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Conserved domains on  [gi|2277095423|gb|KAI5601638|]
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hypothetical protein BDE02_01G104800 [Populus trichocarpa]

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_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 32-103 1.60e-40

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: 139.13  E-value: 1.60e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423  32 ATVVKVDSARKHRILLEAVQVLTDLNLSIKKAYISSDGRWFMDVFHVTDLNGNKLTDESVINYIEQSLGTIH 103
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 244-318 5.67e-40

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: 137.55  E-value: 5.67e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277095423 244 YSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDGTPISSEPERQRVIQCLQAAVERR 318
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 322-393 5.71e-40

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: 137.48  E-value: 5.71e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 322 GVRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGNPADPKLIESVRQKIGVSNL 393
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 114-187 1.22e-34

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: 123.69  E-value: 1.22e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2277095423 114 TALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDCNSGSPIEDTQHIDRIEARLRNVLKG 187
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
 
Name Accession Description Interval E-value
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 32-103 1.60e-40

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: 139.13  E-value: 1.60e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423  32 ATVVKVDSARKHRILLEAVQVLTDLNLSIKKAYISSDGRWFMDVFHVTDLNGNKLTDESVINYIEQSLGTIH 103
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 244-318 5.67e-40

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: 137.55  E-value: 5.67e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277095423 244 YSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDGTPISSEPERQRVIQCLQAAVERR 318
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 322-393 5.71e-40

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: 137.48  E-value: 5.71e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 322 GVRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGNPADPKLIESVRQKIGVSNL 393
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 114-187 1.22e-34

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: 123.69  E-value: 1.22e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2277095423 114 TALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDCNSGSPIEDTQHIDRIEARLRNVLKG 187
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 230-388 2.07e-20

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 94.05  E-value: 2.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 230 DSPVVTVQNWVERGYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLE-FYIRHTDGTPISSEPERQRVI 308
Cdd:COG2844   665 GKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGYALDtFIVLDPDGEPIDDPDRLERIE 744

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 309 QCLQAA----------VERRASEGVR--------------------LELCTPDRQGLLADVTRTFRENGLNVTRAEISTA 358
Cdd:COG2844   745 QALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHSAKIATL 824

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2277095423 359 GDMALNVFYVTDAVGNP-ADPKLIESVRQKI 388
Cdd:COG2844   825 GERVEDVFYVTDLDGQKlTDPERQEALREAL 855
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 227-391 4.06e-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: 74.75  E-value: 4.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 227 PSGDSPVVTVQNWVERGYSVVNVQCKDRTKLLFDVVCTLtDMEYIVFH-ATINTAGD-RAYLEFYIRHTDGTPISSEPER 304
Cdd:TIGR01693 651 LSSGGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGAL-AMLSLSVHdAQVNTTKDgVALDTFVVQDLFGSPPAAERVF 729

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 305 QRVIQCLQAAVERRASE------------GVR--------------------LELCTPDRQGLLADVTRTFRENGLNVTR 352
Cdd:TIGR01693 730 QELLQGLVDVLAGLAKDpdtisarrarrrRLQhfavpprvtilntasrkatiMEVRALDRPGLLARVGRTLEELGLSIQS 809

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2277095423 353 AEISTAGDMALNVFYVTDAVGNPADPKLIESVRQKIGVS 391
Cdd:TIGR01693 810 AKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAAS 848
glnD PRK00275
PII uridylyl-transferase; Provisional
 224-388 5.85e-14

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 74.32  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 224 ILQPSGDSPVVTVQNWVER---GYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLE-FYIRHTDGTPIS 299
Cdd:PRK00275  681 LQHPDDGGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDtYIVLDDDGEPIG 760

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 300 SEPER-----QRVIQCLQ------AAVERRASEGVR--------------------LELCTPDRQGLLADVTRTFRENGL 348
Cdd:PRK00275  761 DNPARieqirEGLTEALRnpddypTIIQRRVPRQLKhfafptqvtisndaqrpvtvLEIIAPDRPGLLARIGRIFLEFDL 840

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2277095423 349 NVTRAEISTAGDMALNVFYVTDAVGNP-ADPKLIESVRQKI 388
Cdd:PRK00275  841 SLQNAKIATLGERVEDVFFITDADNQPlSDPQLCSRLQDAI 881
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 228-376 2.05e-09

