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Conserved domains on  [gi|357163126|ref|XP_003579632|]
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ACT domain-containing protein ACR6 [Brachypodium distachyon]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 351-424 2.38e-28

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: 107.05  E-value: 2.38e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357163126 351 GIELEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVDTFYVSDPMGldYPVEPRTIDTIRAQIGEATL 424
Cdd:cd04926    1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANG--NPVDPKTIEAVRQEIGPACL 72
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 33-101 3.04e-27

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 cd04895:

Pssm-ID: 471857 [Multi-domain]  Cd Length: 72  Bit Score: 104.07  E-value: 3.04e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357163126  33 TFIQVDSVNTHGTLLALVQVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKVTDEATLNYIQTTLES 101
Cdd:cd04895    2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGT 70
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 272-347 2.50e-25

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 cd04897:

Pssm-ID: 471857 [Multi-domain]  Cd Length: 75  Bit Score: 98.65  E-value: 2.50e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357163126 272 YTFVVVRCRDVPKLLFDTVCTITDAQYVVYHGNVSTepDGVTAYQEYYVRNKAGLA-ATEPERLLLKRQLEAAVERR 347
Cdd:cd04897    1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDT--DGDDAHQEYYIRHKDGRTlSTEGERQRVIKCLEAAIERR 75
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 129-202 2.24e-20

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: 84.79  E-value: 2.24e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357163126 129 SSIELTGTDRPGLLSEVCAVLSDVRCAVVSADLWTCNTRVAAVVQVADAATGVAIsADPARVAEISRRLAHLLR 202
Cdd:cd04925    1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPI-DDPIRLASIEDRLDNVLR 73
 
Name Accession Description Interval E-value
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 351-424 2.38e-28

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: 107.05  E-value: 2.38e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357163126 351 GIELEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVDTFYVSDPMGldYPVEPRTIDTIRAQIGEATL 424
Cdd:cd04926    1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANG--NPVDPKTIEAVRQEIGPACL 72
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 33-101 3.04e-27

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: 104.07  E-value: 3.04e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357163126  33 TFIQVDSVNTHGTLLALVQVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKVTDEATLNYIQTTLES 101
Cdd:cd04895    2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGT 70
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 272-347 2.50e-25

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: 98.65  E-value: 2.50e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357163126 272 YTFVVVRCRDVPKLLFDTVCTITDAQYVVYHGNVSTepDGVTAYQEYYVRNKAGLA-ATEPERLLLKRQLEAAVERR 347
Cdd:cd04897    1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDT--DGDDAHQEYYIRHKDGRTlSTEGERQRVIKCLEAAIERR 75
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 2.24e-20

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: 84.79  E-value: 2.24e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357163126 129 SSIELTGTDRPGLLSEVCAVLSDVRCAVVSADLWTCNTRVAAVVQVADAATGVAIsADPARVAEISRRLAHLLR 202
Cdd:cd04925    1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPI-DDPIRLASIEDRLDNVLR 73
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 188-419 3.21e-12

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 69.01  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 188 ARVAEISRRLAHLLRSRSWCHATVAASVA---------EEPSLVAMHkerrLHQLMAADPesgviegdgaylqpapgtTP 258
Cdd:COG2844  608 ERIEERKEEALALLADQGWDEEEIEALWArlpddyflrHDPEEIAWH----ARLLLRADD------------------SG 665

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 259 ATVVEVTDCAQRGYTFVVVRCRDVPKLLFDTVCT-------ITDAQyvvyhgnVSTEPDGVtAYQEYYVRNKAGLAATEP 331
Cdd:COG2844  666 KPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGAlaalglnILDAR-------IHTTRDGY-ALDTFIVLDPDGEPIDDP 737

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 332 ERL-LLKRQLEAA----------VERR---------FADGIE-----------LEVRSGDRAGLLSDVTRIIRENGLTIL 380
Cdd:COG2844  738 DRLeRIEQALEEAlsgevplpepLARRlsrrlrhfpVPPRVTfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIH 817

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 357163126 381 RAGVKSQGGEAVDTFYVSDPMGLDYpVEPRTIDTIRAQI 419
Cdd:COG2844  818 SAKIATLGERVEDVFYVTDLDGQKL-TDPERQEALREAL 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 19-99 8.70e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 64.50  E-value: 8.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  19 PPRVEIDNEISKIGTFIQVDSVNTHGTLLALVQVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKVTDEATLNYIQTT 98
Cdd:PRK05092 830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                 .
gi 357163126  99 L 99
Cdd:PRK05092 910 L 910
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 255-404 3.86e-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: 62.43  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  255 GTTPATVVEVTdcaQRGYTFVVVRCRDVPKLLFDTVCTITDAQYVVYHGNVSTEPDGVtAYQEYYV-------------- 320
Cdd:TIGR01693 654 GGPLALIDGTR---PSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGV-ALDTFVVqdlfgsppaaervf 729

