ID   A0A194V5A1_9PEZI        Unreviewed;       492 AA.
AC   A0A194V5A1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-MAY-2023, entry version 20.
DE   SubName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000313|EMBL:KUI59094.1};
GN   ORFNames=VP1G_06325 {ECO:0000313|EMBL:KUI59094.1};
OS   Valsa mali var. pyri (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI59094.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       {ECO:0000256|ARBA:ARBA00007251, ECO:0000256|RuleBase:RU003814}.
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DR   EMBL; KN714724; KUI59094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194V5A1; -.
DR   STRING; 694573.A0A194V5A1; -.
DR   OrthoDB; 1406448at2759; -.
DR   Proteomes; UP000078576; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR43475; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR43475:SF3; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_2G14290); 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:KUI59094.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT   DOMAIN          20..118
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF00293"
FT   REGION          415..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  54262 MW;  F19F36E4D13492BB CRC64;
     MLHPGYLLLI PSPGMICPAR PHRHRWAVIS GSIEPDDPSP QAAAWREILE ETTLTPSSLE
     LMRQGKSYVL PDESIGREWN INPFAFRLKD ESEGGKGEKA IVLDWEHETW AWYDPFEIED
     SESFGAVPRL AESLRRVWFE KDLGVDAGAV LTNGLDRLKN DHQSGARQLA GAALEILRDI
     VLKMDTRQPL DVWWTKIRFA SWHIWKNGRE SMGAAILSVL LAALKSMEDI IWQHKDDLST
     SARRDASSTI THALRNVIAH TGISLDLRVL ESRPLFEGVS LSSSLINAVP PSFERSTVVH
     ANEPEQHRKA PVPKLQVTLY TDASSALASE DVDIVLIGAD RIAESGAVSN KTGSLPAVLS
     AKHISPGAKT VILSESGKVA PPGVAAAHVV EDNGPTQLVR AWKADFNGER VKRAAGTLPS
     TPTGEHDDGQ SHPQQPLGND TVQVDIRNVL FEWVPPELVD VYVTEQGLWT VADIRKHSEA
     LGIEEERFFK DI
//