Phosphatase Superfamily Rhodanese - Revision history

Gerard at 01:47, 23 August 2015

2015-08-23T01:47:16Z

Gerard at 01:29, 23 August 2015

2015-08-23T01:29:12Z

Mark at 23:22, 31 December 2014

2014-12-31T23:22:40Z

Mark at 23:18, 31 December 2014

2014-12-31T23:18:41Z

Mark at 23:11, 31 December 2014

2014-12-31T23:11:27Z

Mark: Mark moved page Phosphatase Superfamily CC3 to Phosphatase Superfamily Rhodanese

2014-12-31T23:10:38Z

Mark moved page Phosphatase Superfamily CC3 to Phosphatase Superfamily Rhodanese

Gerard at 20:26, 6 December 2014

2014-12-06T20:26:34Z

Gerard: Created page with "NOTOC Phosphatase Classification: Superfamily CC3 (Rhodanese) Phosphatase superfamily Cys-based II has a c..."

2014-12-06T20:25:44Z

Created page with "__NOTOC__ Phosphatase Classification: Superfamily CC3 (Rhodanese) Phosphatase superfamily Cys-based II has a c..."

New page

__NOTOC__

[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC3|Superfamily CC3 (Rhodanese)]]

Phosphatase superfamily Cys-based II has a catalytic phosphatase domain of rhondanese fold. The catalytic domain shares the common Cys-based catalytic motif CX5R with another two superfamilies [[Phosphatase_Superfamily_Cys-based_II| Cys-based I]] and [[Phosphatase_Superfamily_Cys-based_II|Cys-based III]], but it has distinct fold from them. Although the superfamily consists of at least families in SCOP database ([http://scop.berkeley.edu/sunid=52821 here] and [http://phosphatome.net/web/current/doc/scop/ here]), only [[Phosphatase_Family_CDC25|CDC25 family]] has protein phosphatase activitiy.

===== Not all rhodanese domains have phosphatase activity =====

Rhodanese domains are ubiquitous structural domains found in both eukaryotes and prokaryotes. It is named after bovine liver rhodanese, the most well characterized sufurtranferase. The superfamily consists of at least ten families based on different domain combination <cite>bordo02</cite>. The superfamily members have various functions and physiological substrates, such as, thiosulfate:cyanide sulfurtransferase, protein phosphatase, and arsenate reductase. The cysteine at catalytic site is necessary for its activity no matter what its substrate is. But, whether the functional specificity is determined solely by catalytic motif is unknown, though it seems different families have different catalytic motif in length and conserved residues <cite>bordo02</cite>.

The rhodanese domain occurs not only in this superfamily but also in some dual-specificity phosphatases (DSPs) of [[Phosphatase_Superfamily_Cys-based_I|Cys-based I superfamily]]. However, the cysteine at catalytic site is replaced by aspartic acid or glutamic acid in these DSPs, which results in inactive rhodanese domain rather than two active phosphatase domains within the same protein.

=== Reference ===
<biblio>
#bordo02 pmid=12151332
</biblio>

@@ Line 3: / Line 3: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese|Fold CC3 (Rhodanese)]]: [[Phosphatase_Superfamily_Rhodanese|Superfamily CC3 (Rhodanese)]]
-Phosphatase superfamily Cys-based II has a catalytic phosphatase domain of rhondanese fold. The catalytic domain shares the common Cys-based catalytic motif Cx5R with another two superfamilies [[Phosphatase_Superfamily_CC1| CC1]] and [[Phosphatase_Superfamily_CC3|CC3]], but it has distinct fold from them. Although the superfamily consists of at least families in SCOP database ([http://scop.berkeley.edu/sunid=52821 here] and [http://phosphatome.net/web/current/doc/scop/ here]), only  [[Phosphatase_Family_CDC25|CDC25 family]] has protein phosphatase activitiy.
+The CC3 superfamily is the single phosphatase superfamily of the [[Phosphatase_Fold_Rhodanese|CC3]] (Rhodanese) fold, and in turn, contains a single phosphatase family,  [[Phosphatase_Family_CDC25|Family CDC25]].
-−
-===== Not all rhodanese domains have phosphatase activity =====
-−
-Rhodanese domains are ubiquitous structural domains found in both eukaryotes and prokaryotes. It is named after bovine liver rhodanese, the most well characterized sufurtranferase. The fold and its single superfamily consists of at least ten families based on different domain combination <cite>bordo02</cite>. The member proteins have various functions and physiological substrates, such as, thiosulfate:cyanide sulfurtransferase, protein phosphatase, and arsenate reductase. The cysteine at catalytic site is necessary for its activity no matter what its substrate is. But, whether the functional specificity is determined solely by catalytic motif is unknown, though it seems different families have different catalytic motif in length and conserved residues <cite>bordo02</cite>.
-−
-The rhodanese domain occurs  not only in this superfamily but also in some [[Phosphatase_Family_DSP|dual-specificity phosphatases (DSPs)]] of [[Phosphatase_Superfamily_CC1|CC1 superfamily]]. However, the cysteine at catalytic site is replaced by aspartic acid or glutamic acid in these DSPs, which results in inactive rhodanese domain rather than two active phosphatase domains within the same protein.
-−
-=== Reference ===
-<biblio>
-#bordo02 pmid=12151332
-</biblio>

