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Conserved domains on  [gi|2241025607|ref|XP_002515490|]
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ACT domain-containing protein ACR2 isoform X1 [Ricinus communis]

Protein Classification

sigma-54-dependent Fis family transcriptional regulator( domain architecture ID 10141587)

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 ...
 134-207 8.76e-39

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: 135.25  E-value: 8.76e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2241025607 134 TAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISDQSTDTPIDDPHRLATIEDHLTTVIRA 207
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 290-365 9.66e-37

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


:

Pssm-ID: 153169 [Multi-domain]  Cd Length: 75  Bit Score: 129.85  E-value: 9.66e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2241025607 290 YSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAgDDGYAFQEYFIRYIDGYALNTESEKERVIKCLEAAIERR 365
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDT-DGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 38-109 6.19e-36

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


:

Pssm-ID: 153167 [Multi-domain]  Cd Length: 72  Bit Score: 127.57  E-value: 6.19e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607  38 CSVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLTDQHVIDYIHQAIGTTR 109
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 369-440 2.06e-33

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


The actual alignment was detected with superfamily member cd04926:

Pssm-ID: 471857  Cd Length: 72  Bit Score: 120.92  E-value: 2.06e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607 369 GVKVELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISGNEVDMGFVKSMKKEMGAINL 440
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 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 ...
 134-207 8.76e-39

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: 135.25  E-value: 8.76e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2241025607 134 TAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISDQSTDTPIDDPHRLATIEDHLTTVIRA 207
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 290-365 9.66e-37

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


Pssm-ID: 153169 [Multi-domain]  Cd Length: 75  Bit Score: 129.85  E-value: 9.66e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2241025607 290 YSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAgDDGYAFQEYFIRYIDGYALNTESEKERVIKCLEAAIERR 365
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDT-DGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 38-109 6.19e-36

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


Pssm-ID: 153167 [Multi-domain]  Cd Length: 72  Bit Score: 127.57  E-value: 6.19e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607  38 CSVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLTDQHVIDYIHQAIGTTR 109
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 369-440 2.06e-33

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: 120.92  E-value: 2.06e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607 369 GVKVELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISGNEVDMGFVKSMKKEMGAINL 440
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 50-207 6.04e-15

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 77.49  E-value: 6.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  50 GLLLEVVQVLTDLNLTI--SKSYISSDaGWFMDVFHVKDERGKKLTDQHVIDYIHQAIGT--TRETQSPATPKSYVN--- 122
Cdd:COG2844   691 GLFARIAGALAALGLNIldARIHTTRD-GYALDTFIVLDPDGEPIDDPDRLERIEQALEEalSGEVPLPEPLARRLSrrl 769

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 123 ---DV-----FEGEHSSEHTAIEMSGTDRPGLFSEISAALVDLHCNIveahawsHNARLAC-------VAYISDQsTDTP 187
Cdd:COG2844   770 rhfPVpprvtFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNI-------HSAKIATlgervedVFYVTDL-DGQK 841

                         170       180
                  ....*....|....*....|
gi 2241025607 188 IDDPHRLATIEDHLTTVIRA 207
Cdd:COG2844   842 LTDPERQEALREALLEALDE 861
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 273-421 2.07e-14

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 75.95  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 273 DEGRKTVVSIDNCEEKGYSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAGDDGYAFQEYFIRYIDGYALNTESEKE 352
Cdd:COG2844   662 DDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGYALDTFIVLDPDGEPIDDPDRLE 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 353 RVIKCLEAA----------IERRVCEGVK--------------------VELCAENRVGLLSDITRVLRENGLTVVRADV 402
Cdd:COG2844   742 RIEQALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHSAKI 821

