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 Q67NX5

Entry ID Method Resolution Chain Position Source
AF-Q67NX5-F1 Predicted AlphaFoldDB

No variants for Q67NX5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q67NX5

No associated diseases with Q67NX5

6 regional properties for Q67NX5

Type Name Position InterPro Accession
domain Nitrite/Sulfite reductase ferredoxin-like domain 127 - 187 IPR005117-1
domain Nitrite/Sulfite reductase ferredoxin-like domain 420 - 473 IPR005117-2
binding_site Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site 498 - 516 IPR006066-1
binding_site Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site 547 - 565 IPR006066-2
domain Nitrite/sulphite reductase 4Fe-4S domain 224 - 402 IPR006067-1
domain Nitrite/sulphite reductase 4Fe-4S domain 499 - 639 IPR006067-2

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
MTDRPTTALP GAQIAGRPVK VGFISLGCAK NLVDTESMIG LLRNTGYQIT NRAEEADVLV
70 80 90 100 110 120
VNTCGFIDAA KQESVDAILE AAQHKTRGRC QALVVAGCMV PRYGEELARE IPEIDALVGT
130 140 150 160 170 180
ADYPRIGEVV AGILAGQRVQ QISDPDSITD WNFERVLATP GYTAYLKIAE GCDCACAFCS
190 200 210 220 230 240
IPLMRGRHRS RPIESIVDEA RRLAGMGVRE LVVISQDTTY YGLDLYRKPM LARLLRELAQ
250 260 270 280 290 300
VDGIRWIRIH YSYPTRITDE LIEVIVTEPK VLNYLDLPLQ HGSNRVLRIM NRPANAEGYL
310 320 330 340 350 360
RLVQKLRERV PDICLRSTFI AGHPGETEED FELLLDFLRA CEFDHVGVFA YSQEEGTKAG
370 380 390 400 410 420
QMEQLPEEVR LARRDRAMEV QQEIARRRNQ LQVGRELEVL VEGRSPQGRG WFVGRCYGQS
430 440 450 460 470 480
PGIDGVVLFR APAGAELKPG DMVQVRITGV QDYDLLGEAT EPLTVDGIAQ EQDLILPVFH
LTRHQ