ID A0A137QC06_9AGAR Unreviewed; 1127 AA.
AC A0A137QC06;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647};
DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647};
GN ORFNames=AN958_12166 {ECO:0000313|EMBL:KXN84739.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN84739.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN84739.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN84739.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ962572; KXN84739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QC06; -.
DR STRING; 1714833.A0A137QC06; -.
DR OrthoDB; 1382116at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProt.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911:SF8; KLAROID PROTEIN-RELATED; 1.
DR PANTHER; PTHR12911; SAD1/UNC-84-LIKE PROTEIN-RELATED; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR Pfam; PF07738; Sad1_UNC; 2.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS51469; SUN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1127
FT /note="alkaline phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007295138"
FT DOMAIN 907..1113
FT /note="SUN"
FT /evidence="ECO:0000259|PROSITE:PS51469"
FT REGION 332..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 790..817
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 332..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 1127 AA; 123885 MW; E8F90BDE91429D5F CRC64;
MGIMYARNTK LAALGFILFQ FVQPALGQHF KRLGTCPTLG CVLPPDLTDF YPGQLFDIRL
EVHAPLNGSE AFNGGKVNDQ FSFCIQSGTS GHENDGHGNG GGNNCEDAAK FFGVKEPALE
KWSFTYFEDL FAQDANQPTL VNVASKAYRG VHLSQPGDYS AILTFNGKGQ TVARWTVRTA
SKKQTAKNVL FFIGDGMTQA MITAARLISH KSINGRYQTL MQLDQMDALG IQMTHSIDSF
ITDSANSATA LFSGKKSTVS ALNVWVDSSA NSFDDPKMET VAELFRRRRK GGALGTSPPK
PDRWGVKDTS VIIASALHIA AQNEMLPAIN PNNTWTSGVT RPNPAVPRST SVEYEKETQT
TTTRRLAPPP NRFTRPPSSR KPISKNASVR LVPDSEGEED SSAPSPAKGR GKSPFEHVVD
AAKKVLKPAT YYVRQLSLEP EDRSHSTNGN TTHNRDTSYD YAAEEQEFQE AQQAKRTSLS
AHKRGRMPMD NRAYKPSASD IEGDDDEYSD EDKRKRRKKK KKNEPVGGPL TTLPVLSADR
KKKRKSRGTK SGVPGQDDEE SESDEEPSVE PESMQAQQRS SVSRSLQPAS YDISMQDSSV
DTAEQGLDSI PELPEEELPS SHQPKRARSR EKSVSRRVPR SSSRPPREST RPVLWLRTSD
LSLAAKLIKY LTLGALAYAV WYGLMETDIA SHLPTLSLSR PSSRPIYTAP EVPAADIAEL
SERLQRIEVA LSGLSRDSEQ IRAKTEDGVR SHSELMGRLG ALESRLATES KRLVESEVKV
KDALSLGTSV SSVKREIEVL QAQLKAQEKQ RQQDDQQHRA DHINDEEARA KLRALEDRVG
SVEGGVKEAI ELGKKAVSTS ANTKSPTIKV PGGQDLKSII KDVVDDAVLL FSKDTIGKAD
YAMHANGARV IPSLTSASFE LQPHSMRSQI AGFFTGYGSA VGRPPVTALH HESHGGYCWP
FVGSPGQLGV SLAAPIIIDE VTIDHVAKEV AINIASAPKL CEVWAMIEGE ENEKKYLEII
EVREKARVKS ADAEGLAEAE EHPVTLPHNP PYLRIANFTY DAESAKNVQT FSIDEDVKEK
QMDFGIVVLR VLDNWGMEKY TCLYRFRVHG TPLGPMQIPE PVEDIGL
//
