ID A0A0K6FNB6_9AGAM Unreviewed; 352 AA.
AC A0A0K6FNB6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE AltName: Full=Nuclear proteasome inhibitor UBLCP1 {ECO:0000256|ARBA:ARBA00032039};
GN ORFNames=RSOLAG22IIIB_03192 {ECO:0000313|EMBL:CUA67765.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA67765.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA67765.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA67765.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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 -!- 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; CYGV01000224; CUA67765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K6FNB6; -.
DR Proteomes; UP000044841; 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:UP000044841}.
FT DOMAIN 21..99
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 155..324
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
SQ SEQUENCE 352 AA; 39947 MW; F3B7F19BCA45B4A3 CRC64;
MDNAPSASVT DSPVETLVED VYISLKFTWS LKQHTVSVAE SDCVLDLKDK LFALTRVPNE
RQKILGLVKG KLPDDSVRIA DMKFAPTKKF TLVGTPVGEE FKEISEDQLP DVVNDLDLQI
DASSAEAKSM AEDKRNIRKI LEAAKNLSIN VMYPLRPGKK LLVLDLDYTL LDTKPLTSGI
LPADECARPG LHEFLELAYK HYDICIWSQT KWTWLEAKLV ELGMVGDESR NYKISFVLDH
IPMFKVFSTR DGKPFSHAVK ALRIIWEHFP QFGPQNTAHV DDLSRNFVLN PGEGIKISAF
KLDDTLEAQN DRELEKLGRY LVWLASHTDF KEIDHRNWKK VARALKETGH SN
//
