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Conserved domains on  [gi|22328873|ref|NP_194009|]
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ACT domain repeat 7 [Arabidopsis thaliana]

Protein Classification

phosphoglycerate dehydrogenase( domain architecture ID 10141585)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 244-318 7.16e-42

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: 142.94  E-value: 7.16e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328873 244 YSVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSEPERQRLIQCLQAAIERR 318
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 33-103 4.78e-41

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: 140.67  E-value: 4.78e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328873  33 TVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEKSIETSH 103
Cdd:cd04895   2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 322-393 8.21e-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: 134.78  E-value: 8.21e-39
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328873 322 GVRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGNLIDPEIIKSIREKIGIDDL 393
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 114-188 4.06e-35

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: 124.85  E-value: 4.06e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328873 114 TALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGNSGTPIDgDSDRVQRVEGQLRNLLKA 188
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPID-DPIRLASIEDRLDNVLRG 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 ...
 244-318 7.16e-42

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: 142.94  E-value: 7.16e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328873 244 YSVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSEPERQRLIQCLQAAIERR 318
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 33-103 4.78e-41

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: 140.67  E-value: 4.78e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328873  33 TVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEKSIETSH 103
Cdd:cd04895   2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 322-393 8.21e-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: 134.78  E-value: 8.21e-39
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328873 322 GVRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGNLIDPEIIKSIREKIGIDDL 393
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 114-188 4.06e-35

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: 124.85  E-value: 4.06e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328873 114 TALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGNSGTPIDgDSDRVQRVEGQLRNLLKA 188
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPID-DPIRLASIEDRLDNVLRG 74
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 229-388 1.45e-19

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 91.74  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873 229 EKSPIVSVQNLPKRGYSVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGE-TAFLEFYVRHSDGHPVSSEPERQRL 307
Cdd:COG2844 664 SGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDgYALDTFIVLDPDGEPIDDPDRLERI 743

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873 308 IQCLQAA----------IERRTVKGVR--------------------LELCTADRPGLLAEVTRILRENGLNIARAEIST 357
Cdd:COG2844 744 EQALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHSAKIAT 823

                       170       180       190
                ....*....|....*....|....*....|..
gi 22328873 358 KDSIARNVFYVTDANGN-LIDPEIIKSIREKI 388
Cdd:COG2844 824 LGERVEDVFYVTDLDGQkLTDPERQEALREAL 855
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 226-389 1.87e-14

[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: 75.91  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873   226 FDIEKSPIVSVQNLPKRGYSVVNLQCKDRMKLLFDVVCTLtDMAYIVFHAA-IRTV-GETAFLEFYVRHSDGHPVSSEPE 303
Cdd:TIGR01693 650 ALSSGGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGAL-AMLSLSVHDAqVNTTkDGVALDTFVVQDLFGSPPAAERV 728

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873   304 RQRLIQCLQAAIERR-----TVKGVR---------------------------LELCTADRPGLLAEVTRILRENGLNIA 351
Cdd:TIGR01693 729 FQELLQGLVDVLAGLakdpdTISARRarrrrlqhfavpprvtilntasrkatiMEVRALDRPGLLARVGRTLEELGLSIQ 808

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 22328873   352 RAEISTKDSIARNVFYVTDANGNLIDPEIIKSIREKIG 389
Cdd:TIGR01693 809 SAKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLA 846
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 253-373 1.53e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 63.47  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  253 DRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSEPERQRLIQCLQ------AAIERRTVKGVR-- 324
Cdd:PRK03381 608 DRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGSPPDAALLRQDLRRALDgdldvlARLAAREAAAAAvp 687

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328873  325 ----------------------LELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANG 373
Cdd:PRK03381 688 vrrpaapprvlwldgaspdatvLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAG 758
glnD PRK00275
PII uridylyl-transferase; Provisional
 288-388 2.25e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 62.77  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  288 FYVRHSDGHPVSSEPER-----QRLIQCLQ------AAIERRT-------------------VKGVR-LELCTADRPGLL 336
Cdd:PRK00275 749 YIVLDDDGEPIGDNPARieqirEGLTEALRnpddypTIIQRRVprqlkhfafptqvtisndaQRPVTvLEIIAPDRPGLL 828

