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

4 structures for O58035

Entry ID Method Resolution Chain Position Source
2ZZE X-ray 216 A A/B 1-752 PDB
2ZZF X-ray 270 A A 1-752 PDB
2ZZG X-ray 310 A A/B 1-752 PDB
AF-O58035-F1 Predicted AlphaFoldDB

No variants for O58035

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O58035

No associated diseases with O58035

4 regional properties for O58035

Type Name Position InterPro Accession
domain DHHA1 domain 784 - 913 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 704 - 747 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 61 - 605 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 57 - 760 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.

5 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).
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.
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

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
MEFIMKTRMF EEEGWIRKKC KVCGKPFWTL DPDRETCGDP PCDEYQFIGK PGIPRKYTLD
70 80 90 100 110 120
EMREKFLRFF EKHEIYPHGR VKRYPVLPRW RDDVLLVGAS IMDFQPWVIS GEADPPANPL
130 140 150 160 170 180
VISQPSIRFT DIDNVGITGR HFTIFEMMAH HAFNYPGKPI YWMDETVELA FEFFTKELKM
190 200 210 220 230 240
KPEDITFKEN PWAGGGNAGP AFEVLYRGLE VATLVFMQYK KAPENAPQDQ VVVIKGEKYI
250 260 270 280 290 300
PMETKVVDTG YGLERLVWMS QGTPTAYDAV LGYVVEPLKK MAGIEKIDEK ILMENSRLAG
310 320 330 340 350 360
MFDIEDLGDL RYLREQVAKR VGITVEELEK AIRPYELIYA IADHTKALTF MLADGVVPSN
370 380 390 400 410 420
VKAGYLARLL IRKSIRHLRE LGLEVPLSEI VALHIKELHK TFPEFKEMED IILEMIELEE
430 440 450 460 470 480
KKYAETLRRG SDLVRREIAK LKKKGIKEIP VEKLVTFYES HGLTPEIVKE IAEKEGVKVN
490 500 510 520 530 540
IPDNFYSMVA KEAERTKEEK GEELVDFELL KDLPDTRRLY YEDPFMKEFD AKVLRVIKDW
550 560 570 580 590 600
VILDATAFYP EGGGQPYDTG VLIVNGREVK VTNVQKVGKV IIHKVEDPGA FKEGMIVHGK
610 620 630 640 650 660
IDWKRRIQHM RHHTGTHVLM GALVRVLGRH VWQAGSQLTT DWARLDISHY KRISEEELKE
670 680 690 700 710 720
IEMLANRIVM EDRKVTWEWL PRTTAEQKYG FRLYQGGVVP GREIRVVKIE DWDVQACGGT
730 740 750 760 770 780
HLPSTGLVGP IKILRTERIQ DGVERIIFAC GEAAIREWQK ERDLLKKASN VLRVPPEKLP
790 800 810 820 830 840
ETAERFFNEW KEARKEVDKL KKELARLLVY ELESKMQKIG SIEFIGEVVE GSMEDLRELV
850 860 870 880 890 900
EKLKKPKRVV VLISRDGYFA VSVGSEVGVE ANELAKKITL IAGGGGGGRR DIAQGKVKDI
910
SKAKDVIESI KSMFS