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Database: UniProt
Entry: A0A0C9WSZ9_9AGAR
LinkDB: A0A0C9WSZ9_9AGAR
Original site: A0A0C9WSZ9_9AGAR 
ID   A0A0C9WSZ9_9AGAR        Unreviewed;       840 AA.
AC   A0A0C9WSZ9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase {ECO:0000256|ARBA:ARBA00040602, ECO:0000256|RuleBase:RU366066};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081, ECO:0000256|RuleBase:RU366066};
GN   ORFNames=K443DRAFT_6426 {ECO:0000313|EMBL:KIK02010.1};
OS   Laccaria amethystina LaAM-08-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK02010.1, ECO:0000313|Proteomes:UP000054477};
RN   [1] {ECO:0000313|EMBL:KIK02010.1, ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK02010.1,
RC   ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This promotes the activity of RNA polymerase II.
CC       {ECO:0000256|RuleBase:RU366066}.
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         ECO:0000256|RuleBase:RU366066};
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:RU366066};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU366066}.
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DR   EMBL; KN838598; KIK02010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9WSZ9; -.
DR   STRING; 1095629.A0A0C9WSZ9; -.
DR   HOGENOM; CLU_007683_0_1_1; -.
DR   OrthoDB; 73422at2759; -.
DR   Proteomes; UP000054477; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd17729; BRCT_CTDP1; 1.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR039189; Fcp1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR011947; FCP1_euk.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR02250; FCP1_euk; 1.
DR   PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR   PANTHER; PTHR23081:SF0; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   Pfam; PF12738; PTCB-BRCT; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366066};
KW   Nucleus {ECO:0000256|RuleBase:RU366066};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT   DOMAIN          154..378
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   DOMAIN          543..636
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          195..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..779
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..833
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   840 AA;  93311 MW;  7EA7477E69F1B695 CRC64;
     MESSPTDLYL PQSLPYPIKL TSIDATPNST IKRGTRLLSY SFIHLSNGTQ ETRFGTWDSA
     IEGDLQSWLV KVGDVITQNK ANDRPAVIVI EPCKHGIQLG GLCVLCGKDM TSVDYTGFSD
     SSRASIQMTH SAFGPTVSFE EAERIERETA DHLLRSRKLS LIVDLDQTIV HATVDPTVGE
     WITEGEAWEA RQAKKVEVAP HDSDDPDDGS SDDDECNPNW EALRDVKKFR LGPESFVPPS
     LRGAQQGKGK QKLVENEGCM YYIKPRPGWK EFLQEASTKY EMHVYTMGTR AYAEEVCAAI
     DPDGKIFGGR VLSRDESGSL TQKSLQRLFP CDTSMVVIID DRADVWEWSP NLLKVVPYDF
     FVGIGDINSA FLPKLEPLTA ASTSLPTSKP SETANGGSPS PVIVPEHTGA VDATVVGSTV
     PDEAESAKTA TTKALMTRNN AALEAQLEER PLAKKQEALR EHELHPDGPG VPAKKTPSPE
     PEKVPKKPLL KNDDGELDRV GKLLRYVHRR FFEAYDARSP ENSRRKTGPS SKAYDVTRII
     PRLRSEVLEG VHILFSSVIP LDTKPETTEI WRMAHMFGAR CSTELTGDIT HVVAAKRGTV
     KVDMARKRGG IKIVWLAWFT DCIAFWQRRD EKPYLLDDLP AVPIPSSSSP IHADHQISSD
     PDPDEDDWDE EPFEGILKDT GSLQLSAINW SDINDEVEAA MNESDDEDDN DDMKSVRSED
     EWMEVATSSA NNSPRLNRKR LRSVTPSDGG SQNGAGRVQD DDLRSPLSKR KKLAADRSGY
     SRLKEAISAD ELAFGSEGEP SRASPKMVMK NEMEEDEEDD EYEEEEEDDF LARALEEEWG
//
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