ID A0A178DKL7_9PLEO Unreviewed; 821 AA.
AC A0A178DKL7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 6 {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ07DRAFT_649926 {ECO:0000313|EMBL:OAL43579.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL43579.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL43579.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL43579.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR EMBL; KV441666; OAL43579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DKL7; -.
DR STRING; 765867.A0A178DKL7; -.
DR InParanoid; A0A178DKL7; -.
DR OrthoDB; 1342035at2759; -.
DR Proteomes; UP000077535; 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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT DOMAIN 238..354
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 494..812
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 693..803
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 91108 MW; F2AA5616AD4BF540 CRC64;
MNGVAKTPGH VITHKAKEPG TPSPNYFGLQ VNSNADHFSS SAAQHIRGNW SPPTSNVRST
AAASPRIIPV EQNPEFEQFR RQSENNRAFA LGSFDFASSH GTSTKSPFFA NVKTPLSPQS
MTMPARRGSD KDETKDDSDN APKPRSPKRM LSTESPLFLD RPRRNSPASF EGFGRTDAIA
QFAEDRVPRP SLPVKQSHHI SLASHRAETL PANLVDEKGT DGPSMATAQH VVNILESAVD
EVLLLDLRVS TQYAKARIAG ALSLCIPTTL LKRASFNVQK LAETFKDDEQ RERFERWRSS
KHIIVYDANS SQLKDAATCI NTLNKFMSEG WSGSTFIIRG GFQEFSQRFP AWITNQGTQS
PSASATAALT IDSGLPSVAP VIGGCPMPVT QNAANPFFGN IRQNMDLIGG VGQMPIKHPA
SMTQSAEAEL PQWLQNAAAE NDHGKKVSDA FLQIEKREQK RMQEALSGKV VYGTPTSLGS
AKTIQIAGIE KGSKNRYNNI WPYEHSRVKI EGVAEGSCDY VNANHVQSSF SNKRYIATQG
PIPATFKDFW NVVWQQDVRV IVMLTAEQEG GQVKAHNYWS DKHYGHLHLN NLGERRASLE
PSKIHKHREH SRPPLGQRRS TNPARPSNLT KEATTGSPNQ DQPYVIVRKF TLSNDEEPFA
RMREITQLQY SNWPDFGAPA HPTHLLGLIE QCDAVVRSID ATSPSKPEPA NSRPIIVHCS
AGCGRTGTFC TVDSVLDMLK RQRQARNNRQ ITPMDVDSET KLKSKDREEG GWIADDNVDL
ISKTVEDFRL QRLSMVQSLR QFVLCYESVM EWLVEQHPKS A
//
