ID A0A2T4B970_9HYPO Unreviewed; 771 AA.
AC A0A2T4B970;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase {ECO:0000256|RuleBase:RU366066};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366066};
GN ORFNames=BBK36DRAFT_1141703 {ECO:0000313|EMBL:PTB65761.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB65761.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) 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; KZ680214; PTB65761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4B970; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000241546; 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; 2.40.50.100; -; 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:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 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 Reference proteome {ECO:0000313|Proteomes:UP000241546}.
FT DOMAIN 154..333
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 491..586
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 327..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..674
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 85947 MW; 672C1D12A52A24A8 CRC64;
MYDKVVSLGS RLHYPIVITK LLKKPGEPIK KQETIIEYKF HWRRKIGDDE WVDETTYTEF
DSPAEGTLKE WRIEEGQTIA ADMPCMTVEE ACGHEVQIQG LCSLCGADMT EINWASEEKD
TDRAMINMVH DQTGLMVSQN VAKRAEHDTQ KRLLRQRKLS LVVDLDQTII HACIEPTIGE
WQRDPTNPNH EAVKDVKSFQ LNDDGPRGLA SGCTYYIKLR PGLKEFLEAV STKYELHVYT
MGTRAYALNI ARIVDPDKKL FGNRVISRDE NGSITAKSLQ RLFPVSTDMV VIIDDRADVW
PMNRPNLIKV APYDFFKGIG DINSSFLPKR QDILPSPTKP NGLMPNPENA VPGEKVSPLD
ELARMGGGDE ASLKVQTQEQ EKTLEKQLTD RPLLHMQEEL DKEDSEADGS STLHHRAHLL
NDDDEELVTL QDHLTDLHAA FYDMYDRRRA ERKMSEGTHP PGHMKARRKS QPDDGVDLSL
VPDVGDILDE LKSSVLSGLV ICLSGLVPLG VNIEESEIGM QAQSFGAQVV DTISPRVTHL
VVSLARPRTK KVQQAAKIPS IKIVNQSWLA DCLSQWRRLD ESPYYMPILD ADRERSEDDT
AETSAAEMED AGISSMNMGD FDEELKEFLG LDDDDDDDDD NDTENDDGND EGDEEADEDE
DGENDSETTD GEGDDSDDPE KRGTKRKDRE STMESEEDAS NPVGESALAK KQRVSRNRGA
SSLRAVQTPN GEAAGPSSDA APPPPSTEVD SLAEFDELER ELLLGLEAAG S
//
