(data stored in ACNUC7421 zone)

HOGENOM: NEFIS1_695_PE905

ID   NEFIS1_695_PE905                     STANDARD;      PRT;   387 AA.
AC   NEFIS1_695_PE905; A1CY38;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Methylthioribose-1-phosphate isomerase; Short=M1Pi;
DE   Short=MTR-1-P isomerase; EC=5.3.1 23;AltName:
DE   Full=S-methyl-5-thioribose-1-phosphate isomerase;AltName:
DE   Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like
DE   protein; (NEFIS1_695.PE905).
GN   Name=mri1; ORFNames=NFIA_110340;
OS   NEOSARTORYA FISCHERI.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiales;
OC   Trichocomaceae; mitosporic Trichocomaceae; Neosartorya.
OX   NCBI_TaxID=36630;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEFIS1_695.PE905.
CC       Neosartorya fischeri contig 9374 CADRE full sequence 1..2575019 annotat
CC       by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MTNA_NEOFI
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-
CC       phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-methyl-5-thio-alpha-D-ribose 1-phosphate =
CC       S-methyl-5-thio-D-ribulose 1-phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC       1-phosphate: step 1/6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits
CC       family. MtnA subfamily.
CC   -!- GENE_FAMILY: HOG000224730 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Neosartorya_fischeri;CADNFIAG00009596;CADNFIAT00009596;CADNFIAP00009356.
DR   EMBL; DS027685; - ;
DR   UniProtKB/Swiss-Prot; A1CY38; -.
DR   EMBL; DS027685; EAW25540.1; -; Genomic_DNA.
DR   RefSeq; XP_001267437.1; XM_001267436.1.
DR   ProteinModelPortal; A1CY38; -.
DR   EnsemblFungi; CADNFIAT00009596; CADNFIAP00009356; CADNFIAG00009596.
DR   GeneID; 4593349; -.
DR   KEGG; nfi:NFIA_110340; -.
DR   GeneTree; EFGT00050000003245; -.
DR   OrthoDB; EOG4S1XGM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:EC.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR005251; IF-2BI_MTNA.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   PANTHER; PTHR10233; IF-2B_related; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   TIGRFAMs; TIGR00524; EIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; Salvage_mtnA; 1.
DR   HOGENOMDNA; NEFIS1_695.PE905; -.
KW   CADNFIAG00009596985old_1320000031; CADNFIAP00009356861old_1320000031;
KW   DS027685;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   387 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MASILQAIRY SRGKLAIIDQ LQLPYVEKFI TIQTPEDAWH AIKEMRVRGA PAIAIVAALA
     LASELNTLIV HDKLSSGAEE VKLFIREKLD YLVSSRPTAV NLSDAARKLE STISDHADTP
     GATGRTVAEA FIRAAEDMMT KDLDDNMRIG KNGAEWIIKH ALAARKSTAT VLTHCNTGSL
     ATSGYGTALG VIRALASKKA LEHAYCTETR PYNQGSRLTA FELVHDRLPA TLITDSMVAA
     LLANTKAEVD AIVVGADRVA ANGDTANKIG TYGLAVLAKY HGVKFLVAAP LTTIDLGTKS
     GEDIVIEERP AAEVTKIRGP VDGDHSADIV KLETVHIAAK GINVWNPAFD VTPSTLIDGI
     ITEVGVIEKG TDGQFHLERL FIDNSAS
//

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