF HIDYFGEKPK
TIESEASEDK NAKTGKKPKP QTQKNKPPAP EAVVNEILDK HNAATNQRRF NAVLATASIN
HAIEYTNLFK QAQAQKQAED ESYRPLNIAC VFSPPAEGNK DVQQIQEDLP QEKADNQTEP
EKKKAALKAI MADFNTQYGT NHGINEFDLY YQDVQQRIKD QKYSNKDYLH KNKIDIVIVV
DMLLTGFDSK YLNTLYVDKN LKHHGLIQAF SRTNRVLNDT KPHGMILDFR YQEQAVNEAI
ALFSGASRDK AKEIWLVDPA PEVIKQLDGA VSQLEKFMDS QGLACTPEEV NNLKGDAARA
EFINHFKEVQ RLKTQLDQYT DLSDEQKGKV KERLPEEQLR GFKGMYLETA QRLKTQQGKG
GGDPDDPIQQ LDFELVLFAS AVIDYDYIMG LIAKTIDDTP SKQKMTRQQL IDLISSSANL
MDERDDIVDY ISSLQAGEKL SEKAIREGYD KFKAEKSAKE LVAIAEKHGL TSEALQSFVD
VIMDRMIFDG EQLTDLMEPL ELGWKARREA ELALMENLVP LLNKLAQGRD ISGLAAYE
//
