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Conserved domains on  [gi|557536454|gb|ESR47572|]
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hypothetical protein CICLE_v10001100mg [Citrus x clementina]

Protein Classification

sigma-54-dependent Fis family transcriptional regulator( domain architecture ID 10141592)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 268-342 5.00e-43

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: 146.03  E-value: 5.00e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557536454 268 YSVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAISSDGPHASQEYYIRHMDGCILDTEGEKERVIKCLEAAIRRR 342
Cdd:cd04897    1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 35-106 1.48e-39

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: 136.81  E-value: 1.48e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454  35 CTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKALGPKG 106
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 ...
 346-417 2.34e-39

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: 136.33  E-value: 2.34e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454 346 GLSLELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKTIEALRKEIGHTML 417
Cdd:cd04926    1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 129-202 9.83e-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 cd04925:

Pssm-ID: 471857  Cd Length: 74  Bit Score: 115.99  E-value: 9.83e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557536454 129 TAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNDDTTCRAVGDQTRLSLMEEQLKNILRG 202
Cdd:cd04925    1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
 
Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 268-342 5.00e-43

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: 146.03  E-value: 5.00e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557536454 268 YSVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAISSDGPHASQEYYIRHMDGCILDTEGEKERVIKCLEAAIRRR 342
Cdd:cd04897    1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 35-106 1.48e-39

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: 136.81  E-value: 1.48e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454  35 CTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKALGPKG 106
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 ...
 346-417 2.34e-39

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: 136.33  E-value: 2.34e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454 346 GLSLELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKTIEALRKEIGHTML 417
Cdd:cd04926    1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 9.83e-32

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: 115.99  E-value: 9.83e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557536454 129 TAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNDDTTCRAVGDQTRLSLMEEQLKNILRG 202
Cdd:cd04925    1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 249-412 6.28e-19

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 89.82  E-value: 6.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 249 DHTPSFKPEITVERLEDKGYSVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAI--SSDGpHASQEYYIRHMDGCILDTEG 326
Cdd:COG2844  660 RADDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhtTRDG-YALDTFIVLDPDGEPIDDPD 738

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 327 EKERVIKCLEAA----------IRRRVSEGLS--------------------LELCAKDRVGLLSEVTRILRENGLSVTR 376
Cdd:COG2844  739 RLERIEQALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHS 818

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 557536454 377 AGVSTVGEQAVNVFYVRDASGNPV-DMKTIEALRKEI 412
Cdd:COG2844  819 AKIATLGERVEDVFYVTDLDGQKLtDPERQEALREAL 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 22-102 2.79e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 65.66  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  22 PPRASVDNSSCPECTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKA 101
Cdd:PRK05092 830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                 .
gi 557536454 102 L 102
Cdd:PRK05092 910 L 910
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 241-400 3.55e-11

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


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 65.51  E-value: 3.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  241 GVTTADQVDHTPSF-------KPEITVERLEDKGYSVVNVKCRDRAKLMFDIVCTLtDMQYVVFHAA--ISSDGPHASQE 311
Cdd:TIGR01693 634 RFTHKEIAWHAESLrralssgGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGAL-AMLSLSVHDAqvNTTKDGVALDT 712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  312 YYIRHMDGCILDTEGEKERVIKCLEAA------------IRRRVSEGLS--------------------LELCAKDRVGL 359
Cdd:TIGR01693 713 FVVQDLFGSPPAAERVFQELLQGLVDVlaglakdpdtisARRARRRRLQhfavpprvtilntasrkatiMEVRALDRPGL 792

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 557536454  360 LSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPV 400
Cdd:TIGR01693 793 LARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKL 833
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 349-429 3.18e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 62.58  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKT-IEALRKEIGHTMLFNVKKVPASR 427
Cdd:PRK05092 846 IEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEArQAAIRRALLAALAEGEAEARAAR 925


                 ..
gi 557536454 428 SA 429
Cdd:PRK05092 926 PP 927
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 22-102 4.20e-10

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 62.08  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  22 PPRASVDNSSCPECTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKA 101
Cdd:COG2844  775 PPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREA 854


                 .
gi 557536454 102 L 102
Cdd:COG2844  855 L 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 67-213 5.41e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 61.81  E-value: 5.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  67 YISSDGgWFMDVFHVIDQQGKKITDGKTI----DYIEKALgpKGHITA----GAKTWPSKQVGVHSV-----------GD 127
Cdd:PRK05092 766 FTTTDG-RALDTFWIQDAFGRDEDEPRRLarlaKAIEDAL--SGEVRLpealAKRTKPKKRARAFHVpprvtidneasNR 842

