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Database: UniProt
Entry: A0A178DPM9_9PLEO
LinkDB: A0A178DPM9_9PLEO
Original site: A0A178DPM9_9PLEO 
ID   A0A178DPM9_9PLEO        Unreviewed;       364 AA.
AC   A0A178DPM9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:OAL45554.1};
GN   ORFNames=IQ07DRAFT_576090 {ECO:0000313|EMBL:OAL45554.1};
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:OAL45554.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL45554.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL45554.1,
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 phosphoglycerate mutase family.
CC       {ECO:0000256|ARBA:ARBA00038362}.
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DR   EMBL; KV441657; OAL45554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178DPM9; -.
DR   InParanoid; A0A178DPM9; -.
DR   OrthoDB; 1456057at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          345..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..364
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   364 AA;  40935 MW;  755547959B3C7031 CRC64;
     MRRTPNTHKY RICGVGIPLP IFVLSIFLLV VYYLYPSMGD SAEIKKPVPT DDAFHFEYTV
     IKGLFLQSEE KTNDTGFDFR AHNFGLIDRS YDTDAASTSA QEAQWARFER YVRSLDAQSQ
     EGESVKVLFL GRHGQGWHNV AEAKYGTHAW DCYYSALPCF GNLTFFDAHL TPLGVSQARD
     ASHLWTAQIP LQIPVPETYY VSPLTRTLQT ADLTFSSLPL PKGKEYKPLV KELLREALGV
     HTCDQRSTRS EIAAAFPHVA FEEGFKEDDE LWEKDYREPE SARRFRLATL LDDVFGSDGN
     VVLSLTAHSG AIASILEVLG HRVFRLETGG VIPVVVRARR VLGGRQRPPW EPSDAPPMCD
     KPPV
//
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