ID A0A1A5ZYG0_9TREE Unreviewed; 977 AA.
AC A0A1A5ZYG0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=I303_06401 {ECO:0000313|EMBL:OBR82844.1};
OS Kwoniella dejecticola CBS 10117.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR82844.1, ECO:0000313|Proteomes:UP000078595};
RN [1] {ECO:0000313|EMBL:OBR82844.1, ECO:0000313|Proteomes:UP000078595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR82844.1,
RC ECO:0000313|Proteomes:UP000078595};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL Submitted (JUL-2013) 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; KI894034; OBR82844.1; -; Genomic_DNA.
DR RefSeq; XP_018260686.1; XM_018409683.1.
DR AlphaFoldDB; A0A1A5ZYG0; -.
DR STRING; 1296121.A0A1A5ZYG0; -.
DR GeneID; 28970100; -.
DR VEuPathDB; FungiDB:I303_06401; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000078595; 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:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 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:UP000078595}.
FT DOMAIN 186..444
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 598..691
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 51..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..977
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 106777 MW; 3FC5616AF62892C4 CRC64;
MSDPPTPLTL PPTLPYPITI TRLLVRTGDS VERGSHLLEY SFMSKEQRAA LSKRETEGRK
ANISKGEVEG DDGSGTWDCL ITGEVAGWES WVQVGTKLER RHANQTLINV VQPCSHPVRL
HGMCGICGAD LTEDDYLSAP APVNSSEQAG PSRHPGGFEV THDAMGVTVS KNEAHRLDNL
TRDNLLSSRK LSLIVDLDQT IIHTTVDPTV AEWMDEIDAY NRQESSSPSR SSSIDQPEYP
GRSTGPSEQP NGADEKESTT PPTSPPLVTK TLPPESSPSP TRLEKNPNSE ALSDVARFQI
ADDLPPGYVK PRRKPGESIV QMQGRWYFTK PRPGLQKFLD EMSEIYEMHV YTMGTRSYAD
AICKVIDPDG KIFGGRILSR DESGSFSSKN LKRLFPTDTS MVVVIDDRSD VWADCPNLVK
VVPYDFFIGI GDINSSFLPK NKSTPPPSAT ATASTPTSPS LSASDASTPP PATPEDLPSV
EDGLLMKAKL LDDLSESRPL AKMQEELEQV EGDGREVRVQ NDSPTVANTT APVPSTPSTP
PRPRKPLLNP NDYELLRVSD ILREIHHRFY RAFDSLDDWD TGSSLPMSCD VEFIIPELKS
RVLDGCNLVF SGLIPQAANP ETTEIWQTAE TFGALCSLSV HPRITHCVTA TLNTEKTYRT
SRIPGAQIVW ANWFWDSVAL WHRQDESKYL AKKEGRSRTT TPPLAPPPLP SQSGITDGTN
GSSSSSGEQQ GESLKPSENP DDLPTTTTRN GEEEDDHENM DDDAEVGKGW DEGADAEWEA
FLAEEDDVDL ATENGSVKSV DSAPSTPSKK RVRYADEESL PLEDFKDPSP LELDGPMERF
SPDDQPAKRR KPLLLQAPSE SDRNQIPAEN RFQYNDNKHK DKTLHPNTST STSTESSQVE
DQPPTNSAAG TGAGTDADAG DDAGHSGKDA DEHSIAGTEG TEATEGTEED EFAMMLMDSL
ANEDGEGEED EGDHALD
//
