ID A1CQR2_ASPCL Unreviewed; 442 AA.
AC A1CQR2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=USP domain-containing protein {ECO:0000259|PROSITE:PS50235};
GN ORFNames=ACLA_027050 {ECO:0000313|EMBL:EAW07983.1};
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:EAW07983.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07983.1, 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 ---------------------------------------------------------------------------
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; DS027059; EAW07983.1; -; Genomic_DNA.
DR RefSeq; XP_001269409.1; XM_001269408.1.
DR AlphaFoldDB; A1CQR2; -.
DR STRING; 344612.A1CQR2; -.
DR EnsemblFungi; EAW07983; EAW07983; ACLA_027050.
DR GeneID; 4701904; -.
DR KEGG; act:ACLA_027050; -.
DR VEuPathDB; FungiDB:ACLA_027050; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_619591_0_0_1; -.
DR OMA; IQWTINQ; -.
DR OrthoDB; 2184166at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF796; UBL CARBOXYL-TERMINAL HYDROLASE 18-RELATED; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 1..245
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 261..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 49059 MW; 40EF06400752D11C CRC64;
MSNGYWIDVS NRQYHASMNR FWKCLCDPKF KPDHWDKVPG RQEDAPELTA KSVNDLEALF
TVELDQVLIC SICQRKESIP ADGGKFLVVD LPSRVGSVTI NEAIELSMKS KIPRYCDTCN
AQTTQIVQKS ILIPPEMLFI QVNRYTAQGK LQNELDIEEE LVFPDTLIHD IAKTNEELRY
ELYGVIFHKG SVKSFGHYTA AIKAPSDEWA LVNDEQVKFP LTLAQSMSSP EGGKKDAYIL
AYRRLPLQGS PEKFIVNQKK ADTNTGPSAS ASIPLARTPS PGRTRSWTGS PNLSSPGKGL
RNGGVTMVET IQLDGRDIKW TIKQQLNLSV NAGGLVKLKP RAKTQRATLT LTLISEATGE
ILEGNANISF KPRIIREDRI ASPASMNTRT PSPGTKQTTN EVSRKAAKPQ GVKKKTIEGR
RLGSNEQPAP RRSARLLKKA FE
//
