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Database: UniProt
Entry: A0A151WI99_9HYME
LinkDB: A0A151WI99_9HYME
Original site: A0A151WI99_9HYME 
ID   A0A151WI99_9HYME        Unreviewed;      1150 AA.
AC   A0A151WI99;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Venom acid phosphatase Acph-1 {ECO:0000313|EMBL:KYQ47583.1};
GN   ORFNames=ALC60_13338 {ECO:0000313|EMBL:KYQ47583.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ47583.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ47583.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ47583.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ47583.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000032};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; KQ983089; KYQ47583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151WI99; -.
DR   STRING; 64791.A0A151WI99; -.
DR   Proteomes; UP000075809; Unassembled WGS sequence.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:InterPro.
DR   GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 1.20.960.40; -; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR018993; FOP_dimerisation-dom_N.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF09398; FOP_dimer; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT   DOMAIN          54..128
FT                   /note="FGFR1 oncogene partner (FOP) N-terminal
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF09398"
FT   REGION          210..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1150 AA;  130794 MW;  3B9CB5AA4ECB9350 CRC64;
     MIDGNISMEE DTELRDLVVQ TLESNGVLAK IRAELRASVF LALEEQDSVM NPEPLLNKTV
     KQYLSNSEGK LLFSLVREFL EYFGLDYTIS VYDPETYFGK EYNYVGRNKL CEELGIVSTE
     PLLGEILKNS INGAFNSSQK NKTRHDVTNE DSTNFANATF EVSVPKIFHN ESVSSNEILE
     SISEQSPKVP INVTITDKKC KDIPTGADVV TDTSDYDKHQ SSLRENTTDN DRIEGNRNNN
     VNFDKNNSNP YDTCMATNYV AQETDSTVTS IQMSPLSKSE SLIKFDDSIV IDTQKNQNKD
     VTKQNSINSL ELSIENNVQS KKPINAGSNF GKTIYFDEII VGGERKNVST MNKAEPFLEG
     LPTMNQKANS IFSDLPPLNG KKANINDLKE LMDIGLATDG IDNYEEDFVS SASGSANEQS
     PIKEPDKIDS PLKLQTKKEE KPQSARTEDL SEEIEEMDEI LSSTSCTCKK LEDQIQRKKK
     MFLRKLQGIL EEPGGKSRDS NESALFYTGN ARQSSSRKDP AFPHTNVCKD ITRDNYMCYR
     CKHFLEIPRN LSSQPFSDGV PTFIEQCKNE LNFIQAIVWL KSSITCVSQI SVKQLQQIFN
     EQWNTCGEYN YCEDECTDIE QLRSSMDKNL SSRNTIVTST PLNICDISCR TPQRTIRNLY
     ARSEDPRSKP LNSMSANDLN ESVKSLILGS SNNRYIAARE KKKDVKSYII PETDVESILN
     DETYNDLIHE HQPNFELEKD TGCSMQITSK NSIQQKNKKI IENKHIFQKI SQLCNTVIQN
     YFLVFRHGDR TPDNNGREMF PNDPYINYSF YPTGLGQLTI EGKKHEYRLG KFLRFRYNDF
     LGNLYVPKLL SARSSDYERT KMSLQLVLAS LFPPKNVQRW NPLLNWQPIP TLYAPRIDDN
     IFLADECPQF LEEYNRILNS PEGQTKIDLF KDLMGNLTRL TGKNIQTLED LYFLYHTFVA
     ESSLGLTLPE WAYDYFPYGP LFDGIVAAYN VSNFTPLIRR LYAGPMIRAM TDSMIAAQNS
     NAPNTKIYLY SGHETNIAGM LHAFGVYKPH VPEYSSAVIL ELQQIQQEYY VKLVYYRGIP
     PTIKDLTIPG CDTLCPFDKY LDLIDDLIPS DEEMICDKRQ TPSFAGTEYP AGLQNILENL
     IKRSAIEKNT
//
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