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 Q7K4W1

Entry ID Method Resolution Chain Position Source
AF-Q7K4W1-F1 Predicted AlphaFoldDB

No variants for Q7K4W1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7K4W1

No associated diseases with Q7K4W1

11 regional properties for Q7K4W1

Type Name Position InterPro Accession
domain Cadherin-like 49 - 137 IPR002126-1
domain Cadherin-like 138 - 246 IPR002126-2
domain Cadherin-like 246 - 351 IPR002126-3
domain Cadherin-like 352 - 566 IPR002126-4
domain Cadherin-like 583 - 687 IPR002126-5
domain Cadherin, N-terminal 34 - 116 IPR013164
conserved_site Cadherin conserved site 234 - 244 IPR020894-1
conserved_site Cadherin conserved site 444 - 454 IPR020894-2
conserved_site Cadherin conserved site 554 - 564 IPR020894-3
domain Cadherin, C-terminal catenin-binding domain 815 - 936 IPR031904
domain Cadherin, cytoplasmic C-terminal domain 692 - 775 IPR032455

Functions

Description
EC Number 2.8.4.5 Transferring alkylthio groups
Subcellular Localization
  • 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
endomembrane system A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
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).
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
Q5VV42 CDKAL1 Threonylcarbamoyladenosine tRNA methylthiotransferase Homo sapiens (Human) PR
Q91WE6 Cdkal1 Threonylcarbamoyladenosine tRNA methylthiotransferase Mus musculus (Mouse) PR
Q6P4Y0 cdkal1 Threonylcarbamoyladenosine tRNA methylthiotransferase Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q6PG34 cdkal1 Threonylcarbamoyladenosine tRNA methylthiotransferase Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MYHLGQDLPG NDVDDIEDLI SADDVKPRER YENKKTVTVR AKKRSQIRLE SQEEEEKPKP
70 80 90 100 110 120
TIHESVIPGT QKVFVKTWGC AHNNSDSEYM AGQLAAYGYR LSGKEEADLW LLNSCTVKNP
130 140 150 160 170 180
SEDTFRNEIE SGMRNGKHVV VAGCVPQGAP KSDYLNGLSV IGVQQIDRVV EVVEETLKGH
190 200 210 220 230 240
SVQLLQNKKK VHGRRVAGAP LSLPKVRKNP LIEIISINSG CLNQCTYCKT KHARGDLASY
250 260 270 280 290 300
PPEEVVERAR QSFAEGCCEI WLTSEDTGAY GRDIGSSLPE LLWQLVEVIP EHCMLRVGMT
310 320 330 340 350 360
NPPYILEHLE EVANVLQHPR VYSFLHVPVQ SGSDSVLGEM KREYCRQDFE HVVDFLRERV
370 380 390 400 410 420
PGVTIATDII CGFPTETEDD FEETMTLCAK YRFPSLFINQ FFPRPGTPAA KMDRIPANLV
430 440 450 460 470 480
KKRTKRLTDL FYSYEPYADR VGEIYTVLVT EVSHDKLHYV GHNKSYEQVL LPMRDNLLGT
490 500 510 520 530 540
RVHVRITSAS KFSMVGEILD DERDWTRCAK NQELPNVQVQ TRSRERLIQR YFGIALVLGS
550
LAFLIQLVVR LL