ID V8NEE9_OPHHA Unreviewed; 339 AA.
AC V8NEE9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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};
DE Flags: Fragment;
GN Name=UBLCP1 {ECO:0000313|EMBL:ETE59942.1};
GN ORFNames=L345_14324 {ECO:0000313|EMBL:ETE59942.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE59942.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE59942.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE59942.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:ETE59942.1}.
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DR EMBL; AZIM01005095; ETE59942.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NEE9; -.
DR Proteomes; UP000018936; 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 4: Predicted;
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:UP000018936}.
FT DOMAIN 24..102
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 154..315
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE59942.1"
SQ SEQUENCE 339 AA; 39403 MW; 183B0AE266AD788E CRC64;
MLPWRRDRLQ PRQRRPGMVP NMAVSLIIKW GGQEFLITTL SEEDTVLDLK QSLKGLTGVL
PERQKLLGLK VKGKPAENDV KLGSLKLKPN TKIMMMGTRE ESLEDVLGPP PDNEDVVNDF
DIEEEVVEVE NREENLLKIS RRVKEYKIEI LNPPREGKKL LVLDVDYTLF DHRSCAETGI
ELMRPYLHEF LTSAYEDYDI VIWSATNMKW IEAKMKELGV STNANYKITF MLDSAAMITV
HTPRRGLIDV KPLGVIWGKF SEFYSKKNTI MFDDIGRNFL MNPQNGLKIK PFMKAHLNRD
KDKELLKLTQ YLKEIAKLDD FLELNHKHWE RYLSKKQGQ
//
