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Database: UniProt
Entry: A0A0A5FV68_9BACI
LinkDB: A0A0A5FV68_9BACI
Original site: A0A0A5FV68_9BACI 
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
//
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