ID H2CK05_9LEPT Unreviewed; 1089 AA.
AC H2CK05;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=Lepil_1405 {ECO:0000313|EMBL:EHQ06094.1};
OS Leptonema illini DSM 21528.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptonema.
OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ06094.1, ECO:0000313|Proteomes:UP000005737};
RN [1] {ECO:0000313|EMBL:EHQ06094.1, ECO:0000313|Proteomes:UP000005737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ06094.1,
RC ECO:0000313|Proteomes:UP000005737};
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., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL Submitted (OCT-2011) 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|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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DR EMBL; JH597773; EHQ06094.1; -; Genomic_DNA.
DR RefSeq; WP_002771300.1; NZ_JH597773.1.
DR AlphaFoldDB; H2CK05; -.
DR STRING; 183.GCA_002009735_03942; -.
DR REBASE; 88696; Lil3055ORF1409P.
DR HOGENOM; CLU_005762_1_1_12; -.
DR Proteomes; UP000005737; 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; 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 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; 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:UP000005737};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 270..472
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
SQ SEQUENCE 1089 AA; 125443 MW; DF1DB8D5E9265B16 CRC64;
MAVITEEDLE RELVQILKED HGYRVINAAV PYGDTSSDDG SGRQSRSEVV LKGLLLEKVA
ELNPGIPAKD RQRAVEERLL VSRRAMSPLL ASKEIYQMIR DGIPLEYEGE KGKKESGTLR
LIDFQNGEKN DFLAVRQLNI KGDRYTRIPD VLLYINGLPL VYIELKNSNV KIENAYTDNL
TNCRNDIPRL FDFNAFCILS NAVETRVGSS FADWKFFFSW LRVDDETEKV DRKAIEREGT
SIERVIGGLL GKERLLDYIE NFILYHKDTA KIIAKNHQFH GVNKAVASFA DRKVREGRLG
VFWHTQGSGK SYSMIFLSRK IHRKFTGNFT FLIITDRTDL DGQIYGNFVD TDTVKKSDAA
RPTSSMALRE DLVKNKPFIF TLIQKFQSTR GKEFPILHDS TDSSREIIVI VDEAHRTQYL
SLAENMRRGL PGAHYFAFTG TPLLAGSEKG KTQEWFGGYV SEYSYVQSIE DEATLPLYYE
KRVPEVLIEN PNLSEDFAEI VEDEQLNTEQ RERLENKFAK ELEVIRRDDR LETIARDIAY
HFPRRGYLGK GMVISVDKYT AVRMYEKVKH HWEIEKRNIQ KAMTQASEVE RQALKRSLEF
MRNTQMAVVL SEEVGEKEKF AAKGLEIESH RKLLNTPNEE GQTIEDRFKK EDDPLNLVFV
CAMWLTGFDA PSVSTLYLDK PMKGHTLMQT LARANRVTGH LIYGRSKTNG EVIDYYNVFR
NMQQALSDYA TGSEGQTQKE TEATGEDVIP PKSNLFELLD AAIEEGVTFL SKHDIDLMQI
PTKKSVLKQT ALFKEFSDTL LADDLTRQEF FLYENAISSL YDACRPEVTK EQARPIVPLF
SYLREMIEAI IKTKDIDSAV QRVSALLDES VVTTEEGILV KEPAPEYQIR QKGKVWDLSK
LDFEQLKNEF KTKPHKNIEI TVLKEFLIEK LDRMMRENGE RAPFVERLQS IIENYNSGTV
IHESTYEELV NFASDLKVEE ERHIRENLSP DELELFDLLK KEKMTKDEEI SVKKAAKALL
HRLKEESPKV LVQDWFRDST SLIRVKEAVT DILEETLPDS YDRVLFSKKC ERTFEVIRTY
AEKGEKWVA
//
