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 Q07ZD3

Entry ID Method Resolution Chain Position Source
AF-Q07ZD3-F1 Predicted AlphaFoldDB

No variants for Q07ZD3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q07ZD3

No associated diseases with Q07ZD3

2 regional properties for Q07ZD3

Type Name Position InterPro Accession
domain Geminivirus AL1 replication-associated protein, catalytic domain 7 - 119 IPR022690
domain Geminivirus AL1 replication-associated protein, central domain 126 - 229 IPR022692

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.

3 GO annotations of molecular function

Name Definition
adenyl-nucleotide exchange factor activity Binds to and stimulates the hydrolysis and exchange of adenyl nucleotides by other proteins.
chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
protein homodimerization activity Binding to an identical protein to form a homodimer.

1 GO annotations of biological process

Name Definition
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSNESNNTSQ DQVEEAVTPE IVVDEASLMD ELTQANFRIE ELEQLLAESE TALAERKDVE
70 80 90 100 110 120
MRAAAETQNI RTRAAKDVEQ ARKFALEKFA NELLPVIDNM ERALQGTNPE DEATKAIYEG
130 140 150 160 170 180
VELTMKGFLT SVEKFGVTQV NPQGQAFNPE HHQAIGMQPS AEYPANTVMM VMQKGYLLND
190 200
RLLRPAMVMV SQGGGSVDVE A