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 128 HTAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNdDTTCRAVGDQTRLSLMEEQLKNILRGCDDED 207
Cdd:PRK05092 843 FTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVT-DLFGLKITNEARQAAIRRALLAALAEGEAEA 921


                 ....*.
gi 557536454 208 SEKVAR 213
Cdd:PRK05092 922 RAARPP 927
glnD PRK00275
PII uridylyl-transferase; Provisional
 244-412 2.49e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 56.60  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 244 TADQVDHTPSFKPEI----TVERlEDKGYSVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAI-SSDGPHASQEYYIRHMD 318
Cdd:PRK00275 677 TEAILQHPDDGGPLVlikeTTQR-EFEGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDD 755

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 319 G-CILDTEGEKERVIKCLEAA----------IRRRVSEGLS--------------------LELCAKDRVGLLSEVTRIL 367
Cdd:PRK00275 756 GePIGDNPARIEQIREGLTEAlrnpddyptiIQRRVPRQLKhfafptqvtisndaqrpvtvLEIIAPDRPGLLARIGRIF 835

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 557536454 368 RENGLSVTRAGVSTVGEQAVNVFYVRDASGNPV-DMKTIEALRKEI 412
Cdd:PRK00275 836 LEFDLSLQNAKIATLGERVEDVFFITDADNQPLsDPQLCSRLQDAI 881
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 348-413 1.07e-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: 48.84  E-value: 1.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557536454  348 SLELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDmKTIEALRKEIG 413
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLE-EVLEALKKLEG 66
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 129-201 7.83e-07

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 46.15  E-value: 7.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557536454  129 TAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIacvlyvnDDTTCRAVGDQTRLSLMEEQLKNILR 201
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG-------GIVFVVIVVDEEDLEEVLEALKKLEG 66
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 36-86 1.36e-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: 42.68  E-value: 1.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 557536454   36 TVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDG--GWFMDVFHVIDQQG 86
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEdkGGIVFVVIVVDEED 53
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 269-336 1.63e-04

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 39.60  E-value: 1.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557536454  269 SVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAISSDGPHAsqEYYIRHMDGCILDTEGEKERVIKCLE 336
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG--GIVFVVIVVDEEDLEEVLEALKKLEG 66
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
114-169 3.37e-04

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 43.22  E-value: 3.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557536454 114 TWPSKQVGVHSVgdhtAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIA 169
Cdd:COG0317  636 EWGEDSSGVFPV----DIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTA 687
 
Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 268-342 5.00e-43

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: 146.03  E-value: 5.00e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557536454 268 YSVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAISSDGPHASQEYYIRHMDGCILDTEGEKERVIKCLEAAIRRR 342
Cdd:cd04897    1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 35-106 1.48e-39

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: 136.81  E-value: 1.48e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454  35 CTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKALGPKG 106
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 ...
 346-417 2.34e-39

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: 136.33  E-value: 2.34e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454 346 GLSLELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKTIEALRKEIGHTML 417
Cdd:cd04926    1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 129-202 9.83e-32

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: 115.99  E-value: 9.83e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557536454 129 TAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNDDTTCRAVGDQTRLSLMEEQLKNILRG 202
Cdd:cd04925    1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 349-416 1.81e-26

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


Pssm-ID: 153171 [Multi-domain]  Cd Length: 70  Bit Score: 101.38  E-value: 1.81e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKTIEALRKEIGHTM 416
Cdd:cd04899    3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 349-416 1.26e-19

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


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 82.60  E-value: 1.26e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKTIEALRKEIGHTM 416
Cdd:cd04873    3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 249-412 6.28e-19

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 89.82  E-value: 6.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 249 DHTPSFKPEITVERLEDKGYSVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAI--SSDGpHASQEYYIRHMDGCILDTEG 326
Cdd:COG2844  660 RADDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIhtTRDG-YALDTFIVLDPDGEPIDDPD 738

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 327 EKERVIKCLEAA----------IRRRVSEGLS--------------------LELCAKDRVGLLSEVTRILRENGLSVTR 376
Cdd:COG2844  739 RLERIEQALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHS 818

