ID T1K024_TETUR Unreviewed; 422 AA.
AC T1K024;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN Name=107372089 {ECO:0000313|EnsemblMetazoa:tetur03g06160.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur03g06160.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur03g06160.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; CAEY01001131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015795725.1; XM_015940239.1.
DR AlphaFoldDB; T1K024; -.
DR STRING; 32264.T1K024; -.
DR EnsemblMetazoa; tetur03g06160.1; tetur03g06160.1; tetur03g06160.
DR GeneID; 107372089; -.
DR KEGG; tut:107372089; -.
DR eggNOG; KOG3720; Eukaryota.
DR HOGENOM; CLU_030431_1_0_1; -.
DR OrthoDB; 3058791at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
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; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 381..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 422 AA; 48972 MW; E188A61B2B767B0E CRC64;
MISWVYSTII HYLIFSHIVE DSIAAEKDSA VKRLELLTIV HRHGERTPYK FFKNDPYSDP
KYWPDGEIQL IKPGRQRMYQ LGKSIRENYS NFLEDNPRQV YARSSDADRC IESSELVLHG
IFKSKGHWFY SNDTDYLPIP IHTVPTALDG MLTIDCDCPE SSQEKLRLLN SKTAKQVTHQ
YSDTLNLIRE KTGNDLSNLN DISDFYTTLT IEEENIKDFK RPDWYTDKVK EELRIMSDNG
LYISSSSFEI LRLRTSNFFA DLRHRMHAKI SGDSKLGGLK FLSYSTHDNL LASILIALDI
FDHKVPPYGA TLVFELIHVP SKGHFVQIYY WKDTEKEADL MSLSFCNNQM ICSYDRFSRY
ISTYIVDDWQ AACGLKHEPS LWSSGIFVAL VAILALIIVI GLVWFMAIQW YGVRRQYEVI
RS
//
