(data stored in ACNUC7421 zone)

HOGENOM: VITVI_4_PE58

ID   VITVI_4_PE58                         STANDARD;      PRT;   418 AA.
AC   VITVI_4_PE58; D7TCD0;
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; (VITVI_4.PE58).
GN   ORFNames=GSVIVT01015055001;
OS   VITIS VINIFERA.
OC   Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta;
OC   Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; eudicotyledons;
OC   core eudicotyledons; rosids; rosids incertae sedis; Vitales; Vitaceae;
OC   Vitis.
OX   NCBI_TaxID=29760;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS VITVI_4.PE58.
CC       Vitis vinifera chromosome 11 IGGP_12x full sequence 1..19818926 annotat
CC       by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MTNA_VITVI
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   -!- SEQUENCE CAUTION:
CC       Sequence=CBI27788.3; Type=Erroneous gene model prediction;
CC   -!- GENE_FAMILY: HOG000224730 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Vitis_vinifera;GSVIVG01015055001;GSVIVT01015055001;GSVIVT01015055001.
DR   EMBL; FN595756; - ;
DR   UniProtKB/Swiss-Prot; D7TCD0; -.
DR   EMBL; FN595756; CBI27788.3; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002277806.1; XM_002277770.1.
DR   UniGene; Vvi.3396; -.
DR   ProteinModelPortal; D7TCD0; -.
DR   PRIDE; D7TCD0; -.
DR   GeneID; 100268031; -.
DR   KEGG; vvi:100268031; -.
DR   OMA; RPRNQGA; -.
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; VITVI_4.PE58; -.
KW   GSVIVG010150550013820036002503210000011;
KW   FN595756; D7TCD0;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus; Reference proteome.
SQ   SEQUENCE   418 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTWLYKFYFI FFFYNNHIYR GITLTSQQRR GIRVASFTEF KSMADSNSKH QDSLQSICYK
     RGSLQLLDQR KLPLETVYLE IKGADDGWHA IRDMVVRGAP AIAIAAALSL AVEVSNLEDF
     IGTSDDAASF LNSKLDYLVT SRPTAVNLSD AVTKLKGVIS NAAATAFEAM SVFQAFLEAA
     EDMLREDVAA NRAIGLYGAS FLQSHIKDSK NLSILTHCNT GSLATAGYGT ALGVIRSVHA
     EGILLRAYCT ETRPFNQGSR LTAFELVHDN IPATLIADSA AAALMQAGRV DAVIVGADRV
     AANGDTANKI GTYSLALSAK HHHIPFFVAA PLTSIDLTLS SGQEIVIEER SPKELLNSRG
     GLGEQVAASG ICVWNPAFDV TPADLIAGII TEKGVITKTG DVFDIKDFIH NATSHCCK
//

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