ID V5FJX6_BYSSN Unreviewed; 544 AA.
AC V5FJX6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Actin interacting protein 2 {ECO:0000313|EMBL:GAD92068.1};
GN ORFNames=PVAR5_0654 {ECO:0000313|EMBL:GAD92068.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92068.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:GAD92068.1}.
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DR EMBL; BAUL01000016; GAD92068.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FJX6; -.
DR eggNOG; KOG1232; Eukaryota.
DR HOGENOM; CLU_017779_4_1_1; -.
DR InParanoid; V5FJX6; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000018001; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT DOMAIN 112..291
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 544 AA; 59913 MW; 22E9AD0773D7B849 CRC64;
MSTARGVSIA LRRARLPRAS RVARPIVPYT PAAAVRSFSV SSAVGADAKK EIKYTSAAYP
NVKRDPKFAD LTEEHVRYFR SLLDAQSAVI DGVTTEAGDD IEPFNSDWMR KYRGHTRLVL
KPQTKEELSQ ILKYCNENKL AVVPQGGNTG LVGGSVPVFD EIVINTARMN KIRSFDEATG
VLVADAGVIL EVADQYLAER NHLFPLDLGA KGSCHIGGNV ATNAGGLRLL RYGSLHGNVL
GVEAVLPDGT ILDGLSTLRK NNTGYDLKQL FIGAEGTIGI ITGVSILCPP RPKAVNVAYF
GLESFDQVRQ AYREAKGQLS EILSAFELMD GRSQNLVHGV TGKKRPLEGE YPFYCLIETS
GSNAEHDIAK LESFLEHIMG EGIVADGVLA QDETQVQALW GWREGITETL SHLGGTYKYD
VSIPLEELYQ LVEDCRERLT KLGFVGDDDS FPVRDVVGYG HMGDSNLHLN VAVRQYNKDV
EKAIEPWVYE WIQKRNGSIS AEHGLGLAKK EFIGYSQNDT NLKLMKQIKN LYDPNGIMNP
YKYI
//
