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Database: UniProt
Entry: A1CH62_ASPCL
LinkDB: A1CH62_ASPCL
Original site: A1CH62_ASPCL 
ID   A1CH62_ASPCL            Unreviewed;       614 AA.
AC   A1CH62;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=SnRNP assembly factor, putative {ECO:0000313|EMBL:EAW10217.1};
GN   ORFNames=ACLA_046830 {ECO:0000313|EMBL:EAW10217.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10217.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW10217.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; DS027054; EAW10217.1; -; Genomic_DNA.
DR   RefSeq; XP_001271643.1; XM_001271642.1.
DR   AlphaFoldDB; A1CH62; -.
DR   STRING; 344612.A1CH62; -.
DR   EnsemblFungi; EAW10217; EAW10217; ACLA_046830.
DR   GeneID; 4704415; -.
DR   KEGG; act:ACLA_046830; -.
DR   VEuPathDB; FungiDB:ACLA_046830; -.
DR   eggNOG; KOG2026; Eukaryota.
DR   HOGENOM; CLU_016848_2_1_1; -.
DR   OMA; NKFVAER; -.
DR   OrthoDB; 719409at2759; -.
DR   Proteomes; UP000006701; 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:UP000006701};
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          107..204
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          229..599
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..84
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  68824 MW;  782F25CAD10E13A3 CRC64;
     MSKRQAELSL EDEPAVGSPV SKKARVEDEF DENDPRNRAL PLRRATGQEM EEHERNGQNI
     LAAADLEEEE MEEAIPENAD VAESSDVDDD RPAIAAPKRQ SEPMEGYSDL YLDTINRQIL
     DFDFEKQCSI TLSNINVYAC LVCGKYFQGR GPKSHAYFHA LEVGHHVFIN MSTKKVYVLP
     EGYEVKNKSL EDIKYVVDPH YTKEEVSKLD KQVQDAFDLA GNRYRPGFVG MNNIKANDYL
     NVVVQLLAHV FPVRNYFLLH EFPTPGTPQL ALRFSTLVRK LWNPKAFRSH VSPHELLQEI
     ALRSSKRFTL TQQSDPVEFL SWFLNNLHLS LGGSKKPTAT PTSVIHAAFQ GHLRIESQAI
     TAHSDTQNAR LVFTESGTIN SQKTPFLILT LDLPPTPLFQ SANRESIIPQ VPLTTLLNKY
     NGITASEKLA HRVRHRLLHP LPPYLLFHIK RFSKNRFVSE RNPTIVTFPS PRSLDMSPYV
     EPNPDIWPPG EPILYDLVAN IILDPTVAAP GATEDAAEKG VNAAGGSSSA GAGAGSERVA
     WLVQLHDKAM AAENVRHQSQ GAGEHQGPEW LEIQDLFVNK AESETLFTRE GYLMVWERRK
     TPGMANRKGK NAGK
//
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