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 557536454 377 AGVSTVGEQAVNVFYVRDASGNPV-DMKTIEALRKEI 412
Cdd:COG2844  819 AKIATLGERVEDVFYVTDLDGQKLtDPERQEALREAL 855
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 129-200 2.30e-16

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: 73.26  E-value: 2.30e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454 129 TAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNDDTTCRAvgDQTRLSLMEEQLKNIL 200
Cdd:cd04899    1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPL--DPERQEALRAALGEAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 36-102 3.66e-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: 72.58  E-value: 3.66e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557536454  36 TVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKItDGKTIDYIEKAL 102
Cdd:cd04873    1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPL-DPERIARLEEAL 66
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 44-200 1.20e-14

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 76.33  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  44 NKPGILLEVVQVLSDLDLIITKAYI-SSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKAL-----GPKGHITAGAKTwPS 117
Cdd:COG2844  688 DRPGLFARIAGALAALGLNILDARIhTTRDGYALDTFIVLDPDGEPIDDPDRLERIEQALeealsGEVPLPEPLARR-LS 766

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 118 KQVGVHSV-----------GDHTAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNDDTTcRAVGDQ 186
Cdd:COG2844  767 RRLRHFPVpprvtfdndasNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDG-QKLTDP 845

                        170
                 ....*....|....
gi 557536454 187 TRLSLMEEQLKNIL 200
Cdd:COG2844  846 ERQEALREALLEAL 859
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 269-339 2.01e-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: 64.88  E-value: 2.01e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557536454 269 SVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAISSDGPHASQEYYIRHMDGCILDTEgEKERVIKCLEAAI 339
Cdd:cd04873    1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPE-RIARLEEALEDAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 129-200 1.42e-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: 1.42e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454 129 TAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNDDTTCRAvgDQTRLSLMEEQLKNIL 200
Cdd:cd04873    1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPL--DPERIARLEEALEDAL 70
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 22-102 2.79e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 65.66  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  22 PPRASVDNSSCPECTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKA 101
Cdd:PRK05092 830 PPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                 .
gi 557536454 102 L 102
Cdd:PRK05092 910 L 910
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 241-400 3.55e-11

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


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 65.51  E-value: 3.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  241 GVTTADQVDHTPSF-------KPEITVERLEDKGYSVVNVKCRDRAKLMFDIVCTLtDMQYVVFHAA--ISSDGPHASQE 311
Cdd:TIGR01693 634 RFTHKEIAWHAESLrralssgGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGAL-AMLSLSVHDAqvNTTKDGVALDT 712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  312 YYIRHMDGCILDTEGEKERVIKCLEAA------------IRRRVSEGLS--------------------LELCAKDRVGL 359
Cdd:TIGR01693 713 FVVQDLFGSPPAAERVFQELLQGLVDVlaglakdpdtisARRARRRRLQhfavpprvtilntasrkatiMEVRALDRPGL 792

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 557536454  360 LSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPV 400
Cdd:TIGR01693 793 LARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKL 833
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 349-429 3.18e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 62.58  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKT-IEALRKEIGHTMLFNVKKVPASR 427
Cdd:PRK05092 846 IEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEArQAAIRRALLAALAEGEAEARAAR 925


                 ..
gi 557536454 428 SA 429
Cdd:PRK05092 926 PP 927
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 22-102 4.20e-10

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 62.08  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  22 PPRASVDNSSCPECTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKA 101
Cdd:COG2844  775 PPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREA 854


                 .
gi 557536454 102 L 102
Cdd:COG2844  855 L 855
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 67-213 5.41e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 61.81  E-value: 5.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  67 YISSDGgWFMDVFHVIDQQGKKITDGKTI----DYIEKALgpKGHITA----GAKTWPSKQVGVHSV-----------GD 127
Cdd:PRK05092 766 FTTTDG-RALDTFWIQDAFGRDEDEPRRLarlaKAIEDAL--SGEVRLpealAKRTKPKKRARAFHVpprvtidneasNR 842

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 128 HTAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNdDTTCRAVGDQTRLSLMEEQLKNILRGCDDED 207
Cdd:PRK05092 843 FTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVT-DLFGLKITNEARQAAIRRALLAALAEGEAEA 921


