ID C6J3N9_9BACL Unreviewed; 1045 AA.
AC C6J3N9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, 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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN Name=hsdR {ECO:0000313|EMBL:EES72346.1};
GN ORFNames=POTG_02954 {ECO:0000313|EMBL:EES72346.1};
OS Paenibacillus sp. oral taxon 786 str. D14.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES72346.1, ECO:0000313|Proteomes:UP000003981};
RN [1] {ECO:0000313|EMBL:EES72346.1, ECO:0000313|Proteomes:UP000003981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D14 {ECO:0000313|EMBL:EES72346.1,
RC ECO:0000313|Proteomes:UP000003981};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., White A.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Paenibacillus sp. D14.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00011296,
CC 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; GG695982; EES72346.1; -; Genomic_DNA.
DR RefSeq; WP_009225672.1; NZ_GG695982.1.
DR AlphaFoldDB; C6J3N9; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_1_0_9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000003981; Unassembled WGS sequence.
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; 3.
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; IPR021810; T1RH-like_C.
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 Pfam; PF11867; T1RH-like_C; 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:UP000003981};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 292..474
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1045 AA; 119185 MW; 0A660FB664435A02 CRC64;
MAYYTTSYTE SDLEQAALEW FEELNYEKAY GPDISPEGEY PERQFYHDVI LKDRLREALI
RINKHVPREA IEEAIRVIEV PRSPSLLINN KAFQKIITDG IDVQYQAANG DYPTEKVWLF
DTDPDGIDNN DFLVVNQFTV VENQGEKRPD IVVFVNGLPI AVFELKSASN EEVGISDAYN
QVQTYKGAIP SLFTYNSFLV ISDGVNARVG TLTANEDRFM MWRTIDGNDV APSSLPQLEV
LVKGMFEKSR LLDIIKHFVL FQTDGEHLFK ILAGYHQYHA TNKAIASTER ATMDEGDRKI
GVIWHTQGSG KSLSMVFYAG KLVLTLNNPT IVVVTDRNDL DDQLFSTFSK SKDLLRQTPQ
QAENRTHLRE LLSVESGGII FTTVHKFTPD EHEDKYPVLT ERRNVIVIAD EAHRSQYGFQ
ADMVAGDDEA AIKYGYAKYM RDALPNASYI GFTGTPVELT DKNTPAVFGD YIDIYDMTRA
VEDGTTVRIY YESRIARLDL SEAERPVIDS EYEDITEYQE YTQRERLKSR WARLEALAGA
EKRVRKVAQD VVEHFEQRQK AGFGKAMIVV MSRRIAIDMY KAIVALRPDW HSDDDNEGKI
KIVMTGSSSD PEEWQPFIGN KRRREHLAKR MKDVNDPLQI VIVRDMWLTG FDVPSMNTMY
IDKPMKGHNL MQAIARVNRV FRDKPGGLIV DYIGIADLLK SALQQYTEND RKTAGIDTDQ
AVDFMLERLQ LIRELLHGYD YSKFASEKAS ERMKAIVETV DYVLGLGEES KRNFLNWTTE
LARAFSLCAT TPAAEEVNVE ISFFKAVKSG IIKLITDENK RKTTKELDAE LNQLISKSVV
SDEVVDILEA VGLQKPNIAI LSDEFLEHVR GLKQKNLAVE LLRRLLQGKV KAVSRTSIVQ
SKKFSEMLEE AIRKYNNRTI ETTQVIEELI QMAKEMNAAV KRGEDLGLIK EELAFYDALA
SNESAKELMG DLMLKQIAHE LTQAIKSNIK VDWTLRENVR AQMRITVKRL LKKYGYPPDL
EKMAIDLVLQ QAELMAQAET EEFKY
//
