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Database: UniProt
Entry: A0A093S4B5_9PASS
LinkDB: A0A093S4B5_9PASS
Original site: A0A093S4B5_9PASS 
ID   A0A093S4B5_9PASS        Unreviewed;       538 AA.
AC   A0A093S4B5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Eyes absent homolog {ECO:0000256|RuleBase:RU362036};
DE            EC=3.1.3.48 {ECO:0000256|RuleBase:RU362036};
GN   ORFNames=N305_03148 {ECO:0000313|EMBL:KFW77779.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW77779.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW77779.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW77779.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00001490,
CC         ECO:0000256|RuleBase:RU362036};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR628472-2,
CC         ECO:0000256|RuleBase:RU362036};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR628472-2,
CC       ECO:0000256|RuleBase:RU362036};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC       {ECO:0000256|ARBA:ARBA00010501, ECO:0000256|RuleBase:RU362036}.
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DR   EMBL; KL670017; KFW77779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093S4B5; -.
DR   STRING; 328815.ENSMVIP00005010153; -.
DR   Proteomes; UP000053258; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd02601; HAD_Eya; 1.
DR   Gene3D; 3.40.50.12350; -; 1.
DR   InterPro; IPR006545; EYA_dom.
DR   InterPro; IPR042577; EYA_dom_metazoan.
DR   InterPro; IPR038102; EYA_dom_sf.
DR   InterPro; IPR028472; EYA_fam.
DR   NCBIfam; TIGR01658; EYA-cons_domain; 1.
DR   PANTHER; PTHR10190; EYES ABSENT; 1.
DR   PANTHER; PTHR10190:SF7; EYES ABSENT HOMOLOG 2; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362036};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR628472-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR628472-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU362036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU362036}.
FT   REGION          205..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        270
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-1"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-1"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
FT   BINDING         502
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
SQ   SEQUENCE   538 AA;  59522 MW;  F3FEA2074D92ED2E CRC64;
     MLDLVISPSL TVNRECPDRL KLNLSHIYAT APDDIEGSNK AAPQCPLHLY TTKHYPHIVT
     VPSFPTMATY GQTQYSTGIQ QAAAYTAYPP PGQPYGIPSY SIKTEDSLSH SPGQSGFLSY
     GSSFGAPAAG QAPYTYQMHG TTGIYQGANG LTNSAGFSAV HQEYSSYPSF PQSQYSQYYS
     SSYNSPYVSA NSISPSAIPT STYSLQESSH NITSQSTESL SGEYSTTPAK DVETERHHRG
     SDGKVRARSK RSNDPSPTAD SEIERVFVWD LDETIIIFHS LLTGTFASRY GKDTTTSVRI
     GLMMEEMIFN LADTHLFFND LEDCDQIHID DVSSDDNGQD LSTYNFSADG FHSSTASANL
     CLGSGVHGGV DWMRKLAFRY RRVKEMYNTY KNNVGGLIGA PKRETWLQLR AELEALTDLW
     LTHALKALNL IHSRPNCVNV LVTTTQLIPA LAKVLLYGLG TVFPIENIYS ATKTVCVQIK
     ESCFERIMQR FGRKAVYIVI GDGVEEEQGA KKHNMPFWRI SCHADLEALR HALELEYL
//
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