                         170
                  ....*....|....*....
gi 2241025607 403 ATQGEKAVNAFYVRDISGN 421
Cdd:COG2844   822 ATLGERVEDVFYVTDLDGQ 840
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 277-420 2.88e-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: 65.90  E-value: 2.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 277 KTVVSIDNCEEKGYSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAGDDGYAFQEYFIRYIDGYALNTESEKERVIK 356
Cdd:TIGR01693 655 GPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTFVVQDLFGSPPAAERVFQELLQ 734

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 357 CLEAAIE------------RRVCEGVK--------------------VELCAENRVGLLSDITRVLRENGLTVVRADVAT 404
Cdd:TIGR01693 735 GLVDVLAglakdpdtisarRARRRRLQhfavpprvtilntasrkatiMEVRALDRPGLLARVGRTLEELGLSIQSAKITT 814

                         170
                  ....*....|....*.
gi 2241025607 405 QGEKAVNAFYVRDISG 420
Cdd:TIGR01693 815 FGEKAEDVFYVTDLFG 830
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 68-206 4.36e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 65.28  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  68 KSYISSDaGWFMDVFHVKDERGKKLTDQHVIDYIHQAI-----GTTR-----ETQSPATPKSYVNDV-----FEGEHSSE 132
Cdd:PRK05092  764 RIFTTTD-GRALDTFWIQDAFGRDEDEPRRLARLAKAIedalsGEVRlpealAKRTKPKKRARAFHVpprvtIDNEASNR 842

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2241025607 133 HTAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISDqSTDTPIDDPHRLATIEDHLTTVIR 206
Cdd:PRK05092  843 FTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTD-LFGLKITNEARQAAIRRALLAALA 915
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 372-420 1.80e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 57.19  E-value: 1.80e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2241025607 372 VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISG 420
Cdd:PRK05092  846 IEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFG 894
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
280-415 4.99e-08

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 55.51  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 280 VSIDNCEEKGYSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAGDDGYAFQEYFIRYIDGYALNTESEKErvikcLE 359
Cdd:PRK01759  667 VKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDSFIVTELNGKLLEFDRRRQ-----LE 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 360 AAIER-------RVCEGVK-------------------------VELCAENRVGLLSDITRVLRENGLTVVRADVATQGE 407
Cdd:PRK01759  742 QALTKalntnklKKLNLEEnhklqhfhvktevrflneekqeqteMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGE 821


                  ....*...
gi 2241025607 408 KAVNAFYV 415
Cdd:PRK01759  822 KAEDFFIL 829
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 24-105 2.20e-07

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 53.61  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  24 PTcRVCIDNESMEDCSVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLTDQHVIDYIHQ 103
Cdd:COG2844   775 PP-RVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALRE 853


                  ..
gi 2241025607 104 AI 105
Cdd:COG2844   854 AL 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 27-95 8.22e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 51.79  E-value: 8.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2241025607  27 RVCIDNESMEDCSVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLTDQ 95
Cdd:PRK05092  832 RVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNE 900
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 372-424 6.75e-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: 6.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2241025607 372 VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISGNEVD 424
Cdd:pfam01842   3 LEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLE 55
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 134-169 4.92e-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: 35.75  E-value: 4.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2241025607 134 TAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSH 169
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTS 36
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 39-89 7.15e-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: 34.98  E-value: 7.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2241025607  39 SVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISS--DAGWFMDVFHVKDERG 89
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTseDKGGIVFVVIVVDEED 53
 
Name Accession Description Interval E-value
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 134-207 8.76e-39

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: 135.25  E-value: 8.76e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2241025607 134 TAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISDQSTDTPIDDPHRLATIEDHLTTVIRA 207
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 290-365 9.66e-37

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


Pssm-ID: 153169 [Multi-domain]  Cd Length: 75  Bit Score: 129.85  E-value: 9.66e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2241025607 290 YSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAgDDGYAFQEYFIRYIDGYALNTESEKERVIKCLEAAIERR 365
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDT-DGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 38-109 6.19e-36

