ID S5MBW4_9CAUD Unreviewed; 264 AA.
AC S5MBW4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE SubName: Full=Putative homing endonuclease {ECO:0000313|EMBL:AGR48118.1};
GN ORFNames=SmphiM12_486 {ECO:0000313|EMBL:AGR48118.1};
OS Sinorhizobium phage phiM12.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Emdodecavirus; Emdodecavirus M12.
OX NCBI_TaxID=1357423 {ECO:0000313|EMBL:AGR48118.1, ECO:0000313|Proteomes:UP000015089};
RN [1] {ECO:0000313|EMBL:AGR48118.1, ECO:0000313|Proteomes:UP000015089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24503070; DOI=10.1016/j.virol.2013.11.027;
RA Brewer T.E., Elizabeth Stroupe M., Jones K.M.;
RT "The genome, proteome and phylogenetic analysis of Sinorhizobium meliloti
RT phage PhiM12, the founder of a new group of T4-superfamily phages.";
RL Virology 450-451:84-97(2014).
RN [2] {ECO:0000313|EMBL:AGR48118.1, ECO:0000313|Proteomes:UP000015089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24503083; DOI=10.1016/j.virol.2013.11.019;
RA Stroupe M.E., Brewer T.E., Sousa D.R., Jones K.M.;
RT "The structure of Sinorhizobium meliloti phage PhiM12, which has a novel
RT T=19l triangulation number and is the founder of a new group of T4-
RT superfamily phages.";
RL Virology 450-451:205-212(2014).
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DR EMBL; KF381361; AGR48118.1; -; Genomic_DNA.
DR RefSeq; YP_009143289.1; NC_027204.1.
DR GeneID; 24423055; -.
DR KEGG; vg:24423055; -.
DR Proteomes; UP000015089; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR003611; NUMOD3.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF07460; NUMOD3; 2.
DR SMART; SM00496; IENR2; 4.
DR SUPFAM; SSF64496; DNA-binding domain of intron-encoded endonucleases; 1.
DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000313|EMBL:AGR48118.1};
KW Hydrolase {ECO:0000313|EMBL:AGR48118.1};
KW Nuclease {ECO:0000313|EMBL:AGR48118.1}.
FT DOMAIN 108..124
FT /note="Nuclease associated modular"
FT /evidence="ECO:0000259|SMART:SM00496"
FT DOMAIN 128..144
FT /note="Nuclease associated modular"
FT /evidence="ECO:0000259|SMART:SM00496"
FT DOMAIN 152..168
FT /note="Nuclease associated modular"
FT /evidence="ECO:0000259|SMART:SM00496"
FT DOMAIN 172..188
FT /note="Nuclease associated modular"
FT /evidence="ECO:0000259|SMART:SM00496"
FT REGION 112..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 264 AA; 31388 MW; 852FAF2EFAE96FC0 CRC64;
MSEKYGFVYI WYDRKKKLYY IGSHWGTEDD GYICSSNRMR KAYRRRPDDF KRRILSRIYT
DRLSLLDEEQ RWFDMVKRKD RYYNLNFDVK YAWWADPDQK LTVGEKISKA LGNPETKQKL
SDAAKRQKRK PLSDETKAKL SKVRKGRKSP MKGKRHSEDT KEKMSVAQTG RKFGPMSEEQ
KAKISDSKKG KPGTPLSQER KDQLSESKRK TYQFLSPDDV LVSIENLREF CRENDLCRAA
MCKIANDNYY SKSYKGWRHK DYKG
//
