ID A0A1I7TNU8_9PELO Unreviewed; 725 AA.
AC A0A1I7TNU8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000313|WBParaSite:Csp11.Scaffold629.g10293.t2};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g10293.t2};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g10293.t2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000256|ARBA:ARBA00007277}.
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DR AlphaFoldDB; A0A1I7TNU8; -.
DR STRING; 1561998.A0A1I7TNU8; -.
DR WBParaSite; Csp11.Scaffold629.g10293.t2; Csp11.Scaffold629.g10293.t2; Csp11.Scaffold629.g10293.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd05814; CBM20_Prei4; 1.
DR CDD; cd08607; GDPD_GDE5; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034839; CBM20_GPCPD1.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR22958:SF42; GLYCEROPHOSPHOCHOLINE PHOSPHODIESTERASE GPCPD1 HOMOLOG 2-RELATED; 1.
DR PANTHER; PTHR22958; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF03009; GDPD; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..118
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT DOMAIN 324..634
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 180..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 82256 MW; 28C2756B907F1FBC CRC64;
MSVTRPVRVH FAVDVENLQA HQSVYVVGSS DVLGAWEANR AMPLVQDPDR SMRWKATIVS
DVDQLKFRYF IGYNLMSDQG EKLIVDKWEA FLHPRSTLCI AESRNGECRA DRVDLFGYYA
GRKCVSDGWL QHPDENQILL RLHGNALKFY KTAKERKNCR VKMTPLDVRF KAPPSGHISF
SYGEDEEDEE EDPNAPSNKC THSTTHVAVL SDPRPKFYDQ EETGVVFNNN KDYLVFRTHC
LAAEFLAFYI EIFSDERKRI GACYALPSAL QDASGIIHLP FINSSGRPIG QVSIEYLCVR
ALTRLDGPQL MDETYCRHWK KRNALEVGHR GAGNSYTKFA MARENTIHSL NTAAKNGADY
VEFDVQLTKD RIAVIYHDFH VLVSVARRDG HALPPPMTRE QLDSSNLDFH ELPVKDLKLS
QLKLLMLDHL SFPQKKENVK KLVETSEEEE DFKPFPTLVE ALTKVDPDVG FNVEVKYPMM
QNNGEHECDH YFERNLFVDI ILADVLKHAA NRRIMFSSFD PDICSMVATK QNKYPVLFLC
VGETQRYTPF QDQRTSTSMT AVNFAVGADL LGVNFNSEDL LKDPMPVKKA NEFGMVTFVW
GEDLDKKENI QYFKKELGVD GVIYDRIGEE ERRRNVFIVE REQKRALLSC SGASTPQRAP
SPSPVSSSEG NNNSSSPPLS AKKLSMTRNS QSDSALLEES EEDMESMTEK LNITGFQSAP
MVSTK
//
