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Conserved domains on  [gi|1063708906|ref|NP_001327460|]
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ACT domain repeat 6 [Arabidopsis thaliana]

Protein Classification

sigma-54-dependent Fis family transcriptional regulator( domain architecture ID 10289074)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 119-192 1.06e-38

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: 134.09  E-value: 1.06e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSTHSAITDPIRLSTIKELLCNVVRT 192
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 248-322 6.40e-38

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: 132.16  E-value: 6.40e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906 248 YTVVTMRSKDRPKLVFDVVCTLTDMQYVVFHGMVSTEPVEAYQEFYIRHVDGLPINSEAEQERVIQCLEAAIERR 322
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 326-395 2.13e-35

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: 125.15  E-value: 2.13e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 326 GLELELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVESKIVESIRQQIGVS 395
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPA 70
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 28-99 2.78e-32

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


The actual alignment was detected with superfamily member cd04895:

Pssm-ID: 471857 [Multi-domain]  Cd Length: 72  Bit Score: 117.17  E-value: 2.78e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063708906  28 ATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKIRDTQVLDYIQKRIESNA 99
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
 
Name Accession Description Interval E-value
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 119-192 1.06e-38

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: 134.09  E-value: 1.06e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSTHSAITDPIRLSTIKELLCNVVRT 192
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 248-322 6.40e-38

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: 132.16  E-value: 6.40e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906 248 YTVVTMRSKDRPKLVFDVVCTLTDMQYVVFHGMVSTEPVEAYQEFYIRHVDGLPINSEAEQERVIQCLEAAIERR 322
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 326-395 2.13e-35

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: 125.15  E-value: 2.13e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 326 GLELELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVESKIVESIRQQIGVS 395
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPA 70
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 28-99 2.78e-32

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: 117.17  E-value: 2.78e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063708906  28 ATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKIRDTQVLDYIQKRIESNA 99
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 7-189 1.61e-18

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 88.27  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906   7 AKLIRRMNP---PRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYI-SSDGGWFMDVFKVIDQDGNKI 82
Cdd:COG2844   655 ARLLLRADDsgkPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhTTRDGYALDTFIVLDPDGEPI 734

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  83 RDTQVLDYIQKRIE---SNAGWFIPPLRSSVGV------MPT---------DEYTSIELAGTDRPGLLSEVSAVLTDLHC 144
Cdd:COG2844   735 DDPDRLERIEQALEealSGEVPLPEPLARRLSRrlrhfpVPPrvtfdndasNRYTVLEVSALDRPGLLYDIARVLADLGL 814

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1063708906 145 NVVNAEIWTHNTRAAAVIHVTDnSTHSAITDPIRLSTIKELLCNV 189
Cdd:COG2844   815 NIHSAKIATLGERVEDVFYVTD-LDGQKLTDPERQEALREALLEA 858
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 105-326 1.04e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.82  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 105 PLRSSVGVMPTDEYTSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWT-HNTRAAAVIHVTDNSTHsAITDPIRLSTIK 183
Cdd:PRK05092  719 PLATEVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTtTDGRALDTFWIQDAFGR-DEDEPRRLARLA 797

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 184 ELLCNVVrtnSGsraaktvfscsdthrERRLHQIMfDDRDyEGVKRARTSASRPSVTLMN-IEKDYTVVTMRSKDRPKLV 262
Cdd:PRK05092  798 KAIEDAL---SG---------------EVRLPEAL-AKRT-KPKKRARAFHVPPRVTIDNeASNRFTVIEVNGRDRPGLL 857

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063708906 263 FDVVCTLTDMQYVVFHGMVSTEPVEAYQEFYIRHVDGLPINSEAEQERVIQCLEAAIERRASEG 326
Cdd:PRK05092  858 YDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEGEAEA 921
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 15-95 1.95e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.05  E-value: 1.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  15 PPRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKIRDTQVLDYIQKR 94
Cdd:PRK05092  830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                  .
gi 1063708906  95 I 95
Cdd:PRK05092  910 L 910
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 233-395 1.25e-10

