ID A0A1Q5T5Y7_9EURO Unreviewed; 623 AA.
AC A0A1Q5T5Y7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=mRNA-splicing protein ubp10 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSUB_11151 {ECO:0000313|EMBL:OKO95639.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO95639.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO95639.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO95639.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) 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:OKO95639.1}.
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DR EMBL; MNBE01000702; OKO95639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5T5Y7; -.
DR STRING; 1316194.A0A1Q5T5Y7; -.
DR OrthoDB; 719409at2759; -.
DR Proteomes; UP000186955; 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:UP000186955};
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 102..199
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 242..614
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 69496 MW; 4D98ACFF6E94350B CRC64;
MSKRPAELPL EENYPGSPAS KKARVEDDTE ADSRNGSAPA QQLNDQEVGA DRCNGADMSR
AAEPEDQELQ GGMKDLSESS DIDEEVSALS APKRQAQPME GYDDLYLDTV NRGVLDFDFE
KLCSVSLSNI NVYACLVCGK YFQGRGPKSH AYFHSLEDNH HVYINMGTKK VYVLPEGYEV
KSKSLEDIKY VVDPVFTKSE VVKLDKEVHD AWDLSGTRYR PGKTNPLSPM RHVRILIREG
FVGMNNIKAN DYLNVVVQLL AHVHPIRNFF LLHEFPTPGT PELALRFSTL VRKLWNPKAF
RSHVSPHELL QEIAMRSSKR FTLSQQSDPV EFLSWFLNNL HLSLGGSKKP SSTPTSVVQA
AFQGQLRIES QAITAHSDTQ NARLVFTESG DIKSQVTPFQ ILTLDLPPTP LFQSANRESI
IPQVPLTTLL NKYNGREASE KMAHRVRHRL LHPLPPYLFF HIKRFSKNRF VSERNPTIVT
FPSPRSLDMS PYVEPNPSIC PPSEPILYDL VANIILDPSL AAPGATEDAA DKGVNAASGA
GGSSSGAGAA TEKVSWLVQL HDKAVSAENA RHTGGAEQQQ RNAEWLEVQD LFVKRAETET
LFTREGYLMV WERRKAPAQK AKK
//
