Q4ULS3

PR
Gene name
dnaN (RF_0649)
Protein name
Beta sliding clamp
Names
Beta clamp, Sliding clamp, Beta-clamp processivity factor, DNA polymerase III beta sliding clamp subunit, DNA polymerase III subunit beta
Species
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi)
KEGG Pathway
rfe:RF_0649
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

267-341 (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 Q4ULS3

Entry ID Method Resolution Chain Position Source
AF-Q4ULS3-F1 Predicted AlphaFoldDB

No variants for Q4ULS3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4ULS3

No associated diseases with Q4ULS3

3 regional properties for Q4ULS3

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 7 - 14 IPR018181-1
conserved_site Heat shock protein 70, conserved site 193 - 206 IPR018181-2
conserved_site Heat shock protein 70, conserved site 338 - 352 IPR018181-3

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
DNA polymerase III complex The DNA polymerase III holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential sub-assemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core carries out the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork.

3 GO annotations of molecular function

Name Definition
3'-5' exonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.

1 GO annotations of biological process

Name Definition
DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLKLIVETKT LVQSLGFASS VVEKRNVIPE YANIKLSAKD GNLELSSTNM DLYLSQKIAV
70 80 90 100 110 120
QVVSEGELTV STKTLNDIVR KLPDSELTLT DLGTTGLEIK GKNCKFNLFT LPVSSFPPMD
130 140 150 160 170 180
SINPEASFKI SCTDFAKIIE STKFSISLDE TRYNLNGVYL HIKDKEFCSA STDGHRLSIS
190 200 210 220 230 240
WVTLEKQIKN FGVILPQKSA EEILKIVKDP KNINEDIEIL LSSNKIKFIC NENTIMLSKL
250 260 270 280 290 300
IDGTFPDYSA FIPESSSSKL VINRKIFADS IERIAIITVE KFRAVKLSLS RETLEISAVG
310 320 330 340 350 360
EARGNAKEVI NSSQDKESFY EYNSDESLAI GFNPQYLEDV LKAVKSDLVE LYFSDVSAPV
370
LIKFPENPKD IFVVMPVKV