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 59.62  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 228 SGDSPVVTVQnwVERGYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDGTPISSEPERQRV 307
Cdd:PRK03381  585 DGGVHVEIAP--ADPHMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGSPPDAALLRQDL 662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 308 IQCLQ------AAVERRASEGVR------------------------LELCTPDRQGLLADVTRTFRENGLNVTRAEIST 357
Cdd:PRK03381  663 RRALDgdldvlARLAAREAAAAAvpvrrpaapprvlwldgaspdatvLEVRAADRPGLLARLARALERAGVDVRWARVAT 742

                         170
                  ....*....|....*....
gi 2277095423 358 AGDMALNVFYVTDAVGNPA 376
Cdd:PRK03381  743 LGADVVDVFYVTGAAGGPL 761
glnD PRK00275
PII uridylyl-transferase; Provisional
 50-195 3.64e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 52.75  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423  50 VQVLTDLNLSIKKAYI-SSDGRWFMDVFHVTDLNGNKLTDESV-INYIEQSLG-----------TIH------------P 104
Cdd:PRK00275  722 VAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIGDNPArIEQIREGLTealrnpddyptIIQrrvprqlkhfafP 801

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 105 GKTTGSN----GLTALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDCNsGSPIEDTQhidrIEAR 180
Cdd:PRK00275  802 TQVTISNdaqrPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDAD-NQPLSDPQ----LCSR 876

                         170
                  ....*....|....*
gi 2277095423 181 LRNVLKGDNDIRSAK 195
Cdd:PRK00275  877 LQDAICEQLDARNEK 891
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 323-389 3.30e-06

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 44.61  E-value: 3.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2277095423 323 VRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMAlNVFYVTDAVGNPADPKLIESVRQKIG 389
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG-GIVFVVIVVDEEDLEEVLEALKKLEG 66
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 297-382 5.85e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 48.83  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 297 PISSEPERQRVIQCLQAAVERRASE--GVRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGN 374
Cdd:PRK03381  572 PEPLDPAQLALAADGGVHVEIAPADphMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGS 651


                  ....*...
gi 2277095423 375 PADPKLIE 382
Cdd:PRK03381  652 PPDAALLR 659
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
113-195 2.31e-04

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 43.61  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 113 LTALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASL-MYVKdcnsgspIEDTQHIDRIEARLRNVlkgdNDI 191
Cdd:COG0317   646 PVDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTATIrFTVE-------VRDLDHLARVLRKLRKV----PGV 714


                  ....
gi 2277095423 192 RSAK 195
Cdd:COG0317   715 ISVR 718
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 114-185 4.14e-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: 38.44  E-value: 4.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 114 TALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHnGRIASLMYVkdcnsgSPIEDTQHIDRIEARLRNVL 185
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTS-EDKGGIVFV------VIVVDEEDLEEVLEALKKLE 65
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 245-316 5.34e-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: 38.06  E-value: 5.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 245 SVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDgtpissEPERQRVIQCLQAAVE 316
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVD------EEDLEEVLEALKKLEG 66
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
323-390 1.63e-03

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 40.91  E-value: 1.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 323 VRLELCTPDRQGLLADVTRTFRENGLNVTRAEI-STAGDMALNVFYVTdaVGNPAD-PKLIESVRQKIGV 390
Cdd:COG0317   647 VDIRIEALDRPGLLADITSVIAEEKINILSVNTrSRDDGTATIRFTVE--VRDLDHlARVLRKLRKVPGV 714
 
Name Accession Description Interval E-value
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 32-103 1.60e-40

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: 139.13  E-value: 1.60e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423  32 ATVVKVDSARKHRILLEAVQVLTDLNLSIKKAYISSDGRWFMDVFHVTDLNGNKLTDESVINYIEQSLGTIH 103
Cdd:cd04895     1 CTLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSLGTSR 72
ACT_ACR_3 cd04897
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 244-318 5.67e-40

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: 137.55  E-value: 5.67e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277095423 244 YSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDGTPISSEPERQRVIQCLQAAVERR 318
Cdd:cd04897     1 YSVVTVQCRDRPKLLFDVVCTLTDMDYVVFHATIDTDGDDAHQEYYIRHKDGRTLSTEGERQRVIKCLEAAIERR 75
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 322-393 5.71e-40

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: 137.48  E-value: 5.71e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 322 GVRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGNPADPKLIESVRQKIGVSNL 393
Cdd:cd04926     1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPACL 72
ACT_ACR_2 cd04925
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 114-187 1.22e-34

