ID K9FT68_PEND2 Unreviewed; 817 AA.
AC K9FT68;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase {ECO:0000256|ARBA:ARBA00040602, ECO:0000256|RuleBase:RU366066};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081, ECO:0000256|RuleBase:RU366066};
GN ORFNames=PDIG_81250 {ECO:0000313|EMBL:EKV05928.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV05928.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV05928.1}.
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DR EMBL; AKCT01000296; EKV05928.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FT68; -.
DR STRING; 1170229.K9FT68; -.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_007683_0_2_1; -.
DR InParanoid; K9FT68; -.
DR OMA; DQTVIHC; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000009882; 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:SF0; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882}.
FT DOMAIN 155..331
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 503..596
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 410..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 91798 MW; 2F56AD963B2A7B68 CRC64;
MLLRLPTSLH YPITVTSLLK KPGDTVEKDE ALFWYVYQTT VTEGDGLGNT VEVKRRYPTR
FESTVDGEVV KWQIQKGDII DEPVNVVEID EPCAHEIQFG GLCAECGKDM TESTYNTEII
DSMRAPISMA HDNVTLTVSE REATRVEEDA KRRLLASRRL TLVVDLDQTI IHATVDPTVG
EWREDKQNPN HEAVKDVRQF QLIDDGPGMR GCWYYIKLRP GLEEFLQNVA EIYELHIYTM
GTRAYAQHIV DIIDPTRKLF GDRILSRDES GSLTVKDLQR LFPVDTKMVV IIDDRGDIWR
WSPNLIKVSP YDFFVGIGDI NSSFLPKKED IGANKSQIEA KTSENNQEHH VNGKSQEGAE
ISALEQLVTM GGGDSPRLLQ EQTDAQEETI MHQVEDRPLL QKQKELEAED NIAETSDASS
SVEEAQEPAK HRHHLLEDHD QELYQLQNRL EQVHLQFYDE YDKRRTLALG GRVAALRGEK
VHSRDKDVDL KLVPDVKDIM PQIKRRILGG VVLVFSGVLP LGIDFQNADI SLWAKSFGVT
ISSRINTRTT HLVAGRNRTA KVREATRYPN IKIVTTQWLV DALVQWRHVD EEPYLLPLHP
DDRGDPLTPS ELELETSMLS STDEDITGSQ WTQEDDAEDI FKSSGLNETS PIGYDADEQA
AVHDELKDFL GSDDESESDN ESLLDEPSTG GKKRKRNEET ESGTDEEESG DDDGDDHDNP
GSRLSQRIKR SYERNTKLRE ITSIIASSSD QVSPDLPKTP VVEGVSDSET AGTGSALRAD
YPDPDDDDDE LEREMLAAFE GGGYDSQAEA DAAAENG
//