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22328873  337 AEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGN-LIDPEIIKSIREKI 388
Cdd:PRK00275 829 ARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQpLSDPQLCSRLQDAI 881
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 62-190 4.05e-09

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 59.00  E-value: 4.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  62 KAYISSDGKWnMDVFHVSDLNGDKLTDENLIRYIEKSIEtsHYCKTEGYT-----------------------------G 112
Cdd:COG2844 711 RIHTTRDGYA-LDTFIVLDPDGEPIDDPDRLERIEQALE--EALSGEVPLpeplarrlsrrlrhfpvpprvtfdndasnR 787

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328873 113 LTALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGNsGTPIDgDSDRVQRVEGQLRNLLKADD 190
Cdd:COG2844 788 YTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLD-GQKLT-DPERQEALREALLEALDEEA 863
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 20-97 6.94e-09

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 58.34  E-value: 6.94e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328873   20 PRVVIDNGVCPNSTVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEK 97
Cdd:PRK05092 831 PRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRR 908
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 323-389 6.52e-08

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 49.23  E-value: 6.52e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873   323 VRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFyVTDANGNLIDPEIIKSIREKIG 389
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVF-VVIVVDEEDLEEVLEALKKLEG 66
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 20-99 7.11e-06

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 48.60  E-value: 7.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  20 PRVVIDNGVCPNSTVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEKSI 99
Cdd:COG2844 776 PRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREAL 855
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
323-358 9.04e-04

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


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 39.82  E-value: 9.04e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 22328873 323 VRLELCTADRPGLLAEVTRILRENGLNIarAEISTK 358
Cdd:COG2716  91 YVVEVVGNDRPGIVAEVTQFLAERGINI--EDLSTK 124
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
 118-187 1.63e-03

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


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 37.15  E-value: 1.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873   118 LTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVkdgnsgtpiDGDSDRVQRVEGQLRNLLK 187
Cdd:pfam13740   7 ATGPDRPGLTASLTAVLAEHGCNILDSGQAVIHNRLSLGLLV---------SGPWDALARLEKDLLFLAH 67
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 245-316 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: 35.36  E-value: 4.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328873   245 SVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDghpvssEPERQRLIQCLQAAIE 316
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVD------EEDLEEVLEALKKLEG 66
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 111-177 5.14e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 39.20  E-value: 5.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873  111 TGLTALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGnSGTPIDGDSDRVQR 177
Cdd:PRK03381 705 PDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGA-AGGPLADARAAVEQ 770
 
Name Accession Description Interval E-value
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 244-318 7.16e-42

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: 142.94  E-value: 7.16e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328873 244 YSVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSEPERQRLIQCLQAAIERR 318
Cdd:cd04897   1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 33-103 4.78e-41

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: 140.67  E-value: 4.78e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328873  33 TVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEKSIETSH 103
Cdd:cd04895   2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 322-393 8.21e-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: 134.78  E-value: 8.21e-39
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328873 322 GVRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGNLIDPEIIKSIREKIGIDDL 393
Cdd:cd04926   1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 114-188 4.06e-35

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: 124.85  E-value: 4.06e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328873 114 TALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGNSGTPIDgDSDRVQRVEGQLRNLLKA 188
Cdd:cd04925   1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPID-DPIRLASIEDRLDNVLRG 74
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 323-389 3.77e-25

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: 97.91  E-value: 3.77e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873 323 VRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGNLIDPEIIKSIREKIG 389
Cdd:cd04899   1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALG 67
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 229-388 1.45e-19

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 91.74  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873 229 EKSPIVSVQNLPKRGYSVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGE-TAFLEFYVRHSDGHPVSSEPERQRL 307
Cdd:COG2844 664 SGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDgYALDTFIVLDPDGEPIDDPDRLERI 743

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873 308 IQCLQAA----------IERRTVKGVR--------------------LELCTADRPGLLAEVTRILRENGLNIARAEIST 357
Cdd:COG2844 744 EQALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHSAKIAT 823

