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 A4J9S0

Entry ID Method Resolution Chain Position Source
AF-A4J9S0-F1 Predicted AlphaFoldDB

No variants for A4J9S0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4J9S0

No associated diseases with A4J9S0

4 regional properties for A4J9S0

Type Name Position InterPro Accession
domain FAD dependent oxidoreductase 263 - 627 IPR006076
domain MnmC-like methyltransferase 114 - 233 IPR008471
domain tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC, C-terminal 262 - 656 IPR017610
domain tRNA mnm(5)s(2)U biosynthesis bifunctional protein MnmC, N-terminal 19 - 234 IPR047785

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
MRYHAGDYDV IIVGAGHAGC EAGLAAARMG CKTLVLTLNL DNIALMPCNP AVGGPAKSHL
70 80 90 100 110 120
VKEIDALGGQ MGLTTDLAAI QMRMLNTGKG PAVYALRAQA DKVKYQQLMK KNLETQENLD
130 140 150 160 170 180
VKQLLVEEIL VKNGRVTGVA TQIGAEFSAR AVVVTTGTYL KGRIIIGNVH FPGGPNSQFP
190 200 210 220 230 240
SVNLSENLRS LGLELGRFKT GTPARVDRRT IDFTKMTIQP GDEEVHNFSY ISPVTQREQV
250 260 270 280 290 300
PCWLTYTTEK THEIIRENLH RSPLYSGIIE GVGPRYCPSI EDKIVRFADK PQHQIFVEPE
310 320 330 340 350 360
GLHTYEMYVQ GMSTSLPPDV QLKMYRTIPG MENVSIMRPA YAIEYDYIVP TQLRTTLETK
370 380 390 400 410 420
EIIGLYAAGQ INGTSGYEEA AAQGIMAGIN AALQVQEKDP FYLSRSEAYI GVLIDDLVVK
430 440 450 460 470 480
GTNEPYRLMT ARAEYRLLLR QDNADHRLTQ KGYNIGLVSQ VRYDHYMNKW QSISKEMERL
490 500 510 520 530 540
KTIVIPANEE TNKVLKSLES SEITQNTPFI NLLRRPEIKY NTLAGLSDHF LDLPQEVIEE
550 560 570 580 590 600
VEIEVKYEGY IKKQLAQVER FEKLEGRILN IDIDYEMIKG LSLEARQKLK KFKPTSIGQA
610 620
SRISGVSPAD ISVLLIWLEQ ERRKIAGGDA