Q7V287

PR
Gene name
thrS
Protein name
Threonine--tRNA ligase
Names
Threonyl-tRNA synthetase, ThrRS
Species
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
KEGG Pathway
pmm:PMM0597
EC number
6.1.1.3: 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)

205-275 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q7V287

Entry ID Method Resolution Chain Position Source
AF-Q7V287-F1 Predicted AlphaFoldDB

No variants for Q7V287

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7V287

No associated diseases with Q7V287

6 regional properties for Q7V287

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 288 - 491 IPR002314
domain Anticodon-binding 512 - 601 IPR004154
domain Aminoacyl-tRNA synthetase, class II 209 - 505 IPR006195
domain Threonyl-tRNA synthetase, editing domain, archaea 1 - 139 IPR015011
domain Threonine-tRNA ligase catalytic core domain 206 - 510 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 510 - 600 IPR047246

Functions

Description
EC Number 6.1.1.3 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
threonine-tRNA ligase activity Catalysis of the reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).
tRNA binding Binding to a transfer RNA.

1 GO annotations of biological process

Name Definition
threonyl-tRNA aminoacylation The process of coupling threonine to threonyl-tRNA, catalyzed by threonyl-tRNA synthetase. The threonyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a threonine-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
MPEITLPDGS KKVFEKPVTI QEIAQSIGSG LAKATIAGKV NDVLFDATLP IDNDSKVVII
70 80 90 100 110 120
TSRDKDGIEI IRHSFAHLIG HAVKQLYPNI KMAIGPVIDN GFYYDIFSEY RFTPEDLIKI
130 140 150 160 170 180
ENRINNLIKK NYDVEILQVT KKEAIKTFQE RDETFKLRII EEIPDEGLIN LYKHEEYIDM
190 200 210 220 230 240
CRGPHVPNTC HLRHFKLLKL SGSYWRGNSE NESLQRIYGT AWAKEKELND YLKRIEEAEK
250 260 270 280 290 300
RDHRKLGKKH SLFHIQEESP GMIFWHPNGW TIYQVLEKYV REILNKNDYL EIKTPQAVDK
310 320 330 340 350 360
SLWEKSGHWD KFREDMFTTA SENRTYAIKP MNCPCHIQVF NQGLKSYKDL PIRLAEFGSC
370 380 390 400 410 420
HRNEPSGALH GLMRVRNFTQ DDAHIFCTEE QIQAEVSTFI DLVFEVYKTF GFDEIIIKLS
430 440 450 460 470 480
TRPEKRVGSE NIWDKSEEAL MKALDNKSLK WVLQPGEGAF YGPKIEFSLK DCLDRVWQCG
490 500 510 520 530 540
TIQVDFSMPI RLDATYIDLN NEKRNPVMLH RAILGSFERF IGILIEQYEA KFPIWLAPYQ
550 560 570 580 590 600
IILLSITDRN IEKCLKFNQL INSKGYRSKV DIRNEKIGYK IREATIGRIP LIAVIGDKEE
610 620 630
QFDSVALRAL DGKNLGIFKL DDLYKLMNNL IEKKGRTE