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 C0ZL89

Entry ID Method Resolution Chain Position Source
AF-C0ZL89-F1 Predicted AlphaFoldDB

No variants for C0ZL89

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C0ZL89

No associated diseases with C0ZL89

11 regional properties for C0ZL89

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 759 - 1099 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 664 - 739 IPR004365
domain Aminoacyl-tRNA synthetase, class II 783 - 1102 IPR006195
domain Lysyl-tRNA synthetase, class II, C-terminal 795 - 805 IPR018149-1
domain Lysyl-tRNA synthetase, class II, C-terminal 811 - 827 IPR018149-2
domain Lysyl-tRNA synthetase, class II, C-terminal 840 - 853 IPR018149-3
domain Lysyl-tRNA synthetase, class II, C-terminal 858 - 875 IPR018149-4
domain Lysyl-tRNA synthetase, class II, C-terminal 986 - 1002 IPR018149-5
domain Phosphatidylglycerol lysyltransferase, C-terminal 246 - 548 IPR024320
domain Lysyl-tRNA synthetase, N-terminal transmembrane region 19 - 227 IPR031553
domain Lysine-tRNA ligase, class II, N-terminal 663 - 769 IPR044136

Functions

Description
EC Number 2.3.2.3 Aminoacyltransferases
Subcellular Localization
  • Cell membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
lysine-tRNA ligase activity Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).
lysyltransferase activity Catalysis of the reaction: L-lysyl-tRNA + phosphatidylglycerol = tRNA + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol.
magnesium ion binding Binding to a magnesium (Mg) ion.

3 GO annotations of biological process

Name Definition
lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
lysyl-tRNA aminoacylation The process of coupling lysine to lysyl-tRNA, catalyzed by lysyl-tRNA synthetase. The lysyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a lysine-accetping tRNA.
response to antibiotic 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 an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MESPPENPRQ ARRFRKGRFS QVPHISGLIL GVFSVLVFLW SISPVLRHIL RVPREYIDSY
70 80 90 100 110 120
YFDAPDTSLS WALVVALLAA ALASRKRIAW WLLTIYLALI TLTNIASTIV DKNPNNAVAA
130 140 150 160 170 180
VVLLVVIGIL IAARPEFYTR VRRGAGWKAL GVLIGGMAVA TVIGWGLVEL FPGDLPQNQR
190 200 210 220 230 240
FLWALNRVTA AASVDNEVFD GHPRVFVNTV LGLLGAIALL AAVMTLFRAQ RSNNALTGND
250 260 270 280 290 300
ESAIRGLIQN FGADDSLAYF ATRRDKAVIF APSGKAAITY RVEIGVCLAS GDPIGDPEAW
310 320 330 340 350 360
PHAIEAWQDL ASQYGWATAV MGASETGATA YKKAGLSVLQ LGDEAILRTR EFNLNGRDMR
370 380 390 400 410 420
PVRQAVTRVR RHGVTVRMRR HRDIPPEDMA AVIIRADDWR DTDTERGFSM ALGRLGDHLD
430 440 450 460 470 480
GDCLLVEAVM GEGTEDESVV GMLSLVPWGP NGVSLDLMRR KPTAPNGVVE LMVSELATRS
490 500 510 520 530 540
DEIGVVRVSL NFAVFRSVFE EGSRIGAGPI LRIWRSVLVF FSRWWQLEAL YRSNVKYQPD
550 560 570 580 590 600
WEPRFLCFED NRELPRVGFA SAIAEGFVVL PSFGRKSSQV VKHTGTHAAV PAALVTSEGL
610 620 630 640 650 660
HADGSPPDSA PSFTTNGPRR PEQVRVRMNK LAQLADEGIA AYPVAYPPTH TIAAAAKSPE
670 680 690 700 710 720
GTRVRIAGRL LRVRDYGGVV FTDVRDWSGD IQVLVDQDNV GREKLAEFAA EFDLGDLIEV
730 740 750 760 770 780
SGTIGRSRKG ELSLIAVEWR MNGKCLHPLP DKWKGLSDPE TRVRQRYLDI ALNPKARELL
790 800 810 820 830 840
EARSAVVKSL RDSLGGRGYL EVETPILQQV HGGANAAPFL THINAYNLDL YLRIAPELYL
850 860 870 880 890 900
KRLCVAGMEK VFEIGRVFRN EGVDFKHNPE FTILEAYEAH SDYEGMMRMC RELIQAAAVA
910 920 930 940 950 960
AFGREIIMRP GPDGELVEVD ISGEWPVKTM HGAVAEKLGV DVSPETSLED LQKLCDANEI
970 980 990 1000 1010 1020
PYQSSWDTGA IAQEMYEHLV EDYTEFPTFY TNFPTSMSPL TRPHRSIPGV AEKWDLVAWG
1030 1040 1050 1060 1070 1080
VELGTAYSEL TDPVDQRNRL TEQSMLAAGG DPEAMELDED FLQALEHAMP PTGGLGMGVD
1090 1100
RIVMLITGGS IRETLAFPLA KPRQ