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 Q31G14

Entry ID Method Resolution Chain Position Source
AF-Q31G14-F1 Predicted AlphaFoldDB

No variants for Q31G14

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q31G14

No associated diseases with Q31G14

6 regional properties for Q31G14

Type Name Position InterPro Accession
domain TRAM domain 374 - 440 IPR002792
domain Elp3/MiaA/NifB-like, radical SAM core domain 138 - 363 IPR006638
domain Radical SAM 3 - 439 IPR007197
domain Methylthiotransferase, N-terminal 6 - 116 IPR013848
conserved_site Methylthiotransferase, conserved site 142 - 162 IPR020612
domain RimO, TRAM domain 377 - 439 IPR041582

Functions

Description
EC Number 2.8.4.4 Transferring alkylthio groups
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.

3 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
metal ion binding Binding to a metal ion.
protein methylthiotransferase activity Catalysis of the reaction: 2 S-adenosyl-L-methionine + a

2 GO annotations of biological process

Name Definition
peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid The modification of peptidyl-aspartic acid to form peptidyl-L-beta-methylthioaspartic acid, typical of bacterial ribosomal protein S12.
tRNA modification The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSQQQPTVGI VSLGCPKATV DSERILTQLK AEGYHLTNSY EEADAVIVNT CGFIDSAVQE
70 80 90 100 110 120
SLDTIGEALD ENGRVIVTGC LGAKDGVIEK VHPSVLAVSG PAAYEEVLTA VHEAIAPPKH
130 140 150 160 170 180
DPFVDLVPPQ GIKLTPKHFA YLKISEGCNH RCTFCIIPSM RGNLVSRPVS DVVAEARRLK
190 200 210 220 230 240
EAGVKELLVV SQDTAAYGVD VKYKTEFADG RPTKTSMFGL AEALSELGIW VRLHYVYPYP
250 260 270 280 290 300
NVEDVIPLMA EGKLLPYLDM PLQHADPDIL KAMKRPGNVD KTLERIKKWR EQVPDLTIRS
310 320 330 340 350 360
TFIVGFPGET EAQFQNLLDF IEEAQLDRVG CFQYSPVEGA VANDLAEPVP DEVKQERFDR
370 380 390 400 410 420
FMQLQQQISA NKMQAKIGKT IQVLVDEVDE EGAIARSKAD APEIDGMVFI PEGHHLNPGD
430 440 450
FVEVEVFAAD EYDLWATPVG EFVPQETSYV ELG