Q5FA25
Gene name |
prfC |
Protein name |
Peptide chain release factor 3 |
Names |
RF-3 |
Species |
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) |
KEGG Pathway |
ngo:NGO_0209 |
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 Q5FA25
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5FA25-F1 | Predicted | AlphaFoldDB |
No variants for Q5FA25
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5FA25 | |||||
No associated diseases with Q5FA25
6 regional properties for Q5FA25
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Translational (tr)-type GTP-binding domain | 10 - 278 | IPR000795 |
| domain | Translation elongation factor EFTu-like, domain 2 | 312 - 376 | IPR004161 |
| domain | Small GTP-binding protein domain | 16 - 160 | IPR005225 |
| conserved_site | Tr-type G domain, conserved site | 57 - 72 | IPR031157 |
| domain | Peptide chain release factor 3, C-terminal | 385 - 512 | IPR032090 |
| domain | Peptide chain release factor 3, GTP-binding domain | 11 - 277 | IPR041732 |
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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| translation release factor activity, codon specific | A translation release factor that is specific for one or more particular termination codons; acts at the ribosomal A-site and require polypeptidyl-tRNA at the P-site. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| regulation of translational termination | Any process that modulates the frequency, rate or extent of translational termination. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSQEILDQVR | RRRTFAIISH | PDAGKTTLTE | KLLLFSGAIQ | SAGTVKGKKT | GKFATSDWMD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IEKQRGISVA | SSVMQFDYKD | HTVNLLDTPG | HQDFSEDTYR | VLTAVDSALM | VIDAAKGVEA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QTIKLLNVCR | LRDTPIVTFM | NKYDREVRDS | LELLDEVEDI | LQIRCAPVTW | PIGMGKNFKG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VYHILNDEIY | LFEAGGERLP | HEFDIIKGIN | NPELEQRFPL | EIQQLRDEIE | LVQAASNEFN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LDEFLAGELT | PVFFGSAINN | FGIQEILNSL | IDWAPAPKPR | DATMRMVGPD | EPKFSGFIFK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IQANMDPKHR | DRIAFLRVCS | GKFERGMKMK | HLRINREIAA | SSVVTFMSHD | RELAEEAYAG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DIIGIPNHGN | IQIGDSFSEG | EQLAFTGIPF | FAPELFRSVR | IKNPLKIKQL | QKGLQQLGEE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GAVQVFKPMS | GADLILGAVG | VLQFEVVTSR | LANEYGVEAV | FDSASIWSAR | WVSCDDKKKL |
| 490 | 500 | 510 | 520 | 530 | |
| AEFEKANAGN | LAIDAGGNLA | YLAPNRVNLG | LTQERWPDIV | FHETREHSVK | L |