ID A0A1V4KE80_PATFA Unreviewed; 945 AA.
AC A0A1V4KE80;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|EMBL:OPJ82790.1};
GN ORFNames=AV530_008549 {ECO:0000313|EMBL:OPJ82790.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ82790.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ82790.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ82790.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ82790.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OPJ82790.1}.
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DR EMBL; LSYS01003422; OPJ82790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KE80; -.
DR STRING; 372326.A0A1V4KE80; -.
DR Proteomes; UP000190648; 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; 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 Pfam; PF12738; PTCB-BRCT; 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:UP000190648}.
FT DOMAIN 132..298
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 599..698
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 105534 MW; 8E4FC3EE3565FE02 CRC64;
MEGPAERGGA EGPAGTITEI RAPGPRPLRL LEWKRKLKAE RPGVVRELCA RPGQVIAPGG
VLVRLEGCSH PVVMKGLCAE CGQDLTQIQS KNGKQNVPLS TATVSMVHSV PELKVSSEQA
EQLGREDQQR LHRNRKLVLM VDLDQTLIHT TEQHCQQMSN KGIFHFQLGR GEPMLHTRLR
PHCKEFLEKI AKLYELHVFT FGSRLYAHTI AGFLDPEKKL FSHRILSRDE CIDPFSKTGN
LRDLFPCGDS MVCIIDDRED VWKFAPNLIT VKKYVYFQGI GDINAPPGSR EIQMKKKVNH
STKTEALDSA VPSAKGAEEI KNVTCVEEQS NGLKKAEKDT CTANGSTPVS SETSDWDMNS
RDKVSAQDSL NDSTDQKMDS GISNDLTNTK ESQIFSEQVD RTVIEKQETQ GKTTNDLDFE
LSSDSESDGG LDIRKSSPSV SDSENEEKRS WKKSEQPLED ESLHKGSCTD ESEKKDGLVN
HSGDAQSLPN ENISEKTDLE AQEESEQESL CDSGNGCADK KEAETESQIS EQSGITMGES
LDQSMEEEDE EDDTDDDDHL IYLEEILVRV HTDYYTKYDK YLKKEIEEIP DIRKIVPELK
SKVLADVTII FSGLYPTNFP IEKTREHYHA TALGAKIVKN LVLSADDPDK ATHLIAARTG
TEKVRQAQDC KDLHVVNPDW LWSCLERWDK VEEQLFPLKD DYIKTHRENS PAMFPDTHST
FQTALFHPTP IHPKSQPAPE VRLYDPNTGK LIRKGAQTSG QSMYIQSPAP PITLPVHGEH
SSFRVVQPHQ QQMFEEDNLP ASENEEQPGP SKRKRQPSMS ETMPLYTLCK EDLESMDKEV
DDILGEGSDE SDSEKKKPKE KGEKPQMSAT ETLGMKTDQR PGSSSSSSSE RSLTGSVPRG
HKRKLDEDDA ASESSKESSN EDEEGSSSEA DEMAAALEAE LNDFM
//