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: 123.69  E-value: 1.22e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2277095423 114 TALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDCNSGSPIEDTQHIDRIEARLRNVLKG 187
Cdd:cd04925     1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGAPIDDPIRLASIEDRLDNVLRG 74
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 323-389 1.01e-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: 99.45  E-value: 1.01e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2277095423 323 VRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGNPADPKLIESVRQKIG 389
Cdd:cd04899     1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALG 67
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 325-388 8.57e-21

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: 85.68  E-value: 8.57e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2277095423 325 LELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGNPADPKLIESVRQKI 388
Cdd:cd04873     3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEAL 66
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 230-388 2.07e-20

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 94.05  E-value: 2.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 230 DSPVVTVQNWVERGYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLE-FYIRHTDGTPISSEPERQRVI 308
Cdd:COG2844   665 GKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGYALDtFIVLDPDGEPIDDPDRLERIE 744

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 309 QCLQAA----------VERRASEGVR--------------------LELCTPDRQGLLADVTRTFRENGLNVTRAEISTA 358
Cdd:COG2844   745 QALEEAlsgevplpepLARRLSRRLRhfpvpprvtfdndasnrytvLEVSALDRPGLLYDIARVLADLGLNIHSAKIATL 824

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2277095423 359 GDMALNVFYVTDAVGNP-ADPKLIESVRQKI 388
Cdd:COG2844   825 GERVEDVFYVTDLDGQKlTDPERQEALREAL 855
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 114-185 3.95e-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: 78.26  E-value: 3.95e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 114 TALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDcNSGSPIeDTQHIDRIEARLRNVL 185
Cdd:cd04899     1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTD-ADGQPL-DPERQEALRAALGEAL 70
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 122-319 5.86e-18

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 86.73  E-value: 5.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 122 DRIGLLSEVFAVLADLQCSVVDAKVWT-HNGRIASLMYVKDCNsGSPIEDTQHIDRIEARLRNVLKGDNDIRSAKTmvsm 200
Cdd:COG2844   688 DRPGLFARIAGALAALGLNILDARIHTtRDGYALDTFIVLDPD-GEPIDDPDRLERIEQALEEALSGEVPLPEPLA---- 762

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 201 avTHTERRLHQVMFADRdyerkpilqpsgdspvVTVQNWVERGYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTA 280
Cdd:COG2844   763 --RRLSRRLRHFPVPPR----------------VTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATL 824

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2277095423 281 GDRAYLEFYIRHTDGTPISSEPERQRVIQCLQAAVERRA 319
Cdd:COG2844   825 GERVEDVFYVTDLDGQKLTDPERQEALREALLEALDEEA 863
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 3-190 3.44e-17

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


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 84.04  E-value: 3.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423   3 WSACSDEYeklVIRMTTPRVV-----IDNAVSSKATVVKV--DSAR-----------KHRILLEAVQVLTDLNLSIKKAY 64
Cdd:COG2844   635 WARLPDDY---FLRHDPEEIAwharlLLRADDSGKPLVLIrpDPDRggtevfvytpdRPGLFARIAGALAALGLNILDAR 711

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423  65 I--SSDGRWfMDVFHVTDLNGNKLTDESVINYIEQSLG------------------------------TIHPgktTGSNG 112
Cdd:COG2844   712 IhtTRDGYA-LDTFIVLDPDGEPIDDPDRLERIEQALEealsgevplpeplarrlsrrlrhfpvpprvTFDN---DASNR 787

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2277095423 113 LTALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDCNsGSPIEDTQHIDRIEARLRNVLKGDND 190
Cdd:COG2844   788 YTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLD-GQKLTDPERQEALREALLEALDEEAE 864
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 245-314 7.82e-16

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


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 71.81  E-value: 7.82e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 245 SVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDGTPISSEpERQRVIQCLQAA 314
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPE-RIARLEEALEDA 69
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 114-185 2.54e-15

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


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 70.27  E-value: 2.54e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 114 TALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDcNSGSPIeDTQHIDRIEARLRNVL 185
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTD-SDGRPL-DPERIARLEEALEDAL 70
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 227-391 4.06e-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: 74.75  E-value: 4.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 227 PSGDSPVVTVQNWVERGYSVVNVQCKDRTKLLFDVVCTLtDMEYIVFH-ATINTAGD-RAYLEFYIRHTDGTPISSEPER 304
Cdd:TIGR01693 651 LSSGGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGAL-AMLSLSVHdAQVNTTKDgVALDTFVVQDLFGSPPAAERVF 729

