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

2 structures for Q9P7R0

Entry ID Method Resolution Chain Position Source
5SWV X-ray 265 A C 1043-1573 PDB
AF-Q9P7R0-F1 Predicted AlphaFoldDB

12 variants for Q9P7R0

Variant ID(s) Position Change Description Diseaes Association Provenance
I_4694260_G_A 164 V>I No Jeffares_SNPs
I_4694986_G_A 406 D>N No Jeffares_SNPs
I_4695557_T_C 596 I>T No Jeffares_SNPs
I_4696552_A_G 928 K>E No Jeffares_SNPs
I_4696729_A_G 987 T>A No Jeffares_SNPs
I_4696837_A_G 1023 I>V No Jeffares_SNPs
I_4696975_C_T 1069 P>S No Jeffares_SNPs
I_4697062_T_C 1098 S>P No Jeffares_SNPs
I_4697254_T_C 1162 S>P No Jeffares_SNPs
I_4697291_A_T 1174 Y>F No Jeffares_SNPs
I_4697721_G_T 1317 E>D No Jeffares_SNPs
I_4698252_G_T 1494 E>D No Jeffares_SNPs

No associated diseases with Q9P7R0

4 regional properties for Q9P7R0

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 129 - 138 IPR001412
domain Arginyl tRNA synthetase N-terminal domain 5 - 90 IPR005148
domain DALR anticodon binding 450 - 570 IPR008909
domain Arginyl-tRNA synthetase, catalytic core domain 122 - 414 IPR035684

Functions

Description
EC Number 1.1.1.25 With NAD(+) or NADP(+) as acceptor
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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

7 GO annotations of molecular function

Name Definition
3-dehydroquinate dehydratase activity Catalysis of the reaction: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
3-dehydroquinate synthase activity Catalysis of the reaction: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate.
3-phosphoshikimate 1-carboxyvinyltransferase activity Catalysis of the reaction: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
shikimate 3-dehydrogenase (NADP+) activity Catalysis of the reaction: shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+.
shikimate kinase activity Catalysis of the reaction: ATP + shikimate = 3-phosphoshikimate + ADP + 2 H(+).

4 GO annotations of biological process

Name Definition
aromatic amino acid family biosynthetic process The chemical reactions and pathways resulting in the formation of aromatic amino acid family, amino acids with aromatic ring (phenylalanine, tyrosine, tryptophan).
cellular amino acid biosynthetic process The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
chorismate biosynthetic process The chemical reactions and pathways resulting in the formation of the unsymmetrical ether derived from phosphoenolpyruvate and 5-phosphoshikimic acid formed as an intermediate in the biosynthesis of aromatic amino acids and many other compounds.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSNESNIITV PILGKDTVRV GFGIHQYICT EILENFKSST YVVITDSNIA PLYLEKIEST
70 80 90 100 110 120
FNKSIKDAKA EARLLTYVIP PGESSKCRAM KAEIEDWLLT QSCTRDTILI AMGGGVIGDL
130 140 150 160 170 180
VGYVAASFMR GIRFIQMPTT LLAMVDSSIG GKTGIDTPLG KNLVGAFWQP LRVYVDMVFL
190 200 210 220 230 240
HTLPPRQVIN GLSEIIKTAA MWNENDFQLL ENNSAVLLDA LNKPSVPGEY KFDSIKPLLQ
250 260 270 280 290 300
KIILSSIRTK CEVVTLDEHE GGLRNLLNFG HSIGHAYEAI LYPQILHGEC VAIGMVKEAE
310 320 330 340 350 360
LARYLGILKP NAVGRLTKCL VSYNLPISVN DPKVKKYASF KHCPVEKLIE YMAVDKKNQG
370 380 390 400 410 420
SKKRIVILKA IGETYEKHAT VVSDDDIRFI LSRDVKVDEF TKSSWDVVVT PPGSKSISNR
430 440 450 460 470 480
ALVLAAMGNG TCRLTNMLHS DDTQFMMSAL ESLGAATFSW EDGGETLVVK GNGGKLAVPK
490 500 510 520 530 540
EELYLGNAGT AARFLTGIAA LVSSKDGAKV VLTGNHRMKV RPIGPLVDAL RANGCEINYL
550 560 570 580 590 600
EKQGSLPLDL SSKNGLKGGI IELAATVSSQ YVSSILMCAP YASQPVTLKL VGGKPISQLY
610 620 630 640 650 660
IDMTIAMMAS FGVNVTKSTT EENTYNIPCG KYQNPPHYEI ESDASSATYP LAIAAITGTK
670 680 690 700 710 720
CTVPNIGSAS LQGDARFACD VLRPMGCTVE QTATSTTVQG PPKGTLKPLE SIDMETMTDA
730 740 750 760 770 780
FLTASVVAAV ACNVSEGDPV TRITGIANQR VKECNRIAAM VHELAKFGVR TGELEDGIYI
790 800 810 820 830 840
FGKNYKELKK PEEGIYTYDD HRIAMSFSVL SLICPSRTLI IDKACVEKTW PYWWDVLHQS
850 860 870 880 890 900
FGVKLTGATS VASDPLKGSI SKNASIILIG MRGAGKTTIG KIIAKQLNFK FLDLDELLED
910 920 930 940 950 960
YLEMPIAEVI FRMGWDAFRL EEHKVLRKFI TEHPEGYVAA SGGGVIEMDE SRNLLSNFVK
970 980 990 1000 1010 1020
EGGIVLHVHR NLEHIKSYLS EDQTRPTYKD QESIDDVYKR RHVWYRECRS HYFISPVLSN
1030 1040 1050 1060 1070 1080
QVIDEKIQYS MSRFLDVVTG SSQVLQKFKT KKRSTFLTLN YPRIEDALPT LRDVTVGCDA
1090 1100 1110 1120 1130 1140
IEVRVDYLKD PKSSNGISSL DFVAEQISLL RCSTTLPIIF TIRTISQGGL FPNDKEEEAK
1150 1160 1170 1180 1190 1200
ELMLSAMRYG CDFVDVELGW SSETINILYQ HKGYTKLIMS WHDLSGTWSW ARPHEWMQKV
1210 1220 1230 1240 1250 1260
ELASSYADVI KLVGMANNLN DNLELEEFRT RITNSMDIPL ILFNMGRFGQ LSRILNKFMT
1270 1280 1290 1300 1310 1320
PVTHPLLPSK AAPGQLTVKQ LNEARVLIGE ILPEKFFLFG KPIKHSRSPI LHSTAYELLG
1330 1340 1350 1360 1370 1380
LPHTYEAFET DTVDEVQKVL NLPDFGGANV TIPYKLSVMK FMDELSDEAR FFGAVNTIIP
1390 1400 1410 1420 1430 1440
IRIGDKLVLR GDNTDWRGIY DTFANALDGV SLRDTNGLVI GAGGTSRAAI YSLHRLGVSR
1450 1460 1470 1480 1490 1500
IYLLNRTLAN SYRVQDVFPP DYNIHIIDSD NIPSEELSSV TLSAVVSTIP ADIELPEKVA
1510 1520 1530 1540 1550 1560
SVIKALLANK ADGGVFLDMA YKPLHTPLMA VASDLEWKCC NGLEALVRQG LASFHLWTGM
1570
TAPFDAVYQK VIE