(data stored in ACNUC7421 zone)

HOGENOM: LEMAJ1_36_PE516

ID   LEMAJ1_36_PE516                      STANDARD;      PRT;   506 AA.
AC   LEMAJ1_36_PE516; Q4Q0R9;
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; (LEMAJ1_36.PE516).
GN   ORFNames=LmjF_36_4930, LmjF36.4930;
OS   LEISHMANIA MAJOR STRAIN FRIEDLIN.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania.
OX   NCBI_TaxID=347515;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEMAJ1_36.PE516.
CC       Leishmania major strain Friedlin complete genome, chromosome 36
CC       chromosome II, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_LEIMA
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=CAJ09465.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -!- GENE_FAMILY: HOG000224730 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q4Q0R9; -.
DR   EMBL; FR796432; CAJ09465.1; ALT_INIT; Genomic_DNA.
DR   PDB; 2A0U; X-ray; 2.10 A; A/B=1-375.
DR   PDBsum; 2A0U; -.
DR   EuPathDB; EupathDB:LmjF.36.4930; -.
DR   PhylomeDB; Q4Q0R9; -.
DR   ProtClustDB; CLSZ2430389; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:RefGenome.
DR   GO; GO:0005634; C:nucleus; ISS:RefGenome.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; ISS:RefGenome.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:RefGenome.
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; LEMAJ1_36.PE516; -.
KW   CAJ09465.1 20047545old_1320000031;
KW   putative translation initiation factor 2 subunit;
KW   3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Isomerase; Methionine biosynthesis; Nucleus; Reference proteome.
SQ   SEQUENCE   506 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRFFFFAVAG WGGGGNPVRC TLPPVRDAVV HFLSTFLCLS SLHFDVLRSF INRRPTLPKP
     SPPHNPTQPQ GKRRTCETHR SAQRHLPIQK KKSLLKTHPA TSSEGFLARC LYLTTSTTTP
     LNPSLLALST VMMSKPHHAT LESIKYTPGS LRLLDQRKLP LETVFDDVLT VEDIWSAIKE
     MRVRGAPAIA VSAALGIAVA TQRKAANGEL KSGREVQTFL LTSCDFVMTS RPTAVNLFNC
     LRDLKAQVDK LDPTKAAAEV AQAFVELAEA VYTNDVAFNE GIMRHGAAHI LAAAKAEGRD
     KVSILTICNT GALATSRYGT ALGVVRQLFY DGKLERVYAC ETRPWNQGAR LTVYECVQED
     IPCTLICDGA ASSLMLNRKI DAVVVGADRI CQNGDTANKI GTYNLAVSAK FHGVKLYVAA
     PTTTLDVKTA SGNHVEIEER EPTEITTNLV TKQRVVADGP HLSIWNPVFD ITPSELITGG
     IITEKGVQAP AASAPYYDIA SIIAQA
//

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