Search Results
Overview
| Uniprot ID | F1SP18 |
|---|---|
| Protein Name | threonine--tRNA ligase |
| Gene Name | TARS1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 192 | CKKIIKEKQAFERLE |
| 222 | KCRILNEKVNTPTTT |
| 258 | IKTLKIHKNSSTYWE |
| 292 | KMLKEWEKFQEEAKN |
| 298 | EKFQEEAKNRDHRKI |
| 528 | PKIDIQIKDAIGRYH |
| 562 | VSPDGDDKKRPVIIH |
| 660 | LVVGEKEKSSGTVNI |
Function
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage
Protein Sequence
10
MSEEKAHSPS
20
GKMGGEEKPV
30
SGQSRLNPWP
40
EYINTRLEMY
50
NKLKAEHDSI
60
LAEKAEKDSK
70
PIKVTLPDGK
80
QVDAESWKTT
90
PYQIACGISQ
100
GLADNTVVAK
110
VNKVVWDLDR
120
PLEEDCTLEL
130
LKFEDEEAQA
140
VYWHSSAHIM
150
GEAMERVYGG
160
CLCYGPPIEN
170
GFYYDMYLEE
180
GGVSSNDFSS
190
LEALCKKIIK
200
EKQAFERLEI
210
KKETLLEMFK
220
YNKFKCRILN
230
EKVNTPTTTV
240
YRCGPLIDLC
250
RGPHVRHTGK
260
IKTLKIHKNS
270
STYWEGKADM
280
ETLQRIYGIS
290
FPDPKMLKEW
300
EKFQEEAKNR
310
DHRKIGRDQE
320
LYFFHELSPG
330
SCFFLPKGAY
340
IYNTLIDFIR
350
SEYRKRGFQE
360
VVTPNIYNSR
370
LWVTSGHWQH
380
YSDNMFSFEV
390
EKELFALKPM
400
NCPGHCLMFD
410
HRPRSWRELP
420
LRIADFGVLH
430
RNELSGALTG
440
LTRVRRFQQD
450
DAHIFCAMEQ
460
IEDEIKGCLD
470
FLRTVYSIFG
480
FSFKLNLSTR
490
PEKFLGDIEV
500
WNQAEKQLEN
510
SLNEFGEKWE
520
LNPGDGAFYG
530
PKIDIQIKDA
540
IGRYHQCATI
550
QLDFQLPIRF
560
NLTFVSPDGD
570
DKKRPVIIHR
580
AILGSVERMI
590
AILTENYGGK
600
WPFWLSPRQV
610
MVVPVGPTCD
620
EYAQKVQQQF
630
HDAKFMVDID
640
LDPGCTLNKK
650
IRNAQLAQYN
660
FILVVGEKEK
670
SSGTVNIRTR
680
DNKVHGERTI
690
SETVGRLEQL
700
RQSRSKQAEE
EF
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0004829 | threonine-tRNA ligase activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006435 | threonyl-tRNA aminoacylation |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.