ID A0A093ZKS3_9PEZI Unreviewed; 1288 AA.
AC A0A093ZKS3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=USP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V492_04345 {ECO:0000313|EMBL:KFY11650.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY11650.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY11650.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY11650.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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:KFY11650.1}.
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DR EMBL; JPJU01001427; KFY11650.1; -; Genomic_DNA.
DR STRING; 1420902.A0A093ZKS3; -.
DR HOGENOM; CLU_262466_0_0_1; -.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd01446; DSP_MapKP; 1.
DR CDD; cd18533; PTP_fungal; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF551; TYROSINE-PROTEIN PHOSPHATASE 3; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029299}.
FT DOMAIN 128..427
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 687..803
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 940..1263
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1141..1254
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 142670 MW; D9A03EB8E550C9A0 CRC64;
MATVAIQQPT PPRSPMIRKR TFSASSDGMH YGPRVSKQPK TVRQQFSPQR KRKQPPPEEK
KKSVDSAFVD GAKVDLGHSF VPPAASKRDR YSAAKESQAG LEKKCAERQA MAATVSDEWT
EKVSMRQPGF DNIRMSRCYR HSLLQALLHI PKLVNWLLEF HKLGECCSQR PTVCLACKLR
DLATLYWIQN SSRQEIYALL KDIDRTLAIR GWATDNPEEY GDPDDQFTAM LEMMSEDMGA
MGHTRFQAIH STLLTSSIRC SSCGHTTDPH HSAERTLSVP LEAGLSGSGL DAFIAAFLRD
KISGYRCEGC QKSVNVTRDV KIASPADVIS VQLKRAGWNG TVKTKVGITR VLDLTKHAVD
PSTQLRYELV STVSHQGNSR FGHYIAHAVG PDGKWTEFND ECTRKVSPKA VLMPPGFKPV
LLYYKRVQKT PSPAAGSPLT QAIRAPSSAA PTISASFSRT PGGREQARPS SPNYFGHVVD
SGNNARDSGT GHKDNGSPTV SSVHSYVEKT PRNIPLESNV DFEAFRKQSE ANQSFNLGHG
NLSHFSSAPV LPAHAHGYKS AAGHDRNTEA KRTNSAIAIN SDSWLPPRSK SHTFPTESPS
ILGIPMQESP MDTGSSQPLA PVREHTLSEP GDKHPRLSLP GGRPSPSTPH TSQQNDIPRA
VTLPPVLQDG PAFISAPDLR GFLETQNSSD YLLLDLRVAP QYSQSRIRNA LNLCIPTTLL
KRPSFNLAKL TETFKVPDEK AQFSRWSECG YIIVYDSHSA DKKDAVAALN TIKKFTNEGW
NGRAYILKGG FKAFSAIQSD AIDQKPAHDV PNSKNLSLGP LFPNATDVAG GCEMPQAKSV
ANPFFSNIRQ NMDLVGGVGQ IDVRRPDDVD QLADDFVPMW LRSTTDREDH GKAVSDKFLR
IEQTELSRMQ NALSSRVSYG TPTSRPDNDV QIAGFEKGGK NRYNNIWPFE HSRVRLQGRS
EGACDYVNAT HIKPLWSNKR YIASQGPLPA TFEDFWSVIW DQDVRVIVML TAESEGGQVK
CHPYWSAQEY GRFKITSSTE KKVPIEPIKR FRSSIRKESF GRRRANTAIE SSLPEASPGD
NADVVVRTIT LSCSTQPNTP ARQIMQLQYS SWPDFGTTAR PSHLLGIIEL SNSLQHGSLP
PAVASQINSD EPEPDQSMPP MLVHCSAGCG RTGTFCTVDS VIDILKRQRK ENLSGVTPMD
ISTDEEPDYL STKHVSKDME SDWLFNPNID LIERTVADLR KQRISMVQSL RQYVLCYETV
LEWICQQNQA PKRERSGSES LASEERRV
//
