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LACF3:FMT
Contents
Species (Taxon ID) | Lactobacillus fermentum (strain NBRC 3956 / LMG 18251). (334390) | |
Gene Name(s) | fmt (ECO:0000255 with HAMAP-Rule:MF_00182) | |
Protein Name(s) | Methionyl-tRNA formyltransferase (ECO:0000255 with HAMAP-Rule:MF_00182) | |
External Links | ||
UniProt | B2GD55 | |
EMBL | AP008937 | |
RefSeq | YP_001844067.1 | |
ProteinModelPortal | B2GD55 | |
STRING | 334390.LAF_1251 | |
EnsemblBacteria | BAG27587 | |
GeneID | 6232119 | |
KEGG | lfe:LAF_1251 | |
PATRIC | 22226780 | |
eggNOG | COG0223 | |
HOGENOM | HOG000261177 | |
KO | K00604 | |
OMA | KVWQSRV | |
OrthoDB | EOG6B09WV | |
BioCyc | LFER334390:GJ2S-1298-MONOMER | |
Proteomes | UP000001697 | |
GO | GO:0004479 GO:0008168 | |
Gene3D | 3.10.25.10 3.40.50.170 | |
HAMAP | MF_00182 | |
InterPro | IPR005794 IPR005793 IPR002376 IPR011034 IPR001555 IPR015518 | |
PANTHER | PTHR11138 | |
Pfam | PF02911 PF00551 | |
SUPFAM | SSF50486 SSF53328 | |
TIGRFAMs | TIGR00460 | |
PROSITE | PS00373 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0009058 |
biosynthetic process |
ECO:0000315 |
P |
The formylation of initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for the initiation of protein synthesis in eubacteria. |
complete | |||||
involved_in |
GO:0006413 |
translational initiation |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004479 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006413 |
translational initiation |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004479 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006413 |
translational initiation |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004479 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004479 |
methionyl-tRNA formyltransferase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009058 |
biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR002376 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0016742 |
hydroxymethyl-, formyl- and related transferase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR002376 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0071951 |
conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004479 |
methionyl-tRNA formyltransferase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019988 |
charged-tRNA amino acid modification |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001456 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0004479 |
methionyl-tRNA formyltransferase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001456 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006412 |
translation |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Gite, S et al. (2000) Escherichia coli methionyl-tRNA formyltransferase: role of amino acids conserved in the linker region and in the C-terminal domain on the specific recognition of the initiator tRNA. Biochemistry 39 2218-26 PubMed GONUTS page