ID K1X6P9_MARBU Unreviewed; 627 AA.
AC K1X6P9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=Selenoprotein O {ECO:0000256|ARBA:ARBA00031547};
GN ORFNames=MBM_05612 {ECO:0000313|EMBL:EKD16318.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16318.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16318.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16318.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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; JH921439; EKD16318.1; -; Genomic_DNA.
DR RefSeq; XP_007293501.1; XM_007293439.1.
DR AlphaFoldDB; K1X6P9; -.
DR STRING; 1072389.K1X6P9; -.
DR GeneID; 18761547; -.
DR KEGG; mbe:MBM_05612; -.
DR eggNOG; KOG2542; Eukaryota.
DR HOGENOM; CLU_010245_2_1_1; -.
DR InParanoid; K1X6P9; -.
DR OMA; YGPYGWL; -.
DR OrthoDB; 5487961at2759; -.
DR Proteomes; UP000006753; 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:UP000006753};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 70644 MW; 4E497D7468BFF023 CRC64;
MRLAQMASHL SNDSVGASLA ELPKSWTFTS SLPPDPKFPT PDVSHKTARG EIEPRQVRGA
LFTWVRPEEA REPELLSVSP AAMRDLGIRE GDQKTDEFKE TVAGNRLLGW DAEKGQGGYP
WAQCYGGWQF GSWAGQLGDG RAISLFETTS PITNTRYELQ LKGAGITPYS RFADGKAVLR
SSIREYIVSE ALNALNIPTT RALSLTLLPH SKVRRETLEP GAIVARFAQS WLRIGTFDIL
RARGERDLIR QLSTYIAENV FDGWESLPAR NPSETGNDGS QLPTGVARDT IEGPAGLEEN
RFTRLYREIV RRNAKTVAAW QAYAFTNGVL NTDNTSIFGL SVDFGPFAFL DNFDPNYTPN
HDDYMLRYSY RAQPTIIWWN LVRLGESLGE LMGIGEGVDA EEFVAKGVQQ EDADALISRA
EALITRTGEE FKAVFLQEYK RLMTARLGLK VHKQSDFDEL FSELLDTMEA LELDFNQFFR
KLGHLHVADL ETEEQRKEKA GVFFHHEGVT GLGNTDESAR ARISAWLQKW RARVAEDWGA
NGEKDDDDAA RQAAMKKVNP KFIPKSWILD ELIRRVEKGG EREILDRVMH MALNPFEESW
GWDEKEEERF CGDVPRSDRA MQCSCSS
//