@@ Line 3: / Line 3: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese|Fold CC3 (Rhodanese)]]: [[Phosphatase_Superfamily_Rhodanese|Superfamily CC3 (Rhodanese)]]
-Phosphatase superfamily Cys-based II has a catalytic phosphatase domain of rhondanese fold. The catalytic domain shares the common Cys-based catalytic motif CX5R with another two superfamilies [[Phosphatase_Superfamily_CC1| CC1]] and [[Phosphatase_Superfamily_CC3|CC3]], but it has distinct fold from them. Although the superfamily consists of at least families in SCOP database ([http://scop.berkeley.edu/sunid=52821 here] and [http://phosphatome.net/web/current/doc/scop/ here]), only  [[Phosphatase_Family_CDC25|CDC25 family]] has protein phosphatase activitiy.
+Phosphatase superfamily Cys-based II has a catalytic phosphatase domain of rhondanese fold. The catalytic domain shares the common Cys-based catalytic motif Cx5R with another two superfamilies [[Phosphatase_Superfamily_CC1| CC1]] and [[Phosphatase_Superfamily_CC3|CC3]], but it has distinct fold from them. Although the superfamily consists of at least families in SCOP database ([http://scop.berkeley.edu/sunid=52821 here] and [http://phosphatome.net/web/current/doc/scop/ here]), only  [[Phosphatase_Family_CDC25|CDC25 family]] has protein phosphatase activitiy.
 ===== Not all rhodanese domains have phosphatase activity =====

@@ Line 1: / Line 1: @@
 __NOTOC__
-[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese|Fold Rhodanese]]: [[Phosphatase_Superfamily_Rhodanese|Superfamily CC3 (Rhodanese)]]
+[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese|Fold CC3 (Rhodanese)]]: [[Phosphatase_Superfamily_Rhodanese|Superfamily CC3 (Rhodanese)]]
 Phosphatase superfamily Cys-based II has a catalytic phosphatase domain of rhondanese fold. The catalytic domain shares the common Cys-based catalytic motif CX5R with another two superfamilies [[Phosphatase_Superfamily_CC1| CC1]] and [[Phosphatase_Superfamily_CC3|CC3]], but it has distinct fold from them. Although the superfamily consists of at least families in SCOP database ([http://scop.berkeley.edu/sunid=52821 here] and [http://phosphatome.net/web/current/doc/scop/ here]), only  [[Phosphatase_Family_CDC25|CDC25 family]] has protein phosphatase activitiy.

@@ Line 7: / Line 7: @@
 ===== Not all rhodanese domains have phosphatase activity =====
-Rhodanese domains are ubiquitous structural domains found in both eukaryotes and prokaryotes. It is named after bovine liver rhodanese, the most well characterized sufurtranferase. The superfamily consists of at least ten families based on different domain combination <cite>bordo02</cite>. The superfamily members have various functions and physiological substrates, such as, thiosulfate:cyanide sulfurtransferase, protein phosphatase, and arsenate reductase. The cysteine at catalytic site is necessary for its activity no matter what its substrate is. But, whether the functional specificity is determined solely by catalytic motif is unknown, though it seems different families have different catalytic motif in length and conserved residues <cite>bordo02</cite>.
+Rhodanese domains are ubiquitous structural domains found in both eukaryotes and prokaryotes. It is named after bovine liver rhodanese, the most well characterized sufurtranferase. The fold and its single superfamily consists of at least ten families based on different domain combination <cite>bordo02</cite>. The member proteins have various functions and physiological substrates, such as, thiosulfate:cyanide sulfurtransferase, protein phosphatase, and arsenate reductase. The cysteine at catalytic site is necessary for its activity no matter what its substrate is. But, whether the functional specificity is determined solely by catalytic motif is unknown, though it seems different families have different catalytic motif in length and conserved residues <cite>bordo02</cite>.
-The rhodanese domain occurs  not only in this superfamily but also in some dual-specificity phosphatases (DSPs) of [[Phosphatase_Superfamily_CC1|CC1 superfamily]]. However, the cysteine at catalytic site is replaced by aspartic acid or glutamic acid in these DSPs, which results in inactive rhodanese domain rather than two active phosphatase domains within the same protein.
+The rhodanese domain occurs  not only in this superfamily but also in some [[Phosphatase_Family_DSP|dual-specificity phosphatases (DSPs)]] of [[Phosphatase_Superfamily_CC1|CC1 superfamily]]. However, the cysteine at catalytic site is replaced by aspartic acid or glutamic acid in these DSPs, which results in inactive rhodanese domain rather than two active phosphatase domains within the same protein.
 === Reference ===

@@ Line 1: / Line 1: @@
 __NOTOC__
-[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC3|Superfamily CC3 (Rhodanese)]]
+[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese|Fold Rhodanese]]: [[Phosphatase_Superfamily_Rhodanese|Superfamily CC3 (Rhodanese)]]
 Phosphatase superfamily Cys-based II has a catalytic phosphatase domain of rhondanese fold. The catalytic domain shares the common Cys-based catalytic motif CX5R with another two superfamilies [[Phosphatase_Superfamily_CC1| CC1]] and [[Phosphatase_Superfamily_CC3|CC3]], but it has distinct fold from them. Although the superfamily consists of at least families in SCOP database ([http://scop.berkeley.edu/sunid=52821 here] and [http://phosphatome.net/web/current/doc/scop/ here]), only  [[Phosphatase_Family_CDC25|CDC25 family]] has protein phosphatase activitiy.

← Older revision	Revision as of 23:10, 31 December 2014
(No difference)