ID A0A0N4Z129_PARTI Unreviewed; 930 AA.
AC A0A0N4Z129;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000040600.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000040600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR AlphaFoldDB; A0A0N4Z129; -.
DR STRING; 131310.A0A0N4Z129; -.
DR WBParaSite; PTRK_0000040600.1; PTRK_0000040600.1; PTRK_0000040600.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00144; MPP_PPP_family; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF385; SERINE_THREONINE-PROTEIN PHOSPHATASE; 1.
DR Pfam; PF13896; Glyco_transf_49; 1.
DR Pfam; PF00149; Metallophos; 1.
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}.
FT DOMAIN 369..374
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 47..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 108797 MW; 0A6A390F17E4371A CRC64;
MRRSSTTKER RTNKSSAKFE RLKNFKDIQE CTEYKREVSK GNLFSFITKK QKIEDKDNKE
SEGKPRRSVK NKAGSNDLSI TQHVVSKSVG SIVPSEKSKK TNRDSCHTLV KRSSSATEST
NINMKNSNNR IMFMRKTHSL NQRTPTDIKS SIFIRPTEFI GKRLLMSSIS ESNSSVSGRD
ELGGNTKSSD DDQPVTKTKK INISSIDVNN ENDRLFKSQM KRFLMNLPKC KSSTVKIEEA
FTWLSRYMDY IIIRKYNASY FASKEKNYLS NFFSESVIIR IIHHAAMIFE SEPTLLELSI
PNSMKEINVV SDIHGSMEDL MRAFGTCGTP GDSMYLFLGD YVDRGEYEVD IVMLLFLLKI
CYPKYIYLLR GNHEFYDINH RNQFPSHCRQ SFSSGNYWKL LNFVFNRLSL AAIIENEIYC
VHGGISQWIT SRNSIKNLKK PYTDNVLLVE RLIITDTVWS DPSPDLSERM FPASSRNVGF
CFTKNGLKKV LKLLDVKMLL RGHQQPIDGF ANEFGGICCT LHSRQLDITS NASTVKVFRD
KKLNGKLHIK GLIYAIKSFS EDTKSMTHRR IHYIYHKRYT VFPNVIKTDE NVDSNRITLI
LHISNDRNLS MIQEHSKNWK GSISLGVFMH NKILRDARTL CTLCHLKKYS ENETNLSIHL
IFNKLLEPND DFIKQVMENE MYCEEYFNKF SHTNGVCYKK PRDKYEKIER LLSYPINVVK
NVARNHQITK FIIFGNTGYM FSKDFEKKVL PIAKERMEGQ KNVLVLRSFD ILKELSSIDN
INKSLLRDLA FKRKVFFFKN EKKKHFRLPK LKTWLLSKEG NASVQFIYND YPIDWDPIFI
MNNNVDYYIE EINFPSEDNV NLRWQMCKNN FKFLVLNDVF VYKFGWKNEE ERELAYQARK
IAKKINSKVV KLFKEKFNRR FPNSKRKCYE
//
