ID A0A1S3IRH9_LINUN Unreviewed; 319 AA.
AC A0A1S3IRH9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN Name=LOC106166686 {ECO:0000313|RefSeq:XP_013400820.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013400820.1};
RN [1] {ECO:0000313|RefSeq:XP_013400820.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013400820.1};
RG RefSeq;
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 RefSeq; XP_013400820.1; XM_013545366.2.
DR AlphaFoldDB; A0A1S3IRH9; -.
DR STRING; 7574.A0A1S3IRH9; -.
DR EnsemblMetazoa; g57.t1; g57.t1; g57.
DR EnsemblMetazoa; XM_013545366.2; XP_013400820.1; LOC106166686.
DR GeneID; 106166686; -.
DR KEGG; lak:106166686; -.
DR InParanoid; A0A1S3IRH9; -.
DR OMA; DSNAMIS; -.
DR OrthoDB; 49886at2759; -.
DR Proteomes; UP000085678; 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 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:UP000085678}.
FT DOMAIN 4..82
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 135..295
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
SQ SEQUENCE 319 AA; 36937 MW; 38EEEA3ED42963CC CRC64;
MTAKELTVKW SGQEYKITDL DDSDTVADLK NAISKATGVL PERQKLLGLK YKGSVPGDDV
QLSSLKLKPN TKIMMMGTRE ESLVDVLEPP EDIPNVVNDF DVGEEEEIEV KDREEYLNKV
EKRIKSYKVE VINEPREGKK LLVLDVDYTL FDHRSVGETG RDLMRPFLHE FLASAYEDYD
IVIWSATSMK WIEAKMQELG CKSNPNYKIC FMLDSTAMIT VHTPKYGVID VKPLGVIWGK
YPQWSVKNTI MMDDIRRNFI MNPQSGLKIR PFKQAFVNRE TDKELLRLSK YLKDIAQLDS
FEVLNHRHWE KYKPPKYSS
//
