(data stored in ACNUC7421 zone)

HOGENOM: TRIAD_1_PE697

ID   TRIAD_1_PE697                        STANDARD;      PRT;   360 AA.
AC   TRIAD_1_PE697; B3RLE6;
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; (TRIAD_1.PE697).
GN   ORFNames=TRIADDRAFT_19292;
OS   TRICHOPLAX ADHAERENS.
OC   Eukaryota; Metazoa; Placozoa; Trichoplax.
OX   NCBI_TaxID=10228;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS TRIAD_1.PE697.
CC       Trichoplax adhaerens scaffold scaffold_1 TRIAD1  sequence 1..13260704
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MTNA_TRIAD
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:Trichoplax_adhaerens;TRIADG19292;TRIADT19292;TRIADP19292.
DR   EMBL; DS985241; - ;
DR   UniProtKB/Swiss-Prot; B3RLE6; -.
DR   EMBL; DS985241; EDV28753.1; -; Genomic_DNA.
DR   RefSeq; XP_002107955.1; XM_002107919.1.
DR   ProteinModelPortal; B3RLE6; -.
DR   STRING; B3RLE6; -.
DR   EnsemblMetazoa; TriadT19292; TriadP19292; TriadG19292.
DR   GeneID; 6749947; -.
DR   KEGG; tad:TRIADDRAFT_19292; -.
DR   OMA; EDGWKVI; -.
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; TRIAD_1.PE697; -.
KW   TriadG192923.19671820036002503210000011;
KW   B3RLE6; DS985241;
KW   Amino-acid biosynthesis; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   360 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTEQQSLEAI RYDHDHGQLK ILNQLLLPSE YVYENVEGIE DGWQAIRQMK VRGAPAIAIV
     GMLSLAVELR SKSFTEMNEF DKFIRDSLEH LKTARPTAVN IFLACDLITK LIDNLIILGD
     EAVGVAKIEV IRHIEEMLHK DVESNKRIGS YGAEAILAKV PSKEKINVLT HCNTGSLATA
     GYGTALGVIR SLYGRDSIDR VFCTETRPYN QGSRLTAFEL VHDGIPATLI TDSMASLVMK
     KKDISAVVVG ADRVLGNGDT ANKIGTYQLA ITAKYHKIPF YIAAPTTTIV LDDSKDIVIE
     ERSHKEVTEI QGIPIAPSGI NVYNPAFDVT PAELITGIIT EVGVFSPSEM KSKLQTILNS
//

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