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 B1VDL4

Entry ID Method Resolution Chain Position Source
AF-B1VDL4-F1 Predicted AlphaFoldDB

No variants for B1VDL4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1VDL4

No associated diseases with B1VDL4

4 regional properties for B1VDL4

Type Name Position InterPro Accession
domain DHHA1 domain 741 - 882 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 660 - 704 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 5 - 562 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 1 - 717 IPR018165

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
MQTHEIRQRF TDHFVKSGHT EVPSASLILD DPNLLFVNAG MVPFKPYFLG QETPPFGTAT
70 80 90 100 110 120
SIQKCVRTLD IDEVGITTRH NTFFQMAGNF SFGQYFKEGA IKNAWTLLTN SVDDGGLGLN
130 140 150 160 170 180
PDRLWVTVYE DDDEAAQLWH DLVGLPTERI QRLGMEDNYW HMGVPGPCGP CSEIYYDRGP
190 200 210 220 230 240
AYGEDGGPAV DDSRFIEIWN LVFMEFERGE TKPDGSFDIV GNLPKKNIDT GMGVERLAFL
250 260 270 280 290 300
LQGVDNVYET DLLRPVIDTA EKLTGTRYGT QDKDDIRFRV IADHSRTALM LILDGVTPGN
310 320 330 340 350 360
EGRGYILRRL IRRIIRSARL LGAQGAVIEQ LLGTVREAMT PSYPEIEENW ERIRSVGVTE
370 380 390 400 410 420
EKAFLKTLES GSQLFEQFLT EARNSGTSVV PGAVAFSLHD THGFPIDLTR EMAEEASLTV
430 440 450 460 470 480
DEAGFHELMA EQKARAKADS AAKKHVHADL SVYRAFIDSH PTHFTGYENT ADEGKVLGLI
490 500 510 520 530 540
VDGQLADRAS AGQHAQVILD QTPFYAESGG QMADRGSLRG PGGLAKVVDV QKIAKKVWAH
550 560 570 580 590 600
LIEVTEGELA IGELLEARVD QKWRHQARQA HSGTHLIHAA LREVLGPTAV QAGSMNKPGY
610 620 630 640 650 660
LRFDFSYGDQ LTEKQLQQIE EIANSAVDTD YQVNTIETSL EEAKAMGAMA LFGENYGKQV
670 680 690 700 710 720
RVVEIGGPFS MELCGGIHVD HSSQIGPISV LGESSVGSGV RRIEAYTGMD SFRHLAADRS
730 740 750 760 770 780
LVANLAANFK ATSEEIPERI DALTAKLKAA EKQVQQLRAQ QLAAQVGSIV DSAADVSGVK
790 800 810 820 830 840
VLTQNLGEGL GAKELRSVAQ DAIARFNSET AVVLFTSQDG EKVPFVAAAN PQAVERGLKA
850 860 870 880
GDLVKAFGAE VGGRGGGKPA LAQGSGSDAS GVDAGLAAVQ RLVNEILS