ID   U3ITW0_ANAPP            Unreviewed;       804 AA.
AC   U3ITW0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 2.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Serine-threonine kinase receptor-associated protein {ECO:0000256|ARBA:ARBA00040390};
DE            EC=4.1.2.4 {ECO:0000256|ARBA:ARBA00012515};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|ARBA:ARBA00032755};
GN   Name=STRAP {ECO:0000313|Ensembl:ENSAPLP00000010683.2};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000010683.2, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000010683.2, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000010683.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC         3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000764};
CC   -!- SIMILARITY: Belongs to the WD repeat STRAP family.
CC       {ECO:0000256|ARBA:ARBA00038394}.
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DR   AlphaFoldDB; U3ITW0; -.
DR   STRING; 8840.ENSAPLP00000010683; -.
DR   Ensembl; ENSAPLT00000011400.2; ENSAPLP00000010683.2; ENSAPLG00000011004.2.
DR   GeneTree; ENSGT00940000155197; -.
DR   HOGENOM; CLU_053595_3_0_1; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000016666; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00959; DeoC; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR19877; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT I; 1.
DR   PANTHER; PTHR19877:SF13; SERINE-THREONINE KINASE RECEPTOR-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM01133; DeoC; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW   WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   REPEAT          221..262
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          262..303
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          305..345
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          427..468
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          13..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   804 AA;  88196 MW;  3A73D8312DC2AB7B CRC64;
     MVCARFRQDW FADGGGACKE QRSTGGGTEN RLETGCGDVW GTPAFSSPQP PHSNPRGRPR
     APSSHTEQEP GPPPQRTRRR PPGQPLPLAA PAAISGPTEL PRRHFPRRRR QQQQQQQQHR
     GRRSVAGPRG PAPRRRLPPR PPRCLHPPRC CCCRLLLLLL QPPAAAMAMR QTPLTCSGHT
     RPVVDLAFSG VTPYGYFLIS ACKDGKPMLR QGDTGDWIGT FLGHKGAVWG ATLNKDATKA
     ATAAADFTAK VWDAVSGDEL ITLAHKHIVK SVDFTQDSNY LLTGGQDKLL RIYDLSKPEA
     EPDVVSGHTS GIKKALWSSD DKQILSADDK TVRLWDRSTM TEVKALNVAM SVSSMEYVPE
     GQILVITYGK TIAFHSAETL EQIKSFEAPA TINSASLHPE KECLVAGGED FKLYKYDYNT
     GEELESYKGH FGPIHCVRFS PDGELYASGS EDGTLRLWQT TVGKTYGLWK CVVPEEENAE
     AAKARTSLPG TAEEEIELGW ISKVYVNQPA VVRHAEQIQK WRTVKGNWQA AWLLKAVTCI
     DLTTLSGDDT PSNVHRMCFK AKHPIREDLL KAMDMHDKGI TVAAVCVYPA RVADAVNSLK
     AAGCNIPVAS VAAGFPSGQT PLETKLAEIK LAVQYGAREI DIVISRSLVL SGQWESLYEE
     IRQCREACGE AHMKTILATG ELGSLANVYK ASMIAMMAGS DFIKTSTGKE VENATLPVGV
     VMMRAIKEFY WQTGNKVGFK PAGGIRTAKE AITWLMLVKD ELGVEWLKPE LFRLGASSLL
     EDIEKQIFHH VTGSYALQHD LAMA
//