ID A0A2P8WDK9_9CYAN Unreviewed; 898 AA.
AC A0A2P8WDK9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
DE Flags: Fragment;
GN ORFNames=C7271_15310 {ECO:0000313|EMBL:PSN17905.1};
OS filamentous cyanobacterium CCP5.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107701 {ECO:0000313|EMBL:PSN17905.1, ECO:0000313|Proteomes:UP000240885};
RN [1] {ECO:0000313|EMBL:PSN17905.1, ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|EMBL:PSN17905.1,
RC ECO:0000313|Proteomes:UP000240885};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|Proteomes:UP000240885};
RA Moore K., Momper L.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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:PSN17905.1}.
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DR EMBL; PYEQ01000295; PSN17905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8WDK9; -.
DR OrthoDB; 9802848at2; -.
DR Proteomes; UP000240885; 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; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013670; EcoEI_R_C_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF08463; EcoEI_R_C; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF04851; ResIII; 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};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:PSN17905.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000240885};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 173..362
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT NON_TER 898
FT /evidence="ECO:0000313|EMBL:PSN17905.1"
SQ SEQUENCE 898 AA; 101990 MW; BB7CE677B2995A80 CRC64;
MAANQNPEQQ ARDLIDALLR DAGWIVQSKQ QFDLGAGLGV AIREYQTDAG PADYVLFVDR
QPIGVIEAKR EEAGHRLTVV EEQSAEYADS KLKYLNNQPL PFIYESTGVL TRFTDRRDPK
PRSRPVFSFH KPETFQAWLK QGKSLRARLL ELPGLDPEGL RACQISAITQ LEGSFQENRP
RALVQMATGS GKTFTAITSV YRLLKHAKAQ RVLFLVDTKN LGEQAEQEFM AYRPTDDNRQ
FTELYAVQRL QSRYVPRDAQ VCISTIQRLY SILKGEELDE GAEETNPNEM VQPKQPVPVV
YTPRVPIEFF DFIIIDECHR SIYNLWKQVL DYFDAFLIGL TATPDKRTFG FFNENVVSEY
THEQAVADGV NVGHEVYTIE TEITKNGSRL VAKEYVGKRE KLSRRQRWEQ LDEEMTYSGK
QLDRDVVNPS QIRNVIKAYR EKLPEIFPNR TEVPKTLIFA KSDSHADDII HVVREEFGQG
NDFCKKVTYK AEEDAKSVLA QFRNAYNPRI AVTVDMIATG TDVKPIECLL FMRDVRSKNY
FDQMKGRGTR ILDQDSLRKV TPSAQSAKTH FVIVDAVGVT KTLKTETRPL ERKKGVALKD
LMMGVAMGAQ DEDAFVSLAG RLCRLDRQME PREREGLRKL TNGVGPSEMA KTLLNAYDPD
AIREQAQRDH HLSPHEEPTE VQTATAQQGL LRAAASLFNG AVVDYIENVR KVHEQVIDTV
NLDQVTFAGW DTQAQEQSAN LAQDFAQFIE SNKDEITALR IFYNLPYQQR TLTLAMVREV
LEKLKREKPQ LAPARVWQAY ARLDGVQPTN PISELTTLVA LIRRVVGLDE RLTPYASTVD
RHFQTWIFGK QAGAAPKFTE AQVAWLRMVK DHITMSFHIE VADLDYAPFD GGGGLGRM
//
