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Database: UniProt
Entry: A0A178AF37_9PLEO
LinkDB: A0A178AF37_9PLEO
Original site: A0A178AF37_9PLEO 
ID   A0A178AF37_9PLEO        Unreviewed;       479 AA.
AC   A0A178AF37;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:OAK96246.1};
GN   ORFNames=IQ06DRAFT_380605 {ECO:0000313|EMBL:OAK96246.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK96246.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK96246.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK96246.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC       family. {ECO:0000256|ARBA:ARBA00008903}.
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DR   EMBL; KV441720; OAK96246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AF37; -.
DR   STRING; 765868.A0A178AF37; -.
DR   InParanoid; A0A178AF37; -.
DR   OrthoDB; 470839at2759; -.
DR   Proteomes; UP000077206; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT   REGION          91..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  52683 MW;  13FB0AD1ADED0072 CRC64;
     MPLTVLSDDD VRKLLLELTK QDILDLQQSL ADALHYYSTA TADDTDNGCS SSYQPLRTSL
     KRADGQTTLV MPASSNDGTG VKIVTLAGAG GSKAPSLKDT ASTTSSLSHQ SSKSSSTLID
     PPQSLLSAQS TTPKGSLTLF DKNGAPRAFL NAEEITAFRT ALASVMLFKK RRDVHDVVVF
     GAGKQAYWHI RLALLLRGDD IHHLNIINRD FERAHKLLSQ LYAPHEEDHS WSTETHKVPA
     YRTGTHPTLA RPKIQILSPN HGEYDRLLKS TIRASSVIFF TTPSITPLFP AEILTNPEGR
     KKGRYLAAIG SYKPHMVEIH PDIVKQNVQP EHGHRHFHKH AQQGGAIIVD SVEACLKEAG
     EVIQAGLGPN EVVEVGELLM LKRDAERRRA ECKARRSEEG LDEGGVELGE CEATKKKRRG
     SSKKDEDGED KAHKSLMEWL QRGNVIYKSV GLGLMDVVVG MDLVRLADER GIGTRIENF
//
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