                       170       180       190
                ....*....|....*....|....*....|..
gi 22328873 358 KDSIARNVFYVTDANGN-LIDPEIIKSIREKI 388
Cdd:COG2844 824 LGERVEDVFYVTDLDGQkLTDPERQEALREAL 855
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 325-388 2.35e-19

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


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 81.83  E-value: 2.35e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328873 325 LELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGNLIDPEIIKSIREKI 388
Cdd:cd04873   3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEAL 66
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 114-186 1.49e-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: 1.49e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328873 114 TALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDgNSGTPIdgDSDRVQRVEGQLRNLL 186
Cdd:cd04899   1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTD-ADGQPL--DPERQEALRAALGEAL 70
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 245-315 1.76e-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: 73.74  E-value: 1.76e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328873 245 SVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSEpERQRLIQCLQAAI 315
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPE-RIARLEEALEDAL 70
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 226-389 1.87e-14

[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: 75.91  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873   226 FDIEKSPIVSVQNLPKRGYSVVNLQCKDRMKLLFDVVCTLtDMAYIVFHAA-IRTV-GETAFLEFYVRHSDGHPVSSEPE 303
Cdd:TIGR01693 650 ALSSGGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGAL-AMLSLSVHDAqVNTTkDGVALDTFVVQDLFGSPPAAERV 728

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873   304 RQRLIQCLQAAIERR-----TVKGVR---------------------------LELCTADRPGLLAEVTRILRENGLNIA 351
Cdd:TIGR01693 729 FQELLQGLVDVLAGLakdpdTISARRarrrrlqhfavpprvtilntasrkatiMEVRALDRPGLLARVGRTLEELGLSIQ 808

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 22328873   352 RAEISTKDSIARNVFYVTDANGNLIDPEIIKSIREKIG 389
Cdd:TIGR01693 809 SAKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLA 846
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 33-102 1.38e-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: 65.26  E-value: 1.38e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  33 TVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLtDENLIRYIEKSIETS 102
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPL-DPERIARLEEALEDA 69
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 114-186 1.66e-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: 65.26  E-value: 1.66e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328873 114 TALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDgNSGTPIdgDSDRVQRVEGQLRNLL 186
Cdd:cd04873   1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTD-SDGRPL--DPERIARLEEALEDAL 70
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 253-373 1.53e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 63.47  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  253 DRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSEPERQRLIQCLQ------AAIERRTVKGVR-- 324
Cdd:PRK03381 608 DRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGSPPDAALLRQDLRRALDgdldvlARLAAREAAAAAvp 687

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328873  325 ----------------------LELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANG 373
Cdd:PRK03381 688 vrrpaapprvlwldgaspdatvLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAG 758
glnD PRK00275
PII uridylyl-transferase; Provisional
 288-388 2.25e-10

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 62.77  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  288 FYVRHSDGHPVSSEPER-----QRLIQCLQ------AAIERRT-------------------VKGVR-LELCTADRPGLL 336
Cdd:PRK00275 749 YIVLDDDGEPIGDNPARieqirEGLTEALRnpddypTIIQRRVprqlkhfafptqvtisndaQRPVTvLEIIAPDRPGLL 828

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22328873  337 AEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGN-LIDPEIIKSIREKI 388
Cdd:PRK00275 829 ARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQpLSDPQLCSRLQDAI 881
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 288-388 1.20e-09

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 60.65  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  288 FYVRHSDGHPvSSEPER-QRLIQCLQAA----------IERRTVKGVR----------------------LELCTADRPG 334
Cdd:PRK05092 777 FWIQDAFGRD-EDEPRRlARLAKAIEDAlsgevrlpeaLAKRTKPKKRarafhvpprvtidneasnrftvIEVNGRDRPG 855

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22328873  335 LLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANG-NLIDPEIIKSIREKI 388
Cdd:PRK05092 856 LLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGlKITNEARQAAIRRAL 910
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 62-190 4.05e-09

