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 Q9K1Q0

Entry ID Method Resolution Chain Position Source
AF-Q9K1Q0-F1 Predicted AlphaFoldDB

No variants for Q9K1Q0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9K1Q0

No associated diseases with Q9K1Q0

1 regional properties for Q9K1Q0

Type Name Position InterPro Accession
domain NAD-dependent epimerase/dehydratase 2 - 246 IPR001509

Functions

Description
EC Number 6.1.1.10 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.
methionine-tRNA ligase activity Catalysis of the reaction: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).
tRNA binding Binding to a transfer RNA.

1 GO annotations of biological process

Name Definition
methionyl-tRNA aminoacylation The process of coupling methionine to methionyl-tRNA, catalyzed by methionyl-tRNA synthetase. The methionyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a methionine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTRKILVTSA LPYANGSIHL GHMVEHIQTD VWVRFQKLRG HACHYCCADD THGTPVMLAA
70 80 90 100 110 120
QKQGIAPEDM IAKVREEHLA DFTGFFIGYD NYYSTHSPEN KQFSQDIYRA LKANGKIESR
130 140 150 160 170 180
VIEQLFDPEK QMFLPDRFVK GECPKCHAQD QYGDNCEVCG TTYSPTELIN PYSAVSGTKP
190 200 210 220 230 240
ELRESEHFFF KLGECADFLK AWTSGNNPHD GKPHLQAEAL NKMKEWLGEG EETTLSDWDI
250 260 270 280 290 300
SRDAPYFGFE IPDAPGKYFY VWLDAPVGYM ASFKNLCDRI GVDFDEYFKA DSQTEMYHFI
310 320 330 340 350 360
GKDILYFHAL FWPAMLHFSG HRAPTGVYAH GFLTVDGQKM SKSRGTFITA KSYLEQGLNP
370 380 390 400 410 420
EWMRYYIAAK LNSKIEDIDL NLQDFISRVN SDLVGKYVNI AARASGFIAK RFEGRLKDVA
430 440 450 460 470 480
DSELLAKLTA QSEAIAECYE SREYAKALRD IMALADIVNE YVDANKPWEL AKQEGQDERL
490 500 510 520 530 540
HEVCSELINA FTMLTAYLAP VLPQTAANAA KFLNLEAITW ANTRDTLGKH AINKYEHLMQ
550 560 570 580 590 600
RVEQKQVDDL IEANKQSIAA AAAPAAEEGK YEKVAEQASF DDFMKIDMRV AKVLNCEAVE
610 620 630 640 650 660
GSTKLLKFDL DFGFEKRIIF SGIAASYPNP AELNGRMVIA VANFAPRKMA KFGVSEGMIL
670 680
SAATADGKLK LLDVDTGAQP GDKVG