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 A5VL77

Entry ID Method Resolution Chain Position Source
AF-A5VL77-F1 Predicted AlphaFoldDB

No variants for A5VL77

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5VL77

No associated diseases with A5VL77

3 regional properties for A5VL77

Type Name Position InterPro Accession
domain Acetyl-coenzyme A carboxyltransferase, N-terminal 29 - 292 IPR011762
domain Acetyl-CoA carboxylase 65 - 248 IPR034733
domain Acetyl-coA carboxylase zinc finger domain 30 - 55 IPR041010

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
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
translation release factor activity, codon specific A translation release factor that is specific for one or more particular termination codons; acts at the ribosomal A-site and require polypeptidyl-tRNA at the P-site.

1 GO annotations of biological process

Name Definition
regulation of translational termination Any process that modulates the frequency, rate or extent of translational termination.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSPKELAEAV NKRRTFAIIS HPDAGKTTIT EQLLLFGGVV REAGTVKARK TGNFAKSDWM
70 80 90 100 110 120
EIEKKRGISV TSSVMQFDFQ GKRINILDTP GHEDFSEDTY RTLMAVDSAV MVIDSAKGIE
130 140 150 160 170 180
PQTKKLFQIC KMRGIPIFTF MNKFDRDARE PLDLLNEVED VLGIETYPIN WPIGSGHQFK
190 200 210 220 230 240
GIYDRFNHRV ALTHPADENN PYLPLDEDGN VEGDNPLAGD GEWQDAMDGM ELVEVAGNEL
250 260 270 280 290 300
DQEKIAKGDQ TPVFFGSALT NFGVQTFLET YLQFAPAPSD HKTEDGDVVK PLDPEFSGFV
310 320 330 340 350 360
FKIQANMNPR HRDRIAFVRI CSGEFDRGMD VTLSRTKKPM RLSNVTEFMA DTRENVETAV
370 380 390 400 410 420
AGDIIGLYDT GNFQIGDSIY NGKKDIQFEK LPQFTPELFV RVSAKNVMKQ KSFHKGINQL
430 440 450 460 470 480
VQEGAVQLYR SYSTGDYILG AVGQLQFEVF KFRMQNEYNS EVVMEPMGTK TARWIDPDQL
490 500 510 520
DEKMSSSRNI LVKDIHDQPL FLFENQFAEN WFKQKYPDVK LTAKL