ID A0A1S3ALT0_ERIEU Unreviewed; 781 AA.
AC A0A1S3ALT0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 Name=CTDP1 {ECO:0000313|RefSeq:XP_007537160.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007537160.1};
RN [1] {ECO:0000313|RefSeq:XP_007537160.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_007537160.1; XM_007537098.2.
DR AlphaFoldDB; A0A1S3ALT0; -.
DR CTD; 9150; -.
DR eggNOG; KOG0323; Eukaryota.
DR InParanoid; A0A1S3ALT0; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; IPR015388; FCP1_C.
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; PF09309; FCP1_C; 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:UP000079721}.
FT DOMAIN 59..224
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 456..555
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 230..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 85646 MW; A237764847E835B6 CRC64;
MKGLCAECGQ DLTQLQSQSG KQQMPLSTAT VSMVHSVPEL MVSSEQAEKL GREDQQRLHR
NRKLVLMVDL DQTLIHTTEQ HCPQMSNKGI FHFQLGRGEP MLHTRLRPHC KDFLEKVARL
YELHVFTFGS RLYAHTIAGF LDPEKKLFSH RILSRDECID PFSKTGNLRN LFPCGDSMVC
IIDDREDVWK FAPNLITVKK YVYFQGIGDI NAPPGARDPA AKKRAVVNHS PKGADAMEHT
PAARDPGDGK HVCRAERSNG LSKPVRDWPG DAPAEDRGAQ PGCSPPAGRT LAEKRGVQGP
AGSDLQFDLS SDSEGGSESE ERSSSEGEAG DRRGQRRPCA RDLGRAERPG SNHCGEPDGP
EETERDGLCG LGGGCADRKE AETESQNSEQ SGVTAGESLD QSVEEEDEED CDGDDHLVHL
EAILARVHAA YYAQYDRFLR GELPEAPDIR RIVPELRGRV LSGVAVLFSG LHPTNFPVEK
TREHYHARAL GARVLTKLAP DPEDPDRPTH LVAARAGTEK VRQAQESGAL HVVNPDWLWS
CLERWDHVEE QLFPLRDDYG RLQREDSLMA FPDRQGPLPT ALFHPVPVQP RPQPGPEVRV
YDATTGKLIR KGAAGPGDHS SFRAARPQQQ MLGDEVPESA DGARPGPSRR KRQPSLSETM
PLYSLCKEDL ESMDREVDDI LGEGSDDSDS EKRRPEEPEG EPVGAAPPRE PLATEPPQGD
PDLAATPSGK SPAEGRGSRS HKRKLPEEDA GSGDSSVEDE GSSSEADEMA AALEAELGEF
L
//
