ID A0A2G5CH86_AQUCA Unreviewed; 957 AA.
AC A0A2G5CH86;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, 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=AQUCO_05400016v1 {ECO:0000313|EMBL:PIA30628.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA30628.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA30628.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-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};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ305071; PIA30628.1; -; Genomic_DNA.
DR EMBL; KZ305071; PIA30631.1; -; Genomic_DNA.
DR STRING; 218851.A0A2G5CH86; -.
DR OrthoDB; 1200617at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR Gene3D; 3.30.160.20; -; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081:SF0; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1; 1.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..392
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 711..777
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 847..917
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 430..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 107710 MW; 75F5461249895B01 CRC64;
MLKSVVYQGN TLLGEVEIHT LNQHQHHHHN SFNNLFMSKE IRISHFSISS ERCSPLSVLH
TISPLGLSFK MESTTMTTMS QLGDSPLASL HSTCLRENKT AIMQLGEEEL HLVAMSSRKN
SQLYSYFWCF IVGMGLYDSC LIMLNLRCLG IVFDLDETLV VANTMRSFED RIDALQRKIS
TEMDPQRVEG MLAEMKRYHD DKSILKQYLE NDQIVDDGMA YKIQSEIVPA LSDNHPSIVR
PLIRLPEKNI ILTRINPAIR DTSVLVRLRP AWEDLRNYLT ARGRKRFEVY VCTMAEKDYA
LEMWRLLDPG LNLISSKELL NRIVCVKAGS RKSLLNVFHA SICHPKMALV IDDRLKVWEE
KDQPRVHVVP PFVPYYAPQA EVNNTIPVLC VARNVACNVR GGFYKEFDEN LLQRLSDVFY
EDDVPDIPSP DVGNYLISED DTSGSNKDPP RFEGISNAEV ERRLKETIPA QEVVNNLDAR
PAPLHHAGTT SSNTIPQPPS QGPSILFQDK QLSQLGSSVK LLSNLGPSQS SFQGSPGREE
GELPESDIDP DIRRRLLILQ HGQDKRDQMT KDPPYPVRPP VQASQSPVQS HGSWSPLAEE
MSTRQPNQTL PKNLHREFPS ESEANHFDKH QPSHTSYFHG VESSVTSDKT RFEYRKSSKE
ARRGENRFRL KHSLSNLRSV PGEESNLSPL VNSKKDSHIE RGQDSSLHAE TTLEVLQDIA
NKCRTKVEFR PALINSTELQ FSVEVWFAGE KIGEGNGRTR KEAQHQASEC SIKALANKYL
SSVSTDPTSG CENLNKLSQK DETDALGDST SFGHWPLLKE DPMAMSSTSE SSRFLDLKLE
GSKKSEDSVF VLKQLCFKEG LALMIKGQPT LSLNSEQKEE EQAQVEIEGN VLGTGTGSTW
EEAKLQAAEE ALGSLNSMIG TQKRQSSPKL SQALPSKRFN PDSSRVLQRL PSYTRYS
//
