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Conserved domains on  [gi|18411317|ref|NP_565146|]
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ACT domain repeat 3 [Arabidopsis thaliana]

Protein Classification

phosphoglycerate dehydrogenase( domain architecture ID 10141585)

phosphoglycerate dehydrogenase catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, the first step in serine biosynthesis

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 ...
 264-338 1.99e-45

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: 152.19  E-value: 1.99e-45
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18411317 264 YSVINVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHASQEYFIRHKDGCTLDTEGEKERVVKCLEAAIHRR 338
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 35-106 1.13e-42

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: 144.90  E-value: 1.13e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411317  35 CTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKVLGPKG 106
Cdd:cd04895   1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 3.64e-40

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: 138.33  E-value: 3.64e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18411317 129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDNATSRAVDDPERLSSMEEQLNNVLRG 202
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 342-413 1.14e-38

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: 134.40  E-value: 1.14e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411317 342 GWSLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALRGEIGHSMM 413
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
 
Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 264-338 1.99e-45

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: 152.19  E-value: 1.99e-45
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18411317 264 YSVINVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHASQEYFIRHKDGCTLDTEGEKERVVKCLEAAIHRR 338
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 35-106 1.13e-42

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: 144.90  E-value: 1.13e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411317  35 CTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKVLGPKG 106
Cdd:cd04895   1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 3.64e-40

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: 138.33  E-value: 3.64e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18411317 129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDNATSRAVDDPERLSSMEEQLNNVLRG 202
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 342-413 1.14e-38

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: 134.40  E-value: 1.14e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411317 342 GWSLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALRGEIGHSMM 413
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 119-408 1.17e-20

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 95.21  E-value: 1.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317 119 RVGVHSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEA--WTHNRRIAcVLYVNDnATSRAVDDPERLSSMEEQL 196
Cdd:COG2844 670 LIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhtTRDGYALD-TFIVLD-PDGEPIDDPDRLERIEQAL 747

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317 197 NNVLRGCEEQDEKFARtslsigstHVDRRLHQmfFAdrdyeavtklddsascgFEPKITVEHCEEKGYSVINVSCEDRPk 276
Cdd:COG2844 748 EEALSGEVPLPEPLAR--------RLSRRLRH--FP-----------------VPPRVTFDNDASNRYTVLEVSALDRP- 799

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317 277 lmfdivctltdmqyivfhatisssgshasqeyfirhkdgctldtegekervvkcleaaihrrvsegwslelcakdrvGLL 356
Cdd:COG2844 800 -----------------------------------------------------------------------------GLL 802

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 18411317 357 SEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPV-DVKTIEALRGEI 408
Cdd:COG2844 803 YDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLtDPERQEALREAL 855
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 23-201 6.44e-15

[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: 77.07  E-value: 6.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317    23 PSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYI-SSDGGWFMDVFHVTDQQGNKVTDSKT----IDY 97
Cdd:TIGR01693 656 PLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVnTTKDGVALDTFVVQDLFGSPPAAERVfqelLQG 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317    98 IEKVLGPKGHASASQNTWPGKRVGV-------------HSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTH 164
Cdd:TIGR01693 736 LVDVLAGLAKDPDTISARRARRRRLqhfavpprvtilnTASRKATIMEVRALDRPGLLARVGRTLEELGLSIQSAKITTF 815

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 18411317   165 NRRIACVLYVNDNATSRAVDdpERLSSMEEQLNNVLR 201
Cdd:TIGR01693 816 GEKAEDVFYVTDLFGLKLTD--EEEQRLLEVLAASVA 850
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 119-406 1.44e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.82  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  119 RVGVHSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWT-HNRRIACVLYVNDnATSRAVDDPERLSSMEEQLN 197
Cdd:PRK05092 723 EVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTtTDGRALDTFWIQD-AFGRDEDEPRRLARLAKAIE 801