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  321 -----------RNKAGLAATEPERLLLKRQLEA---AVERRFADG-----IELEVRSGDRAGLLSDVTRIIRENGLTILR 381
Cdd:TIGR01693 730 qellqglvdvlAGLAKDPDTISARRARRRRLQHfavPPRVTILNTasrkaTIMEVRALDRPGLLARVGRTLEELGLSIQS 809

                         170       180
                  ....*....|....*....|...
gi 357163126  382 AGVKSQGGEAVDTFYVSDPMGLD 404
Cdd:TIGR01693 810 AKITTFGEKAEDVFYVTDLFGLK 832
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 19-99 1.65e-09

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 60.16  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  19 PPRVEIDNEISKIGTFIQVDSVNTHGTLLALVQVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKVTDEATLNYIQTT 98
Cdd:COG2844  775 PPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREA 854


                 .
gi 357163126  99 L 99
Cdd:COG2844  855 L 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 352-422 2.13e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 56.80  E-value: 2.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357163126 352 IELEVRsgDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVDTFYVSDPMGLDYpVEPRTIDTIRAQIGEA 422
Cdd:PRK05092 846 IEVNGR--DRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKI-TNEARQAAIRRALLAA 913
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 20-159 1.78e-04

[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: 44.32  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126   20 PRVEIDNEISKIGTFIQVDSVNTHGTLLALVQVITDLNLVVRKA-YFTADGDWFMDVFYVTDRDGEKV-----------T 87
Cdd:TIGR01693 656 PLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAqVNTTKDGVALDTFVVQDLFGSPPaaervfqellqG 735

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357163126   88 DEATLNYIQTTLESDDCYYTEARDNSADIVPSE---SEEDSHQYSSIELTGTDRPGLLSEVCAVLSDVRCAVVSA 159
Cdd:TIGR01693 736 LVDVLAGLAKDPDTISARRARRRRLQHFAVPPRvtiLNTASRKATIMEVRALDRPGLLARVGRTLEELGLSIQSA 810
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
262-399 6.51e-04

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 42.42  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 262 VEVTDCAQRGYTFVVVRCRDVPKLLFDTVCTITDAQYVVYHGNVSTEPDGvtayqeyYVRNKagLAATEPERLLLK---- 337
Cdd:PRK01759 667 VKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDG-------YVLDS--FIVTELNGKLLEfdrr 737

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 338 RQLEAAV---------------------------ERRF-----ADGIELEVRSGDRAGLLSDVTRIIRENGLTILRAGVK 385
Cdd:PRK01759 738 RQLEQALtkalntnklkklnleenhklqhfhvktEVRFlneekQEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKIT 817

                        170
                 ....*....|....
gi 357163126 386 SQGGEAVDTFYVSD 399
Cdd:PRK01759 818 TIGEKAEDFFILTN 831
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 354-404 6.60e-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: 38.06  E-value: 6.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 357163126  354 LEVRSGDRAGLLSDVTRIIRENGLTILRA--GVKSQGGEAVDTFYVSDPMGLD 404
Cdd:pfam01842   3 LEVLVPDRPGLLARVLGALADRGINITSIeqGTSEDKGGIVFVVIVVDEEDLE 55
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
 131-157 2.91e-03

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


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 36.38  E-value: 2.91e-03
                          10        20
                  ....*....|....*....|....*..
gi 357163126  131 IELTGTDRPGLLSEVCAVLSDVRCAVV 157
Cdd:pfam13740   5 ITATGPDRPGLTASLTAVLAEHGCNIL 31
 
Name Accession Description Interval E-value
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 351-424 2.38e-28

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: 107.05  E-value: 2.38e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357163126 351 GIELEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVDTFYVSDPMGldYPVEPRTIDTIRAQIGEATL 424
Cdd:cd04926    1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANG--NPVDPKTIEAVRQEIGPACL 72
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 33-101 3.04e-27

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: 104.07  E-value: 3.04e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357163126  33 TFIQVDSVNTHGTLLALVQVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKVTDEATLNYIQTTLES 101
Cdd:cd04895    2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGT 70
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 272-347 2.50e-25

