ID A0A0V0QW86_PSEPJ Unreviewed; 486 AA.
AC A0A0V0QW86;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=FAD-linked oxidase-like, C-terminal {ECO:0000313|EMBL:KRX06433.1};
GN ORFNames=PPERSA_05046 {ECO:0000313|EMBL:KRX06433.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX06433.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX06433.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX06433.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:KRX06433.1}.
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DR EMBL; LDAU01000096; KRX06433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QW86; -.
DR EnsemblProtists; KRX06433; KRX06433; PPERSA_05046.
DR InParanoid; A0A0V0QW86; -.
DR OMA; FDRTVVC; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054937}.
FT DOMAIN 56..235
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 486 AA; 54938 MW; 4FFB1CD95C68AA35 CRC64;
MLSKLFNKVC FSSIQRNPAF KTLQKQDINH FKQILGEKSV KQDELEKYNT DWMEIFQGKS
DLVLFPRTTE QLSDIISYCN QNKLAVVPQS GNTGLVGGSV PVFDEIIVNL SKMNKILNYD
ESSGVLTVEG GVILQEANDY LKQFNSEIPW DLGAKGSCLI GGNIATNAGG SYLVKHGPLR
ASILGLEVVL PSGEVMDLQS SIRKDNTGID LKQLFIGSEG ILGIITKANI LCAKQDKFRN
LIYVNCQSYN DVLQVYKTAR QTLNKNLAAI EWMDSWAFNA VFDSFNHINN PFDNKGENGQ
DYYVLVEINS NHAMEELEDM FFEQLAEIEG FKDAIKAQNE SQFKEIWEIR ESCQPAASKL
SQYEFKYDIS LDISLMDNIL QDLRNKLQKY KDIQVIGYGH IGDGNLHINV ILGDKSVKDE
VQNILEPYIF QYLSEIKGSI SAEHGMGQLK SQYLELQKPK VAIDFMKKIK QQFDPNNILN
PYKCLP
//
