ID A0BS05_PARTE Unreviewed; 447 AA.
AC A0BS05;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Chromosome undetermined scaffold_124, whole genome shotgun sequence {ECO:0000313|EMBL:CAK61322.1};
GN ORFNames=GSPATT00031553001 {ECO:0000313|EMBL:CAK61322.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK61322.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK61322.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK61322.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; CT868013; CAK61322.1; -; Genomic_DNA.
DR RefSeq; XP_001428720.1; XM_001428683.1.
DR AlphaFoldDB; A0BS05; -.
DR EnsemblProtists; CAK61322; CAK61322; GSPATT00031553001.
DR GeneID; 5014504; -.
DR KEGG; ptm:GSPATT00031553001; -.
DR eggNOG; KOG3720; Eukaryota.
DR HOGENOM; CLU_030431_1_2_1; -.
DR InParanoid; A0BS05; -.
DR OMA; IWFRADE; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..447
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002622657"
FT TRANSMEM 406..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 447 AA; 52065 MW; 07AD502B99D0A2BC CRC64;
MIFLLILLSQ AFGDQLVLSQ ILWRNGACTP TYCNWKCKEF EQQGILNGQL TPIGTRQHYV
LGQWLRKRYI EDLKLLSQFY NEAEIYIEST DVNRTILSAL SNLQGMYPAG TGPKINPDLN
RSYLLPPNQK EFEDFGDAAL PGLQQAIPVH VREKQLDIYL KGYDALACPR NEEFRNSNIN
SKLYYQINSK AQSLISDFTQ QLGIVASQLN ITDLYEYQDT FDSCEYNGYD LPKLKESTQS
QMKLLQYLYF SLEHNIDFEQ TRLLATPFFR NLLLNIENVI NNQTEHKFRI FSAHAATVQL
ILNALNLTSF ECVKQVYLNE KVQNKNCIYT FPGYASNIIF ELYRKLGHGN QYYVQVLYNG
TLMPICNNQY KCDYEEFKSR IQFQNVKDYE DECLISPKFK KEAASFILKA INVVITILFI
ISFCIIYLLR RQSKLEEYTK IVQQFDA
//
