ID A0A0A5FV68_9BACI Unreviewed; 1052 AA.
AC A0A0A5FV68;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=N784_12095 {ECO:0000313|EMBL:KGX84681.1};
OS Pontibacillus litoralis JSM 072002.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX84681.1, ECO:0000313|Proteomes:UP000030401};
RN [1] {ECO:0000313|EMBL:KGX84681.1, ECO:0000313|Proteomes:UP000030401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX84681.1,
RC ECO:0000313|Proteomes:UP000030401};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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:KGX84681.1}.
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DR EMBL; AVPG01000033; KGX84681.1; -; Genomic_DNA.
DR RefSeq; WP_036836092.1; NZ_AVPG01000033.1.
DR AlphaFoldDB; A0A0A5FV68; -.
DR STRING; 1385512.N784_12095; -.
DR eggNOG; COG0610; Bacteria.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000030401; 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; 1.20.58.910; -; 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; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME R PROTEIN; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000030401};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 281..469
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 908..935
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1052 AA; 121059 MW; 109C2074E9310E62 CRC64;
MTKLSHNNEA EVERRLIEVL AEGYNQWNYR PDLKSEADLW QNLRQIITQN NLSEIGEHPI
TDKEFDTIKT ELLLRTKTPF EAAKWLKGEN GIARITIERE NVALGPMSLV LYSNHDIGGG
ISRYEVVHQI AKQKATVEDR NRRFDVTLLI NGLPIVQIEL KQASAKDGVF QAFNQVKKYA
EEGMFRGNIF STLQLFVVSN EQTTRYFANA MPKNMYKKFL FSWRTRDNQK VDNLYEFVKQ
ALNIPDAHRL VADYTIVSED QDNKVLMVLK PYQIHAIQAL YTSASKHQSG YIWHATGSGK
TLTSFVSTKL LAKKPGVDRT IMLIDRKDLD SQTTSEFTKF ASEYNTGIST GNARSNSLII
GTGSAKELSD TLLSDANTNT VIIMTRQKLE SAIRYTEKVE EKKGTQRFKK LLGQHIVFIV
DECHRALSAE GMEDMKEFFP NSTWFGFTGT PIFEVNKKQA KGNLARTTRD QYGDVLHTYT
IKNALEDGAV LGFQVEHENT IETTSLQNII FDQLRKSTKY ANAADEEINQ FIDEMDGIEQ
ETYLDPSIYE KQEHIQQVLR KIFRPDNAYM KFNFENGRPQ KSAILTTSSI NMAKRYYHAI
KEMTKDPEWL QNVFANQPIR TGRTMEDPDF PRIAITYSLQ EDDEKAAANQ DEMKEIIKEY
NGYYDTAWSL ESIDRYNGDI NNRLARKRAE FKEFGKQVDL VIVVERLLTG FDAPTVQTLF
VDRNLEYANL IQAFSRTNRT YPGKEKGLIV TFRKPHTMEY NVQEATKVYS NEDEASTLIY
PTYEESKKRF KKSHKKLQSV APNIEEIDEH TPIETRVEFV KAFQELNNAY EALVTYNEYN
DDVESSEALQ GQVKIIEESV GIYNTVKGSL IEVDDGGGEE VDFSDIEFYG ENAVKIYDVD
SSYIDKLLET YSANNKNIRD DIENALQKLE KKEIVKEVYR AILNAIDNDE VAADEDIFIV
KRAYFTDAQN KAILDFSNTW FVDKEALHLS KVQYLVGMDP IPNISDIINS RDFEQYKAVN
PDAKPLKYGP EMKRQWRKIL DDTLIPLRDE LR
//