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: 98.65  E-value: 2.50e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357163126 272 YTFVVVRCRDVPKLLFDTVCTITDAQYVVYHGNVSTepDGVTAYQEYYVRNKAGLA-ATEPERLLLKRQLEAAVERR 347
Cdd:cd04897    1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDT--DGDDAHQEYYIRHKDGRTlSTEGERQRVIKCLEAAIERR 75
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 2.24e-20

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: 84.79  E-value: 2.24e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357163126 129 SSIELTGTDRPGLLSEVCAVLSDVRCAVVSADLWTCNTRVAAVVQVADAATGVAIsADPARVAEISRRLAHLLR 202
Cdd:cd04925    1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPI-DDPIRLASIEDRLDNVLR 73
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 354-422 5.20e-17

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: 75.18  E-value: 5.20e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357163126 354 LEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVDTFYVSDPMGLdyPVEPRTIDTIRAQIGEA 422
Cdd:cd04899    3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQ--PLDPERQEALRAALGEA 69
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 353-422 1.19e-14

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: 68.73  E-value: 1.19e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 353 ELEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVDTFYVSDPMGldYPVEPRTIDTIRAQIGEA 422
Cdd:cd04873    2 VVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDG--RPLDPERIARLEEALEDA 69
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 188-419 3.21e-12

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 69.01  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 188 ARVAEISRRLAHLLRSRSWCHATVAASVA---------EEPSLVAMHkerrLHQLMAADPesgviegdgaylqpapgtTP 258
Cdd:COG2844  608 ERIEERKEEALALLADQGWDEEEIEALWArlpddyflrHDPEEIAWH----ARLLLRADD------------------SG 665

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 259 ATVVEVTDCAQRGYTFVVVRCRDVPKLLFDTVCT-------ITDAQyvvyhgnVSTEPDGVtAYQEYYVRNKAGLAATEP 331
Cdd:COG2844  666 KPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGAlaalglnILDAR-------IHTTRDGY-ALDTFIVLDPDGEPIDDP 737

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 332 ERL-LLKRQLEAA----------VERR---------FADGIE-----------LEVRSGDRAGLLSDVTRIIRENGLTIL 380
Cdd:COG2844  738 DRLeRIEQALEEAlsgevplpepLARRlsrrlrhfpVPPRVTfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIH 817

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 357163126 381 RAGVKSQGGEAVDTFYVSDPMGLDYpVEPRTIDTIRAQI 419
Cdd:COG2844  818 SAKIATLGERVEDVFYVTDLDGQKL-TDPERQEALREAL 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 19-99 8.70e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 64.50  E-value: 8.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  19 PPRVEIDNEISKIGTFIQVDSVNTHGTLLALVQVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKVTDEATLNYIQTT 98
Cdd:PRK05092 830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                 .
gi 357163126  99 L 99
Cdd:PRK05092 910 L 910
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 33-100 1.09e-10

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: 57.17  E-value: 1.09e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357163126  33 TFIQVDSVNTHGTLLALVQVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKvTDEATLNYIQTTLE 100
Cdd:cd04873    1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRP-LDPERIARLEEALE 67
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 255-404 3.86e-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: 62.43  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  255 GTTPATVVEVTdcaQRGYTFVVVRCRDVPKLLFDTVCTITDAQYVVYHGNVSTEPDGVtAYQEYYV-------------- 320
Cdd:TIGR01693 654 GGPLALIDGTR---PSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGV-ALDTFVVqdlfgsppaaervf 729

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  321 -----------RNKAGLAATEPERLLLKRQLEA---AVERRFADG-----IELEVRSGDRAGLLSDVTRIIRENGLTILR 381
Cdd:TIGR01693 730 qellqglvdvlAGLAKDPDTISARRARRRRLQHfavPPRVTILNTasrkaTIMEVRALDRPGLLARVGRTLEELGLSIQS 809

                         170       180
                  ....*....|....*....|...
gi 357163126  382 AGVKSQGGEAVDTFYVSDPMGLD 404
Cdd:TIGR01693 810 AKITTFGEKAEDVFYVTDLFGLK 832
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 65-159 1.54e-09

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 60.54  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  65 FTADGDWFMDVFYVTDRDGEKVTDEATLNYIQTTLE---SDDCYYTEA------RDNSADIVPSE---SEEDSHQYSSIE 132
Cdd:COG2844  713 HTTRDGYALDTFIVLDPDGEPIDDPDRLERIEQALEealSGEVPLPEPlarrlsRRLRHFPVPPRvtfDNDASNRYTVLE 792

