ID A0A2Y9KCY4_ENHLU Unreviewed; 865 AA.
AC A0A2Y9KCY4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=LOC111154232 {ECO:0000313|RefSeq:XP_022369419.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022369419.1};
RN [1] {ECO:0000313|RefSeq:XP_022369419.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022369419.1};
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_022369419.1; XM_022513711.1.
DR AlphaFoldDB; A0A2Y9KCY4; -.
DR Proteomes; UP000248482; 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 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; 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:UP000248482}.
FT DOMAIN 202..365
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 632..731
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..591
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 94135 MW; 1245FD1F4F6E8CE9 CRC64;
MRLLSGGWAC SGKVPQSQPG GESQLDRGPS QARLLALTPA AQKLVAQGGR SAGCPVEVDG
NRRARGPRRG FSWNEDPQRR AGRSLEQEDI FERRHADGKV SGEWCGLLQG RLAGTPGRQA
ESGGGVSVGS VLVRLEGCSH PVVMKGLCAE CGQDLTQLQS KNGGQQVPLS TATVSMVHSV
PELMVSSEQA AKLAKEDQER LHRNRKLVLM VDLDQTLIHT TEQHCQQMSN KGIFHFQLGR
GEPMLHTRVR PHCREFLEKI ARLYELHVFT FGSRLYAHTI AGFLDPEKKL FSHRILSRDE
CIDPFSKTGN LRNLFPCGDS MVCIIDDRED VWKFAPNLIT VKKYVYFQGI GDINAPSGSR
ESQARRKVTP SPRGADVPEQ ALSVRETEES RPGSGVEQSN GLGKPTRELN GSASARGDWP
LPGQEEERGS RPTARGPVAD GRGPLVCAQQ PDRTLPEKRA AQGTAGGDLD FDLSSDSESD
AQSLSDGESG EKRSLERPQG AQGAGKVVQR GGPPGPGGER PCGEPAPGLH PDMQEEGERD
GLCGLGGGSA DRKEAETESQ NSEQSGVTAG ESLDQSVEED DEDEDDGDGD DHLVHLEDIL
ARVHSDYYAR YDRHLLGDSP EAPDIRKIVP ELKSRVLADV AIIFSGLHPT NFPIEKTREH
YHATALGAKV LTQLALDPGS PNRATHLIAA RAGTEKVRQA QECGQLHVVN PDWLWSCLER
WDRVEEQLFP LRDDYGRVQR EDGPAAFPDR QGALPAALFQ PTPVHPRAQA GPEVRIYDAN
TGKLIRKGAA GPGPPGSLAV HAEHSSFRVV QPPRQTLAQE LPDRRPGEQP GPSGRKRQPS
MSETMPLYTL CKEDLESMDK EGPQA
//