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  198 NVLRGCEEQDEKFARtslsigSTHVDRRLHQmfFAdrdyeavtklddsascgFEPKITVEHCEEKGYSVINVSCEDRPkl 277
Cdd:PRK05092 802 DALSGEVRLPEALAK------RTKPKKRARA--FH-----------------VPPRVTIDNEASNRFTVIEVNGRDRP-- 854

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  278 mfdivctltdmqyivfhatisssgshasqeyfirhkdgctldtegekervvkcleaaihrrvsegwslelcakdrvGLLS 357
Cdd:PRK05092 855 ----------------------------------------------------------------------------GLLY 858

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18411317  358 EVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASG----NPVDVKTIE-ALRG 406
Cdd:PRK05092 859 DLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGlkitNEARQAAIRrALLA 912
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 22-102 1.77e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.43  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   22 PPSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKV 101
Cdd:PRK05092 830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                 .
gi 18411317  102 L 102
Cdd:PRK05092 910 L 910
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 22-102 7.22e-11

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 64.39  E-value: 7.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  22 PPSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKV 101
Cdd:COG2844 775 PPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREA 854


                .
gi 18411317 102 L 102
Cdd:COG2844 855 L 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 67-205 2.35e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 62.96  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   67 YISSDGgWFMDVFHVTDQQG---------NKVTDSktidyIEKVLgpKGHASASQ----NTWPGKR---------VGVH- 123
Cdd:PRK05092 766 FTTTDG-RALDTFWIQDAFGrdedeprrlARLAKA-----IEDAL--SGEVRLPEalakRTKPKKRarafhvpprVTIDn 837

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  124 SLGD-HTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDnATSRAVDDPERLSSMEEQLNNVLRG 202
Cdd:PRK05092 838 EASNrFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTD-LFGLKITNEARQAAIRRALLAALAE 916


                 ...
gi 18411317  203 CEE 205
Cdd:PRK05092 917 GEA 919
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 345-396 3.34e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 62.32  E-value: 3.34e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18411317  345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPV 396
Cdd:PRK03381 710 LEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPL 761
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 129-201 3.97e-09

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: 52.69  E-value: 3.97e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18411317   129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIacvlyvnDNATSRAVDDPERLSSMEEQLNNVLR 201
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG-------GIVFVVIVVDEEDLEEVLEALKKLEG 66
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 344-406 2.95e-08

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: 50.38  E-value: 2.95e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18411317   344 SLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQA--VNVFYVKDASGNPVDVKTIEALRG 406
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGgiVFVVIVVDEEDLEEVLEALKKLEG 66
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 265-332 3.01e-06

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: 44.61  E-value: 3.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411317   265 SVINVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHAsqEYFIRHKDGCTLDTEGEKERVVKCLE 332
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG--GIVFVVIVVDEEDLEEVLEALKKLEG 66
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
129-169 3.42e-06

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 49.38  E-value: 3.42e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 18411317 129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIA 169
Cdd:COG0317 647 VDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTA 687
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 36-88 4.24e-06

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: 44.22  E-value: 4.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18411317    36 TLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDG--GWFMDVFHVTDQQGNK 88
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEdkGGIVFVVIVVDEEDLE 55
 
Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 264-338 1.99e-45

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: 152.19  E-value: 1.99e-45
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18411317 264 YSVINVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHASQEYFIRHKDGCTLDTEGEKERVVKCLEAAIHRR 338
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 35-106 1.13e-42

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: 144.90  E-value: 1.13e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411317  35 CTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKVLGPKG 106
Cdd:cd04895   1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 3.64e-40

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: 138.33  E-value: 3.64e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18411317 129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDNATSRAVDDPERLSSMEEQLNNVLRG 202
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 342-413 1.14e-38

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: 134.40  E-value: 1.14e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411317 342 GWSLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALRGEIGHSMM 413
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 345-412 2.90e-26

