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Database: UniProt
Entry: R4G5I7_RHOPR
LinkDB: R4G5I7_RHOPR
Original site: R4G5I7_RHOPR 
ID   R4G5I7_RHOPR            Unreviewed;       350 AA.
AC   R4G5I7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Ubiquitin-like domain-containing CTD phosphatase 1 {ECO:0000256|ARBA:ARBA00014187};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE   AltName: Full=Nuclear proteasome inhibitor UBLCP1 {ECO:0000256|ARBA:ARBA00032039};
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249 {ECO:0000313|EMBL:JAA76985.1};
RN   [1] {ECO:0000313|EMBL:JAA76985.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ribeiro J.M.C., Genta F.A., Sorgine M.H.F., Paiva-Silva G.O.,
RA   Majerowicz D., Medeiros M., Koerich L., Terra W.R., Ferreira C.,
RA   Pimentel A.C., Bisch P.M., Diniz M.M.P., Nascimento R., Salmon D.,
RA   Silber A.M., Alves M., Oliveira M.F., Gondim K.C., Silva Neto M.A.C.,
RA   Atella G.C., Araujo H., Dias F.S., Polycarpo C.R., Fampa P., Melo A.C.,
RA   Tanaka A.S., Balczun C., Oliveira J.H.M., Goncalves R., Lazoski C.,
RA   Pereira M.A., Rivera-Pomar R., Diambra L., Schaub G.A., Garcia E.S.,
RA   Azambuja P., Braz G.R.C., Oliveira P.L.;
RT   "An insight into the transcriptome of the digestive tract of the blood
RT   sucking bug, Rhodnius prolixus.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000015103}
RP   NUCLEOTIDE SEQUENCE.
RA   Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:RPRC005527-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2015) to UniProtKB.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; ACPB03007651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GAHY01000525; JAA76985.1; -; mRNA.
DR   AlphaFoldDB; R4G5I7; -.
DR   STRING; 13249.R4G5I7; -.
DR   EnsemblMetazoa; RPRC005527-RA; RPRC005527-PA; RPRC005527.
DR   VEuPathDB; VectorBase:RPRC005527; -.
DR   eggNOG; KOG1605; Eukaryota.
DR   eggNOG; KOG1872; Eukaryota.
DR   HOGENOM; CLU_046931_1_0_1; -.
DR   InParanoid; R4G5I7; -.
DR   OMA; DSNAMIS; -.
DR   OrthoDB; 49886at2759; -.
DR   Proteomes; UP000015103; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd01813; Ubl_UBLCP1; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR011943; HAD-SF_hydro_IIID.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   NCBIfam; TIGR02245; HAD_IIID1; 1.
DR   PANTHER; PTHR48405; UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; 1.
DR   PANTHER; PTHR48405:SF1; UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; 1.
DR   Pfam; PF03031; NIF; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015103}.
FT   DOMAIN          5..83
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          136..297
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   REGION          321..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   350 AA;  40431 MW;  39DBCA83FF589FC7 CRC64;
     MENEVKLIVK WNCKEYEIDA LSDNDSVGTL KDVIFKKTGV RPERQKLLNL KFKGKLPDND
     CLLAALNLKS GFKVMMMGSL EEAIADANTI PDDLPEVIDD FDIEDGEEVA IENRDVYLAK
     IDRRIKEYTI KILNPPRPGK KLLVLDIDYT LFDHKSVAEK GYELMRPYLH EFLTSAYKDF
     DIAIWSATSM RWIEEKMKLL GVSSHANYKI VFYLDYLAMI SVHTPKYGVI QVKPLGVIWG
     KFPNEYRQSN TIMFDDIRRN FIMNPQNGLR IRPFRQAHLN RATDRELLRL TRYLDAIAPL
     EDLTQLNHRH WERYVSNRRK ELRRQRRSGG TGGGTAGGDV ESSSQDNSSP
//
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