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 305 QRVIQCLQAAVERRASE------------GVR--------------------LELCTPDRQGLLADVTRTFRENGLNVTR 352
Cdd:TIGR01693 730 QELLQGLVDVLAGLAKDpdtisarrarrrRLQhfavpprvtilntasrkatiMEVRALDRPGLLARVGRTLEELGLSIQS 809

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2277095423 353 AEISTAGDMALNVFYVTDAVGNPADPKLIESVRQKIGVS 391
Cdd:TIGR01693 810 AKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAAS 848
glnD PRK00275
PII uridylyl-transferase; Provisional
 224-388 5.85e-14

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 74.32  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 224 ILQPSGDSPVVTVQNWVER---GYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLE-FYIRHTDGTPIS 299
Cdd:PRK00275  681 LQHPDDGGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDtYIVLDDDGEPIG 760

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 300 SEPER-----QRVIQCLQ------AAVERRASEGVR--------------------LELCTPDRQGLLADVTRTFRENGL 348
Cdd:PRK00275  761 DNPARieqirEGLTEALRnpddypTIIQRRVPRQLKhfafptqvtisndaqrpvtvLEIIAPDRPGLLARIGRIFLEFDL 840

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2277095423 349 NVTRAEISTAGDMALNVFYVTDAVGNP-ADPKLIESVRQKI 388
Cdd:PRK00275  841 SLQNAKIATLGERVEDVFFITDADNQPlSDPQLCSRLQDAI 881
ACT_UUR-ACR-like cd04873
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ...
 33-99 6.96e-14

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


Pssm-ID: 153145 [Multi-domain]  Cd Length: 70  Bit Score: 66.42  E-value: 6.96e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423  33 TVVKVDSARKHRILLEAVQVLTDLNLSIKKAYISSDGRWFMDVFHVTDLNGNKLTDE---SVINYIEQSL 99
Cdd:cd04873     1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPEriaRLEEALEDAL 70
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 112-322 1.40e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.82  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 112 GLTALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWT-HNGRIASLMYVKDcNSGSPIEDTQHIDRIEARLRNVLKGdnd 190
Cdd:PRK05092  731 GVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTtTDGRALDTFWIQD-AFGRDEDEPRRLARLAKAIEDALSG--- 806

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 191 irsaktmvsmavthtERRLHQVMfADRDYERK---PILQPsgdsPVVTVQN-WVERgYSVVNVQCKDRTKLLFDVVCTLT 266
Cdd:PRK05092  807 ---------------EVRLPEAL-AKRTKPKKrarAFHVP----PRVTIDNeASNR-FTVIEVNGRDRPGLLYDLTRALS 865

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2277095423 267 DMEYIVFHATINTAGDRAYLEFYIRHTDGTPISSEPERQRVIQCLQAAVERRASEG 322
Cdd:PRK05092  866 DLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEGEAEA 921
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 20-99 1.83e-11

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 66.43  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423  20 PRVVIDNAVSSKATVVKVdSARKHRILLEAV-QVLTDLNLSIKKAYISSDGRWFMDVFHVTDLNGNKLTDESVINYIEQS 98
Cdd:PRK05092  831 PRVTIDNEASNRFTVIEV-NGRDRPGLLYDLtRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRA 909


                  .
gi 2277095423  99 L 99
Cdd:PRK05092  910 L 910
glnD PRK01759
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
232-388 6.67e-11

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 234980 [Multi-domain]  Cd Length: 854  Bit Score: 64.37  E-value: 6.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 232 PVVTVQNWVERGYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLE-FYIRHTDGTPISSEPERQ---RV 307
Cdd:PRK01759  665 LLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDsFIVTELNGKLLEFDRRRQleqAL 744

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 308 IQCLQAA--VERRASEG-----------VR-----------LELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMAL 363
Cdd:PRK01759  745 TKALNTNklKKLNLEENhklqhfhvkteVRflneekqeqteMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEKAE 824

                         170       180
                  ....*....|....*....|....*
gi 2277095423 364 NVFYVTDAVGNPADPKLIESVRQKI 388
Cdd:PRK01759  825 DFFILTNQQGQALDEEERKALKSRL 849
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
224-388 1.27e-10

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 63.46  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 224 ILQPSGDSPVVTVQNWVERGYSVVNVQCKDRTKLlFDVVCTLTDMEYI-VFHATINTAGDRAYLE-FYIRHTDGTPISse 301
Cdd:PRK05007  681 LLQHDLDKPLVLLSKQATRGGTEIFIWSPDRPYL-FAAVCAELDRRNLsVHDAQIFTSRDGMAMDtFIVLEPDGSPLS-- 757

