Q9I0A4
Gene name |
pheT |
Protein name |
Phenylalanine--tRNA ligase beta subunit |
Names |
Phenylalanyl-tRNA synthetase beta subunit, PheRS |
Species |
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
KEGG Pathway |
pae:PA2739 |
EC number |
6.1.1.20: 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
No variants for Q9I0A4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9I0A4 | |||||
No associated diseases with Q9I0A4
6 regional properties for Q9I0A4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | tRNA-binding domain | 39 - 147 | IPR002547 |
| domain | Ferrodoxin-fold anticodon-binding domain | 698 - 791 | IPR005121 |
| domain | B3/B4 tRNA-binding domain | 211 - 384 | IPR005146 |
| domain | tRNA synthetase, B5-domain | 400 - 476 | IPR005147 |
| domain | Phenylalanly tRNA synthetase, tRNA-binding-domain | 45 - 146 | IPR033714 |
| domain | Phenylalanyl tRNA synthetase beta chain, core domain | 474 - 683 | IPR041616 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.20 | 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 |
|---|---|
| phenylalanine-tRNA ligase complex | An enzyme complex that catalyzes the ligation of phenylalanine to tRNA(Phe), forming L-phenylalanyl-tRNA(Phe). |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| phenylalanine-tRNA ligase activity | Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). |
| tRNA binding | Binding to a transfer RNA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| phenylalanyl-tRNA aminoacylation | The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting 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 |
| MKFSEKWLRS | WANPQVSHDE | LVARLSMVGL | EVDADLPVAG | AFSGVVVGEV | LSTEQHPDAD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KLRVCQVSNG | SETFQVVCGA | PNVRAGLKIP | FAMIGAELPD | DFKIKKAKLR | GVESFGMLCS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AKELQISEEN | AGLLELPADA | PVGQDVRTYL | ELADYTIEVG | LTPNRGDCLS | LAGLAREVSA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IYDVPLAPVA | VDAVAAQHDE | TRPVELAAPA | ACPRYLGRVI | RNVDLSRPTP | LWMVERLRRS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DIRSIDPVVD | VTNYVMIELG | QPMHAFDLAE | INGGVRVRMA | EDGEKLVLLD | GQEITLRADT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LVIADHQRAL | AIAGVMGGEH | SGVSDSTRDL | FLEAAFFDTI | ALAGKARSYG | LHTDSSHRFE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RGVDSQLARK | AMERATRLIL | DIVGGEPGPI | VEQVSEAHLP | KVAPITLRAE | RVTQMLGMPL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DAAEIVRLLQ | ALELTVVADG | EGQWSVGVPS | HRFDISLEVD | LIEELARLYG | YNRLPVRYPQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ARLAPNNKPE | ARAALPLLRR | LLVARGYQEA | ITFSFIDPAL | FELFDPGTQP | LTLANPISAD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| MAAMRSSLWP | GLVKALQHNL | NRQQSRVRLF | ESGLRFVGQL | EGLKQEAMLA | GAICGKRLPE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GWANGRDGVD | FFDAKADVEA | VLASAGALGD | FSFVPGEHPA | LHPGQTARIE | REGRLVGYLG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ALHPELAKKL | DLEQPVFLFE | LLLAEVVDGH | LPKFRELSRF | PEVRRDLALL | VDQDVPAQDI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LTQIRAAAGE | WLTDLRLFDV | YHGKGIDPHR | KSLAVGLTWQ | HPSRTLNDDE | VNSTTQNIVT |
| 790 | |||||
| SLEERFNATL | RK |