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Database: UniProt
Entry: A0A420HCV4_9PEZI
LinkDB: A0A420HCV4_9PEZI
Original site: A0A420HCV4_9PEZI 
ID   A0A420HCV4_9PEZI        Unreviewed;       618 AA.
AC   A0A420HCV4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=OnM2_090002 {ECO:0000313|EMBL:RKF55286.1};
OS   Erysiphe neolycopersici.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF55286.1, ECO:0000313|Proteomes:UP000286134};
RN   [1] {ECO:0000313|EMBL:RKF55286.1, ECO:0000313|Proteomes:UP000286134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMSG2 {ECO:0000313|EMBL:RKF55286.1};
RX   PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA   Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA   Deng X., Wei C.I., Xiao S.;
RT   "Comparative genome analyses reveal sequence features reflecting distinct
RT   modes of host-adaptation between dicot and monocot powdery mildew.";
RL   BMC Genomics 19:705-705(2018).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class CDC14 subfamily. {ECO:0000256|ARBA:ARBA00007315}.
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:RKF55286.1}.
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DR   EMBL; MCFK01009090; RKF55286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420HCV4; -.
DR   STRING; 212602.A0A420HCV4; -.
DR   Proteomes; UP000286134; Unassembled WGS sequence.
DR   GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd17657; CDC14_N; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR029260; DSPn.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR23339:SF27; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF14671; DSPn; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286134}.
FT   DOMAIN          228..392
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          312..378
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          34..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  69507 MW;  C828A3BA534092D5 CRC64;
     MTPSIKFGQV IEFIPDRLYL ASYSSPPSAD TLFPYPESIN SRRSPSKKTS RAIDGTSIRP
     PRNRIPPCYF TIDDSLPYNA FHHDFGPLHI GHLYRFAVQF HDILAAPENK DRPVVFWSKA
     NARSRANAAC MLASYMVLIQ SWAPHLALAP ITQVDPPFMP FRDAGYSQAD YEITVQDVVY
     GVWRAKEQGF CALPQFDLEE YERYERVDQG DFNWLTPDFI AFASPQYSPV SEIPKNSPLY
     ESLPRTVEAV DSHSTLPGPF KNILKHFATR NIGLVVRLNS ELYSSSYFTA LGIDHLDMIF
     DDGTCPPLKT VRRFITLAHE MIQIKKKGVA VHCKAGLGRT GCLIGAYLIY RYGFTANEII
     AYMRFIRPGM VVGPQQHWLH LNQGTFREWW VEEQFEIKMK DRLANIMPST PKITSKSVKL
     NTQVVTPPNG NARSPLREVD NDSRNSIGLQ EDCLPAPTPG QPRKTSRSVD YHHPYKRKTS
     SHTTTSDEKI IQREAEIISI HRSSIDNTDE DEIQFRMRSS RKTSGSPSGR SMSQTTTTIY
     TSIHNDSSND IENIGTKSRS KVTSSIKSGS GSIILNKVRG SPKRSNDILK GNMESAGIRK
     TSGKLNGILN TGRKVPGH
//
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