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 59.00  E-value: 4.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  62 KAYISSDGKWnMDVFHVSDLNGDKLTDENLIRYIEKSIEtsHYCKTEGYT-----------------------------G 112
Cdd:COG2844 711 RIHTTRDGYA-LDTFIVLDPDGEPIDDPDRLERIEQALE--EALSGEVPLpeplarrlsrrlrhfpvpprvtfdndasnR 787

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328873 113 LTALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGNsGTPIDgDSDRVQRVEGQLRNLLKADD 190
Cdd:COG2844 788 YTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLD-GQKLT-DPERQEALREALLEALDEEA 863
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 328-388 4.53e-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: 52.87  E-value: 4.53e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328873 328 CTADRPGLLAEVTRILRENGLNIARAEI-STKDSIARNVFYVTDANGNLI-DPEIIKSIREKI 388
Cdd:cd04900   7 YTPDRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIgERERLARIREAL 69
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
227-388 6.57e-09

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 58.21  E-value: 6.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  227 DIEKSPIVSVQNLPKRGYSVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGE-TAFLEFYVRHSDGHPVSSEPERQ 305
Cdd:PRK01759 660 DFRGDLLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDgYVLDSFIVTELNGKLLEFDRRRQ 739

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  306 ---RLIQCLQAAIERR------------TVKG-VR-----------LELCTADRPGLLAEVTRILRENGLNIARAEISTK 358
Cdd:PRK01759 740 leqALTKALNTNKLKKlnleenhklqhfHVKTeVRflneekqeqteMELFALDRAGLLAQVSQVFSELNLNLLNAKITTI 819

                        170       180       190
                 ....*....|....*....|....*....|
gi 22328873  359 DSIARNVFYVTDANGNLIDPEIIKSIREKI 388
Cdd:PRK01759 820 GEKAEDFFILTNQQGQALDEEERKALKSRL 849
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 20-97 6.94e-09

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 58.34  E-value: 6.94e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328873   20 PRVVIDNGVCPNSTVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEK 97
Cdd:PRK05092 831 PRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRR 908
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 112-318 5.07e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 55.26  E-value: 5.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  112 GLTALELTGTDRVGLLSEVFAVLADLECDVVEAKAWT-HNGRIASMIYVKDGnSGTPIDgDSDRVQR----VEGQLRNLL 186
Cdd:PRK05092 731 GVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTtTDGRALDTFWIQDA-FGRDED-EPRRLARlakaIEDALSGEV 808

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  187 KADDGyqndtrtcvsyggnthMERRLHQRMFMdrdyeKKFDIEksPIVSVQNLPKRGYSVVNLQCKDRMKLLFDVVCTLT 266
Cdd:PRK05092 809 RLPEA----------------LAKRTKPKKRA-----RAFHVP--PRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALS 865

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 22328873  267 DMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSEPERQRLIQCLQAAIERR 318
Cdd:PRK05092 866 DLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEG 917
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 323-389 6.52e-08

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 49.23  E-value: 6.52e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873   323 VRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFyVTDANGNLIDPEIIKSIREKIG 389
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVF-VVIVVDEEDLEEVLEALKKLEG 66
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
232-388 1.15e-07

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 54.21  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  232 PIVSVQNLPKRGYSVVNLQCKDRMKLlFDVVCTLTDMAYI-VFHAAIRTVGETAFLE-FYVRHSDGHPVSsePER-QRLI 308
Cdd:PRK05007 689 PLVLLSKQATRGGTEIFIWSPDRPYL-FAAVCAELDRRNLsVHDAQIFTSRDGMAMDtFIVLEPDGSPLS--QDRhQVIR 765

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  309 QCLQAAIERRTVKGVR-----------------------------LELCTADRPGLLAEVTRILRENGLNIARAEISTKD 359
Cdd:PRK05007 766 KALEQALTQSSPQPPKprrlpaklrhfnvptevsflpthtdrrsyMELIALDQPGLLARVGKIFADLGISLHGARITTIG 845

                        170       180
                 ....*....|....*....|....*....
gi 22328873  360 SIARNVFYVTDANGNLIDPEIIKSIREKI 388
Cdd:PRK05007 846 ERVEDLFILATADRRALNEELQQELRQRL 874
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 325-385 1.47e-07

