Q7V436
Gene name |
argJ |
Protein name |
Arginine biosynthesis bifunctional protein ArgJ |
Names |
|
Species |
Prochlorococcus marinus (strain MIT 9313) |
KEGG Pathway |
pmt:PMT_2135 |
EC number |
2.3.1.1: Transferring groups other than amino-acyl groups |
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 Q7V436
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7V436-F1 | Predicted | AlphaFoldDB |
No variants for Q7V436
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7V436 | |||||
No associated diseases with Q7V436
4 regional properties for Q7V436
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 129 - 138 | IPR001412 |
| domain | Arginyl tRNA synthetase N-terminal domain | 5 - 90 | IPR005148 |
| domain | DALR anticodon binding | 450 - 570 | IPR008909 |
| domain | Arginyl-tRNA synthetase, catalytic core domain | 122 - 414 | IPR035684 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.1 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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 |
|---|---|
| acetyl-CoA:L-glutamate N-acetyltransferase activity | Catalysis of the reaction: L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+). |
| glutamate N-acetyltransferase activity | Catalysis of the reaction: N(2)-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate + L-ornithine. |
| methione N-acyltransferase activity | Catalysis of the reaction: L-methionine + acetyl-CoA = N-acetyl-L-methionine + coenzyme A + H+. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| arginine biosynthetic process | The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALVEDVFSL | SPKAVSSALA | SLWRPIQGGV | SAPLGFQAAG | ITAGLKDSGK | PDLALLLAPE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GAVCAGMFTT | SLVRAACVDL | CVDHLQACGG | KARAVLINSG | QANACTGERG | WLDSLRASQA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LAGRLELPVE | QVLICSTGVI | GVPIPMDTLL | AGLDPLVEAL | SDEGGAEAAG | AILTTDLVEK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QFALEAELGG | RSVRIGGMAK | GSGMIHPDMA | TMLGYLSCDV | GVEVDAWQAM | LKRVVDCSFN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AMTVDGDTST | NDSCLAFAAG | ELLEQEHLQA | LEAGLLVAAQ | QLAKAIARDG | EGATCLLEVQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VEGVVGDVEA | RRIARTVCGS | SLVKTAVHGR | DPNWGRIVAA | AGCAGVPFDP | AAVALWLGPH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QLMEFGEPLP | FDRLAASRYM | QERVDGSYLC | DDTVQIRLVV | GDGSGDGMAW | GCDLSDQYVR |
| INADYTT |