A1AW22

PR
Gene name
dnaK
Protein name
Chaperone protein DnaK
Names
HSP70, Heat shock 70 kDa protein, Heat shock protein 70
Species
Ruthia magnifica subsp Calyptogena magnifica
KEGG Pathway
rma:Rmag_0353
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

468-556 (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 A1AW22

Entry ID Method Resolution Chain Position Source
AF-A1AW22-F1 Predicted AlphaFoldDB

No variants for A1AW22

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1AW22

No associated diseases with A1AW22

3 regional properties for A1AW22

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
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

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
unfolded protein binding Binding to an unfolded protein.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSRIIGIDLG TTNSCVAIMD GGNVKIIENS EGDRTTPSII AYPKDSEEVL VGQPAKRQAV
70 80 90 100 110 120
TNPENTLYAI KRLIGRRFDE DAVQKDINLV PYKIVKVDNG DAWVEVKGKK MAAPEISAKV
130 140 150 160 170 180
IGKMKKTAED YLGEEVTEAV ITVPAYFNDS QRQATKDAGK IAGLNVKRII NEPTAAALAY
190 200 210 220 230 240
GVDKVKGNKT IAVYDLGGGT FDVSIIEMED IDGEKHFEVL STNGDTFLGG EDFDQRIIGY
250 260 270 280 290 300
LVDEFKRDQG VDLTNDPMAL QRLKEAAEKA KIELSSSEQT DVNLPYVTAD ASGPKHLNIK
310 320 330 340 350 360
ITRAKLELLV EDLLKRTIEP CKTALKDADL SASDIDEVIL VGGQTRMPKV TKMVQDFFGK
370 380 390 400 410 420
EPKKDVNPDE AVAMGAAIQA GVLGGDVKDV LLLDVTPLSL GIETMGGIMT KLIEKNTTIP
430 440 450 460 470 480
TNASQIFSTA VDNQSAVTVH VLQGERNMSS ANKSLGQFNL EGIPNAPKGQ PQVEVTFDID
490 500 510 520 530 540
SDGILDVSAK DKNTGKEQSI TIKASSGLSD EEVEKMIKDA EAHADEDKKF QELVASKNMA
550 560 570 580 590 600
DSLIHSTKKT LEELKNEVSD DEKSVIEMAI TELEKAIKND DKKAIDAKIQ TLSKKAQPLT
610 620 630
EKVQAKSSAE NTSKEKSKAD DDVVDADFEE VKDDK