ID A0A093VGR0_TALMA Unreviewed; 836 AA.
AC A0A093VGR0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000313|EMBL:KFX51355.1};
GN ORFNames=GQ26_0051720 {ECO:0000313|EMBL:KFX51355.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX51355.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX51355.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX51355.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX51355.1}.
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DR EMBL; JPOX01000005; KFX51355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VGR0; -.
DR eggNOG; ENOG502SKBE; Eukaryota.
DR HOGENOM; CLU_339859_0_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR PANTHER; PTHR46082:SF6; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..836
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001892536"
FT DOMAIN 11..130
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT REGION 579..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 93582 MW; 2E54C55EA8F2361F CRC64;
MRPRSRSDFA IAIICALPLE ADAVEALFDE TYDRLGRLYG KQPGDANAYV NGRIREHDVV
LCYMPRMGKG SAASVASSLR VSYTGVQLAL VVGICGGVPY PSASNNTEIF LGDVIISDAV
VEYDFGRQYP SRFQRKTDGH NKDMLGGPDR EIRTLLTSLR ASQTRNEFQG QIIQQLYSIQ
QLDARWRRPD SWNDILFESG YHHKHYIQES SAICRCFDGD SPDDICDEAL EHSCDSLGCD
WDRIRRCQEE SADTTNKVSV HIGKIASADT VMKSGEHRDQ IARKERVIGF EMEGAGVWDN
IPCIIIKGVC DYADSHKNKN WQDYAAATAA CGLKVFLGYY KIGKNTQSLV EQDMQVSINH
LNEQSRTTII FLFFAFLYFR GLLLTLHTRL TRLINPWSEL PAILEDAHLR RFTIPLDTIN
TWEIFDFILE KHFSDMPGYR QVKTGSYVLE DSISRSAVKH TDAFKACFRP GRRVFMSMLF
HLKQHEKSTC PSCHAANLDS GQSDVCCSFC GMQYRRIMEV VEDDNKNERH LDSANAKRLK
VNPARGHAFI APKTPAEADY PEEDVAQFKR VHIVAAPDTR QPAAGGKMVS NRNGLDTLNK
NKTTNSHSSI PRPITKNKNP RISALQRHFE QLSREFQKEV QRERLQRAAE SQYSRVYPTI
SSKPTVEVYK NIYRRPSLPA PSETSSSDSF FKSTYLGMDD VLQDTDDASS TPDDSIVNAG
GLGERTLTPS GDGVPSRRAM VTRHDDDDGD GRHVTLRTLA EEEYAAFRER ERGGGSNTNS
RSSGSDSRLS GESSNAERAV SVIILPSSDI ESEGGCITLP SSDISSMPPE SIHGLR
//