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Database: UniProt
Entry: A0A2A2JN97_9BILA
LinkDB: A0A2A2JN97_9BILA
Original site: A0A2A2JN97_9BILA 
ID   A0A2A2JN97_9BILA        Unreviewed;       417 AA.
AC   A0A2A2JN97;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=SCP2 domain-containing protein {ECO:0000259|Pfam:PF02036};
GN   ORFNames=WR25_06872 {ECO:0000313|EMBL:PAV63195.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV63195.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV63195.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV63195.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
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:PAV63195.1}.
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DR   EMBL; LIAE01010326; PAV63195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2JN97; -.
DR   STRING; 2018661.A0A2A2JN97; -.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 1.
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   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.
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:UP000218231}.
FT   DOMAIN          315..410
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
FT   REGION          277..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  44935 MW;  49AE4C3C94FCDA5B CRC64;
     MALRFDGRVA IVTGAGGGLG RTYAIELAKR GCKVVAEIKS AGGVAVPNYD SVEFGDKIVK
     TAIDNFGRID IVINNAGILR DVSFLNMKEL DWDLIFKVHV KGAYSVTKAA WPYMREQKYG
     RIVCTSSNAA VFGSFGQTNY SAAKHALIGF SNSLALEGEK YNIKANTLIP TAGSRLTQTV
     MPQELVDALK PEYVTPLVVY MVHETFGENG KLFEAGAGWY GTQQYYRSAG KVITNATAEQ
     VRDGWNQVTD MTGARHMNKI AEATQELMAI LANHSEETGN STTTTTTGGG QTGGDWPSNI
     KTSALFKEMN DGVHADPSAV KGINAIILYS ITDGSKEIGK FTLDFKSATP SVYYGDIKGG
     EKATVTVTVS DDDFMDIAAG KLPPQKAFMG GKLKVKGNVM LLQKMQGILE AKRKAKM
//
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