                         90       100
                 ....*....|....*....|....*..
gi 357163126 133 LTGTDRPGLLSEVCAVLSDVRCAVVSA 159
Cdd:COG2844  793 VSALDRPGLLYDIARVLADLGLNIHSA 819
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 19-99 1.65e-09

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 60.16  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  19 PPRVEIDNEISKIGTFIQVDSVNTHGTLLALVQVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKVTDEATLNYIQTT 98
Cdd:COG2844  775 PPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREA 854


                 .
gi 357163126  99 L 99
Cdd:COG2844  855 L 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 352-422 2.13e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 56.80  E-value: 2.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357163126 352 IELEVRsgDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVDTFYVSDPMGLDYpVEPRTIDTIRAQIGEA 422
Cdd:PRK05092 846 IEVNGR--DRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKI-TNEARQAAIRRALLAA 913
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 131-167 4.54e-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: 49.76  E-value: 4.54e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 357163126 131 IELTGTDRPGLLSEVCAVLSDVRCAVVSADLWTCNTR 167
Cdd:cd04899    3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGER 39
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 185-424 1.79e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 53.84  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 185 ADPARVAEISRRLAHLLRSRSWCHA-TVAASVAEEP--------SLVAmHKERRLHQLMAADPesgviegdgayLQPAPG 255
Cdd:PRK03381 507 DDPATIEAVAEALGGDPVLLELLHAlTEADSLATGPgvwsdwkaSLVG-DLVRRCRAVLAGEP-----------LPEPEP 574

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 256 TTPA---------TVVEVTDCAQRGYTFVVVrCRDVPKLLFDTVCTITDAQYVVYHGNVSTEPDgvTAYQEYYVRNKAGl 326
Cdd:PRK03381 575 LDPAqlalaadggVHVEIAPADPHMVEVTVV-APDRRGLLSKAAGVLALHRLRVRSASVRSHDG--VAVLEFVVSPRFG- 650

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 327 aaTEPERLLLKRQLEAAV----------ERRFADGIE------------------------LEVRSGDRAGLLSDVTRII 372
Cdd:PRK03381 651 --SPPDAALLRQDLRRALdgdldvlarlAAREAAAAAvpvrrpaapprvlwldgaspdatvLEVRAADRPGLLARLARAL 728

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357163126 373 RENGLTILRAGVKSQGGEAVDTFYVSDPMGLDYPVEprtidtiRAQIGEATL 424
Cdd:PRK03381 729 ERAGVDVRWARVATLGADVVDVFYVTGAAGGPLADA-------RAAVEQAVL 773
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 273-343 7.58e-07

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: 46.39  E-value: 7.58e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357163126 273 TFVVVRCRDVPKLLFDTVCTITDAQYVVYHGNVSTepDGVTAYQEYYVRNKAGLAATEPERLLLKRQLEAA 343
Cdd:cd04873    1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARIST--TGERALDVFYVTDSDGRPLDPERIARLEEALEDA 69
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 131-167 1.40e-06

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: 45.62  E-value: 1.40e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 357163126 131 IELTGTDRPGLLSEVCAVLSDVRCAVVSADLWTCNTR 167
Cdd:cd04873    3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGER 39
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 354-422 1.90e-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: 42.84  E-value: 1.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357163126 354 LEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQ-GGEAVDTFYVSDPMGLDYPVEPR--TIDTIRAQIGEA 422
Cdd:cd04927    3 LKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTpDGRVLDLFFITDARELLHTKKRReeTYDYLRAVLGDS 74
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 315-422 8.01e-05

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 45.13  E-value: 8.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 315 YQEYYVRNKAGLAA--TepeRLLLKRQLE-----AAVERRFADGIELEVRSGDRAGLLSDVTRIIRENGLTILRAGV-KS 386
Cdd:COG2844  639 PDDYFLRHDPEEIAwhA---RLLLRADDSgkplvLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhTT 715

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 357163126 387 QGGEAVDTFYVSDPMGLDYPvEPRTIDTIRAQIGEA 422
Cdd:COG2844  716 RDGYALDTFIVLDPDGEPID-DPDRLERIEQALEEA 750
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 20-159 1.78e-04

[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: 44.32  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126   20 PRVEIDNEISKIGTFIQVDSVNTHGTLLALVQVITDLNLVVRKA-YFTADGDWFMDVFYVTDRDGEKV-----------T 87
Cdd:TIGR01693 656 PLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAqVNTTKDGVALDTFVVQDLFGSPPaaervfqellqG 735