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


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 48.06  E-value: 1.47e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328873 325 LELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIAR-NVFYVTDANGNLidPEIIKSIR 385
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEaDIFIVVDGDGDL--EKLLEALE 60
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 329-389 6.85e-07

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: 46.68  E-value: 6.85e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328873 329 TADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGN-LIDPEIIKSIREKIG 389
Cdd:cd04895   8 SARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNkLTDDSLIAYIEKSLG 69
glnD PRK00275
PII uridylyl-transferase; Provisional
 122-315 1.03e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 51.21  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  122 DRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGNSGTPIDGDSDRVQRVEGQLRNLLKADDGYqndtRTCVS 201
Cdd:PRK00275 713 DQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEPIGDNPARIEQIREGLTEALRNPDDY----PTIIQ 788

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  202 yggnTHMERRLhqrmfmdrdyeKKFDIekSPIVSVQNLPKRGYSVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVG 281
Cdd:PRK00275 789 ----RRVPRQL-----------KHFAF--PTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLG 851

                        170       180       190
                 ....*....|....*....|....*....|....
gi 22328873  282 ETAFLEFYVRHSDGHPVsSEPErqrLIQCLQAAI 315
Cdd:PRK00275 852 ERVEDVFFITDADNQPL-SDPQ---LCSRLQDAI 881
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 325-389 2.03e-06

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: 45.11  E-value: 2.03e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873 325 LELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDAN--GNLIDPEIIKSIREKIG 389
Cdd:cd04925   3 IELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEEtgAPIDDPIRLASIEDRLD 69
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 20-99 7.11e-06

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 48.60  E-value: 7.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  20 PRVVIDNGVCPNSTVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEKSI 99
Cdd:COG2844 776 PRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREAL 855
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 296-381 1.95e-05

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 46.91  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  296 HPVSSEPERQRLIQCLQAAIERRTV--KGVRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANG 373
Cdd:PRK03381 571 EPEPLDPAQLALAADGGVHVEIAPAdpHMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFG 650


                 ....*...
gi 22328873  374 NLIDPEII 381
Cdd:PRK03381 651 SPPDAALL 658
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
308-370 3.85e-05

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 46.11  E-value: 3.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328873  308 IQCLQAAIERRTvkgvRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTD 370
Cdd:PRK04374 786 VEFSESAGGRRT----RISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITD 844
glnD PRK00275
PII uridylyl-transferase; Provisional
 20-99 7.72e-05

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 45.05  E-value: 7.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873   20 PRVVIDNGVCPNSTVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEKSI 99
Cdd:PRK00275 802 TQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQDAI 881
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 325-371 1.11e-04

Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153199  Cd Length: 76  Bit Score: 40.53  E-value: 1.11e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 22328873 325 LELCTADRPGLLAEVTRILRENGLNIARAEISTK-DSIARNVFYVTDA 371
Cdd:cd04927   3 LKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTpDGRVLDLFFITDA 50
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 322-351 2.54e-04

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


Pssm-ID: 153155  Cd Length: 72  Bit Score: 39.16  E-value: 2.54e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 22328873 322 GVRLELCTADRPGLLAEVTRILRENGLNIA 351
Cdd:cd04883   1 SSQIEVRVPDRPGQLADIAAIFKDRGVNIV 30
ACT_CM-PDT cd04905
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ...
 329-386 3.81e-04