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


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 63.58  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 233 SASRPSVTLMNIEKDYTV-VTMRSKDRPKLVFDVVCTLtDMQYVVFHG--MVSTEPVEAYQEFYIRHVDGLPINSEAEQE 309
Cdd:TIGR01693 652 SSGGPLALIDGTRPSGGTeVFIYAPDQPGLFAKVAGAL-AMLSLSVHDaqVNTTKDGVALDTFVVQDLFGSPPAAERVFQ 730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 310 RVIQCLEAAIERRA--------------------------------SEGLELELSAEDRVGLLSDITRTFRENSLTIVRA 357
Cdd:TIGR01693 731 ELLQGLVDVLAGLAkdpdtisarrarrrrlqhfavpprvtilntasRKATIMEVRALDRPGLLARVGRTLEELGLSIQSA 810

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063708906 358 EISTREGKAKDTFYVTDVTGNPVESKIVESIRQQIGVS 395
Cdd:TIGR01693 811 KITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAAS 848
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 329-393 3.22e-07

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 47.30  E-value: 3.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906 329 LELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFyVTDVTGNPVESKIVESIRQQIG 393
Cdd:pfam01842   3 LEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVF-VVIVVDEEDLEEVLEALKKLEG 66
glnD PRK00275
PII uridylyl-transferase; Provisional
 329-380 6.20e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 48.51  E-value: 6.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063708906 329 LELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPV 380
Cdd:PRK00275  817 LEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPL 868
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 119-191 6.49e-05

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: 40.75  E-value: 6.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVtdnsthsAITDPIRLSTIKELLCNVVR 191
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVV-------IVVDEEDLEEVLEALKKLEG 66
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
305-394 2.26e-03

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 40.52  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 305 EAEQERVIQcLEAAIERRASEGLELELSAEDRVGLLSDITRTFRENSLTIVRAEISTRegkaKDTFYVTDVT---GNPVE 381
Cdd:COG0317   626 EREPERLID-VEWGEDSSGVFPVDIRIEALDRPGLLADITSVIAEEKINILSVNTRSR----DDGTATIRFTvevRDLDH 700

                          90
                  ....*....|....
gi 1063708906 382 -SKIVESIRQQIGV 394
Cdd:COG0317   701 lARVLRKLRKVPGV 714
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 29-81 2.64e-03

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: 36.13  E-value: 2.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906  29 TVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDG--GWFMDVFKVIDQDGNK 81
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEdkGGIVFVVIVVDEEDLE 55
 
Name Accession Description Interval E-value
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 119-192 1.06e-38

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: 134.09  E-value: 1.06e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSTHSAITDPIRLSTIKELLCNVVRT 192
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 248-322 6.40e-38

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: 132.16  E-value: 6.40e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906 248 YTVVTMRSKDRPKLVFDVVCTLTDMQYVVFHGMVSTEPVEAYQEFYIRHVDGLPINSEAEQERVIQCLEAAIERR 322
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 326-395 2.13e-35

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: 125.15  E-value: 2.13e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 326 GLELELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVESKIVESIRQQIGVS 395
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPA 70
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 28-99 2.78e-32

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: 117.17  E-value: 2.78e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063708906  28 ATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKIRDTQVLDYIQKRIESNA 99
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 329-393 8.38e-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: 88.28  E-value: 8.38e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906 329 LELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVESKIVESIRQQIG 393
Cdd:cd04899     3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALG 67
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 119-190 6.92e-21

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: 85.97  E-value: 6.92e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSTHSaiTDPIRLSTIKELLCNVV 190
Cdd:cd04899     1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQP--LDPERQEALRAALGEAL 70
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 7-189 1.61e-18

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 88.27  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906   7 AKLIRRMNP---PRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYI-SSDGGWFMDVFKVIDQDGNKI 82
Cdd:COG2844   655 ARLLLRADDsgkPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhTTRDGYALDTFIVLDPDGEPI 734

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  83 RDTQVLDYIQKRIE---SNAGWFIPPLRSSVGV------MPT---------DEYTSIELAGTDRPGLLSEVSAVLTDLHC 144
Cdd:COG2844   735 DDPDRLERIEQALEealSGEVPLPEPLARRLSRrlrhfpVPPrvtfdndasNRYTVLEVSALDRPGLLYDIARVLADLGL 814

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1063708906 145 NVVNAEIWTHNTRAAAVIHVTDnSTHSAITDPIRLSTIKELLCNV 189
Cdd:COG2844   815 NIHSAKIATLGERVEDVFYVTD-LDGQKLTDPERQEALREALLEA 858
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 327-392 9.86e-17

