ID A0A176VGI5_MARPO Unreviewed; 992 AA.
AC A0A176VGI5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=AXG93_4794s1140 {ECO:0000313|EMBL:OAE19502.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19502.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19502.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE19502.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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:OAE19502.1}.
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DR EMBL; LVLJ01003848; OAE19502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VGI5; -.
DR OrthoDB; 53548at2759; -.
DR Proteomes; UP000077202; 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; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF26; PROTEIN PHOSPHATASE 2C 50-RELATED; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 193..697
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 316..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 108686 MW; 4E62B9B7BE766D83 CRC64;
MGALAKFTSN LVKTSGYSQV SHEQEQAAVG AFSLSSEESL SAEVTKLSSS NPEHDDLGKC
DKSTFVDEQE LRLPETSDSR HSDFKLECGV GDGIFNANTH DQYNVCGVAL FQGRRPSQED
RAVCLSSLCL LLSGKNHSRI LCCSFFTAIA CCFYPFRYKI VFAKLASLNS LDSVQISAKA
GKDTALIPII CKNAAIYSTT AAVELLTGVK LCDTFVIKTV SRLVSGIENI TVGLYAVFDG
HGGQEASTFA AEVFHHHFVD HFTQIIESSD VAMIRGIKAS QKEGKWTSQG SWSHGSPSLK
GDASADAFEA SSLFSDEDPE RLLPSKSPRD ARTNQVYTSI KPSDMGSSFE NREVPHKSSE
GEREQPGVLN DEARRELIRE VLEDGLIIRR ILAEALSRAV FSIDTMFSVT ARQLGLFSGS
TACIVLQVEE DILVANLGGY LLRNTVEMVM AMQSGKVSCD QKPNGRRKRK SERSKADCQT
GLRVRDLTRD HRPDRDDERQ RIEGAGGFVT THGAVARVNG KLAVSRSIGD VHLKRYGVIA
DPEFTGWLKI PKSQSFLTIA SDGVFEKLNT QSVCDVLYAI NANEDVFTVL GLENSTADAI
IAMPSIAERL NDYWGSVIRQ GSSLSVGEGI WERDSSNLGN SSAAREAGEG NQKGAEGTEE
RLVVKALSLV QSMAEAVGEM ALKLGTMDNV GTIVLSLRPL PALLPDPHLE KTTNESQRLA
DDPQTVIELS DRNTVQGLRD EATVVEAVIE ADSLISNGTS SSRTWSKSHN RNKTSVVMTQ
NLEASYCYEL IESLPRHAIV PLTNVVEGGT VREEDEAGNR EGLLTTDVYY TGPGGGGSVE
LYREQLVCTP KQTHQKEMKE LCRRPVRLSH FLALIGSVPL DSQTLLPDTD IPSDRPVFVP
SSTRYHRYML KKNFARGAFG EVWLAVRRAR SVPDGGDTNE FYNSSCSAGD DRFETTEQNR
NYKDDRTTYV LKRILVNVVF ANNQKVIQLS TI
//
