(data stored in ACNUC7421 zone)

HOGENOM: ASPTE_3_PE1

ID   ASPTE_3_PE1                          STANDARD;      PRT;   377 AA.
AC   ASPTE_3_PE1; Q0CFY3;
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   Flags: Fragments;
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; (ASPTE_3.PE1).
GN   Name=mri1; ORFNames=ATEG_07401;
OS   ASPERGILLUS TERREUS.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiales;
OC   Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=33178;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ASPTE_3.PE1.
CC       Aspergillus terreus supercontig 1.11 CADRE full sequence 1..1534813
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MTNA_ASPTN
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:Aspergillus_terreus;CADATEAG00000893;CADATEAT00000893;CADATEAP00000893.
DR   EMBL; CH476604; - ;
DR   UniProtKB/Swiss-Prot; Q0CFY3; -.
DR   EMBL; CH476604; EAU31663.1; -; Genomic_DNA.
DR   RefSeq; XP_001216022.1; XM_001216022.1.
DR   ProteinModelPortal; Q0CFY3; -.
DR   EnsemblFungi; CADATEAT00000893; CADATEAP00000893; CADATEAG00000893.
DR   GeneID; 4322543; -.
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; ASPTE_3.PE1; -.
KW   CADATEAG00000893affold_1320000031; CADATEAP00000893affold_1320000031;
KW   CH476604;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   377 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTLQAIKYNN GDLAIIDQLQ LPHVEKYVTI HNSEEGWHAI KDMRVRGAPA IAIVAALALA
     SELHGLMAHD KLSPEAEDVQ TFVVEKLRYL VSSRPTAVNL SDAARKLEVV VAQSARAPGA
     TGKTVATAFI QAAEEMLVKD VEDNKKIGEH GAQWILKNSL EGHGKATVLT HCNTGSLATS
     GYGTALGVIR SLASADSLQH AYCTETRPYN QGSRLTAFEL VHDALPATLI TDSMAAALLA
     SKKAGVNAIV VGADRVAANG DTANKIGTYG LAVLAKYHNV KFLVAAPLTT IDLNTKSGDQ
     IVIEERLASE VTSIRGPRDN TGSEDVELVT VCTAAKGINV WNPAFDVTPA ALIDGIITEK
     GVMEKDSAGM FHLEELF
//

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