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: 100.99  E-value: 2.90e-26
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411317 345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALRGEIGHSM 412
Cdd:cd04899   3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 129-200 5.99e-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: 89.05  E-value: 5.99e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411317 129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDNATSRavDDPERLSSMEEQLNNVL 200
Cdd:cd04899   1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQP--LDPERQEALRAALGEAL 70
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 119-408 1.17e-20

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 95.21  E-value: 1.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317 119 RVGVHSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEA--WTHNRRIAcVLYVNDnATSRAVDDPERLSSMEEQL 196
Cdd:COG2844 670 LIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhtTRDGYALD-TFIVLD-PDGEPIDDPDRLERIEQAL 747

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317 197 NNVLRGCEEQDEKFARtslsigstHVDRRLHQmfFAdrdyeavtklddsascgFEPKITVEHCEEKGYSVINVSCEDRPk 276
Cdd:COG2844 748 EEALSGEVPLPEPLAR--------RLSRRLRH--FP-----------------VPPRVTFDNDASNRYTVLEVSALDRP- 799

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317 277 lmfdivctltdmqyivfhatisssgshasqeyfirhkdgctldtegekervvkcleaaihrrvsegwslelcakdrvGLL 356
Cdd:COG2844 800 -----------------------------------------------------------------------------GLL 802

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 18411317 357 SEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPV-DVKTIEALRGEI 408
Cdd:COG2844 803 YDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLtDPERQEALREAL 855
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 345-412 2.32e-19

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: 81.83  E-value: 2.32e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411317 345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALRGEIGHSM 412
Cdd:cd04873   3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 23-200 1.92e-17

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 85.19  E-value: 1.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  23 PSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYI-SSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKV 101
Cdd:COG2844 667 PLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhTTRDGYALDTFIVLDPDGEPIDDPDRLERIEQA 746

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317 102 L-----GPKGHASASQNTWPGK--------RVGVH--SLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAeawthnr 166
Cdd:COG2844 747 LeealsGEVPLPEPLARRLSRRlrhfpvppRVTFDndASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSA------- 819

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18411317 167 RIAC-------VLYVNDnATSRAVDDPERLSSMEEQLNNVL 200
Cdd:COG2844 820 KIATlgervedVFYVTD-LDGQKLTDPERQEALREALLEAL 859
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 36-102 2.41e-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: 76.05  E-value: 2.41e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411317  36 TLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKvTDSKTIDYIEKVL 102
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRP-LDPERIARLEEAL 66
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 129-200 3.54e-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: 75.66  E-value: 3.54e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411317 129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDNATSRavDDPERLSSMEEQLNNVL 200
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRP--LDPERIARLEEALEDAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 265-335 1.11e-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: 71.43  E-value: 1.11e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18411317 265 SVINVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHASQEYFIRHKDGCTLDTEgEKERVVKCLEAAI 335
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPE-RIARLEEALEDAL 70
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 23-201 6.44e-15

[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: 77.07  E-value: 6.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317    23 PSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYI-SSDGGWFMDVFHVTDQQGNKVTDSKT----IDY 97
Cdd:TIGR01693 656 PLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVnTTKDGVALDTFVVQDLFGSPPAAERVfqelLQG 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317    98 IEKVLGPKGHASASQNTWPGKRVGV-------------HSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTH 164
Cdd:TIGR01693 736 LVDVLAGLAKDPDTISARRARRRRLqhfavpprvtilnTASRKATIMEVRALDRPGLLARVGRTLEELGLSIQSAKITTF 815

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 18411317   165 NRRIACVLYVNDNATSRAVDdpERLSSMEEQLNNVLR 201
Cdd:TIGR01693 816 GEKAEDVFYVTDLFGLKLTD--EEEQRLLEVLAASVA 850
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 119-406 1.44e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.82  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  119 RVGVHSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWT-HNRRIACVLYVNDnATSRAVDDPERLSSMEEQLN 197
Cdd:PRK05092 723 EVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTtTDGRALDTFWIQD-AFGRDEDEPRRLARLAKAIE 801

