(data stored in ACNUC7421 zone)

HOGENOM: CANAW_2_PE106

ID   CANAW_2_PE106                        STANDARD;      PRT;   416 AA.
AC   CANAW_2_PE106; C4YJ78;
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; (CANAW_2.PE106).
GN   Name=MRI1; ORFNames=CAWG_03891;
OS   CANDIDA ALBICANS WO-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
OX   NCBI_TaxID=294748;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CANAW_2.PE106.
CC       Candida albicans WO-1 chromosome 2 supercont1.5 genomic scaffold, whole
CC       genome shotgun sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_CANAW
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   UniProtKB/Swiss-Prot; C4YJ78; -.
DR   EMBL; CH672350; EEQ45562.1; -; Genomic_DNA.
DR   ProteinModelPortal; C4YJ78; -.
DR   STRING; C4YJ78; -.
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; CANAW_2.PE106; -.
KW   EEQ45562.100008510fold_1320000031;
KW   hypothetical protein;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus; Reference proteome.
SQ   SEQUENCE   416 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTTTRTLQA IKFDRDNIKL EILDQLLLPY STSYIPINNI EDAFKAIKLM QVRGAPAIAI
     VGAFSVVVEV SNYLKQSDSN QKTIKNLNDS LNYLITSRPT AVNLANALND IKQLLQKYNE
     TDIIDEKIYQ QIYDYAITLY DEDLANNKKI GENGLKYIID TLTEQNFKGP FSIITICNTG
     SLATSGHGTA LGIIRSTYQA LQKNNSKQDF WLDHIYPCET RPYNQGAKLT TYELDYEQIP
     FTLICDNMVS SLINTLSDDN KKPIKTDQSA PVKFIIVGAD RIVENGDTAN KIGTFQLSTI
     ANFFNTNRFN TTATATNKQI KFIVAAPKTT IDLNTKTGDD IVIEERPANE LTTLVGPLLN
     ESGKVGEKLT VGIATPGISV WNPAFDVTPH ELIDSIVTED PHVFTKDKNG EFNLIK
//

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