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 A1BFP7

Entry ID Method Resolution Chain Position Source
AF-A1BFP7-F1 Predicted AlphaFoldDB

No variants for A1BFP7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1BFP7

No associated diseases with A1BFP7

1 regional properties for A1BFP7

Type Name Position InterPro Accession
domain Heat shock protein Hsp90, N-terminal 10 - 213 IPR020575

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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
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
MTNNDTPGMR EYEYKAEMKQ LLELIVHSLY THPEIFLREL ISNASDALSK VRFNALTDES
70 80 90 100 110 120
IINSDAGLAI RITLDPEAHT IVIEDNGTGM TEEELILNLG TVARSGTLGF LQALKEQQKE
130 140 150 160 170 180
LDGNLIGQFG VGFYSVFMVT DEVTVETRSS GADSAGYRWR SGAAGTFTIE RIEKEQRGTK
190 200 210 220 230 240
ISFALKDEFK EFSEAYRIEQ IIRKYSNFVD FPIFLGDNQI NTISALWQRS KNEVSDEERN
250 260 270 280 290 300
EFYKFLSNDF NPPLDSLHLS VEGKVCFKAL LFLPEEAPPE LMYRQGDLES RGPQLYVKKV
310 320 330 340 350 360
LIQQECRDLL PEYLRFVAGV VDTEDLPLNV SREVVQSSKV MANIRQILTG KILSWFESMA
370 380 390 400 410 420
TDQPEKFRKF YKAFGPFLKI GLNTDFTHRD RIIGLMRFES TKTAEGEYVT FKEYVERMEA
430 440 450 460 470 480
GQNEIYYHSG SNRIQLLAHP NLEYFQHKGI EVLLLSDPVD VFVIPSIHEY DKKPLKSIEK
490 500 510 520 530 540
ADIDFTRTGD DKTEPPLPET LSQPLLGLFR QTIGDVIEDV VESHRLVSSP VTLVSGKDSL
550 560 570 580 590 600
DSSMEKMMKM MHAEMPAAKK ILEVNTSHPI IKNLSGMIMA NEHNPLIRTV IQQLYDGALL
610 620
HEGNLDATTG FLQRMNELIE AATMSR