ID S9X9H0_SCHCR Unreviewed; 580 AA.
AC S9X9H0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Selenoprotein O {ECO:0000256|ARBA:ARBA00031547};
GN ORFNames=SPOG_01125 {ECO:0000313|EMBL:EPY50366.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY50366.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY50366.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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; KE546993; EPY50366.1; -; Genomic_DNA.
DR RefSeq; XP_013024851.1; XM_013169397.1.
DR AlphaFoldDB; S9X9H0; -.
DR STRING; 653667.S9X9H0; -.
DR EnsemblFungi; EPY50366; EPY50366; SPOG_01125.
DR GeneID; 25035456; -.
DR eggNOG; KOG2542; Eukaryota.
DR HOGENOM; CLU_010245_2_1_1; -.
DR OMA; YGPYGWL; -.
DR OrthoDB; 5487961at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0070733; F:AMPylase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:EnsemblFungi.
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:UP000015464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 580 AA; 65650 MW; C1E4A7BDD23CFBA9 CRC64;
MRRFLTRSIQ TMSRKLSDLP VSSTFTANLT PDPVVPTVDA LKDASDDMLH IPRKVKNGAL
FTYVIPSMRA KSRLLAYSPS CMRSLGLDES EAETEAFQKL VVGTNIDVDK CCPWSQCYGG
YQFGDWAGQL GDGRVVSLCE LTNPETKERY EIQVKGVGRT PYSRFADGKA VVRSSIREYL
CCEALYALNI PTTRALAIST LDGVTAMRET VEPCAIVCRM APSWIRIGTF DLPGVEGRLD
TTRKLADYCL DHVLTEDFQG RGIGNRYEQL LRDVAIRNAK CVAKWQVYGF MNGVLNTDNT
SILGLSIDFG PFSFMDTYNP SFTPNHDDIF LRYSYQRQPS IIIWNLAKLA SALLELIGAR
DRVDDPQYME NLHSSSELLA EAHEYTLQAF ENIAKEFLSI VREDYFQLMT ARLGLPDGPT
SRKHVIDALD ILENHDLDYP NFFSFLTRMK VEKTDSQSSA EQLFDFCAGS FNKNNPRFRN
EAVQKFQGWL DAYHQLSTEV PEATRLNNMK SVNPHFTLRN WVLEEVNKKA YEGDYDLFHK
VAKMTASPFE DSWGFPKDFE DSYCYGTGPT KSQIQCSCSS
//
