ID A0A1V8TDZ8_9PEZI Unreviewed; 595 AA.
AC A0A1V8TDZ8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phosphoglycerate mutase-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A48_04896 {ECO:0000313|EMBL:OQO09494.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO09494.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQO09494.1}.
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DR EMBL; NAJO01000010; OQO09494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TDZ8; -.
DR STRING; 1507870.A0A1V8TDZ8; -.
DR InParanoid; A0A1V8TDZ8; -.
DR OrthoDB; 2681959at2759; -.
DR Proteomes; UP000192596; 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:UP000192596};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..595
FT /note="Phosphoglycerate mutase-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013274877"
FT TRANSMEM 472..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 447..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 64039 MW; DFACEAAE893C5C23 CRC64;
MAPFHLPSSL VATLVLLSQS SLAQSDTSNY KVWSSVIFQR IGERTPDVLG FIPTTLTSLG
AQQAHNAGSF FRERYVPSAP SVIGTARAAI DGLNANTPSP QEVYALALDT QSSVATAQAF
LQGLYPPFTL NESVAAVLDP TSVLANGSYI ESPLDGYQYI QLHTSGALDP EFPYLAGSLN
CPAYDYNQVN YLMSAAYAAT DNSSSSVYDA IDDTLLASVM SNSQADYINA YAIYDYVNYY
ANHNASFKAQ INDSTLNALR WLADEQQYAM LGNLNAYNNL TSSSVLPDGK AGSIATLGGN
LLLAKMLDQL QTSVQWEGEY YKLSLLFADF PSLVSMFALL GLPDLNSNFA GLPSFASSAV
FEVFSTSDNA TYPSEDDLWV RFYFRNGTDS EDAYQSYPIF RHGPSETDMR WSDFQTSMNG
VLIGSIGDWC TQCEAVTSVF CAAWGNSTTS SGSTSSSSSS TNRGRSHSMS PAVAGVIGAI
VALVIAGLIF GLLALIGGFR VHRNNKYDTK KDLGGFKGSQ KLASDRDLTL PKGGAVVGAT
VERDAMGGTG HERIGSWELK KADMGSGGME RVRPSFEDDD RVNPFRDPVK ADERV
//