                 ....*.
gi 557536454 208 SEKVAR 213
Cdd:PRK05092 922 RAARPP 927
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 46-176 5.99e-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: 61.66  E-value: 5.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454   46 PGILLEVVQVLSDLDLIITKAYI-SSDGGWFMDVFHVIDQQGKKITDGKT----IDYIEKALGPKGHITAGAKTWPSKQV 120
Cdd:TIGR01693 679 PGLFAKVAGALAMLSLSVHDAQVnTTKDGVALDTFVVQDLFGSPPAAERVfqelLQGLVDVLAGLAKDPDTISARRARRR 758

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557536454  121 GV-------------HSVGDHTAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVND 176
Cdd:TIGR01693 759 RLqhfavpprvtilnTASRKATIMEVRALDRPGLLARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTD 827
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 337-400 1.15e-09

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 60.78  E-value: 1.15e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557536454 337 AAIRRRVSEGLS-----LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPV 400
Cdd:PRK03381 693 APPRVLWLDGASpdatvLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPL 761
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 36-103 1.01e-08

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


Pssm-ID: 153171 [Multi-domain]  Cd Length: 70  Bit Score: 51.69  E-value: 1.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557536454  36 TVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKiTDGKTIDYIEKALG 103
Cdd:cd04899    1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQP-LDPERQEALRAALG 67
glnD PRK00275
PII uridylyl-transferase; Provisional
 244-412 2.49e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 56.60  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 244 TADQVDHTPSFKPEI----TVERlEDKGYSVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAI-SSDGPHASQEYYIRHMD 318
Cdd:PRK00275 677 TEAILQHPDDGGPLVlikeTTQR-EFEGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDD 755

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 319 G-CILDTEGEKERVIKCLEAA----------IRRRVSEGLS--------------------LELCAKDRVGLLSEVTRIL 367
Cdd:PRK00275 756 GePIGDNPARIEQIREGLTEAlrnpddyptiIQRRVPRQLKhfafptqvtisndaqrpvtvLEIIAPDRPGLLARIGRIF 835

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 557536454 368 RENGLSVTRAGVSTVGEQAVNVFYVRDASGNPV-DMKTIEALRKEI 412
Cdd:PRK00275 836 LEFDLSLQNAKIATLGERVEDVFFITDADNQPLsDPQLCSRLQDAI 881
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 348-413 1.07e-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: 48.84  E-value: 1.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557536454  348 SLELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDmKTIEALRKEIG 413
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLE-EVLEALKKLEG 66
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 44-104 1.84e-07

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: 48.12  E-value: 1.84e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557536454  44 NKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKItDGKTIDYIEKALGP 104
Cdd:cd04926   10 DRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPV-DPKTIEAVRQEIGP 69
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 129-201 7.83e-07

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 46.15  E-value: 7.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557536454  129 TAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIacvlyvnDDTTCRAVGDQTRLSLMEEQLKNILR 201
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG-------GIVFVVIVVDEEDLEEVLEALKKLEG 66
glnD PRK00275
PII uridylyl-transferase; Provisional
 52-176 3.47e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 49.67  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  52 VVQVLSDLDLIITKAYI-SSDGGWFMDVFHVIDQQGKKI-TDGKTIDYIEKALG-----PKGHITAGAKTWPSK------ 118
Cdd:PRK00275 721 TVAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIgDNPARIEQIREGLTealrnPDDYPTIIQRRVPRQlkhfaf 800

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454 119 --QVGVHS--VGDHTAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVND 176
Cdd:PRK00275 801 ptQVTISNdaQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITD 862
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 36-86 1.36e-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: 42.68  E-value: 1.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 557536454   36 TVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDG--GWFMDVFHVIDQQG 86
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEdkGGIVFVVIVVDEED 53
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 44-102 1.37e-05

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


Pssm-ID: 153172 [Multi-domain]  Cd Length: 73  Bit Score: 42.85  E-value: 1.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  44 NKPGILLEVVQVLSDLDLIITKAYI-SSDGGWFMDVFHVIDQQGKKITDGKTIDYIEKAL 102
Cdd:cd04900   10 DRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGERERLARIREAL 69
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 348-408 1.44e-05

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: 42.80  E-value: 1.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557536454 348 SLELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRD-ASGNPVD----MKTIEAL 408
Cdd:cd04925    2 AIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDeETGAPIDdpirLASIEDR 67
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 349-409 2.76e-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: 41.51  E-value: 2.76e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVrDASGNPVDMKTIEALR 409
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFI-VVDGDGDLEKLLEALE 60
glnD PRK00275
PII uridylyl-transferase; Provisional
 22-91 3.77e-05

