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Database: UniProt
Entry: A0A1V8TJH9_9PEZI
LinkDB: A0A1V8TJH9_9PEZI
Original site: A0A1V8TJH9_9PEZI 
ID   A0A1V8TJH9_9PEZI        Unreviewed;       560 AA.
AC   A0A1V8TJH9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=B0A51_11631 {ECO:0000313|EMBL:OQO20224.1}, B0A51_16849
GN   {ECO:0000313|EMBL:OQO11401.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO11401.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|EMBL:OQO11401.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCFEE 5018 {ECO:0000313|EMBL:OQO11401.1};
RX   PubMed=28684563;
RA   Coleine C., Masonjones S., Selbmann L., Zucconi L., Onofri S., Pacelli C.,
RA   Stajich J.E.;
RT   "Draft Genome Sequences of the Antarctic Endolithic Fungi Rachicladosporium
RT   antarcticum CCFEE 5527 and Rachicladosporium sp. CCFEE 5018.";
RL   Genome Announc. 5:e00397-17(2017).
RN   [2] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
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}.
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:OQO11401.1}.
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DR   EMBL; NAEU01001534; OQO11401.1; -; Genomic_DNA.
DR   EMBL; NAEU01000674; OQO20224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8TJH9; -.
DR   STRING; 1974281.A0A1V8TJH9; -.
DR   Proteomes; UP000192386; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
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   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; 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   Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT   DOMAIN          347..529
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  62254 MW;  8EB0D740AEB610DE CRC64;
     MNSLNILSGF SGTPASTPPS TPPSSRSRTG SSADPESENK NEERDVTANP DRLSEKLDEK
     LPWAGRARTE DDVDGARDVE IKQEAVDEDE RTPLLSKHAT EEQRSSWRLH RRLAEAIIDS
     AVTVVRVIYT ALSAPKRWVV ACFYNEQGQF SAVMPFRQFR ALMGGKRSRK REQPMPAAGS
     DEIKVSAGRR STSAVQEVSE KDEMAVPRTQ QRRSPLRSPS NSSISSATTA DMTSEGEPET
     DADKPSDSPS RNTRSKTPTV KDEINPQKKS IRIKLHAPTD TQRQHRQRPQ SPASATSELA
     QSLKSPIAPP LSQHLKSLTR YPRLPTPPRP LVPRRQPSYS LLAPTPTDQP RKTLVIDLDE
     TLIHSMAKGG RMSQGHMVEV RLTQPMANPV TSIVGSAGVS SNATTTIPIL YYVHERPYVH
     EFLRKVAKWY NLVIFTASVQ EYADPVIDYL ERERKYFSAR YYRQHCTWRA GAYVKDLGVV
     EGDLGRVVIL DNSPMSYVFH EDNALPIEGW ISDPTDRELL HLIALLEGLQ YATDVRAILA
     LRQGMLGTSQ GTGPGFAAQA
//
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