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Conserved domains on  [gi|79316674|ref|NP_001030965|]
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ACT domain repeat 5 [Arabidopsis thaliana]

Protein Classification

sigma-54-dependent Fis family transcriptional regulator( domain architecture ID 10141593)

sigma-54-dependent Fis family transcriptional regulator similar to TyrR which regulates genes involved in the uptake and biosynthesis of aromatic amino acids; contains N-terminal ACT domain and C-terminal HTH domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 269-343 2.23e-37

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the third ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


:

Pssm-ID: 153169 [Multi-domain]  Cd Length: 75  Bit Score: 131.00  E-value: 2.23e-37
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79316674 269 YSIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQRVIKCLKAAIQRR 343
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 38-106 9.28e-36

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the N-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


:

Pssm-ID: 153167 [Multi-domain]  Cd Length: 72  Bit Score: 126.80  E-value: 9.28e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79316674  38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKSLGP 106
Cdd:cd04895   2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGT 70
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 347-418 1.16e-34

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


The actual alignment was detected with superfamily member cd04926:

Pssm-ID: 471857  Cd Length: 72  Bit Score: 123.61  E-value: 1.16e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674 347 GLKLELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASGYQVDTKTIESIRQVIGQTIL 418
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 129-202 1.65e-30

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


The actual alignment was detected with superfamily member cd04925:

Pssm-ID: 471857  Cd Length: 74  Bit Score: 112.52  E-value: 1.65e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79316674 129 TVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCSAITDPERLSKIRKLLGYVLTG 202
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
 
Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 269-343 2.23e-37

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the third ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153169 [Multi-domain]  Cd Length: 75  Bit Score: 131.00  E-value: 2.23e-37
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79316674 269 YSIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQRVIKCLKAAIQRR 343
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 38-106 9.28e-36

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the N-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153167 [Multi-domain]  Cd Length: 72  Bit Score: 126.80  E-value: 9.28e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79316674  38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKSLGP 106
Cdd:cd04895   2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGT 70
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 347-418 1.16e-34

C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153198  Cd Length: 72  Bit Score: 123.61  E-value: 1.16e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674 347 GLKLELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASGYQVDTKTIESIRQVIGQTIL 418
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 1.65e-30

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153197  Cd Length: 74  Bit Score: 112.52  E-value: 1.65e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79316674 129 TVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCSAITDPERLSKIRKLLGYVLTG 202
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 13-196 5.63e-20

UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 92.90  E-value: 5.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  13 DEIA---KFIRRVNP---PRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTD 85
Cdd:COG2844 649 EEIAwhaRLLLRADDsgkPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhTTRDGYALDTFIVLD 728

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  86 QDGNKVTDEIVLEYIRKSL-----GPDE------------SSCFSPSMRSTIGVKQSVDYTVVELTGTDRPGLLSELCAV 148
Cdd:COG2844 729 PDGEPIDDPDRLERIEQALeealsGEVPlpeplarrlsrrLRHFPVPPRVTFDNDASNRYTVLEVSALDRPGLLYDIARV 808

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 79316674 149 LMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCsAITDPERLSKIRKLL 196
Cdd:COG2844 809 LADLGLNIHSAKIATLGERVEDVFYVTDLDGQ-KLTDPERQEALREAL 855
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 25-188 3.59e-13

[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for the nitrogen regulatory protein PII. Not all homologs of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see Prosite pattern PS00496 and document PDOC00439), but the modification site is preserved in the PII homolog of all species with a member of this family. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, Protein interactions]


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 71.67  E-value: 3.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674    25 PRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKS 103
Cdd:TIGR01693 656 PLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVnTTKDGVALDTFVVQDLFGSPPAAERVFQELLQG 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   104 LG-------------------PDESSCFSPSMRSTIGVKQSVDYTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTH 164
Cdd:TIGR01693 736 LVdvlaglakdpdtisarrarRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGLLARVGRTLEELGLSIQSAKITTF 815

                         170       180
                  ....*....|....*....|....
gi 79316674   165 RAKAAAVLQVTDEETcSAITDPER 188
Cdd:TIGR01693 816 GEKAEDVFYVTDLFG-LKLTDEEE 838
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 24-104 2.11e-12

