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Database: UniProt
Entry: U4LQG1_PYROM
LinkDB: U4LQG1_PYROM
Original site: U4LQG1_PYROM 
ID   U4LQG1_PYROM            Unreviewed;       992 AA.
AC   U4LQG1;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Similar to Tyrosine-protein phosphatase non-receptor type 1 acc. no. O13016 {ECO:0000313|EMBL:CCX31580.1};
GN   ORFNames=PCON_11021 {ECO:0000313|EMBL:CCX31580.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX31580.1};
RN   [1] {ECO:0000313|EMBL:CCX31580.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX31580.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX31580.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR   EMBL; HF935615; CCX31580.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4LQG1; -.
DR   STRING; 1076935.U4LQG1; -.
DR   eggNOG; KOG0789; Eukaryota.
DR   OrthoDB; 1342035at2759; -.
DR   Proteomes; UP000018144; Unassembled WGS sequence.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   CDD; cd18533; PTP_fungal; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
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   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF551; TYROSINE-PROTEIN PHOSPHATASE 3; 1.
DR   Pfam; PF00581; Rhodanese; 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; 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.
PE   3: Inferred from homology;
KW   Receptor {ECO:0000313|EMBL:CCX31580.1}.
FT   DOMAIN          240..358
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          498..725
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          673..718
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  106809 MW;  ECCA69F18EED6D56 CRC64;
     MSGLTASTRK SNTTEAPSHN SHSQVRQFHT GPTSSQQQPT FDFPSPQVAL SNATETPAEN
     PSAAGGYFNF VNDDPGLGNH STKNWSPASS SIRSAAARSP LPVLVDNPTT PFQIQTEVLA
     RKLQRKDAPR LDLGSIRSNH TTAFAPASNT VPNLDTLTPQ GNDYFSSVRD SSPDRIDIGD
     NDPWPPLSAP PSLRATPALP SPISMKLPAA RSMTLPIPAK DNNTNMIEPA QLSELITQHN
     TDSLLLLDVR TYKNYSEARI KSAVNLCIPT TLLKRPSFNV TKLSETFANN QDKERFGQWK
     KMKFIVVYDA DSNNLNDSSA LTALHTLNKF SREGWDGLPY ILKGGFSGFA AIFDNQVDRT
     PPPKATTPVK GGLSLNGASG PEKVTGGVFN CPLPQSQSVV NPFFSNIRQN MDLIDGVGEI
     PIQVPTTMSN KNLSQLPTWL NDVACKEDGS KVVADRFLKI EKAEQRRMQD ALNVSVVYDS
     PTSASVRPHT LAGVEKGNKN RYNNIWPYDH SRVKLQEYPT DECDYVNASH ISVPHSQKRY
     IASQAPLPST FRDFWSMIWE QDVRVIVMLT AESEGGRLKS HNYWNSDQYG SLKLTRIQER
     KVSLEPPALK ASPKRRSVSC SSSQVANDIP YITVRKFTLE HTGCPFMPMR EITQLQYTGW
     PDLGAPAHPS HVLGLVEHTD AVVRASSTSS EHPSRRPVLV HCSAGCGRTG TFCTVDSVIG
     MMKRQMMHKR MLAKASGANG SAASSAASSA HSNYAPSVSP GSIAPATING SSQTNGSVNG
     SSQPNGSATN GTASAPLAHP GAVNGASGIL SPNATTAALA QNSGPFFPMT STNHTTTAGA
     SNSPFFSAAP APQSSTTPFF SPTGVVNHQS AISALPPPSA SQGFQLNLPG ALSPSQQASQ
     QASQASQASH LPETSDHGLN LGMGMGTLGL EDDGDWIGRE DEDLVYKAVC ELRDQRISMV
     QCLQQYVLCY ETVLEWLAKE QSSGEMGGKR KA
//
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