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357163126   88 DEATLNYIQTTLESDDCYYTEARDNSADIVPSE---SEEDSHQYSSIELTGTDRPGLLSEVCAVLSDVRCAVVSA 159
Cdd:TIGR01693 736 LVDVLAGLAKDPDTISARRARRRRLQHFAVPPRvtiLNTASRKATIMEVRALDRPGLLARVGRTLEELGLSIQSA 810
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
321-417 2.45e-04

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 43.61  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 321 RNKAGLAATEPERLLlKRQLEAAVERRFAdgIELEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVD---TFYV 397
Cdd:COG0317  619 PNLAELREREPERLI-DVEWGEDSSGVFP--VDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTATirfTVEV 695

                         90       100
                 ....*....|....*....|
gi 357163126 398 SDPMGLDypvepRTIDTIRA 417
Cdd:COG0317  696 RDLDHLA-----RVLRKLRK 710
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 46-89 3.09e-04

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: 38.97  E-value: 3.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 357163126  46 LLALV-QVITDLNLVVRKAYFTADGDWFMDVFYVTDRDGEKVTDE 89
Cdd:cd04899   13 LLADVtRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPE 57
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 351-422 3.30e-04

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: 39.00  E-value: 3.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357163126 351 GIELEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQG-GEAVDTFYVSDPMGLDYpVEPRTIDTIRAQIGEA 422
Cdd:cd04900    1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRdGYALDTFVVLDPDGEPI-GERERLARIREALEDA 72
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 57-159 4.59e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 42.93  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  57 NLVVRKAYFTADGdWFMDVFYVTDRDGEKVTDEATLNYIQTTLE---SDDCYYTEA---RDNS-----ADIVPSE---SE 122
Cdd:PRK05092 759 NIVDARIFTTTDG-RALDTFWIQDAFGRDEDEPRRLARLAKAIEdalSGEVRLPEAlakRTKPkkrarAFHVPPRvtiDN 837

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 357163126 123 EDSHQYSSIELTGTDRPGLLSEVCAVLSDVRCAVVSA 159
Cdd:PRK05092 838 EASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASA 874
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
262-399 6.51e-04

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 42.42  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 262 VEVTDCAQRGYTFVVVRCRDVPKLLFDTVCTITDAQYVVYHGNVSTEPDGvtayqeyYVRNKagLAATEPERLLLK---- 337
Cdd:PRK01759 667 VKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDG-------YVLDS--FIVTELNGKLLEfdrr 737

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126 338 RQLEAAV---------------------------ERRF-----ADGIELEVRSGDRAGLLSDVTRIIRENGLTILRAGVK 385
Cdd:PRK01759 738 RQLEQALtkalntnklkklnleenhklqhfhvktEVRFlneekQEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKIT 817

                        170
                 ....*....|....
gi 357163126 386 SQGGEAVDTFYVSD 399
Cdd:PRK01759 818 TIGEKAEDFFILTN 831
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 354-404 6.60e-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: 38.06  E-value: 6.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 357163126  354 LEVRSGDRAGLLSDVTRIIRENGLTILRA--GVKSQGGEAVDTFYVSDPMGLD 404
Cdd:pfam01842   3 LEVLVPDRPGLLARVLGALADRGINITSIeqGTSEDKGGIVFVVIVVDEEDLE 55
glnD PRK00275
PII uridylyl-transferase; Provisional
 32-167 9.54e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 41.97  E-value: 9.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357163126  32 GTFIQVDSVNTHGTLLALVQVITDLNLVVRKA-YFTADGDWFMDVFYVTDRDGEKV-TDEATLNYIQTTLesddcyyTEA 109
Cdd:PRK00275 704 GTQIFIYAPDQHDFFAATVAAMDQLNLNIHDArIITSSSQFTLDTYIVLDDDGEPIgDNPARIEQIREGL-------TEA 776

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357163126 110 RDNSADI----------------VPSE---SEEDSHQYSSIELTGTDRPGLLSEVCAVLSDVRCAVVSADLWTCNTR 167
Cdd:PRK00275 777 LRNPDDYptiiqrrvprqlkhfaFPTQvtiSNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGER 853
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
 131-157 2.91e-03

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


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 36.38  E-value: 2.91e-03
                          10        20
                  ....*....|....*....|....*..
gi 357163126  131 IELTGTDRPGLLSEVCAVLSDVRCAVV 157
Cdd:pfam13740   5 ITATGPDRPGLTASLTAVLAEHGCNIL 31
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 354-397 6.00e-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: 34.96  E-value: 6.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 357163126 354 LEVRSGDRAGLLSDVTRIIRENGLTILRAGVKSQGGEAVDTFYV 397
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFI 44
 
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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