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 Q5LP30

Entry ID Method Resolution Chain Position Source
AF-Q5LP30-F1 Predicted AlphaFoldDB

No variants for Q5LP30

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5LP30

No associated diseases with Q5LP30

6 regional properties for Q5LP30

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 45 - 56 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 16 - 401 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 434 - 691 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 747 - 888 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 952 - 1016 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 700 - 835 IPR033705

Functions

Description
EC Number 6.1.1.9 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
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.
valine-tRNA ligase activity Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
valyl-tRNA aminoacylation The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-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
MAMEKTFDAA EAEARITKAW EEAGAFKAGA NRSRDESFTI MIPPPNVTGA LHVGHAFNNT
70 80 90 100 110 120
LQDILTRWHR MRGFDTLWQP GQDHAGIATQ MQVEKMLAAT QQPSRRELGR EEFLKKVWEW
130 140 150 160 170 180
KGQYGGTIVE QLKRLGASCD WSRNAFTMAG AAGDPRTGHE NSPNFHDAVI KVFVDMYNKG
190 200 210 220 230 240
LIYRGKRLVN WDPHFETAIS DLEVENIEVA GHMWHFKYPL AGGATYTYVE KDEDGNIVLE
250 260 270 280 290 300
EERDYISIAT TRPETMLGDG AVAVHPSDER YAPIVGKLCE IPVGPKEHRR QIPIITDEYP
310 320 330 340 350 360
DKNFGSGAVK ITGAHDFNDY AVAKRGGIPL YRLMDTRGQM RADGAPYAAE AGKAQDYARG
370 380 390 400 410 420
RAFTENEIDV INLVPDHLRG LDRFEARAKV VDEITSEGLA VMTVASDPRL GTTALKPGAE
430 440 450 460 470 480
GADAIVPLVE AKPIMQPFGD RSKVVIEPML TDQWFVDAEK VVGPALDAVR DGTVKIIPES
490 500 510 520 530 540
GEKTYYHWLE NIEPWCISRQ LWWGHQIPVW YGPNRDDLGA SYKAFCAASE QDALLLAQNY
550 560 570 580 590 600
YGANVEVDFD SGPEELSGGI AFGTIEGPGG QKTLQSVSLT RDPDVLDTWF SSGLWPIGTL
610 620 630 640 650 660
GWPEDTDEMR RYFPTSVLIT GFDILFFWVA RMMMMQLAVV DQVPFHTVYL HQLVRDEKGK
670 680 690 700 710 720
KMSKTTGNVI DPLEIVDEFG ADALRFTNAS MAAIGGVLKL SKERITGYRN FTTKLWNAIR
730 740 750 760 770 780
FAEMNEVFTD AVPQLSAAEL APKAAVNRWI IGETARVREE VDAALDSYRF NDAANALYAF
790 800 810 820 830 840
VWGKVCDWYV ELSKPLLQGE DTEAQAETRA TMRWVMDQCL VLLHPIMPFI TEELWGLTAE
850 860 870 880 890 900
RAKMLVHADW PTYKAADLVD DAADREMNWV ISVIENTRSA RAQMRVPAGL YVPMIVTEID
910 920 930 940 950 960
DHGQAAWDRN EALIKRLARI DSLTKADAMP KGCISIAAPG AAFGLPLAEI IDIGAEKDRL
970 980 990 1000 1010
EKAKGKLAKE LGGLRGRLNN PKFVESAPDE VVEEARENLA AREEEEARLN EALARLAELG