ID A0A1V4KLC8_PATFA Unreviewed; 364 AA.
AC A0A1V4KLC8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-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 Name=CTDSPL {ECO:0000313|EMBL:OPJ85238.1};
GN ORFNames=AV530_011695 {ECO:0000313|EMBL:OPJ85238.1};
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:OPJ85238.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ85238.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ85238.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ85238.1};
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 -!- 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 -!- 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:OPJ85238.1}.
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DR EMBL; LSYS01002888; OPJ85238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KLC8; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210:SF43; CTD SMALL PHOSPHATASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR Pfam; PF03031; NIF; 1.
DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000190648}.
FT DOMAIN 101..259
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT SITE 167
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
FT SITE 205
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
SQ SEQUENCE 364 AA; 41397 MW; EDD412509645CFF5 CRC64;
MDNPSIITQV TNPKEEEILS CTQDKVSQCN ISLKKQRSRS IFSTLFCCFR DYNVEPPSTN
STSALPPLVE ENGGLQKGDQ MQVMPIPSPP AKYLLPELTA SDYGKKCVVI DLDETLVHSS
FKPISNADFI VPVEIDGTIH QVYVLKRPHV DEFLQRMGEL FECVLFTASL AKYADPVADL
LDRWGVFRAR LFRESCVFHR GNYVKDLSRL GRELSKVIIV DNSPASYIFH PENAVPVQSW
FDDMTDTELL DLIPFFEGLS KEEEVYSMLH KLCNRYRLQT QRVTSRWPVH QASRTSRLLP
RVNPGHSSPS NMWSPTCDPW DGLQEVGGDD VQKAIDHAEK CVQHPEKCLI FIHQLNRGCE
LVDI
//
