ID W2YDD7_PHYPR Unreviewed; 421 AA.
AC W2YDD7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=SCP2 domain-containing protein {ECO:0000259|Pfam:PF02036};
GN ORFNames=F442_18616 {ECO:0000313|EMBL:ETP32752.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP32752.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP32752.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP32752.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) 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, ECO:0000256|RuleBase:RU000363}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP32752.1}.
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DR EMBL; ANIY01003940; ETP32752.1; -; Genomic_DNA.
DR AlphaFoldDB; W2YDD7; -.
DR EnsemblProtists; ETP32752; ETP32752; F442_18616.
DR Proteomes; UP000018948; 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; 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 PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55718; SCP-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT DOMAIN 315..410
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
FT REGION 279..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 46397 MW; 86A0D15D7D04B7C3 CRC64;
MISFGSGDLA QVAIVTGAGR GLGRAWAQAL AGRGVRVVVN DNDADRSLVE DVVQSIRSQG
GVAVGDHNCV TDGAKIVKTA MDNFKRVDIL INNATVIRDG SFRKMTKENW DDVYRSSLLG
TFIVTQAVWP IMRQQKYGRI LNCVSGAGLY GNFGQVNYAA MKTGLVGFTV ALNREGIKYN
IAVNAVSPVA GTRLTQPVWP DDVYAKLTPE LTSPIVVYLC HPSCKDNGGL FELGGGWVGA
LRLQRTHGVG FPTDPIQFTP ELVAEQWRDV VDFSRVTHPT STQDSFEPMM RNVTSPPKSL
TTSRSSECAE VFDRLRSTLQ EKGQSLSKQI SGVLEWHINK EVWTITLLNG KGTLLEGRNS
RLTPDLQIHM DEQDFLDLAA GRLRLQQALI RKKLRLQGNL KMAMKLQPFA DLLLQQNQSR
L
//
