ID A0A091H9B7_9AVES Unreviewed; 345 AA.
AC A0A091H9B7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=WW domain-containing oxidoreductase {ECO:0000256|ARBA:ARBA00016094};
DE Flags: Fragment;
GN ORFNames=N303_05051 {ECO:0000313|EMBL:KFO82797.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO82797.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO82797.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO82797.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi
CC apparatus {ECO:0000256|ARBA:ARBA00004555}. Lysosome
CC {ECO:0000256|ARBA:ARBA00004371}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; KL448320; KFO82797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091H9B7; -.
DR STRING; 55661.A0A091H9B7; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR24320; RETINOL DEHYDROGENASE; 1.
DR PANTHER; PTHR24320:SF269; WW DOMAIN-CONTAINING OXIDOREDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00397; WW; 2.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 9..42
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 50..83
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO82797.1"
FT NON_TER 345
FT /evidence="ECO:0000313|EMBL:KFO82797.1"
SQ SEQUENCE 345 AA; 38837 MW; 25CAA3A34B131C20 CRC64;
GLEDTDSEEE LPPGWEERTT ADGWVYYASH LEEKTQWEHP KSGKRKRVAG GLPYGWEQET
DENGQVYFVD HINKRTTYLD PRLAFTVEDN PVKATPRQRY DGNSTAMEIL QGRDLSGKVV
IITGANSGIG FETAKSLALH GAYVILACRN PSRGSEAVQR ILGEWHKAKV EAMTLDLASL
QSVQRFAEAF KSKNVPLHIL ICNAAIFGAP WSLTEDGLES TFQVNHLGHF YLVQLLEDVL
RCSSPARVVV VSSESHRFTD IKDSSGKLDF SLLSPSKKEY WAMLAYNRSK LCNILFSNEL
NRRLSPHGVT SNAVHPGNMI YSSIHRSWWV YTLLFTLARP FTKSM
//
