SELO1_DANRE
ID SELO1_DANRE Reviewed; 692 AA.
AC Q1LVN8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein adenylyltransferase SelO-1, mitochondrial {ECO:0000250|UniProtKB:Q9BVL4};
DE EC=2.7.7.- {ECO:0000250|UniProtKB:Q9BVL4};
DE EC=2.7.7.n1 {ECO:0000250|UniProtKB:Q9BVL4};
DE AltName: Full=Selenoprotein O {ECO:0000250|UniProtKB:Q9BVL4};
DE Short=SelO {ECO:0000250|UniProtKB:Q9BVL4};
DE Flags: Precursor;
GN Name=selenoo1 {ECO:0000305}; Synonyms=selo;
GN ORFNames=si:ch211-15i6.2 {ECO:0000312|EMBL:CAK04189.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC Ser, Thr and Tyr residues of target proteins (AMPylation). May be a
CC redox-active mitochondrial selenoprotein which interacts with a redox
CC target protein. {ECO:0000250|UniProtKB:Q9BVL4}.
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; EC=2.7.7.n1;
CC Evidence={ECO:0000250|UniProtKB:Q9BVL4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC Evidence={ECO:0000250|UniProtKB:Q9BVL4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein]
CC + diphosphate; Xref=Rhea:RHEA:58120, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15073, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:142516; Evidence={ECO:0000250|UniProtKB:Q9BVL4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q87VB1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BVL4}.
CC -!- SIMILARITY: Belongs to the SELO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK04189.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX649566; CAK04189.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001038336.2; NM_001044871.3.
DR STRING; 7955.ENSDARP00000090475; -.
DR PaxDb; Q1LVN8; -.
DR GeneID; 558648; -.
DR KEGG; dre:558648; -.
DR CTD; 558648; -.
DR ZFIN; ZDB-GENE-030131-4485; selenoo1.
DR eggNOG; KOG2542; Eukaryota.
DR InParanoid; Q1LVN8; -.
DR OrthoDB; 454947at2759; -.
DR PhylomeDB; Q1LVN8; -.
DR TreeFam; TF323296; -.
DR PRO; PR:Q1LVN8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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 Pfam; PF02696; SelO; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Selenocysteine; Transferase;
KW Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..692
FT /note="Protein adenylyltransferase SelO-1, mitochondrial"
FT /id="PRO_0000318606"
FT REGION 637..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 142..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 188..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT NON_STD 690
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 692 AA; 77450 MW; CA5B46F9C0C2560D CRC64;
MASVGSRLTR FYISRPGVIA RRFLAHAGMD DMGVSLSRSS LERLEFDNVA LKKLPLDPST
EPGVRQVRGS CFSRVQPTPL KNPEFVAVSA PALALLGLDA EEVLKDPLGP EYLSGSKVMP
GSEPAAHCYC GHQFGQFAGQ LGDGAACYLG EVKAPAGQSP ELLRENPTGR WEIQVKGAGL
TPYSRQADGR KVLRSSIREF LCSEAVFALG VPTTRAGSVV TSDSRVMRDI FYDGNPRMER
CSVVLRIAPS FIRFGSFEIF KRADEFTGRQ GPSYGHDELR TQMLEYVIEN FYPEIHRNYP
DLTERNTAFF KEVTVRTARL VAQWQCVGFC HGVLNTDNMS ILGLTLDYGP FGFMDRFDPD
FICNASDNSG RYSYQAQPAI CRWNLARLAE ALEPDLPPDR AEQVLDEYLP LYNDFYLSNM
RKKLGLLRKE EPEDEMLITE LMQTMHNTGA DFTNTFRSLS QISCPTQEEA EDESETIKQA
TELLLHQSAS LEELKAANRP SMDPRELAML VSMAQSNPAL FQMISDRGTV SRQLERLSRL
KELMDTTEEQ LRVKHTEHWS DWIQKYRQRL ARECESGVDV KDVQTERVRV MNNNNPHVVL
RNYIAQNAIA AAENGDFSEV QRVLKVLEKP FSVQEGLEQP GWMGRGGAAI PGERDETEEE
GSNSSGAGAR GLVPYDSKPP VWANEICVTU SS
