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 Q87I38

Entry ID Method Resolution Chain Position Source
AF-Q87I38-F1 Predicted AlphaFoldDB

No variants for Q87I38

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q87I38

No associated diseases with Q87I38

5 regional properties for Q87I38

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 155 - 492 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 63 - 138 IPR004365
domain Aminoacyl-tRNA synthetase, class II 176 - 491 IPR006195
domain Lysyl-tRNA synthetase, class II, C-terminal 169 - 494 IPR018149
domain Lysine-tRNA ligase, class II, N-terminal 63 - 165 IPR044136

Functions

Description
EC Number 1.11.1.21 Peroxidases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
catalase activity Catalysis of the reaction: 2 hydrogen peroxide = O2 + 2 H2O.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
hydrogen peroxide catabolic process The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSNTNGGSVG KCPVMHGGQT STDKSVMDWW PNALNLDILH QHDSKTNPFG PDFNYKEELK
70 80 90 100 110 120
KLDVDALKQD LKDLMTNSQV WWPADWGHYG GLMIRMAWHA AGSYRIADGR GGAATGNQRF
130 140 150 160 170 180
APLNSWPDNA NLDKARRLLW PIKRKYGNKL SWADLIILAG NMAYESMGFK TFGFGFGRED
190 200 210 220 230 240
IWHPEKDTYW GSEQEWLAPS GAKNSRYSGE RDLENPLAAV MMGLIYVNPE GVDGNPDPLK
250 260 270 280 290 300
TAQDMRVTFA RMAMNDEETV ALTAGGHTVG KCHGNGDAAN LGPDPEGADV HEQGLGWMNH
310 320 330 340 350 360
KTRGIGRDTV TSGLEGAWTT HPTQWDNGYF YLLFKYDWEL KKSPAGAWQW EPIDIEEQDK
370 380 390 400 410 420
PVDVEDGSKR YNPIMTDADM ALKMDPEYRK ISERFQQDPA YFEDMFARAW FKLTHRDMGP
430 440 450 460 470 480
KSCYLGPDVP SEDLIWQDPT PAGKTDYNVD LVKGKIEASG LSIADLVATA WDSARTYRGS
490 500 510 520 530 540
DRRGGANGAR IRLAPQKDWQ GNEPERLSRV LAVLESIAAE EGCSVADAIV LAGNVGIELA
550 560 570 580 590 600
ARAAGHDVSV PFAPGRGDAS QDMTDVESFE VLEPVADGFR NWLKKDYVVK PEELLLDRAQ
610 620 630 640 650 660
LMGLTAPEMT VLIGGLRVLG SNYGGSKDGV FTDRVGTLSN DFFVNLTDMA YTWKPAGENQ
670 680 690 700 710 720
YEIRDRKTDQ VKWTATRVDL VFGSNSILRS YAEVYAQDDN QEKFIHDFVA AWTKVMNADR
FDLQ