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 Q6C255

Entry ID Method Resolution Chain Position Source
AF-Q6C255-F1 Predicted AlphaFoldDB

No variants for Q6C255

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6C255

No associated diseases with Q6C255

6 regional properties for Q6C255

Type Name Position InterPro Accession
domain Elongation factor EFG, domain V-like 459 - 542 IPR000640
domain Translational (tr)-type GTP-binding domain 55 - 235 IPR000795
domain Small GTP-binding protein domain 57 - 224 IPR005225
domain GTP-binding protein LepA, C-terminal 548 - 653 IPR013842
conserved_site Tr-type G domain, conserved site 94 - 109 IPR031157
domain Elongation factor 4, domain IV 461 - 540 IPR035654

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

4 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.
mitochondrial ribosome binding Binding to a mitochondrial ribosome.
ribosome binding Binding to a ribosome.

2 GO annotations of biological process

Name Definition
positive regulation of translation Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MWKGLLQSTR AAWRGPCVRA PRLPFFRRYS LCVDPEIAAL SGPELEARIA AIPIERYRNF
70 80 90 100 110 120
SIVAHVDHGK STLSDRLLEL TGVIAAGGQK QFLDKLDVER ERGITVKAQT CTMLYKHKGE
130 140 150 160 170 180
DYLLHLVDTP GHVDFRAEVS RSYASCGGAL LLVDASQGVQ AQTVANFFLA FSLNLTLLPV
190 200 210 220 230 240
INKIDLEVAD IPRSMDQIES TFELPTDNVL QVSAKTGLNV DQILPNVIEN IPGPDGKLED
250 260 270 280 290 300
PLRALIVDSW YDNYLGVVLL TYVRDGVVSR GTKVISHHTG RKYDVKEVGI MYPGSVKTKE
310 320 330 340 350 360
LKAGQVGYMA LGMKSSSEAH TGDTLIKVNS NAEPLPGFAE TKPMVFVGVF PGEGMDFADL
370 380 390 400 410 420
EESLQHLTLN DRSVTMTKAT SQALGQGWRM GFLGTLHASV FEDRLLQEHG AHVIITAPSV
430 440 450 460 470 480
PYRVVYHPRG KETEPTIVEI DNPANFPDLQ LEKARIQSLE EPMVACTMTL PQEYIGSVMS
490 500 510 520 530 540
LCEANRGEQV DMNYLNQTQV LLKYRIPLNQ LVEDFFGKLK AASQGFASLD YEEDGYMASK
550 560 570 580 590 600
LVRLDMCVNG EVVDALSQVM HVSQAETRAR DWVEKFKTFL RWHQFDVIIQ AKIGNKILAR
610 620 630 640 650
ETIKARKKDV LAKLHAADLS RKAKLLKNQK AGKNRLQTAG RVNIPKEAFS GFLSKT