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 Q6P4Y0

Entry ID Method Resolution Chain Position Source
AF-Q6P4Y0-F1 Predicted AlphaFoldDB

No variants for Q6P4Y0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6P4Y0

No associated diseases with Q6P4Y0

5 regional properties for Q6P4Y0

Type Name Position InterPro Accession
domain TRAM domain 427 - 489 IPR002792
domain Elp3/MiaA/NifB-like, radical SAM core domain 199 - 418 IPR006638
domain Radical SAM 59 - 489 IPR007197
domain Methylthiotransferase, N-terminal 60 - 168 IPR013848
conserved_site Methylthiotransferase, conserved site 204 - 224 IPR020612

Functions

Description
EC Number 2.8.4.5 Transferring alkylthio groups
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

4 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.
N6-threonylcarbomyladenosine methylthiotransferase activity Catalysis of the methylthiolation (-SCH3 addition) at the C2 of the adenosine ring of N6-threonylcarbomyladenosine (t6A) in tRNA, to form 2-methylthio-N6-threonylcarbamoyladenosine (ms2t6A).
tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase Catalysis of the reaction: N(6)-L-threonylcarbamoyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 2-methylthio-N(6)-L-threonylcarbamoyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine.

1 GO annotations of biological process

Name Definition
tRNA methylthiolation The addition of a methylthioether group (-SCH3) to a nucleotide in a tRNA molecule.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q7K4W1 CG6550 Threonylcarbamoyladenosine tRNA methylthiotransferase Drosophila melanogaster (Fruit fly) PR
Q5VV42 CDKAL1 Threonylcarbamoyladenosine tRNA methylthiotransferase Homo sapiens (Human) PR
Q91WE6 Cdkal1 Threonylcarbamoyladenosine tRNA methylthiotransferase Mus musculus (Mouse) PR
Q6PG34 cdkal1 Threonylcarbamoyladenosine tRNA methylthiotransferase Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MPAACESLLD DIEDIVSATD PKPHDRQNAR QNIVPRARKR NKNKIQEEEP PADSTIPGTQ
70 80 90 100 110 120
KIWIRTWGCS HNNSDGEYMA GQLAAYGYSI TEQPEQADLW LLNSCTVKSP AEDHFRNSIK
130 140 150 160 170 180
KAQEANKKVV LSGCVPQAQP RQEYMKGLSI IGVQQIDRVV EVVEETIKGH SVRLLGQKKD
190 200 210 220 230 240
NGKRLGGARL DLPKIRKNPL IEIISINTGC LNACTYCKTK HARGELASYP VEELVDRAAQ
250 260 270 280 290 300
SFQEGVCEIW LTSEDTGAYG RDIGTDLPTL LWKLVEVIPE GAMLRLGMTN PPYILEHLEE
310 320 330 340 350 360
MAKILNHPRV YAFLHIPVQS ASDSVLMDMK REYCIADFKR VVDFLKERVP GITIATDIIC
370 380 390 400 410 420
GFPGETDEDF KETLKLVEEY KFPSLFINQF YPRPGTPAAK MEQVPAHVKK QRTKELSQLF
430 440 450 460 470 480
HSYSPYDHKI GEEQHVLVTE ESFDSQYYVS HNRFYEQVLV PKDPAFVGKM VEVKIFEAGK
490 500 510 520 530 540
HFMKGQPVQD SYIYTPSITK PLAKGEVSGL TEESKPPNNP ESLLQTSREG LQTFFFVTAL
550
LAAVIAFVGI KLL