ID Q82FB8_STRAW Unreviewed; 514 AA. AC Q82FB8; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN Name=prpB8 {ECO:0000313|EMBL:BAC72053.1}; GN ORFNames=SAVERM_4341 {ECO:0000313|EMBL:BAC72053.1}; OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC72053.1, ECO:0000313|Proteomes:UP000000428}; RN [1] {ECO:0000313|EMBL:BAC72053.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428}; RX PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M.; RT "Genome sequence of an industrial microorganism Streptomyces avermitilis: RT deducing the ability of producing secondary metabolites."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001). RN [2] {ECO:0000313|EMBL:BAC72053.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428}; RX PubMed=12692562; DOI=10.1038/nbt820; RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M., Omura S.; RT "Complete genome sequence and comparative analysis of the industrial RT microorganism Streptomyces avermitilis."; RL Nat. Biotechnol. 21:526-531(2003). 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 --------------------------------------------------------------------------- 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; BA000030; BAC72053.1; -; Genomic_DNA. DR AlphaFoldDB; Q82FB8; -. DR KEGG; sma:SAVERM_4341; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_025431_1_0_11; -. DR Proteomes; UP000000428; Chromosome. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR NCBIfam; NF033484; Stp1_PP2C_phos; 1. DR PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000000428}. FT DOMAIN 6..237 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" FT REGION 269..310 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 438..514 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 443..502 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 514 AA; 54175 MW; 81A75FD53971D7AC CRC64; MSLSLRFAAG SHKGMIREGN EDSGYAGPRL LAIADGMGGQ AAGEVASSEV ISTIVALDDD VPGSDILTSL GTAVQRANDQ LRMMVEEDPQ LEGMGTTLTA LLWTGQRLGL VHVGDSRAYL LRDGVLTQIT QDHTWVQRLV DEGRITEEEA TTHPQRSLLM RALGSGDHVE PDLSIREVRA GDRYLICSDG LSGVVSHQTM EDTLASYQGP QETVQELIQL ALRGGGPDNI TVIVADVLDI DAGDTLAVQL SDTPVVVGAV AENQNQLHDN GAMQTPAGRA SHLGRQLPGQ GGGGGEFGPP GSGDTTGYVP AGSFGSYSDE DFVKPRTGLK WLKRSFYIVL ALAVIGGGTY GGYRWTQTQY YVGASGEHVA LYRGISQDLA WVSLSKVQKD HPEIELKYLP PYQQKQVKAT IAEGGLKDAE SKVSELAVQA SACKKDALRR ASESQNNAKT GEGEAGGTTG TTKTSLTSKA TSSPTPNPST SAPSSSKSKT APTPTPGPSL SDEEQKLVSL CGKQ //