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Database: UniProt
Entry: A0A485L3E5_9STRA
LinkDB: A0A485L3E5_9STRA
Original site: A0A485L3E5_9STRA 
ID   A0A485L3E5_9STRA        Unreviewed;       408 AA.
AC   A0A485L3E5;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Aste57867_15125 protein {ECO:0000313|EMBL:VFT91935.1};
GN   Name=Aste57867_15125 {ECO:0000313|EMBL:VFT91935.1};
GN   ORFNames=As57867_015069 {ECO:0000313|EMBL:KAF0693957.1},
GN   ASTE57867_15125 {ECO:0000313|EMBL:VFT91935.1};
OS   Aphanomyces stellatus.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=120398 {ECO:0000313|EMBL:VFT91935.1, ECO:0000313|Proteomes:UP000332933};
RN   [1] {ECO:0000313|EMBL:VFT91935.1, ECO:0000313|Proteomes:UP000332933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 568.67 {ECO:0000313|EMBL:VFT91935.1};
RA   Gaulin E., Dumas B.;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF0693957.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 578.67 {ECO:0000313|EMBL:KAF0693957.1};
RA   Gaulin E.;
RT   "Genomics analysis of Aphanomyces spp. identifies a new class of oomycete
RT   effector associated with host adaptation.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; VJMH01005626; KAF0693957.1; -; Genomic_DNA.
DR   EMBL; CAADRA010005647; VFT91935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A485L3E5; -.
DR   Proteomes; UP000332933; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.4290; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR003033; SCP2_sterol-bd_dom.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF02036; SCP2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF55718; SCP-like; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000332933}.
FT   DOMAIN          321..397
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   408 AA;  43955 MW;  B48372546B46762E CRC64;
     MLRFDGQVAL ITGAAGGLGQ EWAKALHSRG ATCVLVDIDQ RVLQLTPPSS ESAAKWECVV
     ANCANERSGR QVVEHVLTTH GRVDILLHAT TQVQDAAFRK MTRTQWDMVL DNDLTSAFTM
     TRAVWAAMRQ QNYGRILLCT SASGLYGNFG QVNYATTKSG ILGLTKALSI EGRKYKIGVN
     ALAAVAGTTL TQSVMPEDVF HRLKPEYTSP FVVYLCHATC GENGSVLETG GGWIGKLRLQ
     RSVGVGFPLA ATPEAVASSW AQVTNFAHAT YPASTQDSFA AMLDNVNHPP TTLRTPHAAA
     VAAVFDRLRA TLATKREPLR SSGMLEWAIG DAHYTVGLST NTVTVGHDQA AELVLIMTEV
     DFLALVAGTL RPQQAMASKK LTLRGDLKLA MRLQPLLTLL QDPIVAKL
//
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