SELO_SCHPO
ID SELO_SCHPO Reviewed; 568 AA.
AC O13890;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein adenylyltransferase SelO, mitochondrial {ECO:0000305};
DE EC=2.7.7.- {ECO:0000250|UniProtKB:Q08968};
DE AltName: Full=Selenoprotein O {ECO:0000250|UniProtKB:Q08968};
DE Short=SelO {ECO:0000250|UniProtKB:Q08968};
DE Flags: Precursor;
GN ORFNames=SPAC20G4.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC Tyr residues of target mitochondrial proteins (AMPylation). Involved in
CC redox homeostasis by regulating the cellular response to oxidative
CC stress. Regulates protein S-glutathionylation levels possibly by
CC AMPylation of deglutathionylation enzymes such as glutaredoxins.
CC {ECO:0000250|UniProtKB:Q08968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624;
CC Evidence={ECO:0000250|UniProtKB:Q08968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54289;
CC Evidence={ECO:0000250|UniProtKB:Q08968};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q87VB1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q08968}.
CC -!- PTM: Forms probably one or more intrachain disulfide bridges.
CC {ECO:0000250|UniProtKB:Q08968}.
CC -!- SIMILARITY: Belongs to the SELO family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11255.1; -; Genomic_DNA.
DR PIR; T38119; T38119.
DR RefSeq; NP_594740.1; NM_001020168.2.
DR AlphaFoldDB; O13890; -.
DR SMR; O13890; -.
DR STRING; 4896.SPAC20G4.05c.1; -.
DR SwissPalm; O13890; -.
DR MaxQB; O13890; -.
DR PaxDb; O13890; -.
DR EnsemblFungi; SPAC20G4.05c.1; SPAC20G4.05c.1:pep; SPAC20G4.05c.
DR GeneID; 2541666; -.
DR KEGG; spo:SPAC20G4.05c; -.
DR PomBase; SPAC20G4.05c; -.
DR VEuPathDB; FungiDB:SPAC20G4.05c; -.
DR eggNOG; KOG2542; Eukaryota.
DR HOGENOM; CLU_010245_2_1_1; -.
DR InParanoid; O13890; -.
DR OMA; YGPYGWL; -.
DR PhylomeDB; O13890; -.
DR PRO; PR:O13890; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070733; F:protein adenylyltransferase activity; ISS:PomBase.
DR GO; GO:0098869; P:cellular oxidant detoxification; IC:PomBase.
DR HAMAP; MF_00692; SelO; 1.
DR InterPro; IPR003846; SelO.
DR PANTHER; PTHR32057; PTHR32057; 1.
DR Pfam; PF02696; SelO; 1.
PE 3: Inferred from homology;
KW ATP-binding; Disulfide bond; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..568
FT /note="Protein adenylyltransferase SelO, mitochondrial"
FT /id="PRO_0000121402"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 120..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 156..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q08968"
SQ SEQUENCE 568 AA; 63951 MW; 205D02CCD3962269 CRC64;
MSKKLKDLPV SSTFTSNLPP DPLVPTVQAM KKADDRILHV PRFVEGGGLF TYLTPSLKAN
SQLLAYSPSS VKSLGLEESE TQTEAFQQLV VGSNVDVNKC CPWAQCYGGY QFGDWAGQLG
DGRVVSLCEL TNPETGKRFE IQVKGAGRTP YSRFADGKAV LRSSIREYLC CEALYALGIP
TTQALAISNL EGVVAQRETV EPCAVVCRMA PSWIRIGTFD LQGINNQIES LRKLADYCLN
FVLKDGFHGG DTGNRYEKLL RDVAYRNAKT VAKWQAYGFM NGVLNTDNTS ILGLSIDYGP
FGFLDVYNPS FTPNHDDVFL RYSYRNQPDI IIWNLSKLAS ALVELIGACD KVDDLQYMEQ
LHNSTDLLKK AFAYTSEVFE KIVEEYKNIV QNDFYDLMFK RVGLPSDSSN KILITDLLQI
LEDYELDMPN CFSFLSRNSP SSMENEEYAA KLMQACICLN PNNERVRNES VKAFTNWVGR
YSEATKTQED SSRLASMKKV NPHFTLRNWV LEEVIKEAYI GKFELFKKVC KMAACPFEDT
WGFSKEEEDY LCYNTTPSKS QIQCSCSS
