ID A0A3Q1HYW0_ANATE Unreviewed; 318 AA.
AC A0A3Q1HYW0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000012990.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000012990.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 AlphaFoldDB; A0A3Q1HYW0; -.
DR STRING; 64144.ENSATEP00000012990; -.
DR Ensembl; ENSATET00000013206.2; ENSATEP00000012990.1; ENSATEG00000009067.2.
DR GeneTree; ENSGT00390000010107; -.
DR InParanoid; A0A3Q1HYW0; -.
DR OMA; DSNAMIS; -.
DR OrthoDB; 49886at2759; -.
DR Proteomes; UP000265040; Unplaced.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000265040}.
FT DOMAIN 3..81
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 133..294
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT COILED 101..128
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 318 AA; 36873 MW; 9CF9C1985A6D2ACE CRC64;
MSVSVIIKWG GQEYSISSLS EEDTVMDLKQ SIKTLTGVLP ERQKLLGLKV KGKPAEDEVK
LGVLKLKPNT KIMMMGTREE SLEEVLSSPP ENDDVVNDFD IEEEVIEVEN REENLAKIAR
RVKDYKVEEL NPPREGKRLL VLDVDYTLFD HKSCAETGQE LMRPYLHEFL TSAYEDYDIV
IWSATSMKWI DAKMKELGIT DNPNYKITFM LDSAAMITVH TPKRGVVEVK PLGVIWGKYG
TFYNRKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNREK DRELYKLAQY LKEIAKTDDF
SGLNHKHWER YLSKKQHH
//