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 69.51  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   24 PPRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKS 103
Cdd:PRK05092 830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                 .
gi 79316674  104 L 104
Cdd:PRK05092 910 L 910
glnD PRK00275
PII uridylyl-transferase; Provisional
 38-194 1.56e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 66.62  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTDQDGNKVTDEIV-LEYIRKSLG---------- 105
Cdd:PRK00275 705 TQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIGDNPArIEQIREGLTealrnpddyp 784

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  106 -------PDESSCFSPSMRSTIGVKQSVDYTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEE 178
Cdd:PRK00275 785 tiiqrrvPRQLKHFAFPTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDAD 864

                        170
                 ....*....|....*.
gi 79316674  179 TcSAITDPERLSKIRK 194
Cdd:PRK00275 865 N-QPLSDPQLCSRLQD 879
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 129-197 9.25e-07

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 46.15  E-value: 9.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79316674   129 TVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVtdeETCSAITDPERLSKIRKLLG 197
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVV---IVVDEEDLEEVLEALKKLEG 66
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 350-398 9.25e-05

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 44.98  E-value: 9.25e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 79316674  350 LELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASG 398
Cdd:PRK03381 710 LEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAG 758
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 38-101 1.63e-04

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 39.60  E-value: 1.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79316674    38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDG--GWFMDVFNVTDQDGNKVTDEIVLEYIR 101
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEdkGGIVFVVIVVDEEDLEEVLEALKKLEG 66
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
128-197 2.85e-04

Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 41.36  E-value: 2.85e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79316674 128 YTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVT-DEETCSAITdpERLSKIRKLLG 197
Cdd:COG2716   3 HLVITAIGPDRPGIVAALARAVSEHGCNILDSRMARLGGEFAGILLVSgPWDAIAKLE--AALPALAAELG 71
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 356-410 2.88e-04

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 38.83  E-value: 2.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 79316674   356 DRVGLLSDVTRIFRENSLTVTRAEVKTKGDKA--LNTFYVRDASGYQVDTKTIESIR 410
Cdd:pfam01842   9 DRPGLLARVLGALADRGINITSIEQGTSEDKGgiVFVVIVVDEEDLEEVLEALKKLE 65
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 270-331 9.02e-04

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 37.67  E-value: 9.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674   270 SIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQR 331
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEALK 62
 
Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 269-343 2.23e-37

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the third ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153169 [Multi-domain]  Cd Length: 75  Bit Score: 131.00  E-value: 2.23e-37
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79316674 269 YSIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQRVIKCLKAAIQRR 343
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 38-106 9.28e-36

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the N-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153167 [Multi-domain]  Cd Length: 72  Bit Score: 126.80  E-value: 9.28e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79316674  38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKSLGP 106
Cdd:cd04895   2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGT 70
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 347-418 1.16e-34

C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153198  Cd Length: 72  Bit Score: 123.61  E-value: 1.16e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674 347 GLKLELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASGYQVDTKTIESIRQVIGQTIL 418
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 1.65e-30

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153197  Cd Length: 74  Bit Score: 112.52  E-value: 1.65e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79316674 129 TVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCSAITDPERLSKIRKLLGYVLTG 202
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 350-417 1.70e-22

C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_ACR-UUR-like_2, includes the second of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the second and fourth ACT domains of a novel protein composed almost entirely of ACT domain repeats, the ACR protein. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153171 [Multi-domain]  Cd Length: 70  Bit Score: 90.59  E-value: 1.70e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79316674 350 LELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASGYQVDTKTIESIRQVIGQTI 417
Cdd:cd04899   3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 13-196 5.63e-20

UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 92.90  E-value: 5.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  13 DEIA---KFIRRVNP---PRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTD 85
Cdd:COG2844 649 EEIAwhaRLLLRADDsgkPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhTTRDGYALDTFIVLD 728

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  86 QDGNKVTDEIVLEYIRKSL-----GPDE------------SSCFSPSMRSTIGVKQSVDYTVVELTGTDRPGLLSELCAV 148
Cdd:COG2844 729 PDGEPIDDPDRLERIEQALeealsGEVPlpeplarrlsrrLRHFPVPPRVTFDNDASNRYTVLEVSALDRPGLLYDIARV 808

