ID A0A3M0KSK5_HIRRU Unreviewed; 1003 AA.
AC A0A3M0KSK5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=DUI87_08497 {ECO:0000313|EMBL:RMC16282.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC16282.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC16282.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC16282.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC16282.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RMC16282.1}.
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DR EMBL; QRBI01000104; RMC16282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0KSK5; -.
DR STRING; 333673.A0A3M0KSK5; -.
DR Proteomes; UP000269221; 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:InterPro.
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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221}.
FT DOMAIN 148..313
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 613..712
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 111814 MW; 8961E359E497ABE3 CRC64;
MEERPERGGG PGAEGPASVA EIRAPGPRPL RLLEWKVSVG AAVQIGYRAF LKTTAKRSCG
PCTHVLQLAS PLRCRTVLVR LEGCSHPVVM KGLCAECGQD LTQIRNKNGK QSVPLSTATV
SMVHSVPELK VSSEQAEQLG REDQQRLHRN RKLVLMVDLD QTLIHTTEQH CQQMSNKGIF
HFQLGRGEPM LHTRLRPHCK EFLEKIAKLY ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR
ILSRDECIDP FSKTGNLRDL FPCGDSMVCI IDDREDVWKF APNLITVKKY VYFQGIGDIN
APPGSREMQI KKKANLSTKP EALDSTVISA KDVEEIKNVT CVEEHSNGLK KPAKDTCTPN
GNTSVSSGTS DGDMNSHDKV NAQDPLNDST GHKMDSEVTD DLANTKEPQI FSQEVDTTVT
EKQQTQEKTT NDLDFELSSD SESDDGLDTK KSSTSVSDSE NEEKRSWKKS KQPLQDENLQ
QESCTDVSEK KDGLVNHSED TQSSENIQDK IDLEAQEECE QESLCDLGNG SGDKKEAETE
SQISEQSGIT MGESLDQSME EEEEEDDTDD DDHLIYLEEI LVRVHTDYYT KYDKYLKKEI
EEIPDIRKIV PELKSKVLAD VTIIFSGLYP TNFPIEKTRE HYHATALGAK IVKNLVLSAD
DPNKATHLIA ARTGTEKVRQ AQDCKDLHVV NPDWLWSCLE RWDKVEEQLF PLKDDYIKTH
RENSPATFPD TPSTFQTALF HPTPIHLKSQ PGPEVRIYDP NTGKLIRKGT QTSCQSMYIQ
SPAPPITLPV HGEHLSFRVV QPHQQQMFEE DDLPASENEE QPGPSKRKRQ PSMSETMPLY
TLCKEDLESM DKEVLMLRLF GLGVCGPRRG KTSPGGTLLQ CKPVQAQLLC LYPKPLLVDD
ILGEGSDESD TEKKKAEAEG EKPQTGATET LGSKADQRPA SSSSSSSERS LTGSVPRGHK
RKLDEDDAAS ESSKESSNED EEGSSSEADE MAAALEAELN DFM
//
