ID A0A164VJ80_9AGAM Unreviewed; 707 AA.
AC A0A164VJ80;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Selenoprotein O {ECO:0000256|ARBA:ARBA00031547};
GN ORFNames=SISNIDRAFT_453935 {ECO:0000313|EMBL:KZS94206.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS94206.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS94206.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS94206.1,
RC ECO:0000313|Proteomes:UP000076722};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the SELO family.
CC {ECO:0000256|ARBA:ARBA00009747}.
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DR EMBL; KV419405; KZS94206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164VJ80; -.
DR STRING; 1314777.A0A164VJ80; -.
DR OrthoDB; 5487961at2759; -.
DR Proteomes; UP000076722; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR003846; SelO.
DR PANTHER; PTHR32057; PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL; 1.
DR PANTHER; PTHR32057:SF14; PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL; 1.
DR Pfam; PF02696; SelO; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000076722};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 96..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 79114 MW; CB46644AF098C263 CRC64;
MTFEKKPISA FQLPPVSHLL QHNLTPDPVA DSVKAFSEVL ATTPSVQRRS RLLKSSAHFS
YVSPLPISFP YRIEIPEDDS EADKSGYIER WLSRREPREE RPGVKGSPHL KKYSSTERDT
LPEANILALA PTTLTDYFPQ LDVGDSFEVL GEPALSAKHS NALDDKSEEQ GTAVREELVN
ILSGRNVLFS LPTEESSGAS DMPTPYAPWS LRYSGHQFGV WAGQLGDGRA ISILEVAHPN
DPESTYEIQL KGAGRTPFSR GADGLAVLRS SIREFLCAEA MNALHIPTTR SLSIVHIPDL
PVARETMESA SIVARVAPSF IRIGSFEALN PPQDLFFFGG GGQQQADYEA LRILGEWVSR
RVLKLNIPEG EPWGKALVWE CARRNAKMAA GWQAYGFMHG VMNTDNISIM GLTIDYGPYA
FMDVYDSKHI CNHTDQEGRY AFELQPTMIL YALRALLTSL APLIGAELET GKAVGTDWAS
SVSAEKIKEW SAKAQELSND LEVEIQDVFS AEYWTLMRKR LGLRTVEPAD ESQLIRPMLR
LLEEQGLDFH RTFRALCAFR PTQPGDETWD AVAKTLAGKD SIDDASSKEW KEWLSIYSQR
INRERSSWKD GDAWIDDRAQ VMKAANPRFV LRQWLLEELI AKCEKDPDTG KRILAKVLKM
ASSPFEPWGA EEGSQPESEL SEETREERRY CDVGEKQMLG FQCSCSS
//
