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Database: UniProt
Entry: A0A0F5Y9K3_9CYAN
LinkDB: A0A0F5Y9K3_9CYAN
Original site: A0A0F5Y9K3_9CYAN 
ID   A0A0F5Y9K3_9CYAN        Unreviewed;       791 AA.
AC   A0A0F5Y9K3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KKD35322.1};
GN   ORFNames=WN50_25955 {ECO:0000313|EMBL:KKD35322.1};
OS   Limnoraphis robusta CS-951.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX   NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD35322.1, ECO:0000313|Proteomes:UP000033607};
RN   [1] {ECO:0000313|EMBL:KKD35322.1, ECO:0000313|Proteomes:UP000033607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS-951 {ECO:0000313|EMBL:KKD35322.1,
RC   ECO:0000313|Proteomes:UP000033607};
RA   Willis A., Parks M., Burford M.A.;
RT   "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT   robusta strain CS-951.";
RL   Submitted (JUN-2015) 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   -!- 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:KKD35322.1}.
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DR   EMBL; LATL02000043; KKD35322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5Y9K3; -.
DR   PATRIC; fig|1637645.4.peg.735; -.
DR   Proteomes; UP000033607; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 2.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 2.
DR   Pfam; PF00353; HemolysinCabind; 2.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   SUPFAM; SSF51120; beta-Roll; 2.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033607};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   REGION          635..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        173
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         437
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         442
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         446
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         487
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         488
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   791 AA;  83902 MW;  010E73FE128C2B07 CRC64;
     MENNKFSTKN FVVRVNREEN ISNMAKNVII MIGDGMGWEM ARAGAIAKTG ESYTSGVGEG
     LSFQELDGYS FVTTYGTTIA PGSEEPNPAN RVFNTSNSAL YGSGSNLTGT NPLRPDFVFE
     PDFNAGIDAS GGAANPGTTA IGNLVGYDPE RGGINPWTPG NDPEYIKYSY PDSANTATTL
     YTGVKSYNSA IGVDIYEQPL ESILQIAADS DKSTGLVSSV PIDHATPGAA AANVNRRNKY
     DSEFPTLDSI LQQELRIYKP TVILGGGHPL STPEDPLPGE VEPPSDNTFI LESTYQELSA
     NPTDNVYGYT FLERGEDAAA VLAETAAEID PNQGERLLGL YGARGQNGNL PVSSADGDYS
     TTGLDMFSLF SSAQAGSPNN ITPGVPNPDT ERPLLPGETD ESFIAREINE NPTLQDLTEA
     ALDVLAKDED GFWLMIEGGD IDWSAHDNNM DNLIGTMLDF DKSVQSVMDW IEENGGWEEN
     LLVVTADHDH YLTLSPDFPE LLATEGAEAL TYELHTPEES GQYWGSDPEV KYGWGSHTNR
     PVPVYYQGEG SEVLDGLVGE GYNSYGFEIP GLPNHVDQTH IFQTMAAAVT GTDNYINGSQ
     NAETFVGEAG NDLIIALGDN DTVAGLAGDD QIYGGDGNDV LRGDENERSP GGQPGGDDMI
     YGGTGNDRIG GKGGNDKLYG DDGDDQIWGD DGDDLLHGGF GNDTLTGDDF SGGQGADTFV
     LALGEGTDTI TDFELGIDKL ALTAGLTFEQ LSITASGSNA LISVGDERLA ILNGVEAVGL
     IENSAATFAQ I
//
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