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

16 structures for P13551

Entry ID Method Resolution Chain Position Source
1FNM X-ray 280 A A 1-691 PDB
1JQM EM - B 1-691 PDB
1JQS EM - PDB
1KTV X-ray 380 A A/B 1-691 PDB
1PN6 EM 1080 A A 1-691 PDB
2BCW EM 1120 A C 200-257 PDB
2BM0 X-ray 240 A A 1-691 PDB
2BM1 X-ray 260 A A 1-691 PDB
2BV3 X-ray 250 A A 1-691 PDB
2J7K X-ray 290 A A 1-691 PDB
2OM7 EM 730 A L 1-691 PDB
3IZP EM - E 1-688 PDB
4M1K X-ray 295 A A 1-691 PDB
4MYT X-ray 350 A A 1-691 PDB
4MYU X-ray 300 A A 1-691 PDB
AF-P13551-F1 Predicted AlphaFoldDB

No variants for P13551

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P13551

No associated diseases with P13551

9 regional properties for P13551

Type Name Position InterPro Accession
domain Elongation factor EFG, domain V-like 600 - 687 IPR000640
domain Translational (tr)-type GTP-binding domain 10 - 284 IPR000795
domain Translation elongation factor EFTu-like, domain 2 323 - 389 IPR004161
domain Small GTP-binding protein domain 13 - 181 IPR005225
domain Translation elongation factor EFG/EF2, domain IV 479 - 598 IPR005517
domain Elongation factor G, domain III 405 - 480 IPR009022
conserved_site Tr-type G domain, conserved site 53 - 68 IPR031157
domain EFG, domain V 603 - 680 IPR035649
domain Elongation Factor G, domain II 404 - 478 IPR041095

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.

6 GO annotations of molecular function

Name Definition
GDP binding Binding to GDP, guanosine 5'-diphosphate.
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
magnesium ion binding Binding to a magnesium (Mg) ion.
ribosome binding Binding to a ribosome.
translation elongation factor activity Functions in chain elongation during polypeptide synthesis at the ribosome.

1 GO annotations of biological process

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

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA TMDFMEQERE
70 80 90 100 110 120
RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV LDGAIVVFDS SQGVEPQSET
130 140 150 160 170 180
VWRQAEKYKV PRIAFANKMD KTGADLWLVI RTMQERLGAR PVVMQLPIGR EDTFSGIIDV
190 200 210 220 230 240
LRMKAYTYGN DLGTDIREIP IPEEYLDQAR EYHEKLVEVA ADFDENIMLK YLEGEEPTEE
250 260 270 280 290 300
ELVAAIRKGT IDLKITPVFL GSALKNKGVQ LLLDAVVDYL PSPLDIPPIK GTTPEGEVVE
310 320 330 340 350 360
IHPDPNGPLA ALAFKIMADP YVGRLTFIRV YSGTLTSGSY VYNTTKGRKE RVARLLRMHA
370 380 390 400 410 420
NHREEVEELK AGDLGAVVGL KETITGDTLV GEDAPRVILE SIEVPEPVID VAIEPKTKAD
430 440 450 460 470 480
QEKLSQALAR LAEEDPTFRV STHPETGQTI ISGMGELHLE IIVDRLKREF KVDANVGKPQ
490 500 510 520 530 540
VAYRETITKP VDVEGKFIRQ TGGRGQYGHV KIKVEPLPRG SGFEFVNAIV GGVIPKEYIP
550 560 570 580 590 600
AVQKGIEEAM QSGPLIGFPV VDIKVTLYDG SYHEVDSSEM AFKIAGSMAI KEAVQKGDPV
610 620 630 640 650 660
ILEPIMRVEV TTPEEYMGDV IGDLNARRGQ ILGMEPRGNA QVIRAFVPLA EMFGYATDLR
670 680 690
SKTQGRGSFV MFFDHYQEVP KQVQEKLIKG Q