ID Q2HHG9_CHAGB Unreviewed; 828 AA.
AC Q2HHG9;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=CHGG_00335 {ECO:0000313|EMBL:EAQ92100.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ92100.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(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}.
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DR EMBL; CH408029; EAQ92100.1; -; Genomic_DNA.
DR RefSeq; XP_001219556.1; XM_001219555.1.
DR AlphaFoldDB; Q2HHG9; -.
DR STRING; 306901.Q2HHG9; -.
DR GeneID; 4388255; -.
DR VEuPathDB; FungiDB:CHGG_00335; -.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_007683_0_2_1; -.
DR InParanoid; Q2HHG9; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000001056; 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; cd07521; HAD_FCP1-like; 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; 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; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 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:UP000001056}.
FT DOMAIN 158..348
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..587
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..646
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..696
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 90965 MW; 61C34B0B753E23DA CRC64;
MTKTVRLGSR LRYPITVVKL HKRPGDKIKK QETLMEYSFK WMKEVGDTIR GETWQQEQTT
IVTWDSPSDG ELTRWFIREG QHILSDRVAI EVKEECSHEI QFQGLCGMCG KDMTEVNWAT
ETRDTARAPI NMVHDQTNLT VSASHAQRTE QELQRRLLVS RKLSLVVDLD QTIIQACIDP
TVGDWQKDPT NPNHESVKSV KSFQLDDGPT QAANQCSYYI KMRPGLESFL KRIAQMYELH
VYTMGTRAYA QNVARVVDPD KKLFGNRVIS RDENGSIYAK DLQRLFPIST HMVAIIDDRS
DVWPNNRANL IKVSPKRNDA AAESGNKTAE VGDTTLSEWQ VEEQKRELEK QIKDRPLQAL
QEKLDREDEE AEKATVQSDD GSESRSSSPP SQRHHILQDD DDELEHLQKH LTALHRTFYA
EYDNDRNTVP DAGHILDEFK AKQGHNSPRR EHGPARQGEA TRGTTTARTS RSSAQGMAGR
LLHPVGGRRR GPLPFHRAPD GGGQSRAQSP SAAGEEEEEG DENDNNLPNA TTTTITTKTP
NGTTPTKLRL VAASGATRAL ALRTDVAEGG NVDGENDDED GDDEAGLLPS DLPDGATSPI
DAFKDVDWTT TDAELAEFLA SGSDDDDDDE DDDGDDEAEE SGDGGDGDGD VEVRDAPPVP
ASMASASVAV VRKRKGRDEE EEEEEDGENE NVGGDGDDAE VGEKGENGMP AKRLRRTESQ
RGSSLRNLYV ATGEGANDSP GSGLPTPGRS DGQDVDMEGA RNTAAGADAG AEEGGEEEEE
MEFDVAELEA EFEAEFEAEF DKAELEAQMA AEQAYGAEVA GEKDTAKG
//
