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Database: UniProt
Entry: F4RRA1_MELLP
LinkDB: F4RRA1_MELLP
Original site: F4RRA1_MELLP 
ID   F4RRA1_MELLP            Unreviewed;       333 AA.
AC   F4RRA1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   08-NOV-2023, entry version 47.
DE   RecName: Full=Endonuclease {ECO:0000256|RuleBase:RU366055};
DE            EC=3.1.30.- {ECO:0000256|RuleBase:RU366055};
GN   ORFNames=MELLADRAFT_78192 {ECO:0000313|EMBL:EGG05186.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU366055};
CC   -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC       {ECO:0000256|ARBA:ARBA00010052, ECO:0000256|RuleBase:RU366055}.
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DR   EMBL; GL883114; EGG05186.1; -; Genomic_DNA.
DR   RefSeq; XP_007411551.1; XM_007411489.1.
DR   AlphaFoldDB; F4RRA1; -.
DR   STRING; 747676.F4RRA1; -.
DR   EnsemblFungi; EGG05186; EGG05186; MELLADRAFT_78192.
DR   GeneID; 18933077; -.
DR   KEGG; mlr:MELLADRAFT_78192; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_78192; -.
DR   eggNOG; KOG3721; Eukaryota.
DR   HOGENOM; CLU_055174_0_2_1; -.
DR   InParanoid; F4RRA1; -.
DR   OrthoDB; 5487361at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0005736; C:RNA polymerase I complex; IEA:EnsemblFungi.
DR   GO; GO:0004529; F:DNA exonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IEA:EnsemblFungi.
DR   GO; GO:0051607; P:defense response to virus; IEA:EnsemblFungi.
DR   GO; GO:0006310; P:DNA recombination; IEA:EnsemblFungi.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:EnsemblFungi.
DR   CDD; cd00091; NUC; 1.
DR   Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR   InterPro; IPR018524; DNA/RNA_endonuclease_AS.
DR   InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR   InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
DR   InterPro; IPR044925; His-Me_finger_sf.
DR   InterPro; IPR040255; Non-specific_endonuclease.
DR   PANTHER; PTHR13966:SF5; ENDONUCLEASE G, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13966; ENDONUCLEASE RELATED; 1.
DR   Pfam; PF01223; Endonuclease_NS; 1.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
DR   SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR   PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW   ECO:0000256|RuleBase:RU366055}; Hydrolase {ECO:0000256|RuleBase:RU366055};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR640255-2,
KW   ECO:0000256|RuleBase:RU366055};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU366055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001072}.
FT   DOMAIN          83..300
FT                   /note="DNA/RNA non-specific endonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00892"
FT   DOMAIN          84..300
FT                   /note="Extracellular Endonuclease subunit A"
FT                   /evidence="ECO:0000259|SMART:SM00477"
FT   REGION          28..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640255-1"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640255-2"
SQ   SEQUENCE   333 AA;  36915 MW;  182B88CAC7A9DC70 CRC64;
     MASTLTQSAL FVAGIVLGAS TAIVYKNKQT DSSSTSSSST TNPNSDSSNQ PIFTRQFHSE
     FKSQAPNQIL KFGNPGPIND FFSRQAYAMG YDRRMRNPSW TAEHLTSSNI RPPRSPGGDQ
     PDRSHSNFHE DPALPPEFRA KLSDYFRSGY DRGHMVPAAD AKISQEAMNE TFILSNIAPQ
     VGEGFNRDYW AHLENFVRQL TTSFSDVYVF TIPLYLPKQD PITQKQIVSY EVIGNPPNVA
     VPTHFAKIVY GVNGHQGSLG SFVLPNTKIS NQIPLRSFET PVDSVEKASG LKLFPDQIKS
     NSSKLCETVK CEMVIRNFDQ ARKQVTGNKN IGP
//
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