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 46.20  E-value: 3.77e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  22 PPRASVDNSSCPECTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITD 91
Cdd:PRK00275 801 PTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSD 870
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 38-86 4.68e-05

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


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 41.12  E-value: 4.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 557536454  38 VKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDG-GWFMDVFHVIDQQG 86
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGdGGEADIFIVVDGDG 50
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 358-413 4.81e-05

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: 41.29  E-value: 4.81e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557536454 358 GLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPV-DMKTIEALRKEIG 413
Cdd:cd04895   13 GILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLtDDSLIAYIEKSLG 69
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
273-412 4.82e-05

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 45.88  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 273 VKCRDRAKLMFDIVCTLTDMQYVVFHAAI--SSDGpHASQEYYIRHMDGCILDTEGEKErvikcLEAAI----------R 340
Cdd:PRK01759 682 IYCQDQANLFLKVVSTIGAKKLSIHDAQIitSQDG-YVLDSFIVTELNGKLLEFDRRRQ-----LEQALtkalntnklkK 755

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 341 RRVSEGLSL----------------------ELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGN 398
Cdd:PRK01759 756 LNLEENHKLqhfhvktevrflneekqeqtemELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEKAEDFFILTNQQGQ 835

                        170
                 ....*....|....
gi 557536454 399 PVDMKTIEALRKEI 412
Cdd:PRK01759 836 ALDEEERKALKSRL 849
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 131-166 6.42e-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: 40.74  E-value: 6.42e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 557536454 131 IELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNR 166
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGD 36
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
349-409 8.16e-05

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 45.34  E-value: 8.16e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKTIEALR 409
Cdd:PRK04374 799 ISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALR 859
PRK03059 PRK03059
PII uridylyl-transferase; Provisional
 349-395 1.09e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235101 [Multi-domain]  Cd Length: 856  Bit Score: 44.89  E-value: 1.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDA 395
Cdd:PRK03059 789 LSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDGS 835
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 269-336 1.63e-04

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 39.60  E-value: 1.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557536454  269 SVVNVKCRDRAKLMFDIVCTLTDMQYVVFHAAISSDGPHAsqEYYIRHMDGCILDTEGEKERVIKCLE 336
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG--GIVFVVIVVDEEDLEEVLEALKKLEG 66
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
255-409 2.00e-04

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 43.81  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 255 KPEITVERLEDKGYSVVNVKCRDRAKLmFDIVCTLTDMQYVVFHAA---ISSDGpHASQEYYIRHMDGCILDtEGEKERV 331
Cdd:PRK05007 688 KPLVLLSKQATRGGTEIFIWSPDRPYL-FAAVCAELDRRNLSVHDAqifTSRDG-MAMDTFIVLEPDGSPLS-QDRHQVI 764

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 332 IKCLEAAI----------RR------------RVS------EGLS-LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTV 382
Cdd:PRK05007 765 RKALEQALtqsspqppkpRRlpaklrhfnvptEVSflpthtDRRSyMELIALDQPGLLARVGKIFADLGISLHGARITTI 844

                        170       180
                 ....*....|....*....|....*..
gi 557536454 383 GEQAVNVFYVRDASGNPVDMKTIEALR 409
Cdd:PRK05007 845 GERVEDLFILATADRRALNEELQQELR 871
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
114-169 3.37e-04

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 43.22  E-value: 3.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557536454 114 TWPSKQVGVHSVgdhtAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIA 169
Cdd:COG0317  636 EWGEDSSGVFPV----DIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTA 687
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
 131-169 5.49e-04

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: 38.20  E-value: 5.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 557536454 131 IELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIA 169
Cdd:cd04876    1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDGLA 39
PRK03059 PRK03059
PII uridylyl-transferase; Provisional
 73-163 8.13e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235101 [Multi-domain]  Cd Length: 856  Bit Score: 41.81  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  73 GWFMDVFHVIDQqGKKITDGKTIDYIE----KALGPKGHITAGAKTWPSKQVGVHSV-----------GDHTAIELIGRD 137
Cdd:PRK03059 717 GYALDTFQVLDP-EEDVHYRDIINLVEhelaERLAEQAPLPEPSKGRLSRQVKHFPItprvdlrpderGQYYILSVSAND 795

