GenomeNet

Database: UniProt
Entry: A0A437GXL6_9SPHN
LinkDB: A0A437GXL6_9SPHN
Original site: A0A437GXL6_9SPHN 
ID   A0A437GXL6_9SPHN        Unreviewed;       819 AA.
AC   A0A437GXL6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=EKN06_09315 {ECO:0000313|EMBL:RVQ67109.1};
OS   Croceicoccus ponticola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=2217664 {ECO:0000313|EMBL:RVQ67109.1, ECO:0000313|Proteomes:UP000283003};
RN   [1] {ECO:0000313|EMBL:RVQ67109.1, ECO:0000313|Proteomes:UP000283003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GM-16 {ECO:0000313|EMBL:RVQ67109.1,
RC   ECO:0000313|Proteomes:UP000283003};
RA   Yoon J.-H.;
RT   "Croceicoccus ponticola sp. nov., a lipolytic bacterium isolated from
RT   seawater.";
RL   Submitted (DEC-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:RVQ67109.1}.
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; RXOL01000003; RVQ67109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437GXL6; -.
DR   OrthoDB; 9803459at2; -.
DR   Proteomes; UP000283003; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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};
KW   Helicase {ECO:0000313|EMBL:RVQ67109.1};
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:UP000283003};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          180..362
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          582..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..607
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  92114 MW;  7721D383172A09FC CRC64;
     MLDKQSLSER DICTKFITPA VKEAGWDEMT QIREEVSFTK GRIIVRGKMV SRGQGKRADY
     VLYYRPNIPL ALIEAKDNRQ PIGAGIQQGL GYAETLDIPF VFASNGDGFV FHDRTASGEA
     LETTLGLDAF PSPEELWQRY AAWKGLTPEA EGIVLEDYFD DGSGKTPRYY QVNAVNAAMV
     AIAKGQRRVL LVMATGTGKT YTSFQIIWRL WKGGQKKRIL FLADRNVLVD QTMVNDFRPF
     GPAMAKLSAN AKTIERDDGT KIDLTLAMDK KRRVDTAYEI YLGLYQSITG PEERQKLFKE
     FSPGFFDLIV IDECHRGSAA EDSAWREILE HFSEATQIGL TATPKETKYA SNMHYFGEPV
     YSYTLKQGIR DGFLAPYKVI KVHIDRDVEG YRPEKGQVDR EGNEVEDRIY NTKDFDRNLV
     LDDRTKLVAK KVTEFLKASG DRYQKTIVFC VDQEHAARMR QALINENADL VAENHRYVMR
     ITGNDPDGQA QLGNFIDPES RYPVLVTTSR LLSTGVDAQT CRLIVLDREV GSMTEFKQIV
     GRGTRVHEDT HKFFFTLMDF RGATNHFADP DFDGEPVQIY EPSADDPVTP PDDETDIADE
     DTDQDAITGD GETIIDDGSG TDISIDGGEQ KKGKVYVDGV PVVIVAERVE YLDESGKLVT
     ESLRDFSKKA LRKHFASLDD FLKRWNSSDR KQAIVDELAD EGLSLEVIAD ELGKGLDPFD
     VICHIAFDRK PLTRHERAEQ VKKRDIFGKY GEQARNVLDA LLAKYADEGV LNLDDANVLR
     IPPLNKMGTP FQLLKAFGGK AGFEEAVHAL QHEIYQEVA
//
DBGET integrated database retrieval system