ID A0A177D4U1_ALTAL Unreviewed; 622 AA.
AC A0A177D4U1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=Selenoprotein O {ECO:0000256|ARBA:ARBA00031547};
GN ORFNames=CC77DRAFT_1067175 {ECO:0000313|EMBL:OAG14122.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14122.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG14122.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14122.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441502; OAG14122.1; -; Genomic_DNA.
DR RefSeq; XP_018379543.1; XM_018528965.1.
DR AlphaFoldDB; A0A177D4U1; -.
DR STRING; 5599.A0A177D4U1; -.
DR GeneID; 29114559; -.
DR KEGG; aalt:CC77DRAFT_1067175; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1067175; -.
DR OMA; YGPYGWL; -.
DR OrthoDB; 5487961at2759; -.
DR Proteomes; UP000077248; 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 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 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:UP000077248};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 70378 MW; 4E02490BD8C192AA CRC64;
MAHLDNSQTA SNSSNKLQTL QSLPKSNVFT SNLPADDAFP RPKDSHDAPR QMLGPRMVKG
ALYTYVRPDS QGEPELLAVS QRALQDIGLK PEEAETEEFK EVVAGKKILT WNESNPEAGI
YPWAQCYGGY QFGQWAGQLG DGRAISLFES TNPATGTRYE IQLKGAGRTP YSRFADGRAV
LRSSIREFVV SEYLNAINIP STRALALTLN NGSKVMRERT EPGAIVTRFA QSWIRFGTFD
LQRIRGDRKT LRILADYTAE HVYGGWDKLP SKLPAGDAKD VHNQTSSGIS RDTVEGEGAG
EENRYVRLYR AIIRRNAETV AKWQAYGFMN GVLNTDNTSI LGLSIDFGPF AFLDTFDPTY
TPNHDDHMLR YSYRNQPTII WWNLVRLGEA LGELMGAGSK VDEAQFVEKG VTEEEADGIV
KCAESAIDRA GEEYKAVFLA EYRRLMTLRL GLKTQKDSDF EELMSELLDS LEMFELDFHH
AFRRLGAIKL SDVETEDQRK DVAGRFFKKD SAPRQESDGR ERLGKWLEKW AARVKEDWGE
GKDDERKAAM DAVNPNFIPR SWILDELIER VEKQGEREIL PQIMKLALNP FQETWEWNAD
EEERFCGDVP KHKGMMQCSC SS
//
