ID A0A1X2IWP5_9FUNG Unreviewed; 640 AA.
AC A0A1X2IWP5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=Selenoprotein O {ECO:0000256|ARBA:ARBA00031547};
GN ORFNames=BCR42DRAFT_404860 {ECO:0000313|EMBL:ORZ23475.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ23475.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ23475.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ23475.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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}.
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:ORZ23475.1}.
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DR EMBL; MCGE01000003; ORZ23475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IWP5; -.
DR STRING; 90262.A0A1X2IWP5; -.
DR OrthoDB; 5487961at2759; -.
DR Proteomes; UP000193560; 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:UP000193560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 71714 MW; 9DB54DAD0758EE5E CRC64;
MGIRTMTKRS LDSLPSPTNL LTQTLSGDTT NSTSKHFTRI SRPVMAHYAV VYPDPSPDPV
LLSAATPSAN AIDLDPASFT TPQFLSVFSG ETILPGTQPY AINYAGHQFS LFAGQLGDGR
AISLFETENS QGERWDVQIK GAGRTPFSRF GDGYAVLRSS IREYLGAEHM HALGIPTTRS
LALLGSSRQV YRDDTTSRQP ERGAIVVRLA PSWIRFGNFE LFYSRNDMNG VRQLADYCLD
HVFGGGGNKL DSHYSCLKDL ADDHKMPATA ADKGKDKDKS SLNAPVDGNK YAQLFIKIAK
RTAVMVAGWQ ANGFNHGVMN TDNMSVLGLT LDYGPFQILD YYDPSYVCNH SDDAGQYAFK
RQPTVCIYNL FKLGVPLFEL IGAKDKVDTL IYANKDKDAN EEEDTERQQT PTDESTRQEY
REIGKEYVTK ILSEDFTDWF MEALDTKMRA KLGLTRQDET IMHDVIIPLL DWATEYEVDY
HRFFRSLSNY TITADGEDGD ADVALDIENS GSSGGTKLDI VTKDLERLVE CKETLKPWLA
IYRHAILLEE EESTGHHHLQ QQQQTPATTD ARRLRMDANN PEVIDAFENL PEAEAIKILN
DCLYACSHPY QDHYDQEIVE RWISTPVPEW SEGLKCSCSS
//
