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Database: UniProt
Entry: K9GIW1_PEND2
LinkDB: K9GIW1_PEND2
Original site: K9GIW1_PEND2 
ID   K9GIW1_PEND2            Unreviewed;       487 AA.
AC   K9GIW1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=PDIG_30910 {ECO:0000313|EMBL:EKV14638.1};
OS   Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV14638.1, ECO:0000313|Proteomes:UP000009882};
RN   [1] {ECO:0000313|Proteomes:UP000009882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
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. PP-5 (PP-T)
CC       subfamily. {ECO:0000256|ARBA:ARBA00008786}.
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:EKV14638.1}.
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DR   EMBL; AKCT01000131; EKV14638.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9GIW1; -.
DR   STRING; 1170229.K9GIW1; -.
DR   eggNOG; KOG0376; Eukaryota.
DR   HOGENOM; CLU_004962_5_2_1; -.
DR   InParanoid; K9GIW1; -.
DR   OMA; NHFFMSR; -.
DR   OrthoDB; 1107740at2759; -.
DR   Proteomes; UP000009882; 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; cd07417; MPP_PP5_C; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041753; PP5_C.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
FT   DOMAIN          288..293
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   487 AA;  55125 MW;  71A88994F0AE4C70 CRC64;
     MATDQEVATA LKVQGNKAFA QHDWPVAVDF YNQAIAKFDK DPSFFCNRAQ LTVLFCLVSQ
     AQIKLEAFGF AIADATKAIE LDPNYVKAYW RRALANTAIL SYKEALKDFK AVVRREPTNQ
     NAKLKATECE KLVRRREFER AIEISDPPSA FADLDIGAIN VEDGYDGVRL GEEMSQEFID
     DMIERFKDGK KIHRKYVFQI IKAVKDLVYN EPTMVEIGVE SGKKLTVCGD THGQYFDLLE
     IFRRNGAPSD THAYLFNGDF VDRGSWSCEI ALLLYAYKWL RPNGLFLNRG NHETDDMNKV
     YGFEGECKAK YNERVFKVFS ESFSALPLAT LIGEKYLVLH GGLFSDDKIK LDDIRKLNRH
     NQRQPGQAGL MMEMLWTDPQ TENGRGPSKR GVGLQFGPDV TKRFCENNGL KAIIRSHEVR
     MGGYEVEHDG RCITVFSAPK YCDSTENKGA YINIGPELEL AYEVFEAVPH PDIKPMAYAN
     NSILSGM
//
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