B0S104
Gene name |
alaS |
Protein name |
Alanine--tRNA ligase |
Names |
Alanyl-tRNA synthetase, AlaRS |
Species |
Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508) (Peptostreptococcus magnus) |
KEGG Pathway |
fma:FMG_0626 |
EC number |
6.1.1.7: 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 B0S104
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B0S104-F1 | Predicted | AlphaFoldDB |
No variants for B0S104
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B0S104 | |||||
No associated diseases with B0S104
5 regional properties for B0S104
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Forkhead-associated (FHA) domain | 536 - 588 | IPR000253 |
| domain | DHHA1 domain | 732 - 862 | IPR003156 |
| domain | Threonyl/alanyl tRNA synthetase, SAD | 647 - 690 | IPR012947 |
| domain | Alanyl-tRNA synthetase, class IIc, N-terminal | 8 - 548 | IPR018164 |
| domain | Alanyl-tRNA synthetase, class IIc, core domain | 4 - 703 | IPR018165 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.7 | 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| alanine-tRNA ligase activity | Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| tRNA binding | Binding to a transfer RNA. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| alanyl-tRNA aminoacylation | The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKNYGLNEIR | KKFLDYFGER | GHLVIKSFPL | IPQDDKSLLL | INAGMAPLKK | YFTGEKKLKK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DRATSSQRCI | RTADIDEVGK | TQRHGTFFEM | LGNFSFGDYF | KREAITWAWD | FLTNELEVPK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DILWVSVYEE | DEEAYNIWVN | EVGISPERVV | KLGKADNFWE | LDQGPCGPCS | EIHVDRGFEF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DPREDAKPGD | EGERFLEVWN | LVFTQFNKTA | DGKYERIAHP | NIDTGMGLER | ITMVLENADN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IFEIGLVKDI | IKTIEEISGV | KYKENHKNDV | SIRIIADHVR | AMTFLIYDGV | IPSNEQRGYV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LRRLIRRACR | HGKLLGINDS | FIEKVIDSCI | KVYESGYPEL | KEDRDRIVKI | ANAEEKKFQE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TLDLGLNILD | SMLKETDSDV | FSGENAFKLY | DTYGFPIDLT | KELVGEVNKT | VDEVQFKKLM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EEQKERARGS | RNESNMGWSS | DKKYGEELPE | TKFDGYNSLK | DESKVIEIYG | EDENNLKAGQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| MGIIVLDCTT | FYGEGGGQVG | DKGIIYNDNF | KAEVYDTKKT | GKKVFLHYVK | VTEGSLHVGD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KVTIEVDELN | RRDIMKNHSA | THLLHQALKD | VVGDHVNQAG | SYVDGERLRF | DITHFEAVSK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EQLEKVEQIV | NDKIALGIPV | KIDEMSLEES | QSIGARGLFE | DKYQDVVRVV | QMGDYSIELC |
| 670 | 680 | 690 | 700 | 710 | 720 |
| GGTHVKTTSD | IQMLKIISES | SVAAGVRRIE | AITGRAVYKY | LKERDRLIDN | VKHSLKASNE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DEITRRIEMN | TEEIKGLKKK | LKDITNKDLS | SNVDSVINDA | VEVNGTKVCT | FELSGLDNNS |
| 790 | 800 | 810 | 820 | 830 | 840 |
| FRDFGENIKS | KLEDGVVILA | NSDESKVSFI | ALVTDSSVKK | GVFAGDIVRE | VAKVCGGNGG |
| 850 | 860 | 870 | |||
| GRKDFAQAGA | KDSSKVDEAL | QKGIETVKSK | LNA |