ID A0A094ALV4_9PEZI Unreviewed; 1327 AA.
AC A0A094ALV4;
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=V493_05403 {ECO:0000313|EMBL:KFY24150.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY24150.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY24150.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
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:KFY24150.1}.
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DR EMBL; JPJV01002113; KFY24150.1; -; Genomic_DNA.
DR STRING; 1420906.A0A094ALV4; -.
DR HOGENOM; CLU_262466_0_0_1; -.
DR OrthoDB; 1342035at2759; -.
DR Proteomes; UP000029327; 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:UP000029327}.
FT DOMAIN 128..426
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 725..841
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 978..1302
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1179..1293
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 448..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
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 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1327 AA; 147274 MW; F52EF9D343FA102A CRC64;
MATVAIQQPT PPRSPIIRKR TFSSSSDGMH YGPRGSKQPK TVRQQSSPQR KRRPPAPEEK
KKNLDSAFVD GAKVDLAYSF VPPASSSRDR YSAAKESQAD LEKKCAERQA MAATVSDEWA
EKISMRQPGF DNIKMSRCYR HSLLQALLHI PKLVNWLLEF HKLGECCSQR PTVCLACKLR
DLATLYWVQN SSRQELYALL KDIDRTLAIR GWATDNPEEY GDPDDQFTAM LEMMSEDMGA
MGHTRFQAIH STLLTSSIRC SSCGHTTDPH HSAERTLSVP LESGLSGSSL EVFVAAFLRD
KISGYRCEGC QKSVNVTRDV KIASPADVIS VQLKRAGWNG TVKTKVGITR VLDLTKHAVD
ASTPLRYELV STVSHQGNSR FGHYIAHAVG PDGKWTEFND ECTRKAGYEV IEHGPATADV
LFNRSFLARR SIETTEYLNV GKSIQTMKAA TRPPLRSTRS HSHRQKTPSP AGGSPLTQVI
RAPSSAAPTI STSFSPIRTP GGIEQARPSS PNYFGLVVEP AGNNARDSAT CPRDNCSPTV
SSVQSYIEQT PRNVPIESHA EFEAFRKQSE ANQSFSLGHG NLSHFSSAPV LPVHAHGYKS
AAGHDRNTEA KRTNSAVAIN SEAWLTPHSK TFPTGGSPVL GLPMQESPMG AELSQPLPPV
QEDMLSQPSD RHPRLSLPGD RPSLPTPHTS QQKQIPRAET LPPVLHDGPA FISASDLRDF
LKTQSSSDYL LLDLRVAPQY SQSRIRNALN LCIPTTLLKR PSFNLAKLTD TFKVPQEKAQ
FSRWSEYRYI IVYDSHSTEK KDAVAAMNTI KKFTNEGWNG RAYILKGGFK AFSAIQSDAI
DQKPTLDNQN SKNLSLGSLF PNAADVAGGC EMPKAKNVAN PFFSNIRQNM DLVGGVGQID
VRRPDDADLL ADDSVPLWLR SATDRENHGK AVSDKFLHIE QVEQSRMQNA LSSRVSYGTP
ATRPDNDVQI AGFEKGGKNR YNNIWPFEHS RVRLQGRAEG ACDYVNATHI KPLWSNKRYI
ASQGPLPATF EDFWSVIWDQ EVRVIVMLTA ESEGGQVKCH PYWSAQEYGR FKIISSTEKK
VPLEPIKRFR SSIRKESFGR RRANTAVESS VPEAGPGDNP DVVVRTITLS CSTQPNVPAR
QIMQLQYSSW PDFGTTARPS HLLGIIELSN SLQHGALPPA IASQINLDEP EPEESLPPML
VHCSAGCGRT GTFCTVDSVI DILKRQRKEN LSGVTPMDIY TEGGETDYLT TRHVSKDMES
DWLFNPNIDL IERIVADLRK QRISMVQSLR QYVLCYETIL EWICQQYQAP KRERRGSESL
ASEDRRG
//