                         90       100
                 ....*....|....*....|....*.
gi 557536454 138 RPGLLSEISAVLANLRFNVAAAEVWT 163
Cdd:PRK03059 796 RPGLLYAIARVLAEHRVSVHTAKINT 821
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 338-407 9.86e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 41.52  E-value: 9.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557536454 338 AIRRRVSEGLSLEL--CAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAVNVFYVRDASGNPVDMKTIEA 407
Cdd:PRK03381 589 HVEIAPADPHMVEVtvVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGSPPDAALLRQ 660
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
44-163 2.16e-03

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 40.49  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  44 NKPGILLEVVQVLSDLDLIITKAYI-SSDGGWFMDVFHVIDQQGKKITDGKTiDYIEKALgpkghITAGAKTWPSKQVGV 122
Cdd:PRK01759 686 DQANLFLKVVSTIGAKKLSIHDAQIiTSQDGYVLDSFIVTELNGKLLEFDRR-RQLEQAL-----TKALNTNKLKKLNLE 759

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 557536454 123 H------------------SVGDHTAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWT 163
Cdd:PRK01759 760 EnhklqhfhvktevrflneEKQEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKITT 818
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
42-163 2.23e-03

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 40.73  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  42 SVNKPGILLEVVQVLSDLDLIITKAYI-SSDGGWFMDVFHVIDQQGKKITDGK---TIDYIEKALGPKGHITAGAKTWPS 117
Cdd:PRK05007 708 SPDRPYLFAAVCAELDRRNLSVHDAQIfTSRDGMAMDTFIVLEPDGSPLSQDRhqvIRKALEQALTQSSPQPPKPRRLPA 787

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557536454 118 K--------QVG---VHSVGdHTAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWT 163
Cdd:PRK05007 788 KlrhfnvptEVSflpTHTDR-RSYMELIALDQPGLLARVGKIFADLGISLHGARITT 843
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 22-102 3.19e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 39.97  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454  22 PPRASVDNSSCPECTVVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSDGGWFMDVFHVIDQQGKKITDGKtiDYIEKA 101
Cdd:PRK03381 694 PPRVLWLDGASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPLADAR--AAVEQA 771


                 .
gi 557536454 102 L 102
Cdd:PRK03381 772 V 772
ACT_4 pfam13291
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 129-167 5.18e-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: 5.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 557536454  129 TAIELIGRDRPGLLSEISAVLANLRFNVAAaeVWTHNRR 167
Cdd:pfam13291   6 VDLEVEAIDRPGLLADITQVISEEKANIVS--VNAKTRK 42
ACT_TyrKc cd04928
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ...
 38-82 5.49e-03

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


Pssm-ID: 153200  Cd Length: 68  Bit Score: 35.61  E-value: 5.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 557536454  38 VKVDSVNKPGILLEVVQVLSDLDLIITKAYI-SSDGGWFMDVFHVI 82
Cdd:cd04928    4 ITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAfSTDDGLALDIFVVT 49
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 349-395 7.11e-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: 35.52  E-value: 7.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGVSTVGEQAV-NVFYVRDA 395
Cdd:cd04927    3 LKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTPDGRVlDLFFITDA 50
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
126-207 7.59e-03

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 38.79  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557536454 126 GDHTAIELIGRDRPGLLSEISAVLANLRFNVAAAEVWTHNRRIACVLYVNDDTTcRAVGDQTRlslmeEQLKNILRGCDD 205
Cdd:PRK04374 794 GRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHD-RPLSESAR-----QALRDALCACLD 867


                 ..
gi 557536454 206 ED 207
Cdd:PRK04374 868 PV 869
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 37-106 7.84e-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: 7.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557536454  37 VVKVDSVNKPGILLEVVQVLSDLDLIITKAYISSD-GGWFMDVFHVIDQQ---GKKITDGKTIDYIEKALGPKG 106
Cdd:cd04927    2 LLKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTpDGRVLDLFFITDARellHTKKRREETYDYLRAVLGDSM 75
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 349-417 9.60e-03

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


Pssm-ID: 153155  Cd Length: 72  Bit Score: 34.92  E-value: 9.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557536454 349 LELCAKDRVGLLSEVTRILRENGLSVTRAGV--STVGEQAVNVFYVRdaSGNPvdMKTIEALRKEiGHTML 417
Cdd:cd04883    4 IEVRVPDRPGQLADIAAIFKDRGVNIVSVLVypSKEEDNKILVFRVQ--TMNP--RPIIEDLRRA-GYEVL 69
 
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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