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
//