B1LD99
Gene name |
ygfZ |
Protein name |
tRNA-modifying protein YgfZ |
Names |
|
Species |
Escherichia coli (strain SMS-3-5 / SECEC) |
KEGG Pathway |
ecm:EcSMS35_3031 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for B1LD99
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B1LD99-F1 | Predicted | AlphaFoldDB |
No variants for B1LD99
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B1LD99 | |||||
No associated diseases with B1LD99
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| folic acid binding | Binding to folic acid, pteroylglutamic acid. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| RNA modification | The covalent alteration of one or more nucleotides within an RNA molecule to produce an RNA molecule with a sequence that differs from that coded genetically. |
| tRNA processing | The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAFTPFPPRQ | PTASARLPLT | LMTLDDWALA | TITGADSEKY | MQGQVTADVS | QMTEDQHLLA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AHCDAKGKMW | SNLRLFRDGD | GFAWIERRSV | REPQLTELKK | YAVFSKVTIA | PDDERVLLGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AGFQARAALA | NLFSELPSKE | KQVVKEGATT | LLWFEHPAER | FLIVTDEATA | NMLTDKLRGE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AELNNSQQWL | ALNIEAGFPV | IDAANSGQFI | PQATNLQALG | GISFKKGCYT | GQEMVARAKF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RGANKRALWL | LTGSASRLPE | AGEDLELKMG | ENWRRTGTVL | AAVKLEDGQV | VVQVVMNNDM |
| 310 | 320 | ||||
| EPDSIFRVRD | DANTLRIEPL | PYSLEE |