ID   A0A0D2CSM8_9EURO        Unreviewed;       680 AA.
AC   A0A0D2CSM8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Selenoprotein O {ECO:0000256|ARBA:ARBA00031547};
GN   ORFNames=PV04_04152 {ECO:0000313|EMBL:KIW68191.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW68191.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW68191.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW68191.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN846958; KIW68191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2CSM8; -.
DR   STRING; 5601.A0A0D2CSM8; -.
DR   HOGENOM; CLU_010245_2_1_1; -.
DR   OrthoDB; 5487961at2759; -.
DR   Proteomes; UP000054266; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   HAMAP; MF_00692; SelO; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   680 AA;  77013 MW;  EF60D16593C77A24 CRC64;
     MEIVVNIYVL VIFFTALCML LRRVSQLSRP KLTSPSRSIP RVRLAQMASH TNGFNGHANG
     HHKIENTSTT TLADIPKSHT FTSKLPADAQ FPTPLDSHRA PRQKLGPRMV RSALFTYVRP
     EPTEDPELLA VSKAALRDIG LAESEADSEE LKQVVAGNKI YWDEDKPEEG VYPWAQCYGG
     FQFGSWAGQL GDGRAMSLFE TTNPATGVRY EVQLKGAGKT PYSRFADGKA VLRSSIREFI
     VSEYLNAIGI PTTRALSLTL CPKNEVVRER LEPGAIVCRF AQSWVRFGTF DLLRSRGDRD
     LIRTLATYVA EEVLGGWENL PAALPSLDDN KDAHLEPARN VPKDAIQGKE GAEENRFTRL
     YREITRRTAL LVGKLQAYGF MNGVLNTDNT SILGLSLDYG PFAFMDNFDP AYTPNHDDHM
     LRYAYRAQPS VFWWNLVRLG EALGELIGAG DKVDDEIFAT KGVEEEFAPV LIKRAETIID
     QCSDEYKAVF LSEYRRLMTA RLGLKTQKES DFDKLFSELL DTMEALELDF NHFFRRLSSV
     KLSDVETKEG RENTAERFFH HGGVTGLNET NDSGREKIGA WLEQWRQRII EDWDMSTEDA
     DSQRCQSMKS VNPNFVPRGW LLDDIIDRVQ NKNEREILQG VMEMTLHPFE DAWGWKEDVE
     EQYCGDVPRF KRAIQCSCSS
//