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 79316674 149 LMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCsAITDPERLSKIRKLL 196
Cdd:COG2844 809 LADLGLNIHSAKIATLGERVEDVFYVTDLDGQ-KLTDPERQEALREAL 855
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 129-200 1.63e-19

C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_ACR-UUR-like_2, includes the second of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the second and fourth ACT domains of a novel protein composed almost entirely of ACT domain repeats, the ACR protein. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153171 [Multi-domain]  Cd Length: 70  Bit Score: 82.12  E-value: 1.63e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674 129 TVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCSaiTDPERLSKIRKLLGYVL 200
Cdd:cd04899   1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQP--LDPERQEALRAALGEAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 129-200 1.94e-17

ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 76.43  E-value: 1.94e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674 129 TVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEETcsAITDPERLSKIRKLLGYVL 200
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDG--RPLDPERIARLEEALEDAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 350-417 5.95e-17

ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 74.89  E-value: 5.95e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79316674 350 LELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASGYQVDTKTIESIRQVIGQTI 417
Cdd:cd04873   3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 38-104 6.26e-15

ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 69.11  E-value: 6.26e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79316674  38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKvTDEIVLEYIRKSL 104
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRP-LDPERIARLEEAL 66
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 259-413 8.81e-14

UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 73.64  E-value: 8.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674 259 VDVSNLHDLDYSIVMIKCKDRPKLLFDTVFTLTdmnyvVSHASI-DA------EGpQAYQEYYIRHTDGSPVKSEAERQR 331
Cdd:COG2844 669 VLIRPDPDRGGTEVFVYTPDRPGLFARIAGALA-----ALGLNIlDArihttrDG-YALDTFIVLDPDGEPIDDPDRLER 742

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674 332 VIKCLKAA----------IQRRVSEGLK--------------------LELCTSDRVGLLSDVTRIFRENSLTVTRAEVK 381
Cdd:COG2844 743 IEQALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHSAKIA 822

                       170       180       190
                ....*....|....*....|....*....|...
gi 79316674 382 TKGDKALNTFYVRDASGYQV-DTKTIESIRQVI 413
Cdd:COG2844 823 TLGERVEDVFYVTDLDGQKLtDPERQEALREAL 855
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 25-188 3.59e-13

[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for the nitrogen regulatory protein PII. Not all homologs of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see Prosite pattern PS00496 and document PDOC00439), but the modification site is preserved in the PII homolog of all species with a member of this family. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, Protein interactions]


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 71.67  E-value: 3.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674    25 PRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKS 103
Cdd:TIGR01693 656 PLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVnTTKDGVALDTFVVQDLFGSPPAAERVFQELLQG 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   104 LG-------------------PDESSCFSPSMRSTIGVKQSVDYTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTH 164
Cdd:TIGR01693 736 LVdvlaglakdpdtisarrarRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGLLARVGRTLEELGLSIQSAKITTF 815

                         170       180
                  ....*....|....*....|....
gi 79316674   165 RAKAAAVLQVTDEETcSAITDPER 188
Cdd:TIGR01693 816 GEKAEDVFYVTDLFG-LKLTDEEE 838
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 24-104 2.11e-12

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 69.51  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   24 PPRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKS 103
Cdd:PRK05092 830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                 .
gi 79316674  104 L 104
Cdd:PRK05092 910 L 910
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 137-342 4.02e-12

UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 68.63  E-value: 4.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674 137 DRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAA-AVLQVTDEETcSAITDPERLSKIRKLLGYVLTGGSSGRRfrepktt 215
Cdd:COG2844 688 DRPGLFARIAGALAALGLNILDARIHTTRDGYAlDTFIVLDPDG-EPIDDPDRLERIEQALEEALSGEVPLPE------- 759

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674 216 vssaLNETHTDRKLHQLMFAdrdydewennvddedkcgrviPDVDVSNLHDLDYSIVMIKCKDRPKLLFDTVFTLTDMNY 295
Cdd:COG2844 760 ----PLARRLSRRLRHFPVP---------------------PRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGL 814

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 79316674 296 VVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQRVIKCLKAAIQR 342
Cdd:COG2844 815 NIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREALLEALDE 861
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 270-340 1.13e-11

ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 59.87  E-value: 1.13e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79316674 270 SIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVkSEAERQRVIKCLKAAI 340
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPL-DPERIARLEEALEDAL 70
glnD PRK00275
PII uridylyl-transferase; Provisional
 38-194 1.56e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 66.62  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTDQDGNKVTDEIV-LEYIRKSLG---------- 105
Cdd:PRK00275 705 TQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIGDNPArIEQIREGLTealrnpddyp 784

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  106 -------PDESSCFSPSMRSTIGVKQSVDYTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEE 178
Cdd:PRK00275 785 tiiqrrvPRQLKHFAFPTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDAD 864

                        170
                 ....*....|....*.
gi 79316674  179 TcSAITDPERLSKIRK 194
Cdd:PRK00275 865 N-QPLSDPQLCSRLQD 879
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 257-417 1.29e-10

[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for the nitrogen regulatory protein PII. Not all homologs of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see Prosite pattern PS00496 and document PDOC00439), but the modification site is preserved in the PII homolog of all species with a member of this family. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, Protein interactions]


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 63.58  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   257 PDVDVSNLHDLDYSIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDA-EGPQAYQEYYIRHTDGSPVKSEAERQRVIKC 335
Cdd:TIGR01693 656 PLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTtKDGVALDTFVVQDLFGSPPAAERVFQELLQG 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   336 LKAAIQ------------RRVSEGLK--------------------LELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTK 383
Cdd:TIGR01693 736 LVDVLAglakdpdtisarRARRRRLQhfavpprvtilntasrkatiMEVRALDRPGLLARVGRTLEELGLSIQSAKITTF 815

                         170       180       190
                  ....*....|....*....|....*....|....
gi 79316674   384 GDKALNTFYVRDASGYQVDTKTIESIRQVIGQTI 417
Cdd:TIGR01693 816 GEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAASV 849
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 119-347 3.21e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 62.58  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  119 TIGVKQSVDYTVVELT--GTDRPGLLSELCAVLMDLQCNVVNAEIWTHR-AKAAAVLQVTDEETCsAITDPERLSKIRKL 195
Cdd:PRK05092 721 ATEVRPDPARGVTEVTvlAADHPGLFSRIAGACAAAGANIVDARIFTTTdGRALDTFWIQDAFGR-DEDEPRRLARLAKA 799

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  196 LGYVLTGgssgrRFREPKttvssalnethtdrklhqlMFADRDydewenNVDDEDKCGRVIPDVDVSNLHDLDYSIVMIK 275
Cdd:PRK05092 800 IEDALSG-----EVRLPE-------------------ALAKRT------KPKKRARAFHVPPRVTIDNEASNRFTVIEVN 849

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674  276 CKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQRVIKCLKAAIQRRVSEG 347
Cdd:PRK05092 850 GRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEGEAEA 921
glnD PRK00275
PII uridylyl-transferase; Provisional
 269-398 1.06e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 57.76  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  269 YSIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASI-DAEGPQAYQEYYIRHTDGSPV-----KSEAERQRVIKCLK----- 337
Cdd:PRK00275 704 GTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIgdnpaRIEQIREGLTEALRnpddy 783

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  338 -AAIQRRVSEGLK--------------------LELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDA 396
Cdd:PRK00275 784 pTIIQRRVPRQLKhfafptqvtisndaqrpvtvLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDA 863


                 ..
gi 79316674  397 SG 398
Cdd:PRK00275 864 DN 865
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 38-105 1.37e-08

C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_ACR-UUR-like_2, includes the second of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the second and fourth ACT domains of a novel protein composed almost entirely of ACT domain repeats, the ACR protein. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153171 [Multi-domain]  Cd Length: 70  Bit Score: 51.30  E-value: 1.37e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79316674  38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEiVLEYIRKSLG 105
Cdd:cd04899   1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPE-RQEALRAALG 67
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 45-107 4.42e-08

C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153198  Cd Length: 72  Bit Score: 50.04  E-value: 4.42e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79316674  45 ANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEIVlEYIRKSLGPD 107
Cdd:cd04926   9 EDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTI-EAVRQEIGPA 70
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
25-196 1.73e-07

