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 B2HIA2

Entry ID Method Resolution Chain Position Source
AF-B2HIA2-F1 Predicted AlphaFoldDB

No variants for B2HIA2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2HIA2

No associated diseases with B2HIA2

4 regional properties for B2HIA2

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 88 - 98 IPR001412
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 824 - 939 IPR013155
domain Methionyl/Leucyl tRNA synthetase 83 - 190 IPR015413
domain Leucyl-tRNA synthetase, editing domain 313 - 509 IPR025709

Functions

Description
EC Number 6.1.1.4 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.
leucine-tRNA ligase activity Catalysis of the reaction: L-leucine + ATP + tRNA(Leu) = AMP + diphosphate + 2 H(+) + Leu-tRNA(Leu).

1 GO annotations of biological process

Name Definition
leucyl-tRNA aminoacylation The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-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
MTESPTTTPG STSGAPSGVP SGVNDAESDA PRHRYTAELA AGVERTWQQN WARLGTFNVP
70 80 90 100 110 120
NPVGSLAPSD GSPVPEDKLF VQDMFPYPSG EGLHVGHPLG YIATDVFARY HRMKGRNVLH
130 140 150 160 170 180
ALGFDAFGLP AEQYAVQTGT HPRTRTEANV VNFRRQLGRL GLGHDSRRSF STTDVEFYKW
190 200 210 220 230 240
TQWIFLQIYN AWFDAAANKA RPISELVAEF DSGARSLVDG RDWSTLSAGE RADVIDDHRL
250 260 270 280 290 300
VYRADSMVNW CPGLGTVLAN EEVTSDGRSD RGNFPVFRKR LRQWMMRITA YSDRLLDDLD
310 320 330 340 350 360
VLDWPDQVKT MQRNWIGRST GASALFTATR SNGETVGLEV FTTRPDTLFG ATYLVLAPEH
370 380 390 400 410 420
DLVDDLVGAG WPAGVDPLWT GGGATPAEAV AAYRRAIAAK SDLERQESKE KTGVFLGSHA
430 440 450 460 470 480
INPATGQPVP IFIADYVLAG YGTGAIMAVP GHDQRDWDFA RALGLPVVEV IAGGDISQAA
490 500 510 520 530 540
YTGDGVLVNS GFLDGMSVGE AKQAITARLE SDGHGQARIE FKLRDWLFAR QRYWGEPFPI
550 560 570 580 590 600
VYDADGRPHA LDESALPVEL PDVPDYSPVL FDPDDANSEP SPPLGKATEW VHVELDLGDG
610 620 630 640 650 660
LKPYSRDTNV MPQWAGSSWY ELRYTDPHNA DRFCAKENET YWMGPRPAEH GPDDPGGVDL
670 680 690 700 710 720
YVGGAEHAVL HLLYARFWHK VLYDLGHVSS REPYRKLINQ GYIQAFAYTD ARGSYVPAEE
730 740 750 760 770 780
VIERDGGFVY PGADGEIEVF QEFGKIGKSL KNSISPDEIC DDYGADTLRV YEMSMGPIEA
790 800 810 820 830 840
SRPWATKDVI GAYRFLQRVW RLVIDENTGE ILVADTPAEL DTDTLRALHR AIAGVAEDYA
850 860 870 880 890 900
ALRNNTAVAK LIEYTNFLTK RHRDAVPRAA IEPLVLMVAP LAPHLAEELW QRLGHTTSLA
910 920 930 940 950 960
HGPFPAADPA YLIDDTVEYP VQVNGKVRGR VVVAADADDD AVKAAALADE KVQAFLAGAS
970
PRKVIVVAGR LVNLVV