ID A0A1J9PR82_9EURO Unreviewed; 628 AA.
AC A0A1J9PR82;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=U4/U6.U5 tri-snRNP-associated protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AJ78_01263 {ECO:0000313|EMBL:OJD18726.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD18726.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD18726.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD18726.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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:OJD18726.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGRN01000027; OJD18726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9PR82; -.
DR STRING; 1447872.A0A1J9PR82; -.
DR VEuPathDB; FungiDB:AJ78_01263; -.
DR OrthoDB; 719409at2759; -.
DR Proteomes; UP000182235; 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:UP000182235};
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 110..207
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 232..616
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 70114 MW; FD301E4DF40D0CD8 CRC64;
MAKRPAETSL EEASSTTSPA SKRARVEDAE VEQQQQQQQQ PTQQINHRSP LHERRWEDDE
RNGKDILAAA DQEEEEIEEG SLHEARDEDE EEQESAISAP ARQTAPTEGY GDLYLDTIQR
SVLDFDFEKQ CSVSLSNINV YACLVCGRYY QGRGPKSHAY FHALEVGHHV FVNMESKKVY
VLPEGYEVKS RSLDDIKYVV DPQYKKEEVA KLDKVVIDAW DLAGKRYRPG YVGMNNIKSN
DYLNVIVQVL AHVRPIRNFF LLHQFPTPGT PQLPLRFGIL VRKLWNPRAF RSHVSPHELL
QEVALRSSKR FTLTQQSDPV DFLSWFLNNL HLTLGGSKKP SATPTSVIHS AFQGHLRIES
QAITARSDAA NARLVFSESS DTTSQTTPFL ILTLDLPPTP LFQSSNAESI IPQVPLTSLL
NKYNGLVASE KLSHRVRHRL LHPLPPYLLF HIKRFSKNKF VSERNPTIVT FPSPRSLDMS
PYVEPNPSLF PPGEPIWYDL VANVILDATV TAPGVGGSND SSISGPASTA TNSKKGAGTG
GAAGSTATTP GAGAGNDKVS WLVQLHDKAM SVENEHAQAQ QHRGPEWLEI QDLWVQRAES
ETLFTREGYL MVWERRKAGV ESKGKGKA
//