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 Q99KK9

Entry ID Method Resolution Chain Position Source
AF-Q99KK9-F1 Predicted AlphaFoldDB

21 variants for Q99KK9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs252772318 11 A>V No EVA
rs3389442722 33 S>I No EVA
rs3389491227 60 K>Q No EVA
rs3389503463 86 R>G No EVA
rs3389475997 97 F>I No EVA
rs3389496181 157 R>M No EVA
rs3389442655 252 E>K No EVA
rs3389475996 267 I>V No EVA
rs232437923 270 F>Y No EVA
rs3389495803 284 F>Y No EVA
rs3389491226 288 R>K No EVA
rs258762666 300 G>R No EVA
rs3389489403 308 Y>N No EVA
rs3389496160 330 Y>H No EVA
rs3406542888 333 G>AS* No EVA
rs3389499971 436 I>F No EVA
rs3389405632 443 K>R No EVA
rs3389488505 447 K>R No EVA
rs3389489442 454 Y>C No EVA
rs3389510723 467 G>C No EVA
rs13489285 494 L>F No EVA

No associated diseases with Q99KK9

6 regional properties for Q99KK9

Type Name Position InterPro Accession
domain SNF2, N-terminal 243 - 721 IPR000330
domain Helicase, C-terminal 834 - 996 IPR001650
domain Zinc finger, RING-type 760 - 801 IPR001841
domain Helicase superfamily 1/2, ATP-binding domain 236 - 614 IPR014001
domain HIRAN domain 60 - 154 IPR014905
conserved_site Zinc finger, RING-type, conserved site 775 - 784 IPR017907

Functions

Description
EC Number 6.1.1.21 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.
histidine-tRNA ligase activity Catalysis of the reaction: ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His).
identical protein binding Binding to an identical protein or proteins.

1 GO annotations of biological process

Name Definition
histidyl-tRNA aminoacylation The process of coupling histidine to histidyl-tRNA, catalyzed by histidyl-tRNA synthetase. The histidyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3''-OH group of a histidine-accetping tRNA.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q2KI84 HARS1 Histidine--tRNA ligase, cytoplasmic Bos taurus (Bovine) PR
A5D7V9 HARS2 Histidine--tRNA ligase, mitochondrial Bos taurus (Bovine) PR
P12081 HARS1 Histidine--tRNA ligase, cytoplasmic Homo sapiens (Human) PR
P49590 HARS2 Histidine--tRNA ligase, mitochondrial Homo sapiens (Human) PR
Q61035 Hars1 Histidine--tRNA ligase, cytoplasmic Mus musculus (Mouse) PR
P93422 Os09g0504400 Histidine--tRNA ligase, cytoplasmic Oryza sativa subsp japonica (Rice) PR
P34183 hars-1 Histidine--tRNA ligase Caenorhabditis elegans PR
F4IYF8 At3g02760 Histidine--tRNA ligase, cytoplasmic Arabidopsis thaliana (Mouse-ear cress) PR
O82413 At3g46100 Histidine--tRNA ligase, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MPHLGPLRRR AWAALLGQLL RPPSTVCTRG CHSQVAKAVL TSEQLKSHQE KPNFVIKVPK
70 80 90 100 110 120
GTRDLSPQQM VVREKILDKI ISCFKRHGAK GLDTPAFELK EMLTEKYEDN FGLMYDLKDQ
130 140 150 160 170 180
GGELLSLRYD LTVPFARYLA MNKLKKMKRY QVGKVWRRES PAIAQGRYRE FCQCDFDIAG
190 200 210 220 230 240
EFDPMIPDAE CLRIMCEILS GLQLGDFLIK VNDRRVVDGI FAVCGVPESK LRTICSSMDK
250 260 270 280 290 300
LDKMSWEGVR HEMVAKKGLA PEVADRIGDF VQYHGGISLV EDLFKDPRLS QSQLALQGLG
310 320 330 340 350 360
DLKLLFEYLR LFGIADKISL DLSLARGLDY YTGVIYEAVL LESPAQAGKE TLSVGSVAAG
370 380 390 400 410 420
GRYDNLVAQF DPKGHHVPCV GLSIGVERIF YLVEQKMKMS GEKVRTTETQ VFVATPQKNF
430 440 450 460 470 480
LQERLKIIAE LWDAGIKAEM LYKNNPKLLT QLHYCEKADI PLMVIIGEQE RNEGVIKLRS
490 500
VASREEVTIN RESLVAEIQK RLSES