ID A0A6H5KI44_9PHAE Unreviewed; 1142 AA.
AC A0A6H5KI44;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN ORFNames=ESUBFT_38_15 {ECO:0000313|EMBL:CAB1111622.1};
OS Ectocarpus sp. CCAP 1310/34.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=867726 {ECO:0000313|EMBL:CAB1111622.1, ECO:0000313|Proteomes:UP000485383};
RN [1] {ECO:0000313|Proteomes:UP000485383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bft15b / CCAP1310/34 {ECO:0000313|Proteomes:UP000485383};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- FUNCTION: Enzyme with a broad specificity.
CC {ECO:0000256|ARBA:ARBA00003302}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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:CAB1111622.1}.
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DR EMBL; CACKRE030002972; CAB1111622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6H5KI44; -.
DR Proteomes; UP000485383; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
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:UP000485383}.
FT REPEAT 487..509
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 641..1121
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 116414 MW; 9D283E8D8AC5EE32 CRC64;
MDSSPASAAD MLLQRHRSSL QPMAAAATAA EAAGGRKSVQ EQQHRAEEEE PTPVPAASDA
ELERMMQAVR WGGGRQQTPP PPPPPAGVAV PRMQQQPLSP VILPAGEARQ PDIVRHEAAD
MYDVLEYRLR NNDRDLKSLL SRSTDRLAKS EQEPSRPTAG DTSPPSEPPP AAAPVSPPPA
AAATQPALPA VAPHSAAASP SAAAASAVAV LSSPPPDSGG EPTPPQQQPP QQQAAAVSAS
GVVTNTGAAH TSSGGGDDRR IVSIDSAAAG AVAESAGGVA AQMGQAQGMG MPSGPGVGET
AAAAAAAAAA AAAAGEGAVV TPTRPIGGGE SGGRGGSAKA GLGPPVPPSV GGSTGSCGLG
QAAGGGGGGG GSGVWLRPGT TAKSGGNVDG VLVTPPRLPR PQADGMIVEA ATEAARWLAV
DDHTWHQGKK FMDECIADCP NEKNLNRRKL TPEQWRESKI KSIKASIAAD PSLATSRHVN
KSAFPMDGWT PLHAAAAKGN VEFVKVLLEV PGVSAWAVDL QGRTALALAA AEGHLDLCLL
LKARMEMESA DTIVGINAPV DLSGRTPLAW SVKAARQKRN KEVEEHLYAT GDASVCPATP
AALRSGGGRT GTKGAGGGGV GGTARTGAGR GAAESIGDGL PCGYSDAPGW RIEMEDAICR
HNPIPVNDPE SREAPPADPT SMFGIFDGHG GDFTSTFCAR ELIECLRGTS GWKSGDRALA
KLCPAVMEAF VNVDELLAKQ PRMVVTETKN PSDGRRFEAR DGSGSTAVVS FVTPAHVIVA
NAGDSRAILI MVPPDHNNSS SGKGKKSKGN SSSDSTKMTT TGGGGGGGGG GGSSSSSSSV
GVEDRKGAAE TMAEALGLKL GGERNSGVEE VKGEATTGGR PAAEGEWGGL NDSVRLEDQE
EDDDEGCEFD GADKIRELLE SMMLGGEAKE GGGGDDDGAR RDRDDDCGGA GGLMVTAMSR
DHTAADEAER ERVTAAGGKA FEVPYTEPDG TTCVVVRTAY DDKVEGQSVV PTRGFGDLYY
KQRKDDDGNL LPPAQQVVTS CPEIMVHERG SSGKEELLLL ACDGVWDVFD NQDAGEFLVK
TLDVPVGQVT GEQLALACDA LVKECLRRGS TDNITAMAVS LGSGPPPRPS SAGGRVLFSD
GQ
//
