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 Q74CF3

Entry ID Method Resolution Chain Position Source
AF-Q74CF3-F1 Predicted AlphaFoldDB

No variants for Q74CF3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q74CF3

No associated diseases with Q74CF3

1 regional properties for Q74CF3

Type Name Position InterPro Accession
domain Radical SAM 21 - 250 IPR007197

Functions

Description
EC Number 4.3.99.3 Other carbon-nitrogen lyases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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.
carbon-nitrogen lyase activity Catalysis of the release of ammonia or one of its derivatives, with the formation of a double bond or ring. Enzymes with this activity may catalyze the actual elimination of the ammonia, amine or amide, e.g. CH-CH(-NH-R) = C=CH- + NH2-R. Others, however, catalyze elimination of another component, e.g. water, which is followed by spontaneous reactions that lead to breakage of the C-N bond, e.g. L-serine ammonia-lyase (EC:4.3.1.17), so that the overall reaction is C(-OH)-CH(-NH2) = CH2-CO- + NH3, i.e. an elimination with rearrangement. The sub-subclasses of EC:4.3 are the ammonia-lyases (EC:4.3.1), lyases acting on amides, amidines, etc. (EC:4.3.2), the amine-lyases (EC:4.3.3), and other carbon-nitrogen lyases (EC:4.3.99).
magnesium ion binding Binding to a magnesium (Mg) ion.
S-adenosyl-L-methionine binding Binding to S-adenosyl-L-methionine.

1 GO annotations of biological process

Name Definition
queuosine biosynthetic process The chemical reactions and pathways resulting in the formation of queuosines, a series of nucleosides found in tRNA and having an additional pentenyl ring added via an NH group to the methyl group of 7-methylguanosine. The pentenyl ring may carry other substituents.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSKPGAELEE VFSSVQGEGM LIGLRQVFIR FRGCNLTCDY CDTPAGTPAE PCRIEQTPGR
70 80 90 100 110 120
RDFVPADNPV SLDRVAALVE GWQRGWPGVH DSISITGGEP LLRHDILMQW LPVLREHLPV
130 140 150 160 170 180
YLETNGVMHA ALGLVINHVD IIGMDIKIPS TSGCTDLWDD HRQFLEIANT RRAFIKIVVG
190 200 210 220 230 240
EETEDWEITR ASEIIAGVNR DIPLILQPVT RAGDTLGIKP VKALELQELA CRYLAEVRII
PQTHRFMGQL