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  198 NVLRGCEEQDEKFARtslsigSTHVDRRLHQmfFAdrdyeavtklddsascgFEPKITVEHCEEKGYSVINVSCEDRPkl 277
Cdd:PRK05092 802 DALSGEVRLPEALAK------RTKPKKRARA--FH-----------------VPPRVTIDNEASNRFTVIEVNGRDRP-- 854

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  278 mfdivctltdmqyivfhatisssgshasqeyfirhkdgctldtegekervvkcleaaihrrvsegwslelcakdrvGLLS 357
Cdd:PRK05092 855 ----------------------------------------------------------------------------GLLY 858

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18411317  358 EVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASG----NPVDVKTIE-ALRG 406
Cdd:PRK05092 859 DLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGlkitNEARQAAIRrALLA 912
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 22-102 1.77e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.43  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   22 PPSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKV 101
Cdd:PRK05092 830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                 .
gi 18411317  102 L 102
Cdd:PRK05092 910 L 910
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 110-412 2.98e-11

[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: 65.51  E-value: 2.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   110 ASQNTWPGKRVGVHSLGDhTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWT-HNRRIACVLYVNDnATSRAVDDPER 188
Cdd:TIGR01693 651 LSSGGPLALIDGTRPSGG-TEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTtKDGVALDTFVVQD-LFGSPPAAERV 728

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   189 LSSMEEQLNNVLRGCEEQDEkfartslsigsTHVDRRLHQmffadRDYEAVTklddsascgFEPKITVEHceekgysvin 268
Cdd:TIGR01693 729 FQELLQGLVDVLAGLAKDPD-----------TISARRARR-----RRLQHFA---------VPPRVTILN---------- 773

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   269 vscedrpklmfdivctltdmqyivfhatisssgsHASQEYFIrhkdgctldtegekervvkcleaaihrrvsegwsLELC 348
Cdd:TIGR01693 774 ----------------------------------TASRKATI----------------------------------MEVR 785

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18411317   349 AKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALRGEIGHSM 412
Cdd:TIGR01693 786 ALDRPGLLARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAASV 849
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 22-102 7.22e-11

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 64.39  E-value: 7.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  22 PPSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKV 101
Cdd:COG2844 775 PPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREA 854


                .
gi 18411317 102 L 102
Cdd:COG2844 855 L 855
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 44-104 8.31e-11

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: 57.75  E-value: 8.31e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18411317  44 NKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVtDSKTIDYIEKVLGP 104
Cdd:cd04926  10 DRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPV-DPKTIEAVRQEIGP 69
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 36-103 1.79e-10

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: 56.69  E-value: 1.79e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411317  36 TLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKvTDSKTIDYIEKVLG 103
Cdd:cd04899   1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQP-LDPERQEALRAALG 67
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 67-205 2.35e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 62.96  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   67 YISSDGgWFMDVFHVTDQQG---------NKVTDSktidyIEKVLgpKGHASASQ----NTWPGKR---------VGVH- 123
Cdd:PRK05092 766 FTTTDG-RALDTFWIQDAFGrdedeprrlARLAKA-----IEDAL--SGEVRLPEalakRTKPKKRarafhvpprVTIDn 837

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  124 SLGD-HTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDnATSRAVDDPERLSSMEEQLNNVLRG 202
Cdd:PRK05092 838 EASNrFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTD-LFGLKITNEARQAAIRRALLAALAE 916


                 ...
gi 18411317  203 CEE 205
Cdd:PRK05092 917 GEA 919
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 345-396 3.34e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 62.32  E-value: 3.34e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18411317  345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPV 396
Cdd:PRK03381 710 LEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPL 761
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 129-201 3.97e-09

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: 52.69  E-value: 3.97e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18411317   129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIacvlyvnDNATSRAVDDPERLSSMEEQLNNVLR 201
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG-------GIVFVVIVVDEEDLEEVLEALKKLEG 66
glnD PRK00275
PII uridylyl-transferase; Provisional
 52-209 4.40e-09

