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 B2A5J7

Entry ID Method Resolution Chain Position Source
AF-B2A5J7-F1 Predicted AlphaFoldDB

No variants for B2A5J7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2A5J7

No associated diseases with B2A5J7

4 regional properties for B2A5J7

Type Name Position InterPro Accession
domain DHHA1 domain 732 - 870 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 653 - 695 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 5 - 556 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 1 - 708 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
MRTHEIRKKF LEFFETKDHY VRKSYSIIPE NDPSILLIGA GMAPLKPYFT GEKTPPSPRM
70 80 90 100 110 120
ATSQKCVRTP DIEEVGITAR HATFFEMLGN FSFGDYFKRE AIFWGYEFCT EWLSLSPEKL
130 140 150 160 170 180
WASVYLDDDE AYDIWHDEVG IPHERIVRLG KEDNFWEIGT GPCGPCSEIH YDRGAEYGCD
190 200 210 220 230 240
SPDCKPGCDC DRYLEIWNLV FTQFNRDEEG NYTTLKQKNI DTGAGLERLA VLLQDVPSIY
250 260 270 280 290 300
EIDIIKPILD HVIQLSGVNY GEDNDKDISL RIITEHLRSV TFIVGDGVLP ANEGRGYVLR
310 320 330 340 350 360
RILRRASRHG KLLGIKDTFM SDGVDLVIDI MKEAYPELEE RREYIKKIVE IEEDRFNKTV
370 380 390 400 410 420
DQGLGILNEF LENMNKQGKN TLEGSDAFKL YDTYGFPLEL TREIVQENGY TLDEQGFQEE
430 440 450 460 470 480
LNRQREQARK AQQESEGMLT ESNAMKQFQD QKVEFTGYDN LEQESQIIGI IDHKNDDLLK
490 500 510 520 530 540
EVQEGEEVQI LINPTPFYGE SGGQIGDTGE IFSDNGRAHV KNSSVNGYDQ TVLQVKVTDG
550 560 570 580 590 600
QLRTGDKVSG KVDYQRRKDI MKNHSATHML HYALKKVVGA HVEQAGSLVA PDRLRFDFTH
610 620 630 640 650 660
FAPLSEDEIK QIELEVNKLI RENSRVRVIN TDLEEAKELG AVALFEDKYE QEVRVIEIGP
670 680 690 700 710 720
AVELCGGTHA TATGELGLFK IDNQTSVGAG VRRLEALTGQ HALEYLDQKA EQIQDIAELL
730 740 750 760 770 780
KTEENKVVEK TQEFLEDFKA KDKEIEKLKN QIFTFKVDDL LAQSKDISDF KLVANQLNDF
790 800 810 820 830 840
DADSLRDLSE RVKNKLDSGV VVLGSSTNNK ALFVAMVTKD LVEKGVHAGN IVKEVAKITG
850 860 870
GGGGGRPDMA QAGGKEPDKL NEAIMKVETL VRNQLSHS