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 53.59  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   25 PRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTDQDGNKVTDEI--VLE-YI 100
Cdd:PRK01759 665 LLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIiTSQDGYVLDSFIVTELNGKLLEFDRrrQLEqAL 744

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  101 RKSLGPDESSCFSPSMRSTIG---VKQSV--------DYTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAA 169
Cdd:PRK01759 745 TKALNTNKLKKLNLEENHKLQhfhVKTEVrflneekqEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEKAE 824

                        170       180
                 ....*....|....*....|....*..
gi 79316674  170 AVLQVTDEETcSAITDPERLSKIRKLL 196
Cdd:PRK01759 825 DFFILTNQQG-QALDEEERKALKSRLL 850
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
259-413 3.20e-07

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 52.82  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  259 VDVSNLHDLDYSIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASI-DAEGPQAYQEYYIRHTDGSPVKSEAERQ---RVIK 334
Cdd:PRK01759 667 VKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIiTSQDGYVLDSFIVTELNGKLLEFDRRRQleqALTK 746

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  335 CLKAA--IQRRVSEGLKL----------------------ELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNT 390
Cdd:PRK01759 747 ALNTNklKKLNLEENHKLqhfhvktevrflneekqeqtemELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEKAEDF 826

                        170       180
                 ....*....|....*....|...
gi 79316674  391 FYVRDASGYQVDTKTIESIRQVI 413
Cdd:PRK01759 827 FILTNQQGQALDEEERKALKSRL 849
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 129-197 9.25e-07

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 46.15  E-value: 9.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79316674   129 TVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVtdeETCSAITDPERLSKIRKLLG 197
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVV---IVVDEEDLEEVLEALKKLEG 66
glnD PRK00275
PII uridylyl-transferase; Provisional
 24-93 1.75e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 50.44  E-value: 1.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   24 PPRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTD 93
Cdd:PRK00275 801 PTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSD 870
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 137-200 3.65e-06

ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD is the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153172 [Multi-domain]  Cd Length: 73  Bit Score: 44.39  E-value: 3.65e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79316674 137 DRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAA-AVLQVTDEETcSAITDPERLSKIRKLLGYVL 200
Cdd:cd04900  10 DRPGLFARIAGALDQLGLNILDARIFTTRDGYAlDTFVVLDPDG-EPIGERERLARIREALEDAL 73
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 44-104 8.91e-06

ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD is the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153172 [Multi-domain]  Cd Length: 73  Bit Score: 43.24  E-value: 8.91e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674  44 SANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKSL 104
Cdd:cd04900   8 TPDRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGERERLARIREAL 69
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 131-196 1.51e-05

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 42.28  E-value: 1.51e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79316674 131 VELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTdeetcsaITDPERLSKIRKLL 196
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIV-------VDGDGDLEKLLEAL 59
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 350-417 3.35e-05

Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153199  Cd Length: 76  Bit Score: 42.07  E-value: 3.35e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79316674 350 LELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGD-KALNTFYVRDA----SGYQVDTKTIESIRQVIGQTI 417
Cdd:cd04927   3 LKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTPDgRVLDLFFITDArellHTKKRREETYDYLRAVLGDSM 75
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 350-398 9.25e-05

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 44.98  E-value: 9.25e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 79316674  350 LELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASG 398
Cdd:PRK03381 710 LEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAG 758
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
11-188 1.09e-04

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 44.96  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   11 MDDEIAKFIRRVNppRVVIDNevckDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTDQDGN 89
Cdd:PRK04374 670 IEVEIGQTLVKAR--RAVPDN----DALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVlDAPHDAIFDVFEVLPQDTY 743

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   90 KVTDEIVLE-YIRKSLGPDESScFSPSMRST------------IGVKQSVD--YTVVELTGTDRPGLLSELCAVLMDLQC 154
Cdd:PRK04374 744 ADGDPQRLAaALRQVLAGDLQK-VRPARRAVprqlrhfrfaprVEFSESAGgrRTRISLVAPDRPGLLADVAHVLRMQHL 822

                        170       180       190
                 ....*....|....*....|....*....|....
gi 79316674  155 NVVNAEIWTHRAKAAAVLQVTDEETcSAITDPER 188
Cdd:PRK04374 823 RVHDARIATFGERAEDQFQITDEHD-RPLSESAR 855
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
265-411 1.13e-04

