ID   A0A2H3I173_9EURO        Unreviewed;       502 AA.
AC   A0A2H3I173;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Ornithine cyclodeaminase/mu-crystallin {ECO:0000313|EMBL:PCG91261.1};
GN   ORFNames=PENO1_094650 {ECO:0000313|EMBL:PCG91261.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG91261.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG91261.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG91261.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCG91261.1}.
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DR   EMBL; NPFK01000427; PCG91261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3I173; -.
DR   STRING; 290292.A0A2H3I173; -.
DR   OrthoDB; 470839at2759; -.
DR   Proteomes; UP000218381; 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   Pfam; PF02423; OCD_Mu_crystall; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT   REGION          117..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  54418 MW;  496BAEA0EEB05229 CRC64;
     MPLTILSGAQ VRALLLSLSR DDVLNLQHNL ADALREYSTG NQEQGCAASY QPHRTAITGN
     DGKTTIFMPA STGKTTGVKI LSSPLTSSVT DKPGCTTIGQ EFANSRQSAK VSLSLEEYSS
     RRSSSSLSAD VSSMSLTPSH EDDGGSVAGD DSEVESSSFS SSTGGAPSIN HQSLSSQSSS
     PRASKSYIAS VQHLSGKGWP PVGARDSSPQ GTLTLVGQDG LPIGLISAQD LTAFRTALTS
     LFVFNKRKHV KTITVFGAGR QAYWHIRLAL LLRGPEVKRV YIINRSFDRA AKLLRDIYAA
     ENASWRSDVK FHAFSSDFVE YNRLSREAVR KADVIFCCTP SLEPLFPAEF LTSTEGRRKG
     RLVVAIGSYK SHMTELHPDI LKNEVKPSTQ NAHHYHKHAQ RGGVVLVDSL EMCLQEAGEI
     VQAGLGPHQL VEIGELMIMK HAARLGIEQQ KGNGEEGLKK WLEKGNVVYK SVGLGLMDLI
     TGNDMVDIAR RRGVGTFIDD FE
//