ID F2SR85_TRIRC Unreviewed; 542 AA.
AC F2SR85;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Histidine acid phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TERG_05102 {ECO:0000313|EMBL:EGD88853.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD88853.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; GG700652; EGD88853.1; -; Genomic_DNA.
DR RefSeq; XP_003234506.1; XM_003234458.1.
DR AlphaFoldDB; F2SR85; -.
DR STRING; 559305.F2SR85; -.
DR GeneID; 10372583; -.
DR VEuPathDB; FungiDB:TERG_05102; -.
DR eggNOG; ENOG502SM2K; Eukaryota.
DR HOGENOM; CLU_023111_0_0_1; -.
DR InParanoid; F2SR85; -.
DR OMA; STQEWCL; -.
DR OrthoDB; 2681959at2759; -.
DR Proteomes; UP000008864; 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:SF127; -; 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:UP000008864};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..542
FT /note="Histidine acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003289670"
FT TRANSMEM 447..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 490..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60609 MW; 9E2347989A22E0E1 CRC64;
MLVICFFFIF FIAHALAQDN RRQITWGSVV FTRHGETVPL GAVGAHALTP VGAQQLVGAG
RAFRQRYITP HRNPNLSFFN VDGLSPVLNN DEIEISTTPE PNVVSSAQAF IQGLYPPTPE
LASLRGLLSY ATDVNGHLID YPLNGYQYPV ISTYRAEDPM SAHISGHKNC PQHTNAVRAF
AASKEFHDVF DSTQAFYSNI YSRILFGVYP RDMASIYHAT AVYEYLQYQY TYNSTARDII
SRTDVDTARQ YANQWAHATS SGADVHWSKD RVLAIAGRSL AYAIMRSLQQ NERSKGSFNK
LSLIFGGYEP LMAFLEIVVS KAYRESLSGL PNHGASVMID LFSMAEDGIA EFPTDNSKLM
VRLLIRNGTD ASDPESQFKQ YPMFGTNKKE IAMPYKDFVD QMVFNMKSTS EWCRSCNGQE
NFCYQYAEHK STKKCDFTTL PPLDTGALIG LGAVSFALLT LALSCIFCMW RGHRHRRKLR
WNHVDDTESN ANIISPGSSR DIRMSAPPSI APSNKSNTSS YNEDIEMLLS PACQPVKVRD
TV
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