ID A0A443SWY1_9ACAR Unreviewed; 417 AA.
AC A0A443SWY1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Hydroxysteroid dehydrogenase-like protein 2 {ECO:0000256|ARBA:ARBA00040243};
GN ORFNames=B4U80_01493 {ECO:0000313|EMBL:RWS32031.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS32031.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS32031.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS32031.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- FUNCTION: Has apparently no steroid dehydrogenase activity.
CC {ECO:0000256|ARBA:ARBA00037788}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:RWS32031.1}.
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DR EMBL; NCKV01000002; RWS32031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443SWY1; -.
DR STRING; 299467.A0A443SWY1; -.
DR EnsemblMetazoa; LDEU000008-RA; LDEU000008-PA; LDEU000008.
DR VEuPathDB; VectorBase:LDEU000008; -.
DR Proteomes; UP000288716; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd09762; HSDL2_SDR_c; 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; PTHR42808; HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR42808:SF3; HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 2; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55718; SCP-like; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000288716}.
FT DOMAIN 323..410
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
SQ SEQUENCE 417 AA; 45379 MW; 79FFB983264681BB CRC64;
MINTGKFAGK TVFITGASRG IGKAIALKLG KDGANIAIGA KTVDPHPKLE GTIYTAAKEV
EAVGGKCLPV QVDIRDEASV VKAIEETVKK FGGIDILVNN ASAISLTGTE DTPMKRYDLM
HSVNTRGTFM TSKYAIPHLK KSGNGHILNL SPPLVMHPRW FKSHVAYTMA KYGMSMCVLG
MAEELKSSKI AVNALWPRTA IFTAAMEMLG GGKSIANTCR KPDILADAAY FILSKPAKEF
TGNFCIDEDV LKDAGITDLE QYSVVPGSKL LSDFFLPDSH LSPEDLQILD ASQKIQEEIP
QDAGSGRTDN KTGKVFKVIE DMVNEELRKQ INALMLFSIS GKNYFVDFNA SRPFQVSQNE
IGKPDVTLIT DDETFVKMAK GEVKSTNAFM SGKLKIKGNL QVAMKAEKIF NQLKAKL
//
