ID   A0A178E2Y5_9PLEO        Unreviewed;       585 AA.
AC   A0A178E2Y5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:OAL50346.1};
GN   ORFNames=IQ07DRAFT_587018 {ECO:0000313|EMBL:OAL50346.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL50346.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL50346.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL50346.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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; KV441644; OAL50346.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E2Y5; -.
DR   STRING; 765867.A0A178E2Y5; -.
DR   InParanoid; A0A178E2Y5; -.
DR   OrthoDB; 2681959at2759; -.
DR   Proteomes; UP000077535; 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:UP000077535};
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..585
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008085056"
FT   TRANSMEM        457..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          553..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..571
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  64315 MW;  0B10420645E24413 CRC64;
     MLSLTIAAMA SAWLVGAQEE DNNAYHPHGA FAFIRTGERT PLVRPGAAEL TALGANQMYS
     LGQNFRTRYI TGNSPSGLGQ EHIVGMSPNT LDNNQILVQT LDRQYLMSSA QAFMQGLYPP
     RSIGNGTGDA SGLLADGTAI DFPLNGYQYP NIQSSGQLDP ESIFIMGTQN CPIAQRDAMM
     YFTTNEFQQT KAVNEDFYQS LNLDWFEGNF QEDQLDYTYA LEIADYLTYQ YAHNSTIYRT
     LANDSTYTGV YDKIKHLADE EAWYLYGNTS TSSKDADNQA IAGKTLAAVI LGQFQRLILD
     KTSGGDTTDL SFPLTLFFGE QDPMISLISI MTADYRDSNF RSMPPYASAI VFELFSTGNN
     TDFPTRDEDL WVRFYFHNGT DFSQNQLIAF PIFGNGPSRT DMPWHEFQDM FSRIMMSTLS
     EWCDTCASSS LFCTGVDETH VSLILPAPVR KYKLTPAVAG VIGAVVALAV AFLLFGLAML
     LGGLRFHRNP SASAKSALGG FKGSAKLASD PDLSLTKNAA APAFGAVVTS PDQKRGHERV
     GSWELRQKEF GKQVAVGEEG DQSRRESFDA IDAVAGKPVQ PHERV
//