C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme; The C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme, found in plants, fungi, bacteria, and archaea. The P-protein of E. coli (CM-PDT, PheA) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153177 [Multi-domain]  Cd Length: 80  Bit Score: 39.02  E-value: 3.81e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873 329 TADRPGLLAEVTRILRENGLNIARAEiS--TKDSIARNVFYVtDANGNLIDPEIIKSIRE 386
Cdd:cd04905   8 LPNKPGALYDVLGVFAERGINLTKIE-SrpSKGGLWEYVFFI-DFEGHIEDPNVAEALEE 65
PRK08577 PRK08577
hypothetical protein; Provisional
 323-388 4.75e-04

hypothetical protein; Provisional


Pssm-ID: 236301 [Multi-domain]  Cd Length: 136  Bit Score: 39.98  E-value: 4.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328873  323 VRLELCTADRPGLLAEVTRILRENGLNI--ARAEISTKDSIARNVFyVTDANGNLIDPEIIKSIREKI 388
Cdd:PRK08577  57 VEIELVVEDRPGVLAKITGLLAEHGVDIlaTECEELKRGELAECVI-IVDLSKSDIDLEELEEELKKL 123
ACT_3PGDH-like cd04879
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ...
 331-392 5.34e-04

ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153151  Cd Length: 71  Bit Score: 38.22  E-value: 5.34e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328873 331 DRPGLLAEVTRILRENGLNIARAEISTKD--SIARNVFYVTDAngnlIDPEIIKSIREKIGIDD 392
Cdd:cd04879   8 DVPGVIGKVGTILGEHGINIAAMQVGRKEkgGIAYMVLDVDSP----VPEEVLEELKALPGIIR 67
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 249-301 7.06e-04

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


Pssm-ID: 153198  Cd Length: 72  Bit Score: 38.10  E-value: 7.06e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 22328873 249 LQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSE 301
Cdd:cd04926   6 LRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPK 58
PRK03059 PRK03059
PII uridylyl-transferase; Provisional
 324-371 7.41e-04

PII uridylyl-transferase; Provisional


Pssm-ID: 235101 [Multi-domain]  Cd Length: 856  Bit Score: 42.20  E-value: 7.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 22328873  324 RLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDA 371
Cdd:PRK03059 788 ILSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDGS 835
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
323-358 9.04e-04

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


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 39.82  E-value: 9.04e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 22328873 323 VRLELCTADRPGLLAEVTRILRENGLNIarAEISTK 358
Cdd:COG2716  91 YVVEVVGNDRPGIVAEVTQFLAERGINI--EDLSTK 124
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
303-368 1.15e-03

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 41.29  E-value: 1.15e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873 303 ERQRLIQcLQAAIERRTVKGVRLELCTADRPGLLAEVTRILRENGLNIARAEI-STKDSIARNVFYV 368
Cdd:COG0317 628 EPERLID-VEWGEDSSGVFPVDIRIEALDRPGLLADITSVIAEEKINILSVNTrSRDDGTATIRFTV 693
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 33-89 1.53e-03

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: 37.05  E-value: 1.53e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873  33 TVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDE 89
Cdd:cd04899   1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPE 57
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
 118-187 1.63e-03

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


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 37.15  E-value: 1.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873   118 LTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVkdgnsgtpiDGDSDRVQRVEGQLRNLLK 187
Cdd:pfam13740   7 ATGPDRPGLTASLTAVLAEHGCNILDSGQAVIHNRLSLGLLV---------SGPWDALARLEKDLLFLAH 67
ACT_LSD cd04903
C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; ...
 331-395 1.79e-03

C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; The C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillis, and Treponema species. These enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in Escherichia coli, and other enterobacterials, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153175  Cd Length: 71  Bit Score: 36.74  E-value: 1.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873 331 DRPGLLAEVTRILRENGLNIARAEISTKD--SIARNVFYVtDangNLIDPEIIKSIREKIGIDDLSV 395
Cdd:cd04903   8 DKPGAIAKVTSVLADHEINIAFMRVSRKEkgDQALMVIEV-D---QPIDEEVIEEIKKIPNIHQVIL 70
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 114-186 2.17e-03

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 36.52  E-value: 2.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328873   114 TALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVkdgnsgtpIDGDSDRVQRVEGQLRNLL 186
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVV--------IVVDEEDLEEVLEALKKLE 65
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 116-177 2.18e-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: 2.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328873 116 LELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVkdgnsGTPIDGDSDRVQR 177
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFI-----VVDGDGDLEKLLE 57
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
113-161 3.57e-03

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 39.75  E-value: 3.57e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 22328873 113 LTALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASM---IYVKD 161
Cdd:COG0317 646 PVDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTATIrftVEVRD 697
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 115-169 4.23e-03

