YL720_MIMIV
ID YL720_MIMIV Reviewed; 274 AA.
AC Q5UNW7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 02-JUN-2021, entry version 68.
DE RecName: Full=Endonuclease 8-like L720;
DE AltName: Full=Endonuclease VIII-like L720;
GN OrderedLocusNames=MIMI_L720;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV50980.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY653733; AAV50980.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_003987249.1; NC_014649.1.
DR PDB; 4MB7; X-ray; 2.04 A; A=2-274.
DR PDBsum; 4MB7; -.
DR SMR; Q5UNW7; -.
DR GeneID; 9925374; -.
DR KEGG; vg:9925374; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:InterPro.
DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR Gene3D; 3.20.190.10; -; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..274
FT /note="Endonuclease 8-like L720"
FT /id="PRO_0000248636"
FT ZN_FING 241..274
FT /note="FPG-type; degenerate"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 64..79
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:4MB7"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:4MB7"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4MB7"
FT HELIX 206..231
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4MB7"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:4MB7"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:4MB7"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:4MB7"
SQ SEQUENCE 274 AA; 32402 MW; 86F5F7A5D68D4491 CRC64;
MVEAPRIRIT YEKIRHTKNH RIVSISGPSY KRMNVDLIDY IIRKWWFAGK YIYLMLISSN
KPTYVIRTHM MMHGRILVGN QDSPTKRAFM IIQLDNDIVL RWYRSQITLL DPNCLAEIKT
NYTICTTRQA IMDSIKLMKY DLSNNRFDYN LFQSHLKNGI NIHSSEIITD FLLDQEYFPG
VGNILQQEAL YDCKILPLKK VQDIDEPMFD CLCNSLKKII DLLYESYKFR ESGKEFGPIL
RIYRKSLCPL GHKTIRKKIG LRNRMTTWCP VCQL