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Database: UniProt
Entry: A0A139HW15_9PEZI
LinkDB: A0A139HW15_9PEZI
Original site: A0A139HW15_9PEZI 
ID   A0A139HW15_9PEZI        Unreviewed;       623 AA.
AC   A0A139HW15;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   RecName: Full=Selenoprotein O {ECO:0000256|ARBA:ARBA00031547};
GN   ORFNames=AC578_8611 {ECO:0000313|EMBL:KXT06617.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT06617.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT06617.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT06617.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT06617.1}.
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DR   EMBL; LFZN01000005; KXT06617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HW15; -.
DR   STRING; 321146.A0A139HW15; -.
DR   OrthoDB; 5487961at2759; -.
DR   Proteomes; UP000070133; 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:UP000070133};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  70706 MW;  71C97A134AB358C2 CRC64;
     MASHISNGEQ KMFSIRDLPK SNNFTQKLPP DPEFLTPAAS HKAERKQLGP RLVKSAAYTF
     VRPEPFKKSE LVGVSKAALK DLAIDPASVE TEDFKKTVAG EQIVTIDQDK EPGDNDIYPW
     AQCYGGYQFG SWAGQLGDGR AISLFETTNP NTGKRYELQL KGAGKTPYSR FADGKAVVRS
     SIREFVVSEA LNALKIPTTR ALSLTLGPEE HVRREMTEPA AMVARFAESW IRLGTFDLPR
     SRGDRDMVRK LADYVAENVY AGWESLPAKV PSNEEKDVVE PSSGVSKDEI QGEDETAENR
     YTRLFREVAR RNAKTVAAWQ AYGFMNGVLN TDNTSIFGLS IDFGPFAFMD NFDPNYTPNH
     DDHMLRYSYK AQPSIIWWNH VRLAEALGEL IGAGPWCDDE EFATKGVRKE RADELIKRAE
     TLIDRVGEEY KAVFMAEYKR LMTARLGLKQ CKEGDFEELY SELLDTLEAL ELDFNHAFRR
     MSNISMVDID SHEKAKDVAG RFFHHEGLSG LAGNEDDARE RLAKWLGKWR SRILEDWPSS
     EEARKERIAA MKAVNPNFVP RSWVLDELIE RVEKKGEREI LGHIMDMALE PFNDNWGWNK
     EEEDRFCGDV PKYQRAMQCS CSS
//
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