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 44.58  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  265 HDLDYSIVMIK-------------CKDRPKLlFDTVFTLTD-MNYVVSHASI----DAegpQAYQEYYIRHTDGSPVkSE 326
Cdd:PRK05007 684 HDLDKPLVLLSkqatrggteifiwSPDRPYL-FAAVCAELDrRNLSVHDAQIftsrDG---MAMDTFIVLEPDGSPL-SQ 758

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  327 AERQRVIKCLKAAIQ---------RRVSEGLK--------------------LELCTSDRVGLLSDVTRIFRENSLTVTR 377
Cdd:PRK05007 759 DRHQVIRKALEQALTqsspqppkpRRLPAKLRhfnvptevsflpthtdrrsyMELIALDQPGLLARVGKIFADLGISLHG 838

                        170       180       190
                 ....*....|....*....|....*....|....
gi 79316674  378 AEVKTKGDKALNTFYVRDASGYQVDTKTIESIRQ 411
Cdd:PRK05007 839 ARITTIGERVEDLFILATADRRALNEELQQELRQ 872
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
 130-196 1.53e-04

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 39.85  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79316674   130 VVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTdeetcsaiTDPERLSKIRKLL 196
Cdd:pfam13740   4 LITATGPDRPGLTASLTAVLAEHGCNILDSGQAVIHNRLSLGLLVS--------GPWDALARLEKDL 62
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 38-101 1.63e-04

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 39.60  E-value: 1.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79316674    38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDG--GWFMDVFNVTDQDGNKVTDEIVLEYIR 101
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEdkGGIVFVVIVVDEEDLEEVLEALKKLEG 66
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 24-94 2.10e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 43.83  E-value: 2.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79316674   24 PPRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDE 94
Cdd:PRK03381 694 PPRVLWLDGASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPLADA 764
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
128-197 2.85e-04

Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 41.36  E-value: 2.85e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79316674 128 YTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVT-DEETCSAITdpERLSKIRKLLG 197
Cdd:COG2716   3 HLVITAIGPDRPGIVAALARAVSEHGCNILDSRMARLGGEFAGILLVSgPWDAIAKLE--AALPALAAELG 71
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 356-410 2.88e-04

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 38.83  E-value: 2.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 79316674   356 DRVGLLSDVTRIFRENSLTVTRAEVKTKGDKA--LNTFYVRDASGYQVDTKTIESIR 410
Cdd:pfam01842   9 DRPGLLARVLGALADRGINITSIEQGTSEDKGgiVFVVIVVDEEDLEEVLEALKKLE 65
ACT_GcvR_1 cd04893
ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, ...
 128-175 3.18e-04

ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains; This CD includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains. The glycine cleavage enzyme system in Escherichia coli provides one-carbon units for cellular methylation reactions. This enzyme system, encoded by the gcvTHP operon and lpd gene, catalyzes the cleavage of glycine into CO2 + NH3 and transfers a one-carbon unit to tetrahydrofolate, producing 5,10-methylenetetrahydrofolate. The gcvTHP operon is activated by the GcvA protein in response to glycine and repressed by a GcvA/GcvR interaction in the absence of glycine. It has been proposed that the co-activator glycine acts through a mechanism of de-repression by binding to GcvR and preventing GcvR from interacting with GcvA to block GcvA's activator function. Evidence also suggests that GcvR interacts directly with GcvA rather than binding to DNA to cause repression. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153165 [Multi-domain]  Cd Length: 77  Bit Score: 39.23  E-value: 3.18e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 79316674 128 YTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVT 175
Cdd:cd04893   1 HLVISALGTDRPGILNELTRAVSESGCNILDSRMAILGTEFALTMLVE 48
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 132-197 3.72e-04

C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153198  Cd Length: 72  Bit Score: 38.87  E-value: 3.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79316674 132 ELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDeeTCSAITDPERLSKIRKLLG 197
Cdd:cd04926   5 ELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTD--ANGNPVDPKTIEAVRQEIG 68
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 39-106 8.19e-04

Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153199  Cd Length: 76  Bit Score: 37.83  E-value: 8.19e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674  39 VIKVDSANKHGILLEVVQVLTELNLTIKKAYISSD-GGWFMDVFNVTDQD---GNKVTDEIVLEYIRKSLGP 106
Cdd:cd04927   2 LLKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTpDGRVLDLFFITDARellHTKKRREETYDYLRAVLGD 73
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 270-331 9.02e-04

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 37.67  E-value: 9.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79316674   270 SIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQR 331
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEALK 62
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
38-176 1.08e-03

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 41.50  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674   38 TVIKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVTDQDGNKVtDEIVLEYIRKSL---------GPD 107
Cdd:PRK05007 702 TEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIfTSRDGMAMDTFIVLEPDGSPL-SQDRHQVIRKALeqaltqsspQPP 780

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79316674  108 ESSCFSPSMRStIGVKQSVDY--------TVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWT--HRAKAAAVLQVTD 176
Cdd:PRK05007 781 KPRRLPAKLRH-FNVPTEVSFlpthtdrrSYMELIALDQPGLLARVGKIFADLGISLHGARITTigERVEDLFILATAD 858
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 350-394 1.65e-03

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 36.50  E-value: 1.65e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 79316674 350 LELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVR 394
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIV 45
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
 131-195 1.93e-03

ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153148 [Multi-domain]  Cd Length: 71  Bit Score: 36.66  E-value: 1.93e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79316674 131 VELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKaAAVLQVTDEetcsaITDPERLSKI-RKL 195
Cdd:cd04876   1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDG-LATIRLTLE-----VRDLEHLARImRKL 60
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
121-195 2.25e-03

(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 40.52  E-value: 2.25e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79316674 121 GVKQSVDYTV-VELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKaAAVLQVTDEetcsaITDPERLSKI-RKL 195
Cdd:COG0317 638 GEDSSGVFPVdIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDG-TATIRFTVE-----VRDLDHLARVlRKL 708
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 352-393 2.38e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 40.36  E-value: 2.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 79316674  352 LCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYV 393
Cdd:PRK03381 604 VVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVV 645
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
251-413 2.87e-03

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 40.33  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  251 KCGRVIPDVDVSNlhdldysiVMIKCKDRPKLLFDTVFTLTDMNYVVSHASI-DAEGPQAYQEYYI----RHTDGSPVKS 325
Cdd:PRK04374 680 KARRAVPDNDALE--------VFVYSPDRDGLFAAIVATLDRKGYGIHRARVlDAPHDAIFDVFEVlpqdTYADGDPQRL 751

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79316674  326 EAERQRVIK--CLKAAIQRRVSEG---------------------LKLELCTSDRVGLLSDVTRIFRENSLTVTRAEVKT 382
Cdd:PRK04374 752 AAALRQVLAgdLQKVRPARRAVPRqlrhfrfaprvefsesaggrrTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIAT 831

                        170       180       190
                 ....*....|....*....|....*....|.
gi 79316674  383 KGDKALNTFYVRDasgyQVDTKTIESIRQVI 413
Cdd:PRK04374 832 FGERAEDQFQITD----EHDRPLSESARQAL 858
PDCD7 pfam16021
Programmed cell death protein 7;
132-196 4.58e-03

Programmed cell death protein 7;


Pssm-ID: 464979 [Multi-domain]  Cd Length: 305  Bit Score: 38.94  E-value: 4.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79316674   132 ELTGTDRpgLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCSAITDPERLSKIRKLL 196
Cdd:pfam16021   9 ALYSAAR--LVSRLETLCLELRENVEDDSVWSESYSRAAELKHELQEKLLLLEDPELLESLKRKL 71
ACT_TyrKc cd04928
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ...
 40-84 6.17e-03

Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and other related ACT domains; This CD includes a novel, yet uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and other related ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153200  Cd Length: 68  Bit Score: 35.22  E-value: 6.17e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 79316674  40 IKVDSANKHGILLEVVQVLTELNLTIKKAYI-SSDGGWFMDVFNVT 84
Cdd:cd04928   4 ITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAfSTDDGLALDIFVVT 49
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 40-88 9.72e-03

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 34.58  E-value: 9.72e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 79316674  40 IKVDSANKHGILLEVVQVLTELNLTIKKAYISSDG-GWFMDVFNVTDQDG 88
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGdGGEADIFIVVDGDG 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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