ID A0A0P9D8H0_9CHLR Unreviewed; 1066 AA.
AC A0A0P9D8H0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SE17_05600 {ECO:0000313|EMBL:KPV54132.1};
OS Kouleothrix aurantiaca.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Kouleothrix.
OX NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV54132.1, ECO:0000313|Proteomes:UP000050509};
RN [1] {ECO:0000313|EMBL:KPV54132.1, ECO:0000313|Proteomes:UP000050509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COM-B {ECO:0000313|EMBL:KPV54132.1,
RC ECO:0000313|Proteomes:UP000050509};
RA Hemp J.;
RT "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL Submitted (SEP-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPV54132.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJCR01000107; KPV54132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9D8H0; -.
DR PATRIC; fig|186479.3.peg.331; -.
DR Proteomes; UP000050509; 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; 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; 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:UP000050509};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 330..497
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1066 AA; 121983 MW; C6757A0D7192276C CRC64;
MPSTNSYAEE ISSQLPAVQL LIALGWQYLA PNEALRLRGG KESNVVLTGV LESWLRDHND
ISYKGQRHAF SAASIREVVE RLVNEPFQSL IVTNERLYEL LTLGTSLTQT ISGDRKSYSL
HYIDWQHPEQ NVFHVTEEFV VERQGSHSTR RPDIVLFVNG VPFAVIECKR PDLNLGGDKP
VVEAISQMIR NQNNDEIPHL FLTTQLLLAL SGNDALYATT GTKKEFWAGW REEGASDDAV
QSLINTPLDA TVQDTLYGWR QYGHLARQHF ATLGDRLPTE QDRLVYALLR PARLLELAYQ
YIVFDNGTKK IARYQQYFAI RATIDRVAHL NAQGTRTGGV IWHITGSGKS LTMVMLAKAL
ALHPAISNPR IVLVTDRVDL DDQLWRTFKA CGKAVAKADD GKHLVRLVTN KLNQGEQRVD
IITTVINKFE QAARQKVTEK GHNIFVLVDE SHRSQYGAMH AKMQQVFPNA CFIGFTGTPL
TRAEKSTTEK FGGFIHKYPI RQAVADHAVV PLLYEGRIVE QEVDKQQLEL WFERTTRHLT
DEQKADLKRK MSQSEAINAT EQRIKEIAYN IALHYQETFK SDGWKGQVAC ASKRIALKYW
RYLRENGIDA ELVISPPDTR EGHSEVDEEA PEVQRFWKQM LDRFGSEEAY NKELISSFAR
PDGTEILVVV DKLLTGFDEP RNRVLYIDKP LKEHTLLQAI ARVNRIAEHK DNGYIIDYRG
VLGELNDAMN LYDALAEYDA EDVAGTLTDI SAEIARLPQV HSDVWAIFSG IANQRDREAL
ERHLEDEDRR QHFYEALTEF ARVLKVALSS VQFYETTPEA RVNIYKNDLR FFHQLRQSVK
VRYAEAIDYG DYEEKVRKLM DTHIRATGTN VITQLVNVFD ADQFDAEVAR LDTPTAKADT
ILNRMKRTIT ERMDEDPAFY RRFSELIEET INAYRQGRID QVEYMRRAQE ALDQMRAGEH
RGQPPQLARY QHASAYYGAI HEPLATFGLS DERIADVAIR QEAIIEQNKV TDWANNLDVQ
KKIKRQLDHH FYDVEREAGA EFDFDQVDAM IDQVVEIAKA RDSRSS
//
