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 Q9JJL8

Entry ID Method Resolution Chain Position Source
AF-Q9JJL8-F1 Predicted AlphaFoldDB

26 variants for Q9JJL8

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388885653 12 F>V No EVA
rs223730991 25 V>M No EVA
rs3388882545 27 S>I No EVA
rs3388896802 32 R>W No EVA
rs246256556 60 M>L No EVA
rs3388893002 73 S>Y No EVA
rs212438917 116 A>S No EVA
rs3388898047 130 Q>* No EVA
rs3388890312 138 L>M No EVA
rs3388898834 148 Q>* No EVA
rs3388885707 182 D>N No EVA
rs3388854120 188 V>M No EVA
rs3388895194 191 V>L No EVA
rs3388873857 211 K>I No EVA
rs47185959 253 R>K No EVA
rs3397634389 262 D>V No EVA
rs3397305352 264 L>Q No EVA
rs3397724550 265 R>G No EVA
rs3388890452 267 A>V No EVA
rs244040233 274 M>I No EVA
rs3388892933 314 A>G No EVA
rs3388896706 336 G>V No EVA
rs3388898848 360 G>E No EVA
rs3388892983 362 E>G No EVA
rs3388885633 385 H>Y No EVA
rs3388876647 508 K>M No EVA

No associated diseases with Q9JJL8

4 regional properties for Q9JJL8

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 291 - 468 IPR002314
domain Aminoacyl-tRNA synthetase, class II 202 - 478 IPR006195
domain Serine-tRNA synthetase, type1, N-terminal 59 - 172 IPR015866
domain Serine-tRNA ligase catalytic core domain 185 - 485 IPR033729

Functions

Description
EC Number 6.1.1.11 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
serine-tRNA ligase activity Catalysis of the reaction: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).
tRNA binding Binding to a transfer RNA.

3 GO annotations of biological process

Name Definition
mitochondrial seryl-tRNA aminoacylation The process of coupling serine to seryl-tRNA in a mitochondrion, catalyzed by seryl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA.
selenocysteinyl-tRNA(Sec) biosynthetic process The chemical reactions and pathways resulting in the formation of selenocysteinyl-tRNA(Sec). This process occurs through the following steps: a unique serine-tRNA with a UGA recognizing anticodon is first aminoacylated with serine; this is then phosphorylated by phosphoseryl-tRNA
seryl-tRNA aminoacylation The process of coupling serine to seryl-tRNA, catalyzed by seryl-tRNA synthetase. The seryl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a serine-accetping tRNA.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9N0F3 SARS2 Serine--tRNA ligase, mitochondrial Bos taurus (Bovine) PR
Q9NP81 SARS2 Serine--tRNA ligase, mitochondrial Homo sapiens (Human) PR
10 20 30 40 50 60
MAASMARLWW PFLARQGLRS RGRCVCSQNP RRSFATEKRV RNLLYEHARE GYSELPYLDM
70 80 90 100 110 120
ESVCACPEKA ARSLELRKGE LRPADLPAII STWQELRQLR EQIRSLEAEK EAVAEAVRAL
130 140 150 160 170 180
LANQDSDQVQ KDPQYQGLRA RGREIRKQLT PLYPQETQLE EQLYQQALRL PNQTHPDTPV
190 200 210 220 230 240
GDESQARVVR VVGEKPAFSF QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH
250 260 270 280 290 300
GLVNFTLSKL VSRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPSR FEDLNLAGTA
310 320 330 340 350 360
EVGLAGYFMD HSVAFRDLPV RMVCASTCYR AETDTGKEPW GLYRVHHFTK VEMFGVTGPG
370 380 390 400 410 420
LEQSSQLLDE FLSLQVEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRYGEVT
430 440 450 460 470 480
SASNCTDFQS RRLYIMFETE TGELQFAHTV NATACAVPRV LIALLESNQQ KDGSVLVPAA
490 500 510
LQPYLGTDRI TAPTHVPLQY IGPNQPQKPR LPGQSATR