ID A0A0F4YNW2_TALEM Unreviewed; 588 AA.
AC A0A0F4YNW2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Phosphoprotein phosphatase {ECO:0000313|EMBL:KKA19934.1};
DE EC=3.1.3.16 {ECO:0000313|EMBL:KKA19934.1};
GN ORFNames=T310_6094 {ECO:0000313|EMBL:KKA19934.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA19934.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA19934.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA19934.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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:KKA19934.1}.
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DR EMBL; LASV01000304; KKA19934.1; -; Genomic_DNA.
DR RefSeq; XP_013326546.1; XM_013471092.1.
DR AlphaFoldDB; A0A0F4YNW2; -.
DR STRING; 1408163.A0A0F4YNW2; -.
DR GeneID; 25318406; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT DOMAIN 130..475
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 63488 MW; 0164D165099252C8 CRC64;
MFGGSSSPPK EKTDHLQTAL KVNTEEVSVV HEKRTSPSSG SFNRKHSDDQ DPGGEKKRRS
SSVTKAASFF ASAKNSFHFS SSRESSNTTS QTARTPLQKL GKMDPALSVP QGSLNNSAGE
SLPTLRSSFR VGVTEDRNRK CRRTMEDTHA YLYNFLGTPA PATGDSTANG KDSADTSTDS
NESTHVVETD NGYFAIFDGH AGTFAAEWCG KKLHLILEDI MRKNPNTPVP ELLDQAFTSV
DQQLEKLPLR NSGCTAVAAV LRWEDRIPNP QSATGSSALA PAGASAANKP VSGPEADSDS
AQTSAQTGES SNTSQSSADA AAPPKPKQTT VRQRVLYTAN VGDARIVLCR NGKALRLSYD
HKGSDENEGR RIANAGGLIL NNRVNGVLAV TRALGDAYLK DLVTGHPYTT ETVIQPDQDE
FLILACDGLW DVCSDQEAVD LIRHVKDAQE ASKILVDHAL SRFSTDNLSC MVVRFNSDII
RDVMERRTDP IGVEGDPLSK QKGGVSEADK IVEEAQKKLE NSEGLSDKDL GLNAKLKDDL
VSQAAQESPG PEVTIDDKIA ELDVQASIEE EEKDKDKDKD KDKETKPE
//
