ID A0A1Y4L1E4_9FIRM Unreviewed; 1043 AA.
AC A0A1Y4L1E4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=B5F18_11560 {ECO:0000313|EMBL:OUP48601.1};
OS Lachnoclostridium sp. An181.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965575 {ECO:0000313|EMBL:OUP48601.1, ECO:0000313|Proteomes:UP000242090};
RN [1] {ECO:0000313|Proteomes:UP000242090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An181 {ECO:0000313|Proteomes:UP000242090};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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}.
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:OUP48601.1}.
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; NFKJ01000027; OUP48601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4L1E4; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000242090; 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:0004386; F:helicase activity; 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; 1.20.58.2040; -; 1.
DR Gene3D; 3.90.1570.50; -; 2.
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 Helicase {ECO:0000313|EMBL:OUP48601.1};
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:UP000242090};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 310..472
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1043 AA; 121185 MW; F010DE70839C971D CRC64;
MNSFEIVASS TESTVVAEYT PEKRKSTDYQ SEAELEQDFI NRLVSQGYEY ITIKSEQDLI
DNLRAQIEKL NNYTFFDKEW KDFYNSVISN GNDGIIEKTR KIQEDYLQNI ILDNGYVKNI
KLIDKTNIHN NHLQVINQYE EDKGKHDTRY DVTILVNGLP LVHIELKKRG NAIREAFNQI
NRYQRDSFWA GSGLYQYVQL FVISNGTHTK YYSNTTRFQH IKDNAEKNAT KKKKTSNSFE
FTSYWSDEKN RTIPDLVDFT KTFFAKHTLL NILTRYCVFT SEDLLLVMRP YQIAAIEKIL
NRIIVSTNLK KTGRKEAGGY IWHTTGSGKT LTSFKTAQLA QGLNFIDKVL FVVDRKDLDY
QTMKEYDRFE KGAANSNTST KILQKQMEDD NAKIIITTIQ KLDKFISKNQ EHEVYKKHIV
MIFDECHRSQ FGDMHKSITK HFKNYHIFGF TGTPIFPSNS NSSNAPNMRT TAQVFGGDPD
ENGNNVRPLH AYTIVDAIHD GNVLPFRIDY INTIKNPEIL YDKQVKAIDR EKALLDPKRV
SEITQYILEH FEQKTYRNQN RSYYDHKVIT NVEKMAKSKN NTVSEQKIIT KVNGFNSIFA
VASIPAAIVY YNEFKKQMEE TDHKLKIATI FSFNPNEEDP DDILQDESFD TSGLDQTSRD
FLESAIDEYN KMFNVSYDTS ADKFPNYYKD VSLRMKNREI DLLIVVNMFL TGFDATTLNT
LWVDKNLKDH GLIQAFSRTN RILNSVKTFG NIVCFRNLET ATNNALALFG DKNARGIVIL
KTYNEYMNGY EDEHGKHIEG YNELVSRLVN EFPISSQIVG EDNEKEFIKL FSRILKLKNI
LRCFDDFESD SFVCVRDLQD YQSVYIDLYQ NYAKQSDIEK ERINDDIVFE IELIKQVEVN
IDYILMLVAK YHESNCEDKT ILANINKSVN ASVELRSKKA LIEGFVAQMT VKTDVEKDWK
DFVKKQKKHD LETIIKDENL KHDETQKFIE NSFRDGEIKT TGTDLDKILP PISRFSGGSN
RALKKQTVID KLKEFFEKYF GLI
//