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


Pssm-ID: 153167 [Multi-domain]  Cd Length: 72  Bit Score: 127.57  E-value: 6.19e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607  38 CSVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLTDQHVIDYIHQAIGTTR 109
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 369-440 2.06e-33

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: 120.92  E-value: 2.06e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607 369 GVKVELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISGNEVDMGFVKSMKKEMGAINL 440
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 370-437 1.20e-20

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: 85.58  E-value: 1.20e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2241025607 370 VKVELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISGNEVDMGFVKSMKKEMGA 437
Cdd:cd04899     1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGE 68
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 134-205 1.66e-18

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: 79.42  E-value: 1.66e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607 134 TAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISDQSTDTpiDDPHRLATIEDHLTTVI 205
Cdd:cd04899     1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQP--LDPERQEALRAALGEAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 134-205 2.28e-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: 73.35  E-value: 2.28e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607 134 TAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISDQstDTPIDDPHRLATIEDHLTTVI 205
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDS--DGRPLDPERIARLEEALEDAL 70
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 50-207 6.04e-15

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 77.49  E-value: 6.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  50 GLLLEVVQVLTDLNLTI--SKSYISSDaGWFMDVFHVKDERGKKLTDQHVIDYIHQAIGT--TRETQSPATPKSYVN--- 122
Cdd:COG2844   691 GLFARIAGALAALGLNIldARIHTTRD-GYALDTFIVLDPDGEPIDDPDRLERIEQALEEalSGEVPLPEPLARRLSrrl 769

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 123 ---DV-----FEGEHSSEHTAIEMSGTDRPGLFSEISAALVDLHCNIveahawsHNARLAC-------VAYISDQsTDTP 187
Cdd:COG2844   770 rhfPVpprvtFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNI-------HSAKIATlgervedVFYVTDL-DGQK 841

                         170       180
                  ....*....|....*....|
gi 2241025607 188 IDDPHRLATIEDHLTTVIRA 207
Cdd:COG2844   842 LTDPERQEALREALLEALDE 861
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 372-434 1.14e-14

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


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 68.73  E-value: 1.14e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2241025607 372 VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISGNEVDMGFVKSMKKE 434
Cdd:cd04873     3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEA 65
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 273-421 2.07e-14

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 75.95  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 273 DEGRKTVVSIDNCEEKGYSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAGDDGYAFQEYFIRYIDGYALNTESEKE 352
Cdd:COG2844   662 DDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGYALDTFIVLDPDGEPIDDPDRLE 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 353 RVIKCLEAA----------IERRVCEGVK--------------------VELCAENRVGLLSDITRVLRENGLTVVRADV 402
Cdd:COG2844   742 RIEQALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHSAKI 821

                         170
                  ....*....|....*....
gi 2241025607 403 ATQGEKAVNAFYVRDISGN 421
Cdd:COG2844   822 ATLGERVEDVFYVTDLDGQ 840
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 39-107 1.54e-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: 62.57  E-value: 1.54e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2241025607  39 SVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLTDQHvIDYIHQAIGT 107
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPER-IARLEEALED 68
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 291-362 5.66e-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: 5.66e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025607 291 SIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIgAGDDGYAFQEYFIRYIDGYALNtESEKERVIKCLEAAI 362
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARI-STTGERALDVFYVTDSDGRPLD-PERIARLEEALEDAL 70
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 277-420 2.88e-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: 65.90  E-value: 2.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 277 KTVVSIDNCEEKGYSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAGDDGYAFQEYFIRYIDGYALNTESEKERVIK 356
Cdd:TIGR01693 655 GPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTFVVQDLFGSPPAAERVFQELLQ 734

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 357 CLEAAIE------------RRVCEGVK--------------------VELCAENRVGLLSDITRVLRENGLTVVRADVAT 404
Cdd:TIGR01693 735 GLVDVLAglakdpdtisarRARRRRLQhfavpprvtilntasrkatiMEVRALDRPGLLARVGRTLEELGLSIQSAKITT 814

