ID C8X702_NAKMY Unreviewed; 1028 AA.
AC C8X702;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=Namu_4621 {ECO:0000313|EMBL:ACV80900.1};
OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM
OS 9543 / NBRC 105858 / Y-104) (Microsphaera multipartita).
OC Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC Nakamurella.
OX NCBI_TaxID=479431 {ECO:0000313|EMBL:ACV80900.1, ECO:0000313|Proteomes:UP000002218};
RN [1] {ECO:0000313|Proteomes:UP000002218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC Y-104 {ECO:0000313|Proteomes:UP000002218};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nakamurella multipartita DSM 44233.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV80900.1, ECO:0000313|Proteomes:UP000002218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC Y-104 {ECO:0000313|Proteomes:UP000002218};
RX PubMed=21304699;
RA Tice H., Mayilraj S., Sims D., Lapidus A., Nolan M., Lucas S.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Meincke L., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Chen F.;
RT "Complete genome sequence of Nakamurella multipartita type strain (Y-
RT 104).";
RL Stand. Genomic Sci. 2:168-175(2010).
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; CP001737; ACV80900.1; -; Genomic_DNA.
DR RefSeq; WP_015749715.1; NC_013235.1.
DR AlphaFoldDB; C8X702; -.
DR STRING; 479431.Namu_4621; -.
DR REBASE; 22005; Nmu44233ORF4623P.
DR KEGG; nml:Namu_4621; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_1_11; -.
DR InParanoid; C8X702; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000002218; 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:UP000002218};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 261..439
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1028 AA; 116289 MW; 6952E747B508C832 CRC64;
MSDVGQLERK AQDRVVKLFG GQLGYEYLGN WGHREGNSNI EVGLLTQNLT ARGYDSNLIN
RALDQLGKAA SVGVGHDLYE ANKDVYQLLR YGVKVRPGVG EQTETVWLID WKDPEANHFA
VAEEVTVLGH YAKRPDIVLY VNGIALATIE LKRSIVGVSE GIRQTIGNQR PEFIRPFFST
VQFVFAGNDV EGLRYGVIDT PEKYWLEWKE PSNVADRLDR ALLQLCNRGR FLELIHDFIV
FDAGVKKGPR HNQYFGVKAA RARIAKREGG IIWHTQGSGK SLTMVWLAKW IREHQPDARV
LLVTDRTELD EQIEKVFNGV NEQIYRTTSG ADLLDTLNKS QEWLICSLVH KFRGSDDDKA
LDQAGEDFIR ELNAKIPKDF KAKGNLFVFV DEAHRTQSGK MHQAMKQLMP EAMFIGFTGT
PLLKTDKETS IETFGTFIHT YKFDEAVSDG VVLDLRYEAR NIDQQLTSPA QVDKWFEVKT
KGMTDLSKAE LKKRWGTMQK VVSSEPRSKQ IVNDILLDMA TKPRLMDLRG NAMLVGSSIY
QACKFYELFC NAGFKGKCAI ITSYVPHPGD IAKEDSGEGK TEKIRQYDIY RRMLADYFNE
PEDTAVNKVE EFEKAVKKQF IENPGQMQLL IVVDKLLTGF DAPSATYLYI DKKMRDHGLF
QAICRVNRLD GDDKDYGYIV DYQDLFNSLE SAITDYTSGA LDGYEKQDID GLLSDRIEKA
REDLDEALER IRALVEPVLP PKGTLQYQQY FCAMEHGNAE QLKANEPKRV ELYKAVAAVT
RAFGNLANEM ADAGYSDTDA AAIKEEIAHY VNVRAEVKLG AGEDVDFKQY EAGMRFLLDT
YIQASASEVV SEFDDTGLID LIVRLGDGAI DKLPAGIKKD PEAVAATITN NMRKVIVDER
AMNPKYYDKM SELLDAIIEE RRKSAIDYQQ YLARLLDAAK QLGTKESDTK YPAWADNGAR
RALVDFFFPN DALAIEVDTA LWNTKPDGWV GNRMKEKVVR NAIKRALPAD FDQVDELFEL
VKARHEYH
//
