SMAX5B_001675 protein (Scophthalmus maximus)

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SMAX5B_001675

2-(3-amino-3-carboxypropyl)histidine synthase subunit 2; Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2. (495 aa)

Predicted Functional Partners:

SMAX5B_015212

0.999

SMAX5B_002122

0.998

SMAX5B_001038

0.951

SMAX5B_006022

0.940

SMAX5B_022489

0.940

SMAX5B_011220

0.907

GFM1

0.907

EFL1

0.907

SMAX5B_015223

0.857

SMAX5B_002202

0.835

Your Current Organism:

Scophthalmus maximus

NCBI taxonomy Id: 52904
Other names: Pleuronectes maximus, Psetta maxima, Rhombus maximus, S. maximus, turbot

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
EFL1	SMAX5B_001038	ENSSMAP00000027794	ENSSMAP00000024310	Putative elongation factor Tu GTP-binding domain-containing protein 1 isoform 2.	Putative diphthine synthase.	0.843
EFL1	SMAX5B_001675	ENSSMAP00000027794	ENSSMAP00000002231	Putative elongation factor Tu GTP-binding domain-containing protein 1 isoform 2.	2-(3-amino-3-carboxypropyl)histidine synthase subunit 2; Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2.	0.907
EFL1	SMAX5B_002122	ENSSMAP00000027794	ENSSMAP00000000030	Putative elongation factor Tu GTP-binding domain-containing protein 1 isoform 2.	Putative DPH3-like.	0.806
EFL1	SMAX5B_015212	ENSSMAP00000027794	ENSSMAP00000009528	Putative elongation factor Tu GTP-binding domain-containing protein 1 isoform 2.	Putative diphthamide biosynthesis protein 1-like.	0.907
EFL1	SMAX5B_015223	ENSSMAP00000027794	ENSSMAP00000028855	Putative elongation factor Tu GTP-binding domain-containing protein 1 isoform 2.	RNA helicase.	0.653
GFM1	SMAX5B_001038	ENSSMAP00000021619	ENSSMAP00000024310	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mito [...]	Putative diphthine synthase.	0.843
GFM1	SMAX5B_001675	ENSSMAP00000021619	ENSSMAP00000002231	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mito [...]	2-(3-amino-3-carboxypropyl)histidine synthase subunit 2; Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2.	0.907
GFM1	SMAX5B_002122	ENSSMAP00000021619	ENSSMAP00000000030	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mito [...]	Putative DPH3-like.	0.806
GFM1	SMAX5B_015212	ENSSMAP00000021619	ENSSMAP00000009528	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mito [...]	Putative diphthamide biosynthesis protein 1-like.	0.907
GFM1	SMAX5B_015223	ENSSMAP00000021619	ENSSMAP00000028855	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mito [...]	RNA helicase.	0.696
SMAX5B_001038	EFL1	ENSSMAP00000024310	ENSSMAP00000027794	Putative diphthine synthase.	Putative elongation factor Tu GTP-binding domain-containing protein 1 isoform 2.	0.843
SMAX5B_001038	GFM1	ENSSMAP00000024310	ENSSMAP00000021619	Putative diphthine synthase.	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mito [...]	0.843
SMAX5B_001038	SMAX5B_001675	ENSSMAP00000024310	ENSSMAP00000002231	Putative diphthine synthase.	2-(3-amino-3-carboxypropyl)histidine synthase subunit 2; Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2.	0.951
SMAX5B_001038	SMAX5B_002122	ENSSMAP00000024310	ENSSMAP00000000030	Putative diphthine synthase.	Putative DPH3-like.	0.608
SMAX5B_001038	SMAX5B_006022	ENSSMAP00000024310	ENSSMAP00000005440	Putative diphthine synthase.	Putative elongation factor 2-like.	0.922
SMAX5B_001038	SMAX5B_011220	ENSSMAP00000024310	ENSSMAP00000016686	Putative diphthine synthase.	116 kDa U5 small nuclear ribonucleoprotein component.	0.843
SMAX5B_001038	SMAX5B_015212	ENSSMAP00000024310	ENSSMAP00000009528	Putative diphthine synthase.	Putative diphthamide biosynthesis protein 1-like.	0.950
SMAX5B_001038	SMAX5B_022489	ENSSMAP00000024310	ENSSMAP00000018925	Putative diphthine synthase.	Putative elongation factor 2-like.	0.922
SMAX5B_001675	EFL1	ENSSMAP00000002231	ENSSMAP00000027794	2-(3-amino-3-carboxypropyl)histidine synthase subunit 2; Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2.	Putative elongation factor Tu GTP-binding domain-containing protein 1 isoform 2.	0.907
SMAX5B_001675	GFM1	ENSSMAP00000002231	ENSSMAP00000021619	2-(3-amino-3-carboxypropyl)histidine synthase subunit 2; Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2.	Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mito [...]	0.907

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