ID A0A1W5DCS6_9LECA Unreviewed; 995 AA.
AC A0A1W5DCS6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM40958.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) 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 -!- SIMILARITY: Belongs to the dullard family.
CC {ECO:0000256|ARBA:ARBA00038346}.
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DR EMBL; FWEW01003742; SLM40958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5DCS6; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000192927; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002867; IBR_dom.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210:SF70; CTD NUCLEAR ENVELOPE PHOSPHATASE 1; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 336..517
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 795..844
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 995 AA; 110731 MW; FE747D35A6B96533 CRC64;
MNSLNILSAR VIGQAPPQTP STLRSRGQGD TASELGESDE DLDQQVPIAS GEEKDARFVE
DEDSKEEDFG VTPVTKDEKT PLLDERRATP FLDPKRSKLR IVAKQLVDAL TESLRWVLST
IAAPGVYVVT CFYDDDGRFS PFLPLRKLRR AVPTRNGSSS TAQAMGLSGS LGGHDESSDP
TKKQRSGRRK VVAVVERPKV SSAGSFSSTA SESEANSQRK EANGGSSKSS RSKSQVRASS
ENATPTRRSV RIKVYNEDTA RQRKDARKHK HGAGSVSSTG SDASQAPAVT AATLKSPTSP
TSSLRMTKYP RAPAPPRPLI PPRQPSYSTH TSPHSSILAQ KTLVIDLDET LIHSLAKGGR
MSSGHMVEVK LNTTVGIGGT TLGPQHPILY YVHKRPHCDE FLRKVCKWYN LVAFTASVQE
YADPVIDWLE QERKYFSGRY YRQHCTYRNS AYIKDLSSVE PDLSRVMILD NSPLSYIFHE
DNAIPIEGLP AQRETGFEPG PSSRPPGPIK GNPFRRLPTQ APPITHMPLI RTDPNEWWAT
QEIPVLPRGS SLIPQKISSV SETSAENVSG TSADNVNYPS LASSRMPGAG RSRPPSYVEF
EPDNATEANN TIPIKELLQT KKGSVKHLLK PITHRPLKTQ IEDDAALTQR LQYEEDQVGF
TMDLTIPFDD PFENTARNTA TVSDALFAQR LRETEGQVPR GSLTQTSRSP LTREGRLRQA
TAADDSRKLI ASQEEHRSLG AQWKATQQRQ YRREEEHRLK ARRRILTKKD IVRLNHSKAL
PGDDSAVLTT LPGENERIVA DLKAAQALQA ELEEEVRQQD IRTLKELQAK LEEAEYQDAR
LAAQLAAEWE KEDREEIQRI REQRTTCMMC VERYKKSELF KPCSDKEHIW CGKCLHAGFK
TALKTKTRLR CCRNLTTKSL PSLDPAVAKQ YNLMLLEMDT ANPVYCSAKP CGTFIPPSAV
KGDIATCPKC RKRSCVHCKA SEHPDKILSW VSEFD
//
