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 Q04EQ9

Entry ID Method Resolution Chain Position Source
AF-Q04EQ9-F1 Predicted AlphaFoldDB

No variants for Q04EQ9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q04EQ9

No associated diseases with Q04EQ9

3 regional properties for Q04EQ9

Type Name Position InterPro Accession
domain Threonyl/alanyl tRNA synthetase, SAD 685 - 728 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 26 - 585 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 22 - 741 IPR018165

Functions

Description
EC Number 6.1.1.7 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
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.

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
MKKLNSAQIR QMFLDFFQSK GHKIEPSQSL IPQDDPSLLW INSGVATLKK YFDGSVIPDN
70 80 90 100 110 120
PRITNAQKSI RTNDIENVGH TARHHTFFEM LGNFSVGDYF KKEAIPWAWE LLTSPEWYGI
130 140 150 160 170 180
EPEKLFITYY PRDTETKELW ESQADFVAGH TIPQDDNFWD IGEGPSGPDT EVFFDRGPKF
190 200 210 220 230 240
QNLPDNDPEM YPGGENERYL EIWNIVFSQF NHLPGLTDNS KYPELPHKNI DTGMGLERVV
250 260 270 280 290 300
SIFENAPTNF ETDLFLPIIR KVEQLSGKRY GKIKDEDVSF KVITDHIRAV TFAISDGALP
310 320 330 340 350 360
GNTGRGYVIR RLLRRAVMHG RKLEIEKPFL TQLVPIVGKI MEAYYPEILE NEDKIIPVIQ
370 380 390 400 410 420
SEEGRFNKTL TAGLNLLDDL IEKAHKDNAT QISGKDAFKL FDTYGFPLES TEEQAADAGL
430 440 450 460 470 480
TVDTTSFDKE MKDQQNRART AQGKLKTFGF QDEALMSLKV PSVYVGWKQS SVDDAKIAAI
490 500 510 520 530 540
IVDDQQVDDA KAGQKALLIF DKTPFYAEMG GQVADQGTVQ AANGKVLAQV TDVQNAPNKQ
550 560 570 580 590 600
HIHTAKLISD LKIGQKVNLR LDMHRHVAVS KNHTATHLLD QALRNVIAGN IHQAGSLVEP
610 620 630 640 650 660
DYLRFDFTHQ GPVPTETLDR IEDLVNQKIA DALPVSWIET DIESAKKLGA VAVFGEKYGK
670 680 690 700 710 720
KVRVVSIGDF NKEFDGGTHA KNTSELGLFK IVSESGIGAG TRRIEAVTGQ SAFKMLKNHE
730 740 750 760 770 780
KLLKKAAEFL SAQKLADVPD KIVDLQNNLK NVQKQVESLS DKAANVAADK IFEKTLEAGK
790 800 810 820 830 840
YSYIAAQIDN QTVDGLRKIV DEWRQRAVSD LIIIATNNNG KALLVAASAK PNEVKAGNVV
850 860 870 880
KAISPKIQGG GGGRPDFAQA GGKNPAGIAN ALASVSEYLE SLDQR