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 302 PER-QRVIQCLQAAVE---------RRASEGVR--------------------LELCTPDRQGLLADVTRTFRENGLNVT 351
Cdd:PRK05007  758 QDRhQVIRKALEQALTqsspqppkpRRLPAKLRhfnvptevsflpthtdrrsyMELIALDQPGLLARVGKIFADLGISLH 837

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2277095423 352 RAEISTAGDMALNVFYVTDAVGNPADPKLIESVRQKI 388
Cdd:PRK05007  838 GARITTIGERVEDLFILATADRRALNEELQQELRQRL 874
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 228-376 2.05e-09

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 59.62  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 228 SGDSPVVTVQnwVERGYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDGTPISSEPERQRV 307
Cdd:PRK03381  585 DGGVHVEIAP--ADPHMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGSPPDAALLRQDL 662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 308 IQCLQ------AAVERRASEGVR------------------------LELCTPDRQGLLADVTRTFRENGLNVTRAEIST 357
Cdd:PRK03381  663 RRALDgdldvlARLAAREAAAAAvpvrrpaapprvlwldgaspdatvLEVRAADRPGLLARLARALERAGVDVRWARVAT 742

                         170
                  ....*....|....*....
gi 2277095423 358 AGDMALNVFYVTDAVGNPA 376
Cdd:PRK03381  743 LGADVVDVFYVTGAAGGPL 761
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 228-373 6.10e-09

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 58.34  E-value: 6.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 228 SGDSPVVTVQNWVERGYSVVNVQCKDRTKLLFDV--VCTLTDMEyIVfHATINTAGD-RAYLEFYIRHTDGTPISsEPER 304
Cdd:PRK05092  716 AGRPLATEVRPDPARGVTEVTVLAADHPGLFSRIagACAAAGAN-IV-DARIFTTTDgRALDTFWIQDAFGRDED-EPRR 792

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 305 -QRVIQCLQAA----------VERRASEGVR----------------------LELCTPDRQGLLADVTRTFRENGLNVT 351
Cdd:PRK05092  793 lARLAKAIEDAlsgevrlpeaLAKRTKPKKRarafhvpprvtidneasnrftvIEVNGRDRPGLLYDLTRALSDLNLNIA 872

                         170       180
                  ....*....|....*....|..
gi 2277095423 352 RAEISTAGDMALNVFYVTDAVG 373
Cdd:PRK05092  873 SAHIATYGERAVDVFYVTDLFG 894
glnD PRK00275
PII uridylyl-transferase; Provisional
 122-317 1.84e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 56.60  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 122 DRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDCNSGSPI-EDTQHIDRIEARLRNVLKGDNDIRsakTMVSm 200
Cdd:PRK00275  713 DQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEPIgDNPARIEQIREGLTEALRNPDDYP---TIIQ- 788

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 201 avTHTERRLHQVMFADRdyerkpilqpsgdspvVTVQNWVERGYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTA 280
Cdd:PRK00275  789 --RRVPRQLKHFAFPTQ----------------VTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATL 850

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2277095423 281 GDRAYLEFYIRHTDGTPIsSEPERQRVIQclQAAVER 317
Cdd:PRK00275  851 GERVEDVFFITDADNQPL-SDPQLCSRLQ--DAICEQ 884
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 3.15e-08

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: 50.17  E-value: 3.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2277095423 328 CTPDRQGLLADVTRTFRENGLNVTRAEISTAGD-MALNVFYVTDAVGNP-ADPKLIESVRQKI 388
Cdd:cd04900     7 YTPDRPGLFARIAGALDQLGLNILDARIFTTRDgYALDTFVVLDPDGEPiGERERLARIREAL 69
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 122-313 8.24e-08

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 54.61  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 122 DRIGLLSEVFAVLADLQCSVVDAKVWTHNGRiASLMYVKDCNSGSPIEdtqhIDRIEARLRNVLKGDNDIRSAktmvsma 201
Cdd:PRK03381  608 DRRGLLSKAAGVLALHRLRVRSASVRSHDGV-AVLEFVVSPRFGSPPD----AALLRQDLRRALDGDLDVLAR------- 675

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 202 vthTERRlhqvmfaDRDYERKPILQPSGDSPVVtvqnWVE---RGYSVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATIN 278
Cdd:PRK03381  676 ---LAAR-------EAAAAAVPVRRPAAPPRVL----WLDgasