ID A0A317UTD1_9EURO Unreviewed; 520 AA.
AC A0A317UTD1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:PWY65274.1};
GN ORFNames=BO94DRAFT_540896 {ECO:0000313|EMBL:PWY65274.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY65274.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY65274.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY65274.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY65274.1}.
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DR EMBL; MSFK01000060; PWY65274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317UTD1; -.
DR STRING; 1450535.A0A317UTD1; -.
DR OrthoDB; 2681959at2759; -.
DR Proteomes; UP000246702; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:UP000246702};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..520
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016300842"
FT TRANSMEM 457..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 520 AA; 56178 MW; AC231E3A5071E8B6 CRC64;
MLSSRQLVAL ATILHAATRV SAQDLKEQVW AVFAYTLYGD RVPTALPRPN ILTPYGANGL
YAAGSAFRDR YVAIHSTDVS PSTRIESISS YALEDEDLNI LSTTDPSVIA SAQAFMQGLY
PPLNETYDVQ YPDPSYLMAN GTYATAPMGG YQYPRIVTVS SDDPQSVVVA GQDNCFLHQI
TDADYQLNSG TQQIIQESAA FYNRLYDQAL SGDFDRSSVN YANAISVSEF LEYQLLHNET
LLLTVSQEDI LLARWYADQY TFATNGNTES SGAIDSGAVR TIAGQTLAGH ILDAFDTNVL
YRGSSGKMTL LFGGYEPAVA LTSLTQLASP GDGNFYGRPA LGASMTFELF SLENASFPTY
PDPSQLYVRF LLRNGTTSPE FQSYPLFGHS PSNIDIPYTE FKAEMEAFSL NSTEEWCLMC
DSKSVFCPGV LSDESGASAS SKTKPASKGM SPVTAGVIGA IVTLAVTGLV ALGGFLLLGV
RMHRRRRSSL EEIKGGIALG SDSNLALREH AAPPAKTMKP
//
