Phosphatase Subfamily RNGTT - Revision history

Gerard at 22:29, 19 December 2016

2016-12-19T22:29:42Z

Gerard: /* Evolution */

2016-12-19T22:12:04Z

‎Evolution

Gerard at 22:11, 19 December 2016

2016-12-19T22:11:22Z

Gerard at 20:20, 19 December 2016

2016-12-19T20:20:12Z

Gerard: /* Evolution */

2016-02-10T05:37:36Z

‎Evolution

Mark: /* Evolution */

2015-02-27T18:14:39Z

‎Evolution

Mark: /* Evolution */

2015-02-27T17:51:55Z

‎Evolution

Mark: Created page with "NOTOC Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

2015-02-27T17:46:40Z

Created page with "__NOTOC__ Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

New page

__NOTOC__
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_RNGTT|Subfamily RNGTT]]

RNGTT is an mRNA capping enzyme found in holozoan.

=== Evolution ===
RNGTT is ubiquitous in holozoan and usually there is a single copy in each organism. As described in below, RNGTT has two distinct enzymatic domains: RNA triphosphatase and guanylyltransferase. In fungi, the two enzymatic activities are contained in separate but necessarily interacting proteins <cite>Ho99</cite>. However, the RNA triphosphatase in fungi is distinct from that of holozoan RNGTT in sequence and structure <cite>Lima99, Chu11</cite>.

=== Domain ===
Holozoan RNGTT has three conserved regions: N-terminal phosphatase domain removing the gamma phosphate, guanylyltransferase (GTase) domain adding GMP, and C-terminal conserved region.

=== Function ===
RNGTT is an mRNA capping enzyme. Capping of nascent RNA 5′ ends is accomplished in eukaryotic cells and for most viruses in three sequential catalytic steps: removal of the gamma phosphate by RNA triphosphatase (RTase), addition of GMP from GTP by guanylyltransferase (GTase) via a phosphoamide linked GMP–enzyme intermediate, and N7 methylation of the added GMP by RNA (guanine-N7) methyltransferase (MTase) <cite>Chu11</cite>. RNGTT carries out the first two steps through its phosphatase domain (RTase) and GTase domain.

=== References ===
<biblio>
#Chu11 pmid=21636784
#Ho99 pmid=10572165
#Lima99 pmid=10589681
</biblio>

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_RNGTT|Subfamily RNGTT]]
-RNGTT is an mRNA capping enzyme found in holozoa. The phosphatase domain removes the gamma phosphatase from the 5' end of new mRNAs, and a guanylyltransferase (GTase) domain adds GMP, which is then methylated ([https://en.wikipedia.org/wiki/Capping_enzyme Wikipedia]).
+RNGTT is an mRNA capping enzyme. The phosphatase domain removes the gamma phosphatase from the 5' end of new mRNAs, and a guanylyltransferase (GTase) domain adds GMP, which is then methylated by a separate enzyme ([https://en.wikipedia.org/wiki/Capping_enzyme Wikipedia]).
 === Evolution ===

@@ Line 5: / Line 5: @@
 === Evolution ===
-RNGTT is ubiquitous in holozoa, and found in most other eukaryotic lineages as a multi-domain protein with both phosphatase and GTase activities (e.g. Arabidopsis NP_974263.1). Some clades, including Dictyostelium (XP_636333.1), Entamoeba and Phytophthora have replaced the RNGTT phosphatase domain with a phosphatase of the CYTH-like fold, but maintain the GTase domains. Many fungi have further separated the protein into a CYTH-like Pfam: (PF02940) phosphatase protein (CET1 in S. cerevisiae) <cite>Lima99, Chu11</cite> and a separate GTase (CEG1 in S. cerevisiase) <cite>Ho99</cite>
+RNGTT is ubiquitous in holozoa, and found in most other eukaryotic lineages as a multi-domain protein with both phosphatase and GTase activities (e.g. Arabidopsis NP_974263.1). Some clades, including Dictyostelium (XP_636333.1), Entamoeba and Phytophthora have replaced the RNGTT phosphatase domain with a phosphatase of the CYTH-like fold, but maintain the GTase domains. Many fungi have further separated the protein into a CYTH-like (Pfam:PF02940) phosphatase protein (CET1 in S. cerevisiae) <cite>Lima99, Chu11</cite> and a separate GTase (CEG1 in S. cerevisiase) <cite>Ho99</cite>
 The RNGTT domain is highly divergent from other DSPs, but is closest to [[Phosphatase_Subfamily_DSP11|DSP11]], the other RNA phosphatase.

