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Database: UniProt
Entry: M1HD38_9PHYC
LinkDB: M1HD38_9PHYC
Original site: M1HD38_9PHYC 
ID   M1HD38_9PHYC            Unreviewed;       314 AA.
AC   M1HD38;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   SubName: Full=GIY-YIG catalytic domain-containing endonuclease {ECO:0000313|EMBL:AGE49697.1};
GN   Name=Can18-4_056L {ECO:0000313|EMBL:AGE49697.1};
GN   ORFNames=PBCVCan184_056L {ECO:0000313|EMBL:AGE49697.1};
OS   Paramecium bursaria Chlorella virus Can18-4.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=1278252 {ECO:0000313|EMBL:AGE49697.1, ECO:0000313|Proteomes:UP000246183};
RN   [1] {ECO:0000313|EMBL:AGE49697.1, ECO:0000313|Proteomes:UP000246183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeanniard A., Dunigan D.D., Gurnon J.R., Agarkova I., Kang M., Vitek J.,
RA   Duncan G., McClung O.W., Larsen M., Claverie J.-M., Van Etten J.L.,
RA   Blanc G.;
RT   "Towards defining the chloroviruses: a genomic journey through a genus of
RT   large DNA viruses.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: To endonucleases of group I introns of fungi and phage.
CC       {ECO:0000256|ARBA:ARBA00010045}.
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DR   EMBL; JX997157; AGE49697.1; -; Genomic_DNA.
DR   Proteomes; UP000246183; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   CDD; cd10443; GIY-YIG_HE_Tlr8p_PBC-V_like; 1.
DR   Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR006350; Intron_endoG1.
DR   InterPro; IPR003647; Intron_nuc_1_rpt.
DR   InterPro; IPR003611; NUMOD3.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR01453; grpIintron_endo; 2.
DR   Pfam; PF07460; NUMOD3; 7.
DR   SMART; SM00465; GIYc; 1.
DR   SMART; SM00497; IENR1; 1.
DR   SMART; SM00496; IENR2; 7.
DR   SUPFAM; SSF64496; DNA-binding domain of intron-encoded endonucleases; 4.
DR   SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
PE   4: Predicted;
KW   Endonuclease {ECO:0000313|EMBL:AGE49697.1};
KW   Hydrolase {ECO:0000313|EMBL:AGE49697.1};
KW   Nuclease {ECO:0000313|EMBL:AGE49697.1}.
FT   DOMAIN          1..90
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|SMART:SM00465"
FT   DOMAIN          92..108
FT                   /note="Nuclease associated modular"
FT                   /evidence="ECO:0000259|SMART:SM00496"
FT   DOMAIN          116..132
FT                   /note="Nuclease associated modular"
FT                   /evidence="ECO:0000259|SMART:SM00496"
FT   DOMAIN          133..149
FT                   /note="Nuclease associated modular"
FT                   /evidence="ECO:0000259|SMART:SM00496"
FT   DOMAIN          157..173
FT                   /note="Nuclease associated modular"
FT                   /evidence="ECO:0000259|SMART:SM00496"
FT   DOMAIN          181..197
FT                   /note="Nuclease associated modular"
FT                   /evidence="ECO:0000259|SMART:SM00496"
FT   DOMAIN          205..221
FT                   /note="Nuclease associated modular"
FT                   /evidence="ECO:0000259|SMART:SM00496"
FT   DOMAIN          229..245
FT                   /note="Nuclease associated modular"
FT                   /evidence="ECO:0000259|SMART:SM00496"
FT   REGION          87..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   314 AA;  35358 MW;  043F9A6051D732B0 CRC64;
     MGFIYKATYR VSRKAYIGQT IQPIEKRLLQ HQYPSSKCRA FLGAIKKYGW ENFDVDWYEC
     PDEDLNDLEE YLVAVLGTLA PGGYNLKEGG GAHGKPSVET REKMSEAHKG EKNHMYGKTL
     SKETKQKLSE AHTGKTLSKE TKQKMSEALS GEKHPMFGKT LSKETKQKIS EALSGEKSHM
     FGKTLSKETK QKISEALSGE KCYMYGKTLS KETKQKMSES TKGENNHFYG KTHAKETKEK
     ISAAKTGAKN PRSKKVYRYE LNGTFVDYFG SSGEAARHVM SSEENEGSVK ASIGKCARGE
     REYVHGFKWS YTKL
//
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