ID A0A0A8L329_9SACH Unreviewed; 730 AA.
AC A0A0A8L329;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=KLDO_g1760 {ECO:0000313|EMBL:CDO93463.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO93463.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO93463.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) 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}.
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:CDO93463.1}.
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DR EMBL; CCBQ010000025; CDO93463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8L329; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000031516; 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 Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366066};
KW Nucleus {ECO:0000256|RuleBase:RU366066}.
FT DOMAIN 153..340
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 492..586
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 387..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 350..381
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 392..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..674
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..720
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 83365 MW; F0C159445CAF9C58 CRC64;
MSLESIVKLT NDLPYPITVA QLYVKVGDHI EKGQRLFAYE YWDFQDVLVK DEEKAKKQRV
DRVATFDSPV SGTVHSWHCA VKEEFASANH DVITIKQDCN HDITYGGLCV QCGNTVDEED
DGKNLTISHV NTNIKVSEKQ AETLERSSLT RLRQEKKLVL VVDLDQTVIH CGVDPTIGDW
MKDPKNPNYK ALQDVRSFTL EDEPIVPSFY FGPRPPTRKS WYYVKLRPGL KEFFEAVSPH
FEMHIYTMAT RSYALEIAKI IDPTGELFGD RILSRDENGS LTTKSLERLF PMDQSMVVII
DDRGDVWNWV ENLIKVVPYS FFVGIGDINS NFLPRQQNSV LHLGRHHRKK QEEERLISDI
IDNEKKLKEK IDEEVKRQEE IISHIGDENG RKDSSVNTGV NVGVSSGASG AAPNKEDISK
KLEHSASLEV QQQNRPLAEL QKHLHNQTLL IDEDDELPHL SKILLRVHRA YFKEFAKSSL
TPPDIKYLLP KIKSRVFQGC HLVFSGLIPL ETDIRKADIV LWTEMFGSSS TSNIDYETTH
VITRTSRTFK ARLAKSFNPH IKIVHPDWLF ECLVQWERVS ESPYELLIED PVDDETLKEF
KEALDNKQVN GFSSGDENGD ASDSPDYQDE EEVLGDEFHL LAGNDSWLDN DEDEMDELLN
DAGEEEEEDE DEGEDLPSAK RHKTDAGLKE DVPTASGHEP EHGEDQYEDD EDDEDDEDDL
EAELLLELEN
//