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 58.91  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   52 VVQVLTDLDLTITKAYI-SSDGGWFMDVFHVTDQQGNKV-TDSKTIDYIEKVLG-----PKGHASASQNTWPGK------ 118
Cdd:PRK00275 721 TVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIgDNPARIEQIREGLTealrnPDDYPTIIQRRVPRQlkhfaf 800

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  119 --RVGVHS--LGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDnATSRAVDDPERLSSMEE 194
Cdd:PRK00275 801 ptQVTISNdaQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITD-ADNQPLSDPQLCSRLQD 879

                        170
                 ....*....|....*
gi 18411317  195 QLnnvlrgCEEQDEK 209
Cdd:PRK00275 880 AI------CEQLDAR 888
glnD PRK00275
PII uridylyl-transferase; Provisional
 345-408 2.10e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 56.60  E-value: 2.10e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18411317  345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPV-DVKTIEALRGEI 408
Cdd:PRK00275 817 LEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLsDPQLCSRLQDAI 881
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 344-406 2.95e-08

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: 50.38  E-value: 2.95e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18411317   344 SLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQA--VNVFYVKDASGNPVDVKTIEALRG 406
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGgiVFVVIVVDEEDLEEVLEALKKLEG 66
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 131-196 2.23e-07

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: 47.67  E-value: 2.23e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411317 131 IEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNR-RIACVLYVndnatsraVDDPERLSSMEEQL 196
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDgGEADIFIV--------VDGDGDLEKLLEAL 59
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
237-405 3.88e-07

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 52.67  E-value: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  237 EAVTKLDDSascgfEPKITVEHCEEKGYSVINVSCEDRPKLmFDIVCTLTDMQYI-VFHATISSSgshasqeyfirhKDG 315
Cdd:PRK05007 679 RHLLQHDLD-----KPLVLLSKQATRGGTEIFIWSPDRPYL-FAAVCAELDRRNLsVHDAQIFTS------------RDG 740

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  316 CTLDT------------EGEKERVVKCLEAAI------------------HRRV----------SEGWS-LELCAKDRVG 354
Cdd:PRK05007 741 MAMDTfivlepdgsplsQDRHQVIRKALEQALtqsspqppkprrlpaklrHFNVptevsflpthTDRRSyMELIALDQPG 820

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18411317  355 LLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALR 405
Cdd:PRK05007 821 LLARVGKIFADLGISLHGARITTIGERVEDLFILATADRRALNEELQQELR 871
glnD PRK00275
PII uridylyl-transferase; Provisional
 22-91 5.48e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 51.98  E-value: 5.48e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   22 PPSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTD 91
Cdd:PRK00275 801 PTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSD 870
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
 131-169 7.55e-07

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: 46.29  E-value: 7.55e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18411317 131 IEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIA 169
Cdd:cd04876   1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDGLA 39
PRK03059 PRK03059
PII uridylyl-transferase; Provisional
 343-391 2.13e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 235101 [Multi-domain]  Cd Length: 856  Bit Score: 50.29  E-value: 2.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 18411317  343 WSLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDA 391
Cdd:PRK03059 787 YILSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDGS 835
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 265-332 3.01e-06

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: 44.61  E-value: 3.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411317   265 SVINVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHAsqEYFIRHKDGCTLDTEGEKERVVKCLE 332
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG--GIVFVVIVVDEEDLEEVLEALKKLEG 66
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
129-169 3.42e-06

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 49.38  E-value: 3.42e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 18411317 129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIA 169
Cdd:COG0317 647 VDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTA 687
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 36-88 4.24e-06

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: 44.22  E-value: 4.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18411317    36 TLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDG--GWFMDVFHVTDQQGNK 88
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEdkGGIVFVVIVVDEEDLE 55
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
23-200 5.22e-06

