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 Q2LTR7

Entry ID Method Resolution Chain Position Source
AF-Q2LTR7-F1 Predicted AlphaFoldDB

No variants for Q2LTR7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2LTR7

No associated diseases with Q2LTR7

6 regional properties for Q2LTR7

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 95 - 457 IPR002314
domain Anticodon-binding 473 - 563 IPR004154
domain Aminoacyl-tRNA synthetase, class II 38 - 466 IPR006195
domain YbaK/aminoacyl-tRNA synthetase-associated domain 259 - 377 IPR007214
domain Prokaryote proline-tRNA ligase core domain 17 - 456 IPR033730
domain Proline--tRNA ligase, anticodon binding domain 471 - 564 IPR044140

Functions

Description
EC Number 6.1.1.15 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.

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.
proline-tRNA ligase activity Catalysis of the reaction: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

1 GO annotations of biological process

Name Definition
prolyl-tRNA aminoacylation The process of coupling proline to prolyl-tRNA, catalyzed by prolyl-tRNA synthetase. The prolyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a methionine-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
MRYSEMFLPT EREIPSDAEV VSHQLMLRAG MIRKLSAGIY SYLPLGYRVL RKVEQIIREE
70 80 90 100 110 120
MNRAGAQEVY LPMVQPAELW QESGRWEHYG KELLRFRDRH DREYCLGPTH EEVITDLVRH
130 140 150 160 170 180
EIKTYRQLPK NLYQIQTKFR DEIRPRFGVM RGREFGMKDA YSFDADEEGA EISYQKMFEA
190 200 210 220 230 240
YKRIFARCGL RFRPVEADSG TIGGSFSHEF MVMADSGEDG LVFCATCSYA ANLEKAEVHP
250 260 270 280 290 300
PEKMEISNDE MLLLTEVHTP NARTIDEVCA FLNVTPQEIV KTLIFNADGN PVAVLVRGDE
310 320 330 340 350 360
EVNEIKVKNY LKCQELELAM DDMIQDVTGA PRGFAGAIGI KKARILADYS LLNMKNVVMG
370 380 390 400 410 420
ANKEDYHLRN VNEGRDFQIS AFADLKVARE TDSCPRCQGA LKFARGIEVG HVFKLGTKYS
430 440 450 460 470 480
KAMGASYLDK NGKEQIMIMG CYGIGTGRTV AACIEQNHDE NGIVWPMPIS PYQVIITPVN
490 500 510 520 530 540
MNDKALAETA ERLYESLAGK GAEVLLDDRD ERAGVKFKDA DLIGIPIRVT VGPKKLAEGK
550 560 570
VEVRLRDTGE TSDVQVDSVE KMILRVIEGK MSESYLIF