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


Pssm-ID: 153198  Cd Length: 72  Bit Score: 35.79  E-value: 4.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22328873 115 ALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGNsGTPID 169
Cdd:cd04926   3 RLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDAN-GNPVD 56
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 245-316 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: 35.36  E-value: 4.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328873   245 SVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDghpvssEPERQRLIQCLQAAIE 316
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVD------EEDLEEVLEALKKLEG 66
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 111-177 5.14e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 39.20  E-value: 5.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328873  111 TGLTALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGnSGTPIDGDSDRVQR 177
Cdd:PRK03381 705 PDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGA-AGGPLADARAAVEQ 770
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
329-412 5.47e-03

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 39.19  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328873  329 TADRPGLLAEVTRILRENGLNIARAEI-STKDSIARNVFYVTDANGNLIDPEIIKSIREKIgIDDLSVKEPFPISCREAV 407
Cdd:PRK05007 708 SPDRPYLFAAVCAELDRRNLSVHDAQIfTSRDGMAMDTFIVLEPDGSPLSQDRHQVIRKAL-EQALTQSSPQPPKPRRLP 786


                 ....*
gi 22328873  408 EKEQH 412
Cdd:PRK05007 787 AKLRH 791
ACT_TyrKc cd04928
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ...
 329-369 5.61e-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: 5.61e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 22328873 329 TADRPGLLAEVTRILRENGLNIARAEI-STKDSIARNVFYVT 369
Cdd:cd04928   8 AGDKPKLLSQLSSLLGDLGLNIAEAHAfSTDDGLALDIFVVT 49
ACT_PDH-BS-like cd04889
C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) ...
 331-357 6.21e-03

C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate; Included in this CD is the C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Also included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153161  Cd Length: 56  Bit Score: 34.79  E-value: 6.21e-03
                        10        20
                ....*....|....*....|....*..
gi 22328873 331 DRPGLLAEVTRILRENGLNIARAEIST 357
Cdd:cd04889   7 NKPGRLAEVTEILAEAGINIKAISIAE 33
ACT_HSDH-Hom cd04881
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ...
 325-352 6.45e-03

ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153153 [Multi-domain]  Cd Length: 79  Bit Score: 35.57  E-value: 6.45e-03
                        10        20
                ....*....|....*....|....*...
gi 22328873 325 LELCTADRPGLLAEVTRILRENGLNIAR 352
Cdd:cd04881   3 LRLTVKDKPGVLAKITGILAEHGISIES 30
ACT_3PGDH cd04901
C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in ...
 324-388 6.57e-03

C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria; The C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In Escherichia coli, the SerA 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. In the homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153173  Cd Length: 69  Bit Score: 35.18  E-value: 6.57e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328873 324 RLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNvfyVTDangnlIDPEIIKSIREKI 388
Cdd:cd04901   1 RILHIHKNVPGVLGQINTILAEHNINIAAQYLQTRGEIGYV---VID-----IDSEVSEELLEAL 57
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
 116-161 6.82e-03

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


Pssm-ID: 153148 [Multi-domain]  Cd Length: 71  Bit Score: 35.12  E-value: 6.82e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 22328873 116 LELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASM---IYVKD 161
Cdd:cd04876   1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDGLATIrltLEVRD 49
ACT_F4HF-DF cd04875
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ...
 324-350 7.48e-03

N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase); This CD includes the N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase) which catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formyl-FH4 hydrolase generates the formate that is used by purT-encoded 5'-phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase, a hexamer which is activated by methionine and inhibited by glycine, is proposed to regulate the balance FH4 and C1-FH4 in response to changing growth conditions. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153147 [Multi-domain]  Cd Length: 74  Bit Score: 35.23  E-value: 7.48e-03
                        10        20
                ....*....|....*....|....*..
gi 22328873 324 RLELCTADRPGLLAEVTRILRENGLNI 350
Cdd:cd04875   1 ILTLSCPDRPGIVAAVSGFLAEHGGNI 27
 
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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