ID Q0H744_SCLSC Unreviewed; 516 AA.
AC Q0H744;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN Name=cna1 {ECO:0000313|EMBL:ABB13418.1};
OS Sclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=5180 {ECO:0000313|EMBL:ABB13418.1};
RN [1] {ECO:0000313|EMBL:ABB13418.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1980 {ECO:0000313|EMBL:ABB13418.1};
RX PubMed=16776301; DOI=10.1094/MPMI-19-0682;
RA Harel A., Bercovich S., Yarden O.;
RT "Calcineurin is required for sclerotial development and pathogenicity of
RT Sclerotinia sclerotiorum in an oxalic acid-independent manner.";
RL Mol. Plant Microbe Interact. 19:682-693(2006).
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 ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Composed of two components (A and B), the A component is the
CC catalytic subunit and the B component confers calcium sensitivity.
CC {ECO:0000256|ARBA:ARBA00011112}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000256|ARBA:ARBA00009905}.
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DR EMBL; DQ182488; ABB13418.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0H744; -.
DR VEuPathDB; FungiDB:sscle_01g006030; -.
DR PHI-base; PHI:2361; -.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IEA:InterPro.
DR CDD; cd07416; MPP_PP2B; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041751; MPP_PP2B.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 145..150
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 59050 MW; 2E1E83F3C59CE2D3 CRC64;
MEDGSQVSTM ERVCKDVQAP AMVPPTDQQF FSPQDPSKPN LQFLKQHFYR EGRLTEEQAL
FILEEGTKVL KQEPNLLEMD APITVCGDVH GQYYDLMKLF EVGGDPAETR YLFLGDYVDR
GYFSIECVLY LWSLKIWYPN TLWLLRGNHE CRHLTDYFTF KLECKHKYSE RIYEACMDSF
CALPLAAVMN KQFLCIHGGL SPELHTLDDL KSVIDRFREP PTHGLMCDIL WADPLEEFGQ
EKTSEYFIHN HVRGCSYFFS YPAACNFLEK NNLLSIIRAH EAQDAGYRMY RKTRTTGFPS
VMTIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCTPHPY WLPNFMDVFT WSLPFVGEKI
TDMLLAILST SSEDELKDDQ TPSSTSPGPI SPPINAAMDP ESIEYKRRAI KNKILAIGRL
SRVFQVLREE SERVTELKTA AGGRLPAGTL MLGAEGIKSA ISSFEDARKV DLQNERLPPS
HEEVTRQTEE GREQALERAK READNDKGVT NALQKA
//
