ID E4UR32_ARTGP Unreviewed; 660 AA.
AC E4UR32;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647};
DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647};
GN ORFNames=MGYG_03153 {ECO:0000313|EMBL:EFR00147.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC {ECO:0000256|RuleBase:RU003946}.
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DR EMBL; DS989823; EFR00147.1; -; Genomic_DNA.
DR RefSeq; XP_003175629.1; XM_003175581.1.
DR AlphaFoldDB; E4UR32; -.
DR STRING; 535722.E4UR32; -.
DR GeneID; 10030937; -.
DR VEuPathDB; FungiDB:MGYG_03153; -.
DR eggNOG; KOG4126; Eukaryota.
DR HOGENOM; CLU_008539_3_0_1; -.
DR InParanoid; E4UR32; -.
DR OMA; YSGHKST; -.
DR OrthoDB; 35876at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF72; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..660
FT /note="alkaline phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003190601"
FT ACT_SITE 223
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 494
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 660 AA; 73877 MW; 84CAD85AD6D2C5CD CRC64;
MKFTVLVASA FASTAFAQTF QRLGGCPELG CIFPPDKAEF LSGQFFDIRL EVHSPVNGSE
ARVGDPDEKF TFTIERKGRG HQRPEPATKF FKTEEPKLEK WQFSWYEDLF AKDAKKPSVV
NVASKAFRRV SLDRPGIYEA VLTYYNGKKT TATWEVKELR TRRRAKNVIL FIGDGMTTNM
ITAARLMAHQ SINGKYQSKM QMDQFPVLGH QMTHSMDSFI TDSANSATAL YTGHKSTVNA
LNVYRDSSKS PFDDPKFETI AEIFRRVHPG AGIGIVSTAH LSDATPAALT AHTSDRGQSA
HVIDTYFHGL SNYTWTQWDG PDVLFGGGAE DFLPNDDNKK QNYYEMFKKK GYSLFWNATA
LAQASNDDRA LGVFSTSVMA KWLDRNVYKD NLKNQKNYPD GSDKDADDQP GLKEMTLKAI
DILHTRNRNN RESRGKGFFL MSEAASIDKQ MHTMDYDRAL GELLELDDTI RATIAKLRAL
GELDDTLIVV TADHGHGFDV TGSVDTKYLA EQKSDREKRN AIGTYYNSGL SQYTVQKQGS
LKYSEGVHFP AQWDPRYTLH SGLGAHPDKR ENYQVHKDGP RLPATAARGS KDYYVNYKDA
VSGFIVNGTI APDEGQGVHS LTDVPVFAMG PCQEDFGGVY NSVDVFFRMA QCLGLSKTRW
//