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 48.96  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   23 PSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYI-SSDGGWFMDVFHVTDQQGNKV------------ 89
Cdd:PRK01759 665 LLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIiTSQDGYVLDSFIVTELNGKLLefdrrrqleqal 744

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   90 TDSKTIDYIEKVLGPKGHASASQNTWPGKRVGVHSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRiA 169
Cdd:PRK01759 745 TKALNTNKLKKLNLEENHKLQHFHVKTEVRFLNEEKQEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEK-A 823

                        170       180       190
                 ....*....|....*....|....*....|.
gi 18411317  170 CVLYVNDNATSRAVDDPERlssmeEQLNNVL 200
Cdd:PRK01759 824 EDFFILTNQQGQALDEEER-----KALKSRL 849
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
42-189 5.88e-06

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 48.82  E-value: 5.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   42 SMNKPGILLEVVQVLTDLDLTITKAYI-SSDGGWFMDVFHVTDQQGNKVTDSK---TIDYIEKVLG------PKGHASAS 111
Cdd:PRK05007 708 SPDRPYLFAAVCAELDRRNLSVHDAQIfTSRDGMAMDTFIVLEPDGSPLSQDRhqvIRKALEQALTqsspqpPKPRRLPA 787

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  112 Q----------NTWPGKRVGvhslgdHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRiACVLYVNDNATSR 181
Cdd:PRK05007 788 KlrhfnvptevSFLPTHTDR------RSYMELIALDQPGLLARVGKIFADLGISLHGARITTIGER-VEDLFILATADRR 860


                 ....*...
gi 18411317  182 AVDDPERL 189
Cdd:PRK05007 861 ALNEELQQ 868
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 36-102 7.56e-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: 43.62  E-value: 7.56e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411317  36 TLVKVDSMNKPGILLEVVQVLTDLDLTITKAYI-SSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKVL 102
Cdd:cd04900   2 TEVFIYTPDRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGERERLARIREAL 69
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 37-106 1.74e-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: 1.74e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18411317  37 LVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSD-GGWFMDVFHVTDQQ---GNKVTDSKTIDYIEKVLGPKG 106
Cdd:cd04927   2 LLKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTpDGRVLDLFFITDARellHTKKRREETYDYLRAVLGDSM 75
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 345-405 2.04e-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: 41.89  E-value: 2.04e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18411317 345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVkDASGNPVDVKTIEALR 405
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFI-VVDGDGDLEKLLEALE 60
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 129-200 2.93e-05

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: 42.08  E-value: 2.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18411317 129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIAC-VLYVNDNATsRAVDDPERLSSMEEQLNNVL 200
Cdd:cd04900   2 TEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALdTFVVLDPDG-EPIGERERLARIREALEDAL 73
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
345-405 2.94e-05

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 46.65  E-value: 2.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18411317  345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALR 405
Cdd:PRK01759 786 MELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEKAEDFFILTNQQGQALDEEERKALK 846
ACT_4 pfam13291
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 129-161 4.83e-05

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.


Pssm-ID: 463831 [Multi-domain]  Cd Length: 79  Bit Score: 41.39  E-value: 4.83e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 18411317   129 TSIEIIARDRPGLLSEVSAVLADLNINVVAAEA 161
Cdd:pfam13291   6 VDLEVEAIDRPGLLADITQVISEEKANIVSVNA 38
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
345-405 6.18e-05

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 45.73  E-value: 6.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18411317  345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALR 405
Cdd:PRK04374 799 ISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALR 859
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
130-164 6.78e-05

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


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 43.29  E-value: 6.78e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 18411317 130 SIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTH 164
Cdd:COG2716  92 VVEVVGNDRPGIVAEVTQFLAERGINIEDLSTKTY 126
PRK03059 PRK03059
PII uridylyl-transferase; Provisional
 73-159 7.70e-05

PII uridylyl-transferase; Provisional


Pssm-ID: 235101 [Multi-domain]  Cd Length: 856  Bit Score: 45.28  E-value: 7.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317   73 GWFMDVFHVTDQqGNKVTDSKTIDYIEKVLG------------PKGHASASQNTWPGK-RVgvhSL-----GDHTSIEII 134
Cdd:PRK03059 717 GYALDTFQVLDP-EEDVHYRDIINLVEHELAerlaeqaplpepSKGRLSRQVKHFPITpRV---DLrpderGQYYILSVS 792

                         90       100
                 ....*....|....*....|....*
gi 18411317  135 ARDRPGLLSEVSAVLADLNINVVAA 159
Cdd:PRK03059 793 ANDRPGLLYAIARVLAEHRVSVHTA 817
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 354-411 1.05e-04

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: 40.52  E-value: 1.05e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18411317 354 GLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPV-DVKTIEALRGEIGHS 411
Cdd:cd04895  13 GILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLtDDSLIAYIEKSLGTS 71
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 344-404 1.06e-04

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: 40.49  E-value: 1.06e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18411317 344 SLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKD-ASGNPVD----VKTIEAL 404
Cdd:cd04925   2 AIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDeETGAPIDdpirLASIEDR 67
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 131-188 1.38e-04

C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD includes the C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB. AcuB is putatively involved in the anaerobic catabolism of acetoin, and related proteins. Studies report the induction of AcuB by nitrate respiration and also by fermentation. Since acetoin can be secreted and later serve as a source of carbon, it has been proposed that, during anaerobic growth when other carbon sources are exhausted, the induction of the AcuB protein results in acetoin catabolism. AcuB-like proteins have two N-terminal tandem CBS domains and a single C-terminal ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153155  Cd Length: 72  Bit Score: 39.93  E-value: 1.38e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18411317 131 IEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNR---RIAcVLYVNDNATSRAVDDPER 188
Cdd:cd04883   4 IEVRVPDRPGQLADIAAIFKDRGVNIVSVLVYPSKEednKIL-VFRVQTMNPRPIIEDLRR 63
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 38-86 1.54e-04

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: 39.58  E-value: 1.54e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18411317  38 VKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDG-GWFMDVFHVTDQQG 86
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGdGGEADIFIVVDGDG 50
PRK08577 PRK08577
hypothetical protein; Provisional
 131-194 2.57e-04

hypothetical protein; Provisional


Pssm-ID: 236301 [Multi-domain]  Cd Length: 136  Bit Score: 41.13  E-value: 2.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411317  131 IEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNR--RIACVLYVNdnaTSRAVDDP----ERLSSMEE 194
Cdd:PRK08577  59 IELVVEDRPGVLAKITGLLAEHGVDILATECEELKRgeLAECVIIVD---LSKSDIDLeeleEELKKLEE 125
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 347-403 2.63e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 43.44  E-value: 2.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18411317  347 LCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEA 403
Cdd:PRK03381 604 VVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGSPPDAALLRQ 660
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 130-196 3.12e-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: 3.12e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411317 130 SIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDnATSRAVdDPERLSSMEEQL 196
Cdd:cd04926   3 RLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTD-ANGNPV-DPKTIEAVRQEI 67
ACT_GcvR_2 cd04869
ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, ...
 130-156 8.49e-04

ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains; This CD includes the second 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: 153141 [Multi-domain]  Cd Length: 81  Bit Score: 37.97  E-value: 8.49e-04
                        10        20
                ....*....|....*....|....*..
gi 18411317 130 SIEIIARDRPGLLSEVSAVLADLNINV 156
Cdd:cd04869   1 VVEVVGNDRPGIVHEVTQFLAQRNINI 27
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 127-191 9.11e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 41.90  E-value: 9.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18411317  127 DHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDNATSRAVDDPERLSS 191
Cdd:PRK03381 706 DATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPLADARAAVEQ 770
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 22-92 2.95e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 39.97  E-value: 2.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18411317   22 PPSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDS 92
Cdd:PRK03381 694 PPRVLWLDGASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPLADA 764
ACT_ThrD-II-like cd04886
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and ...
 131-166 2.99e-03

C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains; This CD includes the C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains. The Escherichia coli tdcB gene product, ThrD-II, anaerobically catalyzes the pyridoxal phosphate-dependent dehydration of L-threonine and L-serine to ammonia and to alpha-ketobutyrate and pyruvate, respectively. Tetrameric ThrD-II is subject to allosteric activation by AMP, inhibition by alpha-keto acids, and catabolite inactivation by several metabolites of glycolysis and the citric acid cycle. Also included in this CD are N-terminal ACT domains present in smaller (~170 a.a.) archaeal proteins of unknown function. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153158 [Multi-domain]  Cd Length: 73  Bit Score: 36.37  E-value: 2.99e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 18411317 131 IEIIARDRPGLLSEVSAVLADLNINVVAAEawtHNR 166
Cdd:cd04886   1 LRVELPDRPGQLAKLLAVIAEAGANIIEVS---HDR 33
ACT_Af1403 cd04874
N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid ...
 131-160 3.10e-03

N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, and related domains; This CD includes the N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, from Archaeoglobus fulgidus and other related archeal ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153146 [Multi-domain]  Cd Length: 72  Bit Score: 36.12  E-value: 3.10e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 18411317 131 IEIIARDRPGLLSEVSAVLADLNINVVAAE 160
Cdd:cd04874   3 LSIIAEDKPGVLRDLTGVIAEHGGNITYTQ 32
ACT_1ZPV cd04872
ACT domain proteins similar to the yet uncharacterized Streptococcus pneumoniae ACT domain ...
 131-157 3.20e-03

ACT domain proteins similar to the yet uncharacterized Streptococcus pneumoniae ACT domain protein; This CD, ACT_1ZPV, includes those single ACT domain proteins similar to the yet uncharacterized Streptococcus pneumoniae ACT domain protein (pdb structure 1ZPV). Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153144 [Multi-domain]  Cd Length: 88  Bit Score: 36.83  E-value: 3.20e-03
                        10        20
                ....*....|....*....|....*..
gi 18411317 131 IEIIARDRPGLLSEVSAVLADLNINVV 157
Cdd:cd04872   4 ITVVGKDRVGIVAGVSTKLAELNVNIL 30
ACT_TyrKc cd04928
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ...
 38-82 4.10e-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: 35.99  E-value: 4.10e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18411317  38 VKVDSMNKPGILLEVVQVLTDLDLTITKAYI-SSDGGWFMDVFHVT 82
Cdd:cd04928   4 ITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAfSTDDGLALDIFVVT 49
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 267-332 6.32e-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: 6.32e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18411317 267 INVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHASQEYFIRhkdgctLDTEGEKERVVKCLE 332
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIV------VDGDGDLEKLLEALE 60
ACT COG3830
ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];
131-157 7.08e-03

ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];


Pssm-ID: 443042 [Multi-domain]  Cd Length: 212  Bit Score: 37.76  E-value: 7.08e-03
                        10        20
                ....*....|....*....|....*..
gi 18411317 131 IEIIARDRPGLLSEVSAVLADLNINVV 157
Cdd:COG3830   7 ITVTGKDRPGITAAVSGVLAEHGVNIL 33
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 342-397 7.81e-03

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: 35.15  E-value: 7.81e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18411317 342 GWSLELCAKDRVGLLSEVTRILREHGLSVSRAGV-TTVGEQAVNVFYVKDASGNPVD 397
Cdd:cd04900   1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIG 57
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 345-412 8.10e-03

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: 35.14  E-value: 8.10e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18411317 345 LELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAV-NVFYVKDA----SGNPVDVKTIEALRGEIGHSM 412
Cdd:cd04927   3 LKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTPDGRVlDLFFITDArellHTKKRREETYDYLRAVLGDSM 75
 
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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