B2HIA2
Gene name |
leuS |
Protein name |
Leucine--tRNA ligase |
Names |
Leucyl-tRNA synthetase, LeuRS |
Species |
Mycobacterium marinum (strain ATCC BAA-535 / M) |
KEGG Pathway |
mmi:MMAR_0057 |
EC number |
6.1.1.4: Ligases forming aminoacyl-tRNA and related compounds |
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 B2HIA2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B2HIA2-F1 | Predicted | AlphaFoldDB |
No variants for B2HIA2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B2HIA2 | |||||
No associated diseases with B2HIA2
4 regional properties for B2HIA2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 88 - 98 | IPR001412 |
| domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | 824 - 939 | IPR013155 |
| domain | Methionyl/Leucyl tRNA synthetase | 83 - 190 | IPR015413 |
| domain | Leucyl-tRNA synthetase, editing domain | 313 - 509 | IPR025709 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.4 | Ligases forming aminoacyl-tRNA and related compounds |
| 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 |
|---|---|
| aminoacyl-tRNA editing activity | The hydrolysis of an incorrectly aminoacylated tRNA. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| leucine-tRNA ligase activity | Catalysis of the reaction: L-leucine + ATP + tRNA(Leu) = AMP + diphosphate + 2 H(+) + Leu-tRNA(Leu). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| leucyl-tRNA aminoacylation | The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTESPTTTPG | STSGAPSGVP | SGVNDAESDA | PRHRYTAELA | AGVERTWQQN | WARLGTFNVP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NPVGSLAPSD | GSPVPEDKLF | VQDMFPYPSG | EGLHVGHPLG | YIATDVFARY | HRMKGRNVLH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ALGFDAFGLP | AEQYAVQTGT | HPRTRTEANV | VNFRRQLGRL | GLGHDSRRSF | STTDVEFYKW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TQWIFLQIYN | AWFDAAANKA | RPISELVAEF | DSGARSLVDG | RDWSTLSAGE | RADVIDDHRL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VYRADSMVNW | CPGLGTVLAN | EEVTSDGRSD | RGNFPVFRKR | LRQWMMRITA | YSDRLLDDLD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VLDWPDQVKT | MQRNWIGRST | GASALFTATR | SNGETVGLEV | FTTRPDTLFG | ATYLVLAPEH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DLVDDLVGAG | WPAGVDPLWT | GGGATPAEAV | AAYRRAIAAK | SDLERQESKE | KTGVFLGSHA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| INPATGQPVP | IFIADYVLAG | YGTGAIMAVP | GHDQRDWDFA | RALGLPVVEV | IAGGDISQAA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YTGDGVLVNS | GFLDGMSVGE | AKQAITARLE | SDGHGQARIE | FKLRDWLFAR | QRYWGEPFPI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VYDADGRPHA | LDESALPVEL | PDVPDYSPVL | FDPDDANSEP | SPPLGKATEW | VHVELDLGDG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LKPYSRDTNV | MPQWAGSSWY | ELRYTDPHNA | DRFCAKENET | YWMGPRPAEH | GPDDPGGVDL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YVGGAEHAVL | HLLYARFWHK | VLYDLGHVSS | REPYRKLINQ | GYIQAFAYTD | ARGSYVPAEE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| VIERDGGFVY | PGADGEIEVF | QEFGKIGKSL | KNSISPDEIC | DDYGADTLRV | YEMSMGPIEA |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SRPWATKDVI | GAYRFLQRVW | RLVIDENTGE | ILVADTPAEL | DTDTLRALHR | AIAGVAEDYA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| ALRNNTAVAK | LIEYTNFLTK | RHRDAVPRAA | IEPLVLMVAP | LAPHLAEELW | QRLGHTTSLA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| HGPFPAADPA | YLIDDTVEYP | VQVNGKVRGR | VVVAADADDD | AVKAAALADE | KVQAFLAGAS |
| 970 | |||||
| PRKVIVVAGR | LVNLVV |