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Database: UniProt
Entry: M2RR28_CERS8
LinkDB: M2RR28_CERS8
Original site: M2RR28_CERS8 
ID   M2RR28_CERS8            Unreviewed;      1519 AA.
AC   M2RR28;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Protein-tyrosine-phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CERSUDRAFT_78993 {ECO:0000313|EMBL:EMD41341.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD41341.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD41341.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD41341.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(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; KB445791; EMD41341.1; -; Genomic_DNA.
DR   STRING; 914234.M2RR28; -.
DR   HOGENOM; CLU_002713_0_0_1; -.
DR   OrthoDB; 1342035at2759; -.
DR   Proteomes; UP000016930; 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:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE S; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00102; Y_phosphatase; 3.
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   Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT   DOMAIN          41..158
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          640..956
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          899..938
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          157..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          741..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1110..1294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..870
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1214..1252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1270..1294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1441..1456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1480..1497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1498..1519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1519 AA;  161787 MW;  7F414BF48E7B05C4 CRC64;
     MQRPPPPIGS SSASSAPSIR APLPPSAFPA VTPAELSDVL SDTNALILDI RPHAAYAAAR
     IPHAVSLSVP STLLKRPLFS LARLAEMLPG PAARAQLARW PTASRIVVYD ADTAALAEGN
     VVGLMRKFRA EGFPAERQVA WLRGGFHAVV RNRPDLVDTA PVHDDEGDAD EGGGADEAPN
     IGKSVSAPAG VSSFAPPPPR SAPLRTKRLP MSAFTHASTL RPSISMHALP EGIASTSAVP
     PTPMAVARAD PFNNATAIPQ TPAGEFPPMG RSVSTQSGHF SLRMPMQRGG ASSMPTISPG
     HGHQYPALGP RVAHYSLPPR QVAFNPFFDS IRQNIELAGG PASQRGTGIQ LRLPRRVRRR
     VGELPFEWLR EIARRSGRAK ESDSDSDSMS EDSVSGAENV QPARTAKPSS VRTVKQQAHT
     QAPVRRHPLP HEHRGHGDPL SSPPSSPTRA LPPRSRTSSG ARPSPLHTMH EQPTPTATQP
     SQAHQAQDDN LPGSSSSDSR SPASAEDLTR ELEMQFYKIE LGEQRRLMGV MERHSKDSGG
     VVSIASPGTA TGPVHSSSHS AGSPSGTAGA VELAQAARLP KVAKKLEEVA GEVEKEEVGV
     DVEVEGLGVG QRKRGKGKGK GKGGEEFPFS ITAGLEKGSK NRYRYIWPFE HARVRLRKIH
     PEDDDYMNAS HVQPLGTTKR YIATQGPLPA TYIDFWKLCW EQNVHVIVML TREIEGASVK
     CGKYWADGEY GPLRLRIIET NDSPERERRR REAEMNGGFF SAHIPQMKPK PKRRRRKSQA
     TDPLRDEDSD ASDSDHRTTI RRVFELTHSG YPAAPPRIVT QLQYLEWPDM NVPEDPRGVL
     RLMRKVEDVV DRARKDGDRP WGEGPLRRRA GAAKHQPASS VSMYASATPE PTTDEGGLSD
     DVDPVTGIAK HAKGNAPVLL HCSAGVGRTG GYIAVDAVLD GVRRDIRKRR EAGADVVVSS
     VSASASLSTS GSAGRSSPNR PSDSRASSQG VDQDAMDVDS NSSPPGESVD VRAPASGPAH
     TVPLGGLTMP VLVGGSEVHV PVAGFAGSAP MDVDGGLVAG NNNPDKSRPR RPSAHSPPGS
     LDGAVPALVL SASPALVEEV RRASLNRWPS TSTAMSSITE QATPMSSRDS LSSSSGSVAV
     KASSSPGTTS GWASTSDSMI HGHSRSSVSP PTSNTGSSAS LSGAMQKTAN LTLRSSSSPA
     PSASTAADSD PHARAMSVQS SLSSASDSKT SRSTSEAQQS SRLDTWRSEV RTSGSPPHRE
     GDGSPPATDA PGESTKQTAE QAEEDGSTSS EPRTYNFALP RRLHDDSSPP LLSTYDEPIR
     RVIEDMREQR MSLCQSLRQY VFVHRAIIEG ALMIVDEEKA REREEMEQAM EERAYAPKGS
     RIVLDDLGVA DMDISPVEEE AQESVGVEPA FPRAARSQEL GHSLVSAQTG GEAIIKGSES
     GSKAPNPSSA PTTLESVLSP GKMKRGASPT ELQQDAAKLS KRPSVKRKQR SDDDGSLRLE
     TMSMTSASGS SALPGPRQQ
//
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