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 Q5B6J8

Entry ID Method Resolution Chain Position Source
AF-Q5B6J8-F1 Predicted AlphaFoldDB

No variants for Q5B6J8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5B6J8

No associated diseases with Q5B6J8

8 regional properties for Q5B6J8

Type Name Position InterPro Accession
domain Elongation factor EFG, domain V-like 698 - 785 IPR000640
domain Translational (tr)-type GTP-binding domain 97 - 384 IPR000795
domain Translation elongation factor EFTu-like, domain 2 423 - 486 IPR004161
domain Small GTP-binding protein domain 100 - 281 IPR005225
domain Translation elongation factor EFG/EF2, domain IV 577 - 696 IPR005517
domain Elongation factor G, domain III 503 - 578 IPR009022
conserved_site Tr-type G domain, conserved site 143 - 158 IPR031157
domain Elongation Factor G, domain II 502 - 575 IPR041095

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
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.

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 elongation factor activity Functions in chain elongation during polypeptide synthesis at the ribosome.

1 GO annotations of biological process

Name Definition
mitochondrial translational elongation The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis in a mitochondrion.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRCPSLARLP HRAVSGLTRT PVRFQSQAFL TARCASTAAL RSATPVHQSV LNRRYQQTRN
70 80 90 100 110 120
ASGTAAAVLE AAAQTPDSLS QEAIIENLDP VEAERLSRVR NIGIAAHIDS GKTTCTERVL
130 140 150 160 170 180
FYTGRIKAIH EVRGRDSVGA KMDSMDLERE KGITIQSAAT FCDWVKKDED GKEQKYHMNL
190 200 210 220 230 240
IDTPGHIDFT IEVERALRVL DGAVMILCAV SGVQSQTITV DRQMRRYNVP RISFVNKMDR
250 260 270 280 290 300
MGANPFKSVD QINTKLKLPA AAVQVPIGAE DEFEGVVDLV RMKAIYNQGS NGENIVVKDE
310 320 330 340 350 360
IPEKVRELAE ERRRMLIETL ADVDDDMAEI FLNEEEPTEK QIKDAIRRAT IGLKFTPVFM
370 380 390 400 410 420
GSALANKSVQ PMLDGVIDYL PNPSEVQNTA LDKKRNEAQV KLVPYNALPL VCLAFKLEES
430 440 450 460 470 480
SFGQLTYIRV YQGTLRKGSY VFNARTDKKV RIPRIVRMHS NEMEDVSEIG AGEICAVFGV
490 500 510 520 530 540
ECASGDSFTD GQLGYTMSSM FVPEPVISLS IKPKHSKDYA NFSKAMARFQ REDPTFRVSF
550 560 570 580 590 600
DPESEQTLIS GMGELHLDIY VERMRREYRV DCETGPPQVA YRETISQRVE FDHLLKKQSG
610 620 630 640 650 660
GPGDYARVVG WLEPTGKLEE NQFEEQIVGG SISEKFIFAC EKGFHLSCEK GPLIGHKVLG
670 680 690 700 710 720
TKMVINDGAT HMTDSSEMAF KNATQQAFRK AFQEGNPAVL EPMMKTVVTA PAEFQGDVIG
730 740 750 760 770 780
LLNKRGATIN DSEVGVDEFT VYADCSLNGM FGFSSHLRAA TQGKGEYTME FSHYEKAPPQ
790
EQRELVKKYL QAQADRHKK