GenomeNet

Database: UniProt
Entry: G3ARF5_SPAPN
LinkDB: G3ARF5_SPAPN
Original site: G3ARF5_SPAPN 
ID   G3ARF5_SPAPN            Unreviewed;       363 AA.
AC   G3ARF5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=SPAPADRAFT_154183 {ECO:0000313|EMBL:EGW31276.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW31276.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
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|ARBA:ARBA00001482,
CC         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-2A subfamily.
CC       {ECO:0000256|ARBA:ARBA00034714}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL996503; EGW31276.1; -; Genomic_DNA.
DR   RefSeq; XP_007376054.1; XM_007375992.1.
DR   AlphaFoldDB; G3ARF5; -.
DR   STRING; 619300.G3ARF5; -.
DR   GeneID; 18870973; -.
DR   KEGG; spaa:SPAPADRAFT_154183; -.
DR   eggNOG; KOG0371; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; G3ARF5; -.
DR   OMA; CMKVRYP; -.
DR   OrthoDB; 19833at2759; -.
DR   Proteomes; UP000000709; 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; -; 1.
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:SF12; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT   DOMAIN          168..173
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   363 AA;  40760 MW;  872F0A0B1E46C4F9 CRC64;
     MELDTDVPME DVEDLKQVST SATSSSTSGK QPTGITSIGG DASVSDAAAA AKKADLNVSS
     VNQLDQWIDK LSQCEPLAEA DVKKLCDMAI EVLQFEENVQ PVQVPVTICG DVHGQFHDLM
     ELFKIGGPCP DTNYLFMGDY VDRGYYSVET VSYLVCMKVR YPNRITILRG NHESRQITQV
     YGFYDECLRK YGSANVWKLF TDLFDYFPIT ALVDNKVFCL HGGLSPMIET IDQVRELNRI
     QEVPHEGPMC DLLWSDPDDR GGWGISPRGA GFTFGQDISE QFNHTNDLSL IARAHQLVME
     GFSWSHQESV VTIFSAPNYC YRCGNQAAIM EVDEQHNRQF LQYDPSQRPG EPTVTRKTPD
     YFL
//
DBGET integrated database retrieval system