ID A0A2K8SN85_9NOSO Unreviewed; 1136 AA.
AC A0A2K8SN85;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=COO91_02828 {ECO:0000313|EMBL:AUB36899.1};
OS Nostoc flagelliforme CCNUN1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB36899.1, ECO:0000313|Proteomes:UP000232003};
RN [1] {ECO:0000313|EMBL:AUB36899.1, ECO:0000313|Proteomes:UP000232003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB36899.1,
RC ECO:0000313|Proteomes:UP000232003};
RA Shang J.;
RT "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT its photosynthetic adaptation to extreme terrestrial habitat.";
RL Submitted (NOV-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|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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DR EMBL; CP024785; AUB36899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8SN85; -.
DR REBASE; 225813; NflNUN1ORF2827P.
DR KEGG; nfl:COO91_02828; -.
DR Proteomes; UP000232003; Chromosome.
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; cd07344; M48_yhfN_like; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 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; IPR002725; YgjP-like_metallopeptidase.
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; PF01863; YgjP-like; 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 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:UP000232003};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 342..513
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1136 AA; 130443 MW; 3A7E88B6FB048B39 CRC64;
MRQLPGGLGW EHIKANHLAA IPEQRDDYHE VLLLSRLQRQ LREINLDPNG QPWLDQRRIN
QAINQLQNLG PGKLMEKNET LTKLLLTGVK VEGLTGKQTT INLIDFDHPE RNDFLAISQF
RIDPPGINGP KGHYRPDIIL FVNGIPLVVI ECKAPGADML KSGIKDLLKY SNQRNSPQPE
GIERVFHYNQ LMISCTSGRA VVGTVGSQPK HYLEWKDTSP FESSLIAQVL DITNPTLPEE
ELISSASNYL LPESTPTRED EALAAVKSGE KLEDLIDLSK LNRRQQLIAG MLHPASLLDI
LRHYILFTTK HNRRIKIVPR YQQFRGVSKA VDRLIHGKTK TEHGSQDQRG GIIWHYQGSG
KSLDMVFILR KLRTIPQLQQ FKAIIVTDRT DLEDQLQQTA TLSGQTLQVA QNIKDLANKL
RQTGPGIVFG MVQKFNKINE AKEYADIEEL NNALNPSEGI LLLIDEAHRS HSNTLHAYLS
KALPNCAKIG FTGTPIISAK KKKTKDIFAH DENPYIDIYS IRDSQKDKVT VPIFYEGLEA
MGAVKGATTL DQLFEVLFQD YTPQERAAIK SKYVGKRNVL KAKELMRAKA RHILRHYVTR
IMPDKFKAQV AASDREACVL YQQYLTAAKD ELIQELESNA VILQSLKLES APAEYRTLLE
AYPYLNTIKR LEFAAIISAN SKQDPQAWKQ WTDENNHTTY KNRFWKNLDE DGLAFLIVNN
KLLVGFDAPL EQVLYVDRSL VEHDLLQAIA RTNRTAEGKG YGLIVDYYGI DIAAAMSVYD
QEDVDGAWFD IQEELPKLNE AHRRAMNFWQ ERNLNIYDDK EACINILNHD ERSRAEFYQL
LREFLQAMDA FLPRPQALRY LKDAKELGEL KKLVDDIFRD ERPEDAKEKV QALIDQHIQS
QGINLKVSRA SIFDLDFELR ESPRRRTVEI TIERDGQLII TTPPQVPVEK LGQIIEQRRF
WIYSKLLKKS AIKQPSEQKT YLPGEGFHYL GRSYRLKLVD SADNPLRLYQ GRFELLRSHQ
EQGRDLFIQW YRGHIQQHLE LITTSIANRI GAKPTSIQVR ELGNRWGSCN PKGDIYFHWR
VALLPNAMIE YVVVHEMVHL VQPNHNRYFW DRVERILPDC VERKDWLAKN GAIFSL
//
