(data stored in ACNUC14238 zone)

HOGENOM: EMENI_33_PE1

ID   EMENI_33_PE1                         STANDARD;      PRT;   560 AA.
AC   EMENI_33_PE1; Q5AYZ4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Putative uncharacterized protein; (EMENI_33.PE1).
GN   ORFNames=AN6486.2;
OS   EMERICELLA NIDULANS.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiales;
OC   Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=162425;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS EMENI_33.PE1.
CC       Aspergillus nidulans chromosome I CADRE2 full sequence 1..3704807 annot
CC       by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:Q5AYZ4_EMENI
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
CC   -!- GENE_FAMILY: HOG000251017 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aspergillus_nidulans;CADANIAG00006475;CADANIAT00006475;CADANIAP00006475.
DR   EMBL_PREDICTED; AACD01000108; - ;
DR   EMBL; BN001301; - ;
DR   UniProtKB/Swiss-Prot; Q5AYZ4; -.
DR   EMBL; AACD01000108; EAA58508.1; -; Genomic_DNA.
DR   RefSeq; XP_664090.1; XM_658998.1.
DR   ProteinModelPortal; Q5AYZ4; -.
DR   GeneID; 2871382; -.
DR   KEGG; ani:AN6486.2; -.
DR   OrthoDB; EOG4WM835; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   InterPro; IPR002938; mOase_FAD-bd.
DR   InterPro; IPR012941; Phe_hydrox_C_dim.
DR   InterPro; IPR003042; Rng_hydrolase-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR002227; Tyrosinase.
DR   InterPro; IPR008922; Unchr_di-copper_centre.
DR   Gene3D; G3DSA:1.10.1280.10; Di-copper_centre; 1.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   Pfam; PF07976; Phe_hydrox_dim; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper_centre; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
DR   HOGENOMDNA; EMENI_33.PE1; -.
KW   CADANIAG00006475575old_1320000031; CADANIAP00006475631old_1320000031;
KW   BN001301;
KW   Complete proteome; Metal-binding; Reference proteome.
SQ   SEQUENCE   560 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRSESSTDVL IVGAGPAGLT TALWLAHTGV QFRIIDKRPN IPRRGQADGL SPRTMEILET
     FEVAHEVTRL WERATDEMLW CRDAQGNLTR MERFRNQPPQ GVRWGHGTLQ QGVVEEIMKK
     KITEVCGVEV EYETTLFELS LDTTKANDPE AFPWSATVRY GTDEPAGQML SKTMLAKYVV
     GADGGRSFVR QTMGIEMQGT KGEAVWGVMD IIGTSDFPDD IDGAVDFVRR EKDRDAITPE
     SIIVKCEYII RPYKLYIKEH VWWSAFTVAQ RISNSMAVHN RGFLVGDAVH THSPLCGAGM
     NTAVQLHRDA YNLGWKLAGV LKHQLNPEIL QTYGAERRPV AEALLDADKT ILALFHAPLG
     PEAEALLAKA DHIQAYLSGR GIQYRASLLT HGSAEGLRSL AVLPGHCIPD ITVQNYMTGR
     ASNLHSWIMA DGGWSVIFWA SDLSCASRVE NIHNCCKQVE SIRAKTSSKV GYMLDAFLIH
     CNEWPSVDLA ALPGLFLPPS KYGCLDYGKI FVREETASCK SERMNNLGGI AVVRPDKYVG
     WVGGLDDMVG LGLYFSKIFL
//

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