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 Q9RNN8

Entry ID Method Resolution Chain Position Source
AF-Q9RNN8-F1 Predicted AlphaFoldDB

No variants for Q9RNN8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9RNN8

No associated diseases with Q9RNN8

No regional properties for Q9RNN8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9RNN8

Functions

Description
EC Number 6.1.1.7 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.

4 GO annotations of molecular function

Name Definition
alanine-tRNA ligase activity Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
alanyl-tRNA aminoacylation The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MITTNEIRRS FLEYFEKNGH RIVPSAPLVP QNDPTLMFVN AGMVPFKNTF TGLESRPYKT
70 80 90 100 110 120
ATSSQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKERVIELA WGLITKEWGL
130 140 150 160 170 180
DPERLCVTVY HTDEEAFNLW RKIAGLPEDR IIKIATSDNF WSMGDTGPCG PCSEIFYDHG
190 200 210 220 230 240
PEIPGGPPGS PDEDGDRFVE IWNLVFMQYE QVNAETRLNL PRPSIDTGMG LERIASVLQG
250 260 270 280 290 300
VHDNYDTDTF KALIAASGEL THTATDGQFK ASHRVIADHL RAAGFLVADG VLPANEGRGY
310 320 330 340 350 360
VLRRIMRRAM RHAHLIGAKE PLMYRLVPAL LSEMGMAYPE LVRAKALIEE TLRLEETRFR
370 380 390 400 410 420
QTLANGLKIL EDETQHLKSG DTLPGAVAFR LYDTYGFPYD LTADALRARN LTVDQAGFDA
430 440 450 460 470 480
AMAEQRKAAR AAWKGSGEKA SDEIWFDIAD QLGGTEFTGY TAEKGSGQII ALIKDGKRVE
490 500 510 520 530 540
TAKQGDDITI ITNQTPFYGE SGGQKGDIGV ITGNNDLKMT VTDTQKPLGR IHAHIAKIEK
550 560 570 580 590 600
GEIKIGDDIQ LQVDINHRNR LRANHSATHL LHAALRDQLG QHVSQKGSMV SAERLRFDFS
610 620 630 640 650 660
HQKALSDQEL AAIEAEVNQQ ILNNSVVTTR LMTPESAVEA GAMALFGEKY GNEVRVLSMG
670 680 690 700 710 720
SCLNDQNEES SWSVELCGGT HVSALGQIGL FHIVSETAVS SGIRRIEAVT GEEARLWLVG
730 740 750 760 770 780
RDRLLRETAS ILKAVPEEVP TRTAAILDER RKSERALADA QKALALANAN GGQGGNNAAP
790 800 810 820 830 840
EKVGAYQFIG QVIEGLDPKA LRGLIDENKK IIESGVIALI TVNEGRASVA IGVSDSLKDK
850 860 870 880
ISAVDLVRKA VETLGGKGGG GRPDMAQGGG PNGNEAAQAL EAVKALLEKA