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Database: UniProt
Entry: D7KMX3_ARALL
LinkDB: D7KMX3_ARALL
Original site: D7KMX3_ARALL 
ID   D7KMX3_ARALL            Unreviewed;       210 AA.
AC   D7KMX3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=RNA polymerase II C-terminal domain phosphatase-like {ECO:0000256|RuleBase:RU366066};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU366066};
GN   ORFNames=ARALYDRAFT_473765 {ECO:0000313|EMBL:EFH67514.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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; GL348713; EFH67514.1; -; Genomic_DNA.
DR   RefSeq; XP_002891255.1; XM_002891209.1.
DR   AlphaFoldDB; D7KMX3; -.
DR   STRING; 81972.D7KMX3; -.
DR   EnsemblPlants; fgenesh2_kg.1__3719__AT1G43600.1; fgenesh2_kg.1__3719__AT1G43600.1; fgenesh2_kg.1__3719__AT1G43600.1.
DR   GeneID; 9330011; -.
DR   Gramene; fgenesh2_kg.1__3719__AT1G43600.1; fgenesh2_kg.1__3719__AT1G43600.1; fgenesh2_kg.1__3719__AT1G43600.1.
DR   KEGG; aly:9330011; -.
DR   eggNOG; KOG0323; Eukaryota.
DR   HOGENOM; CLU_023960_0_0_1; -.
DR   OrthoDB; 11699at2759; -.
DR   Proteomes; UP000008694; 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; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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:SF22; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE; 1.
DR   PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 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   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          1..184
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
SQ   SEQUENCE   210 AA;  24870 MW;  B042479657D52F83 CRC64;
     MKKKLHLVLD LDHTLIHTVL VSDLSEREKY LLEEADSRQD LWRCNKDSPY EFIIKLRPFV
     HEFLLEANKL FTMHVYTMGN SCYAQDVLKL IDPDKVYFGN RVITREASPC NKTLDLLVAD
     TRRVVIVDDT ISVWPHHKRN LLQITKYIYF RVDGTKWDSY AEEKKDESRK SGSLANVLKF
     LEDVHKRFEE DLDSKDLRLL IPYPCRQCCF
//
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