                         170
                  ....*....|....*.
gi 2241025607 405 QGEKAVNAFYVRDISG 420
Cdd:TIGR01693 815 FGEKAEDVFYVTDLFG 830
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 68-206 4.36e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 65.28  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  68 KSYISSDaGWFMDVFHVKDERGKKLTDQHVIDYIHQAI-----GTTR-----ETQSPATPKSYVNDV-----FEGEHSSE 132
Cdd:PRK05092  764 RIFTTTD-GRALDTFWIQDAFGRDEDEPRRLARLAKAIedalsGEVRlpealAKRTKPKKRARAFHVpprvtIDNEASNR 842

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2241025607 133 HTAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISDqSTDTPIDDPHRLATIEDHLTTVIR 206
Cdd:PRK05092  843 FTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTD-LFGLKITNEARQAAIRRALLAALA 915
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 142-205 8.80e-09

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: 52.09  E-value: 8.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2241025607 142 DRPGLFSEISAALVDLHCNIVEA--HAWSHNARLAcVAYISDQStDTPIDDPHRLATIEDHLTTVI 205
Cdd:cd04900    10 DRPGLFARIAGALDQLGLNILDAriFTTRDGYALD-TFVVLDPD-GEPIGERERLARIREALEDAL 73
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 372-420 1.80e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 57.19  E-value: 1.80e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2241025607 372 VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISG 420
Cdd:PRK05092  846 IEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFG 894
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
280-415 4.99e-08

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 55.51  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 280 VSIDNCEEKGYSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAGDDGYAFQEYFIRYIDGYALNTESEKErvikcLE 359
Cdd:PRK01759  667 VKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDSFIVTELNGKLLEFDRRRQ-----LE 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 360 AAIER-------RVCEGVK-------------------------VELCAENRVGLLSDITRVLRENGLTVVRADVATQGE 407
Cdd:PRK01759  742 QALTKalntnklKKLNLEEnhklqhfhvktevrflneekqeqteMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGE 821


                  ....*...
gi 2241025607 408 KAVNAFYV 415
Cdd:PRK01759  822 KAEDFFIL 829
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 24-105 2.20e-07

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 53.61  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  24 PTcRVCIDNESMEDCSVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLTDQHVIDYIHQ 103
Cdd:COG2844   775 PP-RVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALRE 853


                  ..
gi 2241025607 104 AI 105
Cdd:COG2844   854 AL 855
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 372-420 3.01e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 53.07  E-value: 3.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2241025607 372 VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISG 420
Cdd:PRK03381  710 LEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAG 758
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 27-95 8.22e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 51.79  E-value: 8.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2241025607  27 RVCIDNESMEDCSVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLTDQ 95
Cdd:PRK05092  832 RVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNE 900
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 39-108 1.21e-06

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: 45.91  E-value: 1.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  39 SVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKLtDQHVIDYIHQAIGTT 108
Cdd:cd04899     1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPL-DPERQEALRAALGEA 69
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 47-107 3.05e-06

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: 44.65  E-value: 3.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2241025607  47 NKQGLLLEVVQVLTDLNLTISKSYISSDAGWFMDVFHVKDERGKKlTDQHVIDYIHQAIGT 107
Cdd:cd04926    10 DRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNP-VDPKTIEAVRQEIGP 69
glnD PRK00275
PII uridylyl-transferase; Provisional
 286-421 5.15e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 49.28  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 286 EEKGYSIVSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAGDDGYAFQEYFIRYIDGYALNTESEK-ERVIKCLEAA--- 361
Cdd:PRK00275  700 EFEGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEPIGDNPARiEQIREGLTEAlrn 779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 362 -------IERRVCEGVK--------------------VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFY 414
Cdd:PRK00275  780 pddyptiIQRRVPRQLKhfafptqvtisndaqrpvtvLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFF 859