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_RNGTT|Subfamily RNGTT]]
-RNGTT is an mRNA capping enzyme found in holozoa.
+RNGTT is an mRNA capping enzyme found in holozoa. The phosphatase domain removes the gamma phosphatase from the 5' end of new mRNAs, and a guanylyltransferase (GTase) domain adds GMP, which is then methylated ([https://en.wikipedia.org/wiki/Capping_enzyme Wikipedia]).
 === Evolution ===
-RNGTT is ubiquitous in holozoa, usually as a single-copy gene. As described in below, RNGTT has two distinct enzymatic domains: RNA triphosphatase and guanylyltransferase (GTase). In fungi, the two enzymatic activities are contained in separate but necessarily interacting proteins <cite>Ho99</cite>. The GTase is conserved across eukaryotes; The phosphatase is found across eukaryotes including plants except fungi. Fungi have unique RNA triphosphatase distinct from that of RNGTT in other clades in sequence and structure <cite>Lima99, Chu11</cite>. Thus, RNGTT emerged in early eukaryotes but lost in fungi perhaps through gene fission.
+RNGTT is ubiquitous in holozoa, and found in most other eukaryotic lineages as a multi-domain protein with both phosphatase and GTase activities (e.g. Arabidopsis NP_974263.1). Some clades, including Dictyostelium (XP_636333.1), Entamoeba and Phytophthora have replaced the RNGTT phosphatase domain with a phosphatase of the CYTH-like fold, but maintain the GTase domains. Many fungi have further separated the protein into a CYTH-like Pfam: (PF02940) phosphatase protein (CET1 in S. cerevisiae) <cite>Lima99, Chu11</cite> and a separate GTase (CEG1 in S. cerevisiase) <cite>Ho99</cite>
 === Domain ===
-Holozoan RNGTT has three conserved regions: N-terminal phosphatase domain removing the gamma phosphate, a guanylyltransferase (GTase) domain that adds GMP (mRNA_cap_enzyme), and C-terminal conserved region (mRNA_cap_C). Monosiga has a divergent RNGTT-like phosphatases (RNGTT-2) which lacks the GTase and C-terminal region, but has an N-terminal AB-hydolase domain, and this domain architecture is also seen in many fungi (e.g. Candida albicans KGU18713.1, Rhizopus microsporus EI89000.1),  and in Caspaspora (XP_004364216.2), and is similar to an algal protein that encodes only the phosphatase domain (e.g. Volvox carteri XP_002954283.1).
+Holozoan RNGTT has three conserved regions: an N-terminal phosphatase domain, a guanylyltransferase (GTase) domain that adds GMP (mRNA_cap_enzyme), and C-terminal conserved region (mRNA_cap_C).
 === Function ===

@@ Line 5: / Line 5: @@
 === Evolution ===
-RNGTT is ubiquitous in holozoan and usually there is a single copy in each organism. As described in below, RNGTT has two distinct enzymatic domains: RNA triphosphatase and guanylyltransferase (GTase). In fungi, the two enzymatic activities are contained in separate but necessarily interacting proteins <cite>Ho99</cite>. The GTase is conserved across eukaryotes; The phosphatase is found across eukaryotes including plants except fungi. Fungi have unique RNA triphosphatase distinct from that of RNGTT in other clades in sequence and structure <cite>Lima99, Chu11</cite>. Thus, RNGTT emerged in early eukaryotes but lost in fungi perhaps through gene fission.
+RNGTT is ubiquitous in holozoa, usually as a single-copy gene. As described in below, RNGTT has two distinct enzymatic domains: RNA triphosphatase and guanylyltransferase (GTase). In fungi, the two enzymatic activities are contained in separate but necessarily interacting proteins <cite>Ho99</cite>. The GTase is conserved across eukaryotes; The phosphatase is found across eukaryotes including plants except fungi. Fungi have unique RNA triphosphatase distinct from that of RNGTT in other clades in sequence and structure <cite>Lima99, Chu11</cite>. Thus, RNGTT emerged in early eukaryotes but lost in fungi perhaps through gene fission.
 === Domain ===

@@ Line 5: / Line 5: @@
 === Evolution ===
-RNGTT is ubiquitous in holozoan and usually there is a single copy in each organism. As described in below, RNGTT has two distinct enzymatic domains: RNA triphosphatase and guanylyltransferase (GTase). In fungi, the two enzymatic activities are contained in separate but necessarily interacting proteins <cite>Ho99</cite>. The GTase is conserved across eukaryotes, but fungi has a unique RNA triphosphatase distinct from that of holozoan RNGTT in sequence and structure <cite>Lima99, Chu11</cite>.
+RNGTT is ubiquitous in holozoan and usually there is a single copy in each organism. As described in below, RNGTT has two distinct enzymatic domains: RNA triphosphatase and guanylyltransferase (GTase). In fungi, the two enzymatic activities are contained in separate but necessarily interacting proteins <cite>Ho99</cite>. The GTase is conserved across eukaryotes; The phosphatase is found across eukaryotes including plants except fungi. Fungi have unique RNA triphosphatase distinct from that of RNGTT in other clades in sequence and structure <cite>Lima99, Chu11</cite>. Thus, RNGTT emerged in early eukaryotes but lost in fungi perhaps through gene fission.
 === Domain ===

Phosphatase Subfamily RNGTT - Revision history

Gerard at 22:29, 19 December 2016

Gerard: /* Evolution */

Gerard at 22:11, 19 December 2016

Gerard at 20:20, 19 December 2016

Gerard: /* Evolution */

Mark: /* Evolution */

Mark: /* Evolution */

Mark: Created page with "__NOTOC__ Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

Mark: Created page with "NOTOC Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."