ID A0A0G2HWD1_9EURO Unreviewed; 917 AA.
AC A0A0G2HWD1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=EMCG_02953 {ECO:0000313|EMBL:KKZ62547.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ62547.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ62547.1}.
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DR EMBL; LCZI01001061; KKZ62547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HWD1; -.
DR VEuPathDB; FungiDB:EMCG_02953; -.
DR Proteomes; UP000034164; 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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366066};
KW Nucleus {ECO:0000256|RuleBase:RU366066}.
FT DOMAIN 155..334
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 519..612
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 430..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..859
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..887
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 101431 MW; CE58416B5D987BE4 CRC64;
MLLKLSASLH YPITVTELLK RPGDTVQQGE AIFAYHYRTT VTEGDGLGNK HDVLKTFPTR
FESAVDGELV AWRVREGAVI AGPIDVVEID EPCSHEVQFG GMCANCGKDM TEFNYNTEVL
DSSRAPIRMV HDNTSLTVSE NEATRVEEDA KRRLLSSRRL SLVVDLDQTI IHATVDPTVA
EWQQDKDNPN HEAVKDVRAF QLVDDGPGMK GCWYYIKLRP GLEEFLREIS TLYELHIYTM
GTRAYAQHIA NIVDPDRKIF GDRILSRDES GSLTAKSLQR LFPVDTKMVV IIDDRGDVWK
WTDNLIKVSP YDFFVGIGDI NSSFLPKKQE FKALPGGAAK STKELDSREV EAARATINGS
GAMDVDGKTT TEISALEQLV TMGGGDNPVL LQEQANEQEE AIAHQVEERP LLQKQKQLDA
EDDAAELMAA GENGDSSSDD SHDSSRHRHH LLEDNDSELY KLQERLKAVH KAFFDEYDRR
RTSSLGGRVS ALRGERVASR DKGIDLRIVP DIKLIMPQIK RPVLESVVLV FSGVLPLGTD
TQNADISLWA KSFGAAISQK ISSRTTHLVA GRNRTAKVRE ATRYPKIKIV TVQWLLDSIT
QWKRLDEEPY LVPVHPEDRG EPIGSSINAS PGGSAKASNG SLDDYSFLSS SEEDDNITDD
NNTETDDSDA SKLRVRTHDL LDIDEEILQS AGLTDHSPIG YDAEQQAAVH DELKAFLGSD
NEDSESDSEF SLRSFSGTQQ QGTPSGRKRK RGTESDESGG ESSTGEEDRV EKTAPLIGSD
RAVSGPTAGS SGSRLAQKIK LSHERNTGLK HVATIRSRGS SEAPVPVPAP VYEHVPVPNP
PPNVEEEEEE DDDDESDTTE YNNNNYNNNS NNDDVDPEDD EDALEREMLA AFEDGGWEED
GGREEEGVGV REEMDPE
//