                  ....*..
gi 2241025607 415 VRDISGN 421
Cdd:PRK00275  860 ITDADNQ 866
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 372-424 6.75e-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: 6.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2241025607 372 VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRDISGNEVD 424
Cdd:pfam01842   3 LEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLE 55
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 368-415 7.08e-05

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 45.37  E-value: 7.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2241025607 368 EGVKVELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYV 415
Cdd:PRK03381  598 HMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVV 645
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
359-417 3.98e-04

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 43.03  E-value: 3.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2241025607 359 EAAIERRVcegvKVELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRD 417
Cdd:PRK04374  790 ESAGGRRT----RISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITD 844
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
134-174 9.62e-04

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


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 40.20  E-value: 9.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2241025607 134 TAIemsGTDRPGLFSEISAALVDLHCNIVEahawSHNARLA 174
Cdd:COG2716     7 TAI---GPDRPGIVAALARAVSEHGCNILD----SRMARLG 40
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 136-201 1.06e-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: 37.27  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2241025607 136 IEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISdqstdtpIDDPHRLATIEDHL 201
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIV-------VDGDGDLEKLLEAL 59
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 293-362 2.07e-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: 36.69  E-value: 2.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 293 VSIECKDRPRLMFDTVCTLTDMQYVIFHASIGAGDDGYAFQEYFIRYIDGYALNTESEKERVIKCLEAAI 362
Cdd:cd04900     4 VFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGERERLARIREALEDAL 73
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 372-416 2.45e-03

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


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 36.12  E-value: 2.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2241025607 372 VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVR 416
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIV 45
glnD PRK00275
PII uridylyl-transferase; Provisional
 55-201 4.18e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 39.66  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  55 VVQVLTDLNLTISKSYI-SSDAGWFMDVFHVKDERGKKL-TDQHVIDYIHQAIgtTRETQSPA---------TPK----- 118
Cdd:PRK00275  721 TVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIgDNPARIEQIREGL--TEALRNPDdyptiiqrrVPRqlkhf 798

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607 119 ------SYVNDVfegehSSEHTAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSHNARLACVAYISDqSTDTPIDDPH 192
Cdd:PRK00275  799 afptqvTISNDA-----QRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITD-ADNQPLSDPQ 872


                  ....*....
gi 2241025607 193 RLATIEDHL 201
Cdd:PRK00275  873 LCSRLQDAI 881
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 134-169 4.92e-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: 35.75  E-value: 4.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2241025607 134 TAIEMSGTDRPGLFSEISAALVDLHCNIVEAHAWSH 169
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTS 36
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 47-105 5.02e-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: 35.53  E-value: 5.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025607  47 NKQGLLLEVVQVLTDLNLTISKSYI-SSDAGWFMDVFHVKDERGKKLTDQHVIDYIHQAI 105
Cdd:cd04900    10 DRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGERERLARIREAL 69
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 39-89 7.15e-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: 34.98  E-value: 7.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2241025607  39 SVVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISS--DAGWFMDVFHVKDERG 89
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTseDKGGIVFVVIVVDEED 53
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 372-417 7.26e-03

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: 35.48  E-value: 7.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2241025607 372 VELCAENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYVRD 417
Cdd:cd04925     3 IELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRD 48
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 40-106 8.85e-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: 8.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2241025607  40 VVKVDSVNKQGLLLEVVQVLTDLNLTISKSYISSDA-GWFMDVFHVKDER---GKKLTDQHVIDYIHQAIG 106
Cdd:cd04927     2 LLKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTPdGRVLDLFFITDARellHTKKRREETYDYLRAVLG 72
PRK03059 PRK03059
PII uridylyl-transferase; Provisional
 376-422 9.49e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235101 [Multi-domain]  Cd Length: 856  Bit Score: 38.73  E-value: 9.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2241025607 376 AENRVGLLSDITRVLRENGLTVVRADVATQGEKAVNAFYvrdISGNE 422
Cdd:PRK03059  793 ANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFL---IDGSG 836
 
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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