(data stored in SCRATCH zone)

SWISSPROT: A2Q7J2_ASPNC

ID   A2Q7J2_ASPNC            Unreviewed;       937 AA.
AC   A2Q7J2;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 86.
DE   SubName: Full=Aspergillus niger contig An01c0050, genomic contig {ECO:0000313|EMBL:CAK43468.1};
GN   ORFNames=An01g00900 {ECO:0000313|EMBL:CAK43468.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43468.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000256|SAAS:SAAS01128831};
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DR   EMBL; AM269952; CAK43468.1; -; Genomic_DNA.
DR   PaxDb; A2Q7J2; -.
DR   EnsemblFungi; CAK43468; CAK43468; An01g00900.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTPase_domain.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; TYR_PHOSPHATASE_dom.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   4: Predicted;
DR   PRODOM; A2Q7J2.
DR   SWISS-2DPAGE; A2Q7J2.
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00160,
KW   ECO:0000256|SAAS:SAAS01031440};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01031415}.
FT   DOMAIN          620..896
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          806..887
FT                   /note="TYR_PHOSPHATASE_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          195..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          903..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..249
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..470
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..561
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        829
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   937 AA;  105628 MW;  6BA4668FF25E7673 CRC64;
     MAIASRAAEC AQLFDKYART LDGDELLKQD MENEIFRFNL WAANNFILTP GRASMDWRLR
     NAPLLQSTMA ELLDDLKADL INQSNFPFNS TIPTGMLYEL PLHAVSETLD GLFRLSRAIR
     RSGILRRYVK VGNYVEFDEN GVNLTEAFRN GVKTLIEFRM KESKSSNGLR ERIINTVCLR
     QQYFSYLKAK KATNAPISGA DQSHQSTPRS ALRATASVTG SLTSKAQGAA RQQSSPMRRP
     GPSIMTATTA QPDRIPKAYS VKSAHEQQTY DVDCNDADIP PPPNVSGNRK ESECPYCFLA
     CSKEELSGRR WKHHIIQDLM PYICVLEPCP TPNSLFESGK DWLSHMKNQH PVSGWTCVDS
     THDTTFFFQS ESGFREHLHQ YHEDQFDDDD IDDIATACYQ KLPDDIIIRE CPFCPTVQKL
     ELKPKDMINH VANHLISLAQ ISLAGHIDDG RSQSAWSGSS RDSSSLPASI GSLPERLHSE
     FRDDDETEYL ASISGEVIPD ADEELIYALW QKVQKPQDDP SLDLTLRHFI AQSGMQAKVT
     TEGAVVGSND LDTGQSSEKE QATAPELDRS SEDSAGVLQD TAREGSLKIV EMFDEEGNPR
     LFDEITDDVP PFLCQSDSEI YDKFEELEWE ERVRLNEGML TNDPAHPYAL EQDPEVSARN
     RYDNVQAWAN SRIHLRVPEG ECDFINASPI ILRDSVTQEE RTYIATQAPI IGYLSHFWHM
     VFHESKDVAV IVMLTQTFEA GREKCAQYFP LHLDQASMFL ESTFDVKSRS EIRKLELTIG
     SETKIVWHFL FAGWPEYSKP EGDDCEALLE LIRLSASKSG PQNPRVVHCS SGVGRTGTFI
     ALEHLLQELE SGQLLQLADP EADPVFDTVN QMREQRMMMV YNVKQFQFIY DVLREQTDIK
     LGKVRPRNNG SLGSQMEEPR PAKLAKIGDQ ANKVPAS
//

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