ID A0A0A0AUY7_CHAVO Unreviewed; 684 AA.
AC A0A0A0AUY7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE SubName: Full=Dihydropyrimidinase-related protein 1 {ECO:0000313|EMBL:KGL97697.1};
GN ORFNames=N301_16057 {ECO:0000313|EMBL:KGL97697.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL97697.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL97697.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL97697.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
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DR EMBL; KL873024; KGL97697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AUY7; -.
DR STRING; 50402.A0A0A0AUY7; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR02033; D-hydantoinase; 1.
DR PANTHER; PTHR11647:SF54; DIHYDROPYRIMIDINASE-RELATED PROTEIN 1; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053858}.
FT DOMAIN 176..565
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 74668 MW; AB68A7846E2575A6 CRC64;
MAERKRNWNK EDDLPVYLAR PGTTAQTPRQ KYGGMFASVE GAYENKTIDF DAYSVGKKGS
RTPRSGSRHD MLDGGDNYSE TASDISEVSG SVISSPGDRE DKTPVSVKCS FPSSPEFLRP
SKILKSDRLL IKGGRIINDD HSFYADIYLE DGLIKQIGEN LIVPGGVKTI EANGRMVIPG
GIDVNTYLQK PYQGMTAVDD FYQGTKAALA GGTTMIIDHV LPEPGSSLLT SFEKWHEAAD
TKSCCDYSLH VDITSWYDGI REELEILVQD KGVNSFQVYM AYKDLYQMSD SQLYEAFTFL
KSLGAVILVH AENGDLIAQE QKRILEMGIT GPEGHALSRP EELEAEAVFR AITIASRINC
PVYITKVMSK SAADIIALAR KKGPLVFGEP ITASLGTDGT HYWSKNWAKA AAFVTSPPLS
PDPTTPDHLN SLLACGDLQV TGSGHCPYST AQKAIGKDNF TMIPEGVNGI EERMTVVWDK
AVATGKMDES QFVAVTSTNA AKIFNLYPRK GRIAVGSDAD VVIWDPDKVK TITAKSHKSA
IEYNIFEGME CHGAPLVVIS QGKIVFEDGN LHVNKGMGRF IPRKPFPEYL YQRIKIRNKV
GGLQGVSRGM YDGPVYEIPA TPKYATPAPS TKSSPAKNQP PPIRNLHQSN FSLSGAQIDD
NNPRRTGHRI VAPPGGRSNI TSLG
//
