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Database: UniProt
Entry: A0A2H3IKR3_9EURO
LinkDB: A0A2H3IKR3_9EURO
Original site: A0A2H3IKR3_9EURO 
ID   A0A2H3IKR3_9EURO        Unreviewed;       637 AA.
AC   A0A2H3IKR3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   28-MAR-2018, entry version 3.
DE   SubName: Full=Aminotransferase, class I/classII {ECO:0000313|EMBL:PCH05392.1};
GN   ORFNames=PENO1_022790 {ECO:0000313|EMBL:PCH05392.1};
OS   Penicillium occitanis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH05392.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH05392.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH05392.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A.,
RA   Gargouri A., 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
RT   Pathogen Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PCH05392.1}.
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DR   EMBL; NPFK01000041; PCH05392.1; -; Genomic_DNA.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:PCH05392.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000218381};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Transferase {ECO:0000313|EMBL:PCH05392.1}.
FT   DOMAIN       61    412       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
FT   DOMAIN      423    503       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      518    624       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
SQ   SEQUENCE   637 AA;  71381 MW;  7F6575D2814B0876 CRC64;
     MLSSRGETYA KAGLADGYLR PREPYNKGTK EGIVSFGNAE NFLMQDILLE YIRTKAFQHL
     DNASLTYHEG PFGPKRLREA MAKLIIRYFH PAIPISPDHV LFTSGITSLN AMYAMCLTDP
     GDGILLGQPI YGSFNGDLQV PSGCQLIYTP FHEDDPFGRN AVEHYEETFL QAREKGVSIK
     ALLICNPHNP LGRCYPRDIL EALMQFCQKY QIHLISDEIY ALSVYEEDHS SGFVSILSID
     PAPLGVDPAI IHVLYGMSKD FAAAGLRLGC LISRNQKFMH AALSISRFHW PSEISCSIAT
     TLLEDHGFID SFLRKSRELL RSQRDFAVQI LDEAGIPYAR GCNAGFFLWI DLSKCLNARI
     VDTQGEWAAE LDLSQQLQEI GVEMSSGHAY HNETAGWFRV IFSIEREILE EGLSRQLALP
     KMYTLPPLPY AYEALEPVIS AEIMTLHHQK HHQTYINNLN AALSAQQAAT TSNDIPALLA
     LQQKIKFNGG GHINHSHFWR NLAPAGSAET NINAVAPNIK ASIEVKWGSV DNFINDFKQT
     LLGIQGSGWG WLIVKQGPAE KKTRSLEIVT TKDQDSVVAP DESVVPLFGV DMWEHAYYLQ
     YLNNKAGYVT EIWKIINWKV VEERFSRGIQ GEVSFQL
//
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