ID A0A507C7W1_9FUNG Unreviewed; 1207 AA.
AC A0A507C7W1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=SCP2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SmJEL517_g03507 {ECO:0000313|EMBL:TPX33585.1};
OS Synchytrium microbalum.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Synchytriales;
OC Synchytriaceae; Synchytrium.
OX NCBI_TaxID=1806994 {ECO:0000313|EMBL:TPX33585.1, ECO:0000313|Proteomes:UP000319731};
RN [1] {ECO:0000313|EMBL:TPX33585.1, ECO:0000313|Proteomes:UP000319731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL517 {ECO:0000313|EMBL:TPX33585.1,
RC ECO:0000313|Proteomes:UP000319731};
RX PubMed=31209237; DOI=.1038/s41598-019-45128-9;
RA van de Vossenberg B.T.L.H., Warris S., Nguyen H.D.T.,
RA van Gent-Pelzer M.P.E., Joly D.L., van de Geest H.C., Bonants P.J.M.,
RA Smith D.S., Levesque C.A., van der Lee T.A.J.;
RT "Comparative genomics of chytrid fungi reveal insights into the obligate
RT biotrophic and pathogenic lifestyle of Synchytrium endobioticum.";
RL Sci. Rep. 9:8672-8672(2019).
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
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:TPX33585.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QEAO01000019; TPX33585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A507C7W1; -.
DR STRING; 1806994.A0A507C7W1; -.
DR EnsemblFungi; TPX33585; TPX33585; SmJEL517_g03507.
DR OrthoDB; 2140828at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000319731; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd03448; HDE_HSD; 1.
DR CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 2.
DR Gene3D; 1.10.287.4290; -; 2.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 2.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
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; 2.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF02036; SCP2; 2.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55718; SCP-like; 2.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR PROSITE; PS00061; ADH_SHORT; 2.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000319731}.
FT DOMAIN 797..915
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
FT DOMAIN 967..1061
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
FT DOMAIN 1104..1198
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
FT REGION 783..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 127561 MW; 6207A88217F94948 CRC64;
MSELRFDNKV IVVTGAGGGL GKAYALFFAS RGAKVVVNDL GGSVSGDGGA VSHRAADVVV
NEIVANKGVA VANYDSVEDG DKIIETAIKA YGRVDILINN AGILRDKTLA RMTDQDFDLV
QRVHVRGAYK CAKAAWPHMQ KQNYGRIVNT ASAAGIYGNF GQANYSAAKY ALHGFTLTLA
REGEKKNIHC NSIAPVAASR MTESVMPKEM FDNLKPDYIV PLVAYLVHDS CEANGGLFEC
GAGFVGKLRW ERSKGAHFKT DPTFTPAAVQ AKWKEVTAFD GAEHPVNLGD SDWLAHLQTA
STSPPFTGNP GALRYDGKVA VVTGAGAGLG RQYALMFARL GAAVVVNDLG GSFKGDGGDA
RAADTVVNEI LQLGGKAVAN YNSVEDGDKV IETAMKAFGR VDILVNNAGI LRDISFQRMA
DSDWDLVHKV HLRGTYKCTK AAFDVMMKQK YGRIINTTSA VGLYGNFGQA NYSAAKLGIL
GLSNTVAIEG KKYNITCNTV GPNAGTRMTA TVMPPEMVEA LKPDYVAPLT GFLAHESCTE
TGSLFEVGCG WIAKLRLQST GGVGFPHSRT LLPEHIAAKF AEICNFDDGR ATYPATIGES
IARIIANTTN QGSDASKAAP AAKKAGKGGL KPGDVNVEAA KKMVFEKDVF TYTERDVILY
ALGVGAKRYD LNFVYENSEN FSALPTFGVM PAFFSVTKSV KFGDFLPNFN PMMLLHGEQY
IVIKRPFPTS GTLSSTCRII DIQDKSSGAA VVVGTTTVDE SGNVVAENEM TTFIRGLGGF
GSGAQQASER GEATAANNPP KRPADAVVRD KTTEEQAVLY RLSGDYNPLH VDPSMAKMGG
FDVPILHGLC TLGFAGRHIL QKYCDSDPKK FKAMKVRFAG PVFPGETVET SMWKEGSKVI
FQVKVVERDV IVISNAAVEL AGSGASATAS APATASAPFG SKVSVAGFAA SALFERIESG
MGAMPSAERK KIVDKTKAIF QFDLTNSAKK TASWFVDLKN GDGAVGAGAA PGKADCIIIL
SDDDLVNLAS GKGNAQTMFM SGKIKLKGNM ALATKLQTVF QAFPAPSSVP AKAAATSAPK
LSVPGYESSA IIEAVAAGIT AMSEADRKKQ VTSVKAVFQF DITNDAKKMS SWFIDLKNGT
GSVGTGAAPT KADVVISIAD KDFVALAGGK ADAQKLFMGG KIKLKGNMML ATKLQTVLAA
ARPKGKM
//
