ID A0A1N7IQ80_9CORY Unreviewed; 443 AA.
AC A0A1N7IQ80;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=SAMN05444817_101249 {ECO:0000313|EMBL:SIS39141.1};
OS Corynebacterium appendicis CIP 107643.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1161099 {ECO:0000313|EMBL:SIS39141.1, ECO:0000313|Proteomes:UP000186292};
RN [1] {ECO:0000313|Proteomes:UP000186292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44531 {ECO:0000313|Proteomes:UP000186292};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FTOF01000001; SIS39141.1; -; Genomic_DNA.
DR RefSeq; WP_076598222.1; NZ_FTOF01000001.1.
DR AlphaFoldDB; A0A1N7IQ80; -.
DR STRING; 1161099.SAMN05444817_101249; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000186292; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR Pfam; PF13672; PP2C_2; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..236
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 275..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 47481 MW; B268838749AC6805 CRC64;
MTNLKLNFHT ASDRGLVRDN NEDSAYAGPH LLLLADGMGG HAAGEIASQL MVEHMEHLDR
EPADADTLAL LGAAADDANA SISDSISEHP EQDGMGTTLT ALMFDGENMG LIHVGDSRGY
RLRDGELTQI TEDDTFVQSL VNDGKLQPED VSSHPQKSLI LKAYTGRPVE PYLELLPVKA
GDRFMLCSDG LSDPVTHSTM EATLAEGTPE EAAARLIELA LRSGGPDNVT VVVADVVDTD
DADSPELPTA PAIAGALITG EEPTHPDTAA GRAAKLMGAK RDKGESSISK KEEPASDDED
DHRRRSAWPW VIGVLALALA ALGGLWWFDS ARGDTYFVAV NDREEFVIEQ GMDATIFGRD
MHEPVQQVCI NNDNQIRLVG IGDVPDDCHV FAVRDLPEST QSRVDNLGSG SYAEVTDQLN
SLADEALPAC VDSTDDGNCR EVK
//
