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Database: UniProt
Entry: K9FT68_PEND2
LinkDB: K9FT68_PEND2
Original site: K9FT68_PEND2 
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
//
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