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


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 74.12  E-value: 9.86e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063708906 327 LELELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVESKIVESIRQQI 392
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEAL 66
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 119-189 7.27e-16

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: 71.81  E-value: 7.27e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSTHsaITDPIRLSTIKELLCNV 189
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGR--PLDPERIARLEEALEDA 69
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 229-392 7.78e-15

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 76.72  E-value: 7.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 229 RARTSASRPSVTLMNI-EKDYTVVTMRSKDRPKLVFDVVCTLTDMQYVVF--------HGMV-STepveayqeFYIRHVD 298
Cdd:COG2844   659 LRADDSGKPLVLIRPDpDRGGTEVFVYTPDRPGLFARIAGALAALGLNILdarihttrDGYAlDT--------FIVLDPD 730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 299 GLPINSEAEQERVIQCLEAA----------IERRASEGLE--------------------LELSAEDRVGLLSDITRTFR 348
Cdd:COG2844   731 GEPIDDPDRLERIEQALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLA 810

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1063708906 349 ENSLTIVRAEISTrEG-KAKDTFYVTDVTGNPVESK-IVESIRQQI 392
Cdd:COG2844   811 DLGLNIHSAKIAT-LGeRVEDVFYVTDLDGQKLTDPeRQEALREAL 855
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 249-319 8.13e-13

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: 63.34  E-value: 8.13e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063708906 249 TVVTMRSKDRPKLVFDVVCTLTDMQYVVFHGMVSTEPVEAYQEFYIRHVDGLPINSEaEQERVIQCLEAAI 319
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPE-RIARLEEALEDAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 29-96 4.20e-12

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: 61.02  E-value: 4.20e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063708906  29 TVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKIrDTQVLDYIQKRIE 96
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPL-DPERIARLEEALE 67
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 105-326 1.04e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.82  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 105 PLRSSVGVMPTDEYTSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWT-HNTRAAAVIHVTDNSTHsAITDPIRLSTIK 183
Cdd:PRK05092  719 PLATEVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTtTDGRALDTFWIQDAFGR-DEDEPRRLARLA 797

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 184 ELLCNVVrtnSGsraaktvfscsdthrERRLHQIMfDDRDyEGVKRARTSASRPSVTLMN-IEKDYTVVTMRSKDRPKLV 262
Cdd:PRK05092  798 KAIEDAL---SG---------------EVRLPEAL-AKRT-KPKKRARAFHVPPRVTIDNeASNRFTVIEVNGRDRPGLL 857

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063708906 263 FDVVCTLTDMQYVVFHGMVSTEPVEAYQEFYIRHVDGLPINSEAEQERVIQCLEAAIERRASEG 326
Cdd:PRK05092  858 YDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEGEAEA 921
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 15-95 1.95e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.05  E-value: 1.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  15 PPRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKIRDTQVLDYIQKR 94
Cdd:PRK05092  830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                  .
gi 1063708906  95 I 95
Cdd:PRK05092  910 L 910
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 233-395 1.25e-10

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


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 63.58  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 233 SASRPSVTLMNIEKDYTV-VTMRSKDRPKLVFDVVCTLtDMQYVVFHG--MVSTEPVEAYQEFYIRHVDGLPINSEAEQE 309
Cdd:TIGR01693 652 SSGGPLALIDGTRPSGGTeVFIYAPDQPGLFAKVAGAL-AMLSLSVHDaqVNTTKDGVALDTFVVQDLFGSPPAAERVFQ 730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 310 RVIQCLEAAIERRA--------------------------------SEGLELELSAEDRVGLLSDITRTFRENSLTIVRA 357
Cdd:TIGR01693 731 ELLQGLVDVLAGLAkdpdtisarrarrrrlqhfavpprvtilntasRKATIMEVRALDRPGLLARVGRTLEELGLSIQSA 810

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063708906 358 EISTREGKAKDTFYVTDVTGNPVESKIVESIRQQIGVS 395
Cdd:TIGR01693 811 KITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAAS 848
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 16-166 1.34e-10

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


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 63.58  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  16 PRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYI-SSDGGWFMDVFKVIDQDGNKIRDTQVL------ 88
Cdd:TIGR01693 656 PLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVnTTKDGVALDTFVVQDLFGSPPAAERVFqellqg 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  89 ----------DY----IQKRIESNAGWFIPPLRssVGVMPT--DEYTSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIW 152
Cdd:TIGR01693 736 lvdvlaglakDPdtisARRARRRRLQHFAVPPR--VTILNTasRKATIMEVRALDRPGLLARVGRTLEELGLSIQSAKIT 813

                         170
                  ....*....|....
gi 1063708906 153 THNTRAAAVIHVTD 166
Cdd:TIGR01693 814 TFGEKAEDVFYVTD 827
glnD PRK00275
PII uridylyl-transferase; Provisional
 26-187 1.73e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 56.60  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  26 DDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYI-SSDGGWFMDVFKVIDQDGNKIRD------------TQVLDY-- 90
Cdd:PRK00275  702 EGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIGDnparieqireglTEALRNpd 781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  91 -----IQKRIESNAGWFIPPLRSSVGVMPTDEYTSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVT 165
Cdd:PRK00275  782 dyptiIQRRVPRQLKHFAFPTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFIT 861

                         170       180
                  ....*....|....*....|..
gi 1063708906 166 DNSTHsAITDPIRLSTIKELLC 187
Cdd:PRK00275  862 DADNQ-PLSDPQLCSRLQDAIC 882
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 329-393 3.22e-07

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 47.30  E-value: 3.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906 329 LELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFyVTDVTGNPVESKIVESIRQQIG 393
Cdd:pfam01842   3 LEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVF-VVIVVDEEDLEEVLEALKKLEG 66
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 326-392 7.55e-07

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: 46.32  E-value: 7.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063708906 326 GLELELSAEDRVGLLSDITRTFRENSLTIVRAEI-STREGKAKDTFYVTDVTGNPVES-----KIVESIRQQI 392
Cdd:cd04900     1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGErerlaRIREALEDAL 73
glnD PRK00275
PII uridylyl-transferase; Provisional
 4-95 2.65e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 49.67  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906   4 DEYAKLIRRMNP---------PRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKV 74
Cdd:PRK00275  781 DDYPTIIQRRVPrqlkhfafpTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFI 860

                          90       100
                  ....*....|....*....|.
gi 1063708906  75 IDQDGNKIRDTQVLDYIQKRI 95
Cdd:PRK00275  861 TDADNQPLSDPQLCSRLQDAI 881
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
16-186 6.12e-06

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 48.58  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  16 PRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYI-SSDGGWFMDVFKVIDQDGNKI---RDTQVLDYI 91
Cdd:PRK01759  665 LLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIiTSQDGYVLDSFIVTELNGKLLefdRRRQLEQAL 744

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  92 QKRIESNAgwfIPPLRSS-------------VGVMPTD--EYTSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNT 156
Cdd:PRK01759  745 TKALNTNK---LKKLNLEenhklqhfhvkteVRFLNEEkqEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGE 821

                         170       180       190
                  ....*....|....*....|....*....|
gi 1063708906 157 RAAAVIHVTdNSTHSAITDPIRLSTIKELL 186
Cdd:PRK01759  822 KAEDFFILT-NQQGQALDEEERKALKSRLL 850
glnD PRK00275
PII uridylyl-transferase; Provisional
 329-380 6.20e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 48.51  E-value: 6.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063708906 329 LELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPV 380
Cdd:PRK00275  817 LEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPL 868
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
17-166 8.16e-06

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 48.42  E-value: 8.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  17 RVVIDnnasDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYI-SSDGGWFMDVFKVIDQDGNKIRDTQVLDYIQKRI 95
Cdd:PRK04374  683 RAVPD----NDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVlDAPHDAIFDVFEVLPQDTYADGDPQRLAAALRQV 758

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  96 ESNAGWFIPPLRSSVG-------VMPTDEY--------TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAA 160
Cdd:PRK04374  759 LAGDLQKVRPARRAVPrqlrhfrFAPRVEFsesaggrrTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAED 838


                  ....*.
gi 1063708906 161 VIHVTD 166
Cdd:PRK04374  839 QFQITD 844
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 229-380 8.17e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 48.06  E-value: 8.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 229 RARTSASRPSVTLMNIEKDYTVVTMRSKDRPKLVFDVVCTLTDMQYVVFHGMVSTEPVEAYQEFYIRHVDGLPINSEAEQ 308
Cdd:PRK03381  580 LALAADGGVHVEIAPADPHMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGSPPDAALLR 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 309 ERVIQCLE------AAIERRASEGLE------------------------LELSAEDRVGLLSDITRTFRENSLTIVRAE 358
Cdd:PRK03381  660 QDLRRALDgdldvlARLAAREAAAAAvpvrrpaapprvlwldgaspdatvLEVRAADRPGLLARLARALERAGVDVRWAR 739

                         170       180
                  ....*....|....*....|..
gi 1063708906 359 ISTREGKAKDTFYVTDVTGNPV 380
Cdd:PRK03381  740 VATLGADVVDVFYVTGAAGGPL 761
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 120-185 1.69e-05

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: 42.72  E-value: 1.69e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063708906 120 SIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSTHsaitdPIRLSTIKEL 185
Cdd:cd04926     3 RLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGN-----PVDPKTIEAV 63
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 329-389 1.76e-05

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


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 42.28  E-value: 1.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063708906 329 LELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVtDVTGNPVESKIVESIR 389
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFI-VVDGDGDLEKLLEALE 60
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
16-158 3.30e-05

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 46.12  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  16 PRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYI-SSDGGWFMDVFKVIDQDGNKIrDTQVLDYIQKR 94
Cdd:PRK05007  689 PLVLLSKQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIfTSRDGMAMDTFIVLEPDGSPL-SQDRHQVIRKA 767

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906  95 IE---SNAGWFIPPLR------------SSVGVMPT--DEYTSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTR 157
Cdd:PRK05007  768 LEqalTQSSPQPPKPRrlpaklrhfnvpTEVSFLPThtDRRSYMELIALDQPGLLARVGKIFADLGISLHGARITTIGER 847


                  .
gi 1063708906 158 A 158
Cdd:PRK05007  848 V 848
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 119-191 6.49e-05

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: 40.75  E-value: 6.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVtdnsthsAITDPIRLSTIKELLCNVVR 191
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVV-------IVVDEEDLEEVLEALKKLEG 66
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 329-374 8.26e-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: 40.91  E-value: 8.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1063708906 329 LELSAEDRVGLLSDITRTFRENSLTIVRAEISTR-EGKAKDTFYVTD 374
Cdd:cd04927     3 LKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTpDGRVLDLFFITD 49
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 121-172 8.73e-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: 40.35  E-value: 8.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063708906 121 IELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAA-VIHVTDNSTHSA 172
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEAdIFIVVDGDGDLE 53
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
328-392 1.95e-04

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 43.96  E-value: 1.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906 328 ELELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVESKIVESIRQQI 392
Cdd:PRK01759  785 EMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEKAEDFFILTNQQGQALDEEERKALKSRL 849
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 15-79 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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906  15 PPRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDG 79
Cdd:PRK03381  694 PPRVLWLDGASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAG 758
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
255-390 5.98e-04

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 42.27  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 255 SKDRPKLvFDVVCTLTDMQYVVFHG---MVSTEPVeAYQEFYIRHVDGLPInSEAEQERVIQCLEAAIE---------RR 322
Cdd:PRK05007  708 SPDRPYL-FAAVCAELDRRNLSVHDaqiFTSRDGM-AMDTFIVLEPDGSPL-SQDRHQVIRKALEQALTqsspqppkpRR 784

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 323 ASEGLE--------------------LELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVES 382
Cdd:PRK05007  785 LPAKLRhfnvptevsflpthtdrrsyMELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFILATADRRALNE 864


                  ....*...
gi 1063708906 383 KIVESIRQ 390
Cdd:PRK05007  865 ELQQELRQ 872
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 29-96 6.02e-04

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


Pssm-ID: 153171 [Multi-domain]  Cd Length: 70  Bit Score: 38.20  E-value: 6.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063708906  29 TVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKiRDTQVLDYIQKRIE 96
Cdd:cd04899     1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQP-LDPERQEALRAALG 67
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 127-189 6.75e-04

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


Pssm-ID: 153172 [Multi-domain]  Cd Length: 73  Bit Score: 38.23  E-value: 6.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063708906 127 DRPGLLSEVSAVLTDLHCNVVNAEIwtHNTR---AAAVIHVTDnSTHSAITDPIRLSTIKELLCNV 189
Cdd:cd04900    10 DRPGLFARIAGALDQLGLNILDARI--FTTRdgyALDTFVVLD-PDGEPIGERERLARIREALEDA 72
PRK03059 PRK03059
PII uridylyl-transferase; Provisional
 329-374 7.81e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235101 [Multi-domain]  Cd Length: 856  Bit Score: 41.81  E-value: 7.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1063708906 329 LELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTD 374
Cdd:PRK03059  789 LSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDG 834
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
312-392 9.08e-04

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 41.88  E-value: 9.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 312 IQCLEAAIERRAseglELELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPveskIVESIRQQ 391
Cdd:PRK04374  786 VEFSESAGGRRT----RISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRP----LSESARQA 857


                  .
gi 1063708906 392 I 392
Cdd:PRK04374  858 L 858
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
305-394 2.26e-03

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 40.52  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708906 305 EAEQERVIQcLEAAIERRASEGLELELSAEDRVGLLSDITRTFRENSLTIVRAEISTRegkaKDTFYVTDVT---GNPVE 381
Cdd:COG0317   626 EREPERLID-VEWGEDSSGVFPVDIRIEALDRPGLLADITSVIAEEKINILSVNTRSR----DDGTATIRFTvevRDLDH 700

                          90
                  ....*....|....
gi 1063708906 382 -SKIVESIRQQIGV 394
Cdd:COG0317   701 lARVLRKLRKVPGV 714
ACT_GcvR_1 cd04893
ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, ...
 125-187 2.55e-03

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


Pssm-ID: 153165 [Multi-domain]  Cd Length: 77  Bit Score: 36.53  E-value: 2.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063708906 125 GTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSthSAITdpiRLSTIKELLC 187
Cdd:cd04893     8 GTDRPGILNELTRAVSESGCNILDSRMAILGTEFALTMLVEGSW--DAIA---KLEAALPGLA 65
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 29-81 2.64e-03

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: 36.13  E-value: 2.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063708906  29 TVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDG--GWFMDVFKVIDQDGNK 81
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEdkGGIVFVVIVVDEEDLE 55
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
119-165 2.74e-03

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 40.14  E-value: 2.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRaAAVIHVT 165
Cdd:COG0317   647 VDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDG-TATIRFT 692
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 37-96 3.66e-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: 35.92  E-value: 3.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063708906  37 NKHGTLLEVVQVLTDMNLVIKKAYI-SSDGGWFMDVFKVIDQDGNKIRDTQVLDYIQKRIE 96
Cdd:cd04900    10 DRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGERERLARIREALE 70
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 37-95 3.82e-03

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: 35.79  E-value: 3.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063708906  37 NKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKIrDTQVLDYIQKRI 95
Cdd:cd04926    10 DRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPV-DPKTIEAVRQEI 67
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
125-201 4.59e-03

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


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 37.89  E-value: 4.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063708906 125 GTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSTHSA--ITDPIRLSTIKELLCNVVRTNSGSRAAKT 201
Cdd:COG2716    10 GPDRPGIVAALARAVSEHGCNILDSRMARLGGEFAGILLVSGPWDAIAklEAALPALAAELGLLVTVKRTEPHEAPPAG 88
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
 121-165 5.43e-03

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


Pssm-ID: 153148 [Multi-domain]  Cd Length: 71  Bit Score: 35.50  E-value: 5.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1063708906 121 IELAGTDRPGLLSEVSAVLTDLHCNVVNaeIWTHNTRA-AAVIHVT 165
Cdd:cd04876     1 IRVEAIDRPGLLADITTVIAEEKINILS--VNTRTDDDgLATIRLT 44
ACT_4 pfam13291
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 119-165 6.01e-03

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: 35.61  E-value: 6.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1063708906 119 TSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVT 165
Cdd:pfam13291   6 VDLEVEAIDRPGLLADITQVISEEKANIVSVNAKTRKKDGTAEIKIT 52
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 318-391 7.28e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 38.82  E-value: 7.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063708906 318 AIERRASEGLELELS--AEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVESKIVesiRQQ 391
Cdd:PRK03381  589 HVEIAPADPHMVEVTvvAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGSPPDAALL---RQD 661
 
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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