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SEGC_BPT4
ID   SEGC_BPT4               Reviewed;         198 AA.
AC   P16010; P39233; Q9T0U9; Q9T0V0;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   12-AUG-2020, entry version 101.
DE   RecName: Full=Putative endonuclease segC;
DE            EC=3.1.-.-;
DE   AltName: Full=Endodeoxyribonuclease segC;
GN   Name=segC; Synonyms=5.1;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kadyrov F.A., Kryukov V.M.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
RX   PubMed=2488704;
RA   Mosig G., Lin G.W., Franklin J., Fan W.H.;
RT   "Functional relationships and structural determinants of two bacteriophage
RT   T4 lysozymes: a soluble (gene e) and a baseplate-associated (gene 5)
RT   protein.";
RL   New Biol. 1:171-179(1989).
RN   [4]
RP   IDENTIFICATION, AND POSSIBLE FUNCTION.
RX   PubMed=1631169; DOI=10.1073/pnas.89.14.6658;
RA   Sharma M., Ellis R.L., Hinton D.M.;
RT   "Identification of a family of bacteriophage T4 genes encoding proteins
RT   similar to those present in group I introns of fungi and phage.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6658-6662(1992).
CC   -!- FUNCTION: Probably involved in the movement of the endonuclease-
CC       encoding DNA.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: To endonucleases of group I introns of fungi and phage.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD42656.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z69339; CAA93271.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42656.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AF158101; AAD42484.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X15728; CAA33750.1; -; Genomic_DNA.
DR   PIR; S10110; S10110.
DR   RefSeq; NP_049761.1; NC_000866.4.
DR   RefSeq; NP_049762.1; NC_000866.4.
DR   SMR; P16010; -.
DR   GeneID; 1258701; -.
DR   GeneID; 1258721; -.
DR   KEGG; vg:1258701; -.
DR   KEGG; vg:1258721; -.
DR   Proteomes; UP000009087; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR003611; NUMOD3.
DR   Pfam; PF07460; NUMOD3; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SUPFAM; SSF82771; SSF82771; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Magnesium; Nuclease; Reference proteome.
FT   CHAIN           1..198
FT                   /note="Putative endonuclease segC"
FT                   /id="PRO_0000164982"
FT   DOMAIN          7..90
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00977"
SQ   SEQUENCE   198 AA;  22217 MW;  13BF7A0F174003D5 CRC64;
     MPMQDHKYFY LYSITNKTTE KIYVGVHKTS NLDDGYMGSG VAIKNAIKKY GIDNFYKHII
     KFFESEKAMY DAEAEIVTEE FVKSKKTYNM KLGGIGGFPK HNTAGAKNGF YGKSHSRETR
     LKISIKSSRK RGPRGPRGKT LKMCGANNPR YGKIAPNAKS VIINGVLYKS IKIAAKALNI
     NYSTLKGRVK AGYYKCQD
 
 
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