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Database: UniProt
Entry: A0A094G3V9_9PEZI
LinkDB: A0A094G3V9_9PEZI
Original site: A0A094G3V9_9PEZI 
ID   A0A094G3V9_9PEZI        Unreviewed;       480 AA.
AC   A0A094G3V9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=F-box domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V498_03227 {ECO:0000313|EMBL:KFY95643.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY95643.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY95643.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC       family. {ECO:0000256|ARBA:ARBA00008903}.
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:KFY95643.1}.
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DR   EMBL; JPKA01000534; KFY95643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094G3V9; -.
DR   HOGENOM; CLU_042088_0_1_1; -.
DR   Proteomes; UP000029270; Unassembled WGS sequence.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   InterPro; IPR023401; ODC_N.
DR   PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR   PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
FT   REGION          383..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  51584 MW;  6201323EB887D3A6 CRC64;
     MSLTVLTDAD VCEVLERLTI DDAHALQRSL RKALHEYSTG TQGEAACAMH QPERTAMMAP
     SGKTTLFMPS TSSSGIGMKV VTLATPGAKG PTAATADMTP HGALTIMSSN GTPTGFLNAE
     EVTAFRTALC SSLLFCRRKS FKSITVFGAG RQAFWHIRLA LLLRGSSLKT VNIISRTFSD
     RVRDLLKTFY AIDLAIKERE GWENVKFSIL TPSYGEYARL LKEQLRAADV IITTVPSTTP
     LFDPSILTST EGRRRGRLII AIGSYKPHMI EIPIEVVQQA VKPHEHRHFH KHAAEGGVVV
     VDTLTGCLKE AGEIIQSGLS PNQLVEVGEL VMLEGQLAEP DNSDDHEVDA DGKQIDLDGL
     RRELSDISST GEGSMHAVMR QGSDLSTVST ESAGRKSIDS ASSSKGSRKS LGPGGIGNKI
     RSLSMDNKKV KSKDDAMATW LGEGNVVYKC VGMGLMDLVV GGGLITLARE KGVGTTIPNF
//
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