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Database: UniProt
Entry: A0A0L1J3L6_ASPNO
LinkDB: A0A0L1J3L6_ASPNO
Original site: A0A0L1J3L6_ASPNO 
ID   A0A0L1J3L6_ASPNO        Unreviewed;      1056 AA.
AC   A0A0L1J3L6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   31-JUL-2019, entry version 17.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=ANOM_004726 {ECO:0000313|EMBL:KNG86344.1};
OS   Aspergillus nomius NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG86344.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG86344.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG86344.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus
RT   nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KNG86344.1}.
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DR   EMBL; JNOM01000119; KNG86344.1; -; Genomic_DNA.
DR   RefSeq; XP_015407267.1; XM_015549983.1.
DR   EnsemblFungi; KNG86344; KNG86344; ANOM_004726.
DR   GeneID; 26806530; -.
DR   OrthoDB; 776380at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd12212; Fis1; 1.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR033745; Fis1_cytosol.
DR   InterPro; IPR028061; Fis1_TPR_C.
DR   InterPro; IPR028058; Fis1_TPR_N.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR033932; YtcJ-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF07969; Amidohydro_3; 2.
DR   Pfam; PF14853; Fis1_TPR_C; 1.
DR   Pfam; PF14852; Fis1_TPR_N; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000037505};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM    126    147       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      426    467       RING-type. {ECO:0000259|PROSITE:PS50089}.
FT   REGION      156    284       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      392    416       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      473    548       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    168    190       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    222    238       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    265    284       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    481    495       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    504    534       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1056 AA;  115682 MW;  041766652C5051BB CRC64;
     MGSNLPYAAD AESPLKPAEL QVLRSQYEKE GDYVGIQTKF NFAWGLIKSN ARTDQQEGVR
     LLSEIFRAAP ERRRECLYYL ALGNYKLGNY GEARRYNDLL LEKEPANLQA ASLGTLIDER
     VSKEGLLGFA IVGGLALAAG VVGGMVFRGA KRRTPTLTGQ IEIPPDTEGE FPDPPTSVPE
     DRPAPPRNPW ADHNPWDHDD LNRDTDWGSG NGYRHHTYRS PDGRFTFSST TFTRRGSGQQ
     MPPDPLMPMT EYRQPNERDS PPAPWRSDRQ NQQRFSPNGS RVYSTSFDFD MNTRSNGGMG
     SEFHTAGGLH PRDADSPQPM GTPLRTLGDI LELFRNDFGS NGSPGSPGVR VMTGPNPIAI
     LSTLLNLDRH GDAVYSQEEL DRVISQLIDQ NARGTAPPPA APSAIQSLPK KKVDQDMLGS
     EGKAECSICM DPVELGTEVT ELPCKHWFHY NCIEMWLSQH NTCPHCRRGI NIPAEPEGSS
     ENPVVINSSP ETSPRRPSGA AREHSGQSPP QWFGTGPETG QEQDQRSSRN DNQGGGFAGW
     VRSHFGGGNP STSTPHTICL SLSLLLPSFL VNSYTALRET ALAMKTLYRN GHFVTPQSPN
     PTCMVTENDR IIYLGEESTA TTLHPDSEIH DLGGRKVLPG FIDGHMHLLL FGASLSKINL
     GNCTSLSDIR STIKAAAAAN PTAARLFCRG WMHSMTNGEA LASMLDDLDP RPIFIDSKDL
     HSAWCNSAAL AELNVAHTPD PAGGVIHRDA AGTPTGLLSE AAAVNIVWPH VAQVASLDEK
     LHFIRAGIRE YTRAGYTGVV EMATDENLWS TVLALREREE VNIRLAAHWI ISPRTTRKRH
     QGHLRRVVDA CTAALTEPYA SNGDNCAPLW DADILKKVVR KADRAGLQCA LHAIGDATDA
     KRLGDLGITA SVQPVHADPA ILRAWPRLLG PDRCGRAFAY KDFLDHGAHL AIGTDSPTAP
     HLPLRNLYTA TTRRSAREPE SLETVNEHFS LGLLEAITAA TAGSAYSCFA DGFAGTLEVG
     KKADFVVVDM AWEAERLLQA EVWETWFDGR RVWRRE
//
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