A6U9H4

PR
Gene name
Smed_1459
Protein name
UPF0758 protein Smed_1459
Names
Species
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
KEGG Pathway
smd:Smed_1459
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-70 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A6U9H4

Entry ID Method Resolution Chain Position Source
AF-A6U9H4-F1 Predicted AlphaFoldDB

No variants for A6U9H4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6U9H4

No associated diseases with A6U9H4

3 regional properties for A6U9H4

Type Name Position InterPro Accession
conserved_site Uncharacterised protein family UPF0758, conserved site 209 - 214 IPR020891
domain RadC-like JAB domain 140 - 256 IPR025657
domain MPN domain 138 - 260 IPR037518

Functions

Description
EC Number
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

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
metallopeptidase activity Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTKTPPAPEP DVLFGATDER QFIPQQQTPA AAPAPAEDAH YHGHRDRLRA RYREYGDAAL
70 80 90 100 110 120
ADYEILELIL FRLIPRRDTK PIAKALLARF GTLAGVFGAP LHLLHEVKGV KESVALDLKL
130 140 150 160 170 180
VATASHRMLK SELRNKQVLS SWSAVIDYCH AAMAHETKEQ FRILFLDKRN TLIADEVQQQ
190 200 210 220 230 240
GTIDHTPVYP REVVKRALEL SATALILVHN HPSGDPTPSC ADIEMTKLIA EAAKPLGIAL
250
HDHVIIGKDG HVSLKGLQLF