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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//