ID V6U4C8_GIAIN Unreviewed; 614 AA.
AC V6U4C8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=GSB_150939 {ECO:0000313|EMBL:ESU45487.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU45487.1, ECO:0000313|Proteomes:UP000018040};
RN [1] {ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GS {ECO:0000313|Proteomes:UP000018040};
RA Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA Nash T.;
RT "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT Pig).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESU45487.1, ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS {ECO:0000313|EMBL:ESU45487.1,
RC ECO:0000313|Proteomes:UP000018040};
RX PubMed=24307482; DOI=10.1093/gbe/evt197;
RA Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA Nash T.E.;
RT "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT Pig).";
RL Genome Biol. Evol. 5:2498-2511(2013).
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:ESU45487.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHHH01000005; ESU45487.1; -; Genomic_DNA.
DR AlphaFoldDB; V6U4C8; -.
DR EnsemblProtists; ESU45487; ESU45487; GSB_150939.
DR VEuPathDB; GiardiaDB:DHA2_150794; -.
DR VEuPathDB; GiardiaDB:GL50581_4453; -.
DR VEuPathDB; GiardiaDB:GL50803_0010190; -.
DR VEuPathDB; GiardiaDB:QR46_0328; -.
DR Proteomes; UP000018040; 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 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; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
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 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}.
FT DOMAIN 56..315
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 433..493
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 573..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 69724 MW; A78E168F61953E0A CRC64;
MFARSCGHDL VAMQSLACTR CGQKLPHAEV VIHYQYRDGK FVKRANCLQQ YKDAVVKSKK
LILFLDIDNT ILYAWSNPKG QTPPNIQRIS STSLASHHAF RMSRDIISKR TSYASRSEYR
EAYLEAYLAE AEDFFCGSPE RGLEPTAVEV QELRMTIMFR PGIFRFFLQT YKTVAIIIST
LGTQEYAQQM IRIIDPQRML VYELLDRKLA DRHGDSNTEV AHDDDSGAII SFEGEHSNLV
SQNFSDLDNH IMKGVNRFLG GISLLIDNSI AIDNSSAPWR GTKCGFLKSF DFYVANSWDS
SNYMWQQQVY PVESLTKVIR GYCKNDFTFL VHRSNPAYKH RFYNFSIAQL LSFENILHHI
QSSMHCTEPE LVNRLQCQSA REAVEEIMGQ VLKGCLIYIP FLPNAADLVT EGPYIVAAQW
KHTVGTLLDF RVELIRLLGG RVAVTFNKEV THVLVSESGS SWKKSYAKCA HLLLQCKPAE
VSPERVKAVL GDWTHLQVCG GSVTDQEISE LFVVPDAFTC YEPGIVEKGC TSVFPFHAVT
QNWLMTSALL YRRQNELFYT HYFLAQGLLP SKEKPDQPPV GEVDNKKDGH IRDTDCHEEG
RLIGQCADES HSYP
//
