ID A0A177DD79_ALTAL Unreviewed; 451 AA.
AC A0A177DD79;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=AA0117_g10871 {ECO:0000313|EMBL:RYN69326.1}, CC77DRAFT_234764
GN {ECO:0000313|EMBL:OAG17773.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG17773.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG17773.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG17773.1,
RC ECO:0000313|Proteomes:UP000077248};
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.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN69326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN69326.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; KV441485; OAG17773.1; -; Genomic_DNA.
DR EMBL; PDXD01000044; RYN69326.1; -; Genomic_DNA.
DR RefSeq; XP_018383194.1; XM_018530776.1.
DR STRING; 5599.A0A177DD79; -.
DR GeneID; 29116370; -.
DR KEGG; aalt:CC77DRAFT_234764; -.
DR VEuPathDB; FungiDB:CC77DRAFT_234764; -.
DR OMA; QSTMPID; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; Unassembled WGS sequence.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR Gene3D; 3.60.21.10; -; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR047129; PPA2-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR PANTHER; PTHR45619:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC SUBUNIT; 1.
DR Pfam; PF00149; Metallophos; 2.
DR PIRSF; PIRSF033096; PPPtase_5; 2.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT DOMAIN 112..117
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 211..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48979 MW; D09C8CCCF0032530 CRC64;
MSAGGSDLDK AIQQLRACRP IPENQVRELC YKARELLIEE GNVVGVDAPV TICGDIHGQF
HDLMELFRVG GDVPDTNYLF MGDFVDRGFY SLESFLLLLC LKVRYPDRIT LIRGNHESRQ
ITTVYGFYDE CLRKYGSANV WRYCCEVFDY LALGALVQGA ATSLQATDGP IAESSNAENM
PDIDQDIEIE TLNANGEVMY RYARNSDSQS SAASQVSANM GSSSPVAPTP GRVGPAGTGA
TSSANGSARN DTGAILCVHG GLSPLVDSVD KIRLLDRKQE VPHEGAMCDL LWSDPDEIDG
WGLSPRGAGF LFGADIVKTF NHKNDLSLIA RAHQLVMEGF KEMFDSTIVT VWSAPNYCYR
CGNVAAILEL GEDGSNAGFQ RRSNGDRAGG GGGWVLGSNA GPNGERRLSS VLNDNFQKNR
DGPGRRYRVF EAAPQDSRGM PAKKPVADYF L
//
