ID A0A2H3J5W7_WOLCO Unreviewed; 1670 AA.
AC A0A2H3J5W7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phosphatases II {ECO:0008006|Google:ProtNLM};
GN ORFNames=WOLCODRAFT_147143 {ECO:0000313|EMBL:PCH33038.1};
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phaeolaceae; Wolfiporia.
OX NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH33038.1, ECO:0000313|Proteomes:UP000218811};
RN [1] {ECO:0000313|EMBL:PCH33038.1, ECO:0000313|Proteomes:UP000218811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104 {ECO:0000313|EMBL:PCH33038.1,
RC ECO:0000313|Proteomes:UP000218811};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR EMBL; KB467831; PCH33038.1; -; Genomic_DNA.
DR STRING; 742152.A0A2H3J5W7; -.
DR OMA; TDFWTLC; -.
DR OrthoDB; 1342035at2759; -.
DR Proteomes; UP000218811; Unassembled WGS sequence.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000218811}.
FT DOMAIN 246..364
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 853..1141
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1110..1134
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1670 AA; 176352 MW; ECF9856DEFC55F2D CRC64;
MQPSPSPQIA STYATPLTSF PHTEPHAEHP ADPRPDAERV DQFAAAIHAR FALHPTHLTK
LSPPVAAPGP SSPFFPARAL PPAPSLPPPA MSSGTSSSFK LPPSVPLRAP SHTPAASSAA
ALKPTTSSAL PSMGTFSISS LQPTSLTNER VRTRHGPAAT APPRPSISFA PSTAPRAMSR
PSMSSPLAGT FSARTSASRF PPSPINTPRA AMSPLSPSSA TATSPTTPSS SDFVALAPAD
LPAVLADPST LVLDIRPHNA YATARLPSAL SLSVPSTLLK RPTFQLARVA PMIHAPAARA
RFAAWREASR ILVYDADAPG LAERPALLGL LRKFRTEGFD AARPVAWLRG GFNAAARECP
ALVDTSPLAE EEEEEEDAER EDALGEMAAP GGVEMSKSQS APAPLRTRAL PRVAFTGAST
LAPARPFGAP TQVPATPAGP RADPFASVPP TPGPSLLAAR GAGPAAGQFT LRLPGLVRGG
ASAPGASVSI SLNANVTATA PATGVPGGLA GGPAAQTVAK GGAEGMHAFP ALAASSMSVP
TLSASPGAGG FGGVAAQKTY HHSVPHTRPV AVNPFFDAIR QNLELGRGED IESGRSAGIA
LKLPRRVRRR VGDLPFEWLR EIARRGGRAQ ESSSSTEDED EDMDRGAGNK AREREEPEGM
VEKELGKGKP PRAAHVQVKA REARSTTPPP SPPSSPTISH PPGHARPGAK AHANARLAAR
APAPAQSRPQ PIPGRKPLPL GASPPSSPGA EAGDDSSTSQ SPPSADELTR ALELQFYRIE
LGEQHRLMGI MEHHSMESHT GAQGAGVSVS SAGVVRAAEA EAAEARGKEG EKGKERQKEV
FPFSITAGLE KGNKNRYRNI WPFEHARVRL RKARPEDDDY MNASYVQPLG TTKRYIATQG
PLQATFADFW TLVWEQNVHV IVMLTREIEG ATVKCGKYWD EGEYGQLHLK LLATDDTPER
EKRRRESESG FFGVHAAPQQ AKRKGGKSEH GEHDTVRRVF KLTHRAFPRA PPRIVTQLQY
LDWPDFNVPS DPRGVLGLIR EVEEAVARSK RMGDRAWGEG PLLPGPWPAR VVLPERSPRT
SPPPQAAVEG AQELDGGMEP TLGVARHALG NPPVLLHCSA GVGRTGGFIA VDAVLDGLRR
EMRKRKKTQA ANTAPGSTSA GVSGSAGTGG SGSGSGSGSR SRSSPRTRSP HSGGSSRGEP
MEVDSSPSPP SMVQDEPPLP DLTVPVSVGQ SEVHVRVAGF TESVPMDVDG TKEPQGPPRS
PPAGARTKPK DLPRTVLPAS PELVDEVRRA TLFRWPSHST STTMGDAVLE SKDSETSSSD
SYPTRSGAGS ASHSGTGVRS HSHTSTSPPT SQAGSSTSLS AAMTSKAAQM SLKAGPPKVA
SPERPTPMDV DQEAPKFTLS PPGTSPSKLD ATEPSRLDTW RSEVRTSGEP PREDVRSPSK
SPAAADAPGE HDQGGGSLDQ RVNMQRGRTF DYAQPRRLHE DLSPPLLSTY DEPIRRVVED
MREQRMSLCQ SLRQYVFVHR AVIEGALMVV DEERERERLC REATDDVGSD EAQTGTAMDV
STPARNVEGP MMEARTTGLG APGAAGDKEL SRKRSLSDVM REGALGEEHA QAQASPGRPK
RGASPTELQK ESKRGEVMLT KRPSVKRAPR TDSDSSASAE FAPMGAHETR
//
