ID R7YSL8_CONA1 Unreviewed; 484 AA.
AC R7YSL8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=W97_03854 {ECO:0000313|EMBL:EON64621.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON64621.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; JH767569; EON64621.1; -; Genomic_DNA.
DR RefSeq; XP_007779938.1; XM_007781748.1.
DR AlphaFoldDB; R7YSL8; -.
DR STRING; 1168221.R7YSL8; -.
DR GeneID; 19901165; -.
DR eggNOG; KOG3720; Eukaryota.
DR HOGENOM; CLU_023111_1_0_1; -.
DR OMA; REWAQAC; -.
DR OrthoDB; 2315929at2759; -.
DR Proteomes; UP000016924; 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; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567:SF142; -; 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:UP000016924};
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..484
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004450063"
FT TRANSMEM 415..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 453..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 52857 MW; 11438A4ABE6300B4 CRC64;
MFSNLALLAV STTIGAALGE TILGVTVFTR HGDRTSKHFP GYSLTSLGAQ QNFQVGQDYR
GIYLDSDSPK RILGVSEDKY VSSQVYASAP DQKILLDTTT AFLQGLYPPL EEVTRLTLAN
GSAYTNPLNG YQYVHIRSEP STSPNSIWLK GDDSCPAYTR ASSSFKASPE FQQRTEATAP
FYARFWDALR NVHDYNPANL TYANAYDIYD LLNTASIQNA SSAPANHAIS HDISAPDLAR
LRTLADSAEF AANYGRDEPM RAIGGATLAG AVLARLNETV VTHGRRKFSL LAGSYDTFLS
FFGLAELTAA STDFYGLPAY ASTMAFEIFT ENNVTVFPAL EDVSVRFLFR NGSDVEELRA
FPLFGRSETA LPWSEFVAEM GKRAVTSVKE WCEACESTEG FCMVYSVPTT KWNPAAYAVS
GVISGIVVGT AVVLFILAYR KLAERARARK ARRARQDDVH RAEMGMPDKG AVSERTDSVG
SESV
//
