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 A3CRB1

Entry ID Method Resolution Chain Position Source
AF-A3CRB1-F1 Predicted AlphaFoldDB

No variants for A3CRB1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A3CRB1

No associated diseases with A3CRB1

5 regional properties for A3CRB1

Type Name Position InterPro Accession
conserved_site MnmG-related, conserved site 276 - 290 IPR020595-1
conserved_site MnmG-related, conserved site 371 - 394 IPR020595-2
domain tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG, C-terminal 404 - 619 IPR026904
domain MnmG, N-terminal domain 10 - 401 IPR040131
domain tRNA uridine 5-carboxymethylaminomethyl modification enzyme, C-terminal subdomain 549 - 620 IPR047001

Functions

Description
EC Number
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.

1 GO annotations of molecular function

Name Definition
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

1 GO annotations of biological process

Name Definition
tRNA wobble uridine modification The process in which a uridine in position 34 of a tRNA is post-transcriptionally modified.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSHNFTESYD IIVIGAGHAG VEASLAASRM GCKVLLATIN IEMLAFMPCN PSIGGSAKGI
70 80 90 100 110 120
VVREVDALGG EMAKNIDKSY IQMKMLNTGK GPAVRALRAQ ADKELYSKEM RKTVENQENL
130 140 150 160 170 180
TLRQTMINEI LVEDGKVIGV KTATHQEYAA KAVIVTTGTA LRGEIIIGDL KYSSGPNHSL
190 200 210 220 230 240
AAIPLADNLR DLGFEIGRFK TGTPPRVKAS SINYDVTEIQ PGDEKANHFS YTSRDEDYVK
250 260 270 280 290 300
DQVPCWLTYT NAESHEIIQN NLHRAPMFSG IVKGVGPRYC PSIEDKIVRF ADKERHQLFL
310 320 330 340 350 360
EPEGRDTEEV YVQGLSTSLP EDVQKDLVHS IKGLENAEMM RTGYAIEYDM IMPHQLRATL
370 380 390 400 410 420
ETKKISGLFT AGQTNGTSGY EEAAGQGIIA GINAALKIQG KQELILKRSD GYIGVMIDDL
430 440 450 460 470 480
VTKGTVEPYR LLTSRAEYRL ILRHDNADMR LTEMGREIGL VDDERWARFE IKKNQFDNEM
490 500 510 520 530 540
KRLESIKLKP VKETNAKVEA LGFKPLTDAV TAKEFMRRPE VSYQDVVQFI GPAAEELDEK
550 560 570 580 590 600
IIELIETEIK YEGYISKALD QVEKMKRMEE KRIPANIDWD DIDSIATEAR QKFKKINPET
610 620 630
IGQASRISGV NPADISILMV YLEGKSRSIS KNQAK