ID A0A099YUI9_TINGU Unreviewed; 534 AA.
AC A0A099YUI9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Eyes absent homolog {ECO:0000256|RuleBase:RU362036};
DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU362036};
GN ORFNames=N309_05514 {ECO:0000313|EMBL:KGL72986.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL72986.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL72986.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL72986.1};
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; KL885512; KGL72986.1; -; Genomic_DNA.
DR RefSeq; XP_010216867.1; XM_010218565.1.
DR AlphaFoldDB; A0A099YUI9; -.
DR STRING; 94827.A0A099YUI9; -.
DR GeneID; 104571458; -.
DR KEGG; tgt:104571458; -.
DR CTD; 2139; -.
DR OrthoDB; 452222at2759; -.
DR Proteomes; UP000053641; 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 InterPro; IPR036412; HAD-like_sf.
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.
DR SUPFAM; SSF56784; HAD-like; 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:UP000053641};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU362036}.
FT REGION 204..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..224
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 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
SQ SEQUENCE 534 AA; 58532 MW; 5D8974D5E6340523 CRC64;
MLDLVISPSL TVNRECPDRL KLNLSNAYAA APDDIEGNSK AAAQCPLHLY STKHYPHIVT
VPPFPAMAAY GQTQYSAGLQ QAAAYTAYPP PGQPYGIPSY SIKTEEGLSH SPGQSGFLGY
GSGFGTPAAG QAPYTYQVHG TTGIYQGANG LANSAGFGAV HQEYSSYPSF PQSQYSQYYS
SSYSSPYVSA NSISPSAIPT SAYSLQDSSH TITSQSTESL SGEYATTPAK EAEAERHQRG
ADGKVRTRSK RSTDPCPPAD SEIERVFVWD LDETIIIFHS LLTGTFASRY GKDTTTSVRI
GLMMEEMIFN LADTHLFFND LEDCDQIHID DVSSDDNGQD LSTYNFSADG FHSSTASANL
CLGSGVHGGV DWMRKLAFRY RRVKEMYNTY KNNVGGLIGA PKRETWLQLR AELEALTDLW
LTHALKALNL IHSRSNCVNV LVTTTQLIPA LAKVLLYGLG TVFPIENIYS ATKTGKESCF
ERIMQRFGRK AVYIVIGDGV EEEQGAKKHN MPFWRISCHA DLEALRHALE LEYL
//
