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Database: UniProt
Entry: A0A0L1IXJ3_ASPNO
LinkDB: A0A0L1IXJ3_ASPNO
Original site: A0A0L1IXJ3_ASPNO 
ID   A0A0L1IXJ3_ASPNO        Unreviewed;       616 AA.
AC   A0A0L1IXJ3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=SnRNP assembly factor {ECO:0000313|EMBL:KNG84130.1};
GN   ORFNames=ANOM_007169 {ECO:0000313|EMBL:KNG84130.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG84130.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG84130.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG84130.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KNG84130.1}.
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DR   EMBL; JNOM01000226; KNG84130.1; -; Genomic_DNA.
DR   RefSeq; XP_015405053.1; XM_015552425.1.
DR   AlphaFoldDB; A0A0L1IXJ3; -.
DR   STRING; 1509407.A0A0L1IXJ3; -.
DR   GeneID; 26808973; -.
DR   OrthoDB; 719409at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR   CDD; cd02669; Peptidase_C19M; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR033809; USP39.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646:SF16; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          108..205
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          230..601
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..89
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  68952 MW;  3DF6AA1F2ABA835F CRC64;
     MMSKRQAELS LEEDTVAGSP AIKKARVEDD FEEGDPRHGA LPLRRASGQE REEDERKGYD
     ILAAADQEGE ELEEAAVDNG AESDFDDADD DRPVIAAPKR QSAPMEGYSD LYLDTINREI
     LDFDFEKLCS VTLSNINVYA CLVCGKYFQG RGPKSHAYFH ALEVGHHVFI NMGTKKVYVL
     PEGYEVKNKS LDDIKYVVDP HYSKDEVSKL DKEVHDAFDL AGNRYRPGFV GMNNIKANDY
     LNVVVQLLAH VFPIRNYFLL HEFPTPGTPQ LALRFSTLVR KLWNPKAFRS HVSPHELLQE
     IALRSSKRFT LTQQSDPVEF MSWFLNNLHL SLGGSKKPSK TPTSVVQAAF QGHLKIESQA
     ITAHSDTQNA RLVFTESGDI KSQTTPFLIL TLDLPPTPLF QSANRESIIP HVPLTTLLNK
     YNGITASEKL AHRVRHRLLH PLPPYLLFHI KRFSKNRFVS ERNPTIVTFP SPRSLDMSPY
     VEPNPDVWPP GEPILYDLVA NIILDPAVAV PGATDEAAAD KGVNAASGSS STGAGAGSEK
     VSWMVQLHDK AMSAENSRQH SERAGEQQGP EWLEVQDLFV KKAETETLFT REGYLMVWER
     RKVPGMNSRK GKNPAK
//
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