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 A8F522

Entry ID Method Resolution Chain Position Source
AF-A8F522-F1 Predicted AlphaFoldDB

No variants for A8F522

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8F522

No associated diseases with A8F522

6 regional properties for A8F522

Type Name Position InterPro Accession
binding_site IQ motif, EF-hand binding site 537 - 566 IPR000048
conserved_site MnmG-related, conserved site 273 - 287 IPR020595-1
conserved_site MnmG-related, conserved site 368 - 391 IPR020595-2
domain tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG, C-terminal 403 - 616 IPR026904
domain MnmG, N-terminal domain 8 - 398 IPR040131
domain tRNA uridine 5-carboxymethylaminomethyl modification enzyme, C-terminal subdomain 546 - 617 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
MEAALATARL GFKTALLTSN LDRVAWAPCN PAIGGPAKGI IVREIDALGG EMAKVTDETM
70 80 90 100 110 120
INVRMLNTSK GASVRALRAQ IDKVSYSQKM KRILEETQNL YLRHSQVCDI LVEKGKVKSV
130 140 150 160 170 180
VDTLGIEYKS RAIILTAGTF LNGKIFIGHA TFEAGRLGDF PSKGLTESLE KYGIRFQRFK
190 200 210 220 230 240
TGTPARILGK SIDFSKMIRQ DTSKEPLCFS YFDKPVILSK DYPCWLTYTN EKTHEIIRKN
250 260 270 280 290 300
LRFSPLYGDV KLIVGKGPRY CPSIEDKVVK FPSKNMHQIF VEPEGKTTGE YYLNGLSTSL
310 320 330 340 350 360
PYEVQLEMIR TIPGLENAHI TRPAYAIEYD YADPTQLYHT LESKIVEGLF LAGQINGTSG
370 380 390 400 410 420
YEEAAGQGLI AGINAALKLR GENQFTLDRS EAYIGVMIDD IVTKGVDEPY RILTSRAEFR
430 440 450 460 470 480
LLLRHDNAHL RLSKKGYQIG LIPKWFYEEI LTLESRIKTE IERLKQVSIK PTGQINDFLT
490 500 510 520 530 540
SINTHPLRQP TTLFQILKRP DITYEQLRSL DPSPMDSPEV IEQIELTAKY EDYIEKMLEE
550 560 570 580 590 600
TKVFNDLEKI TIPEAIDYGK IPNLSVVARE KLEKIRLRNV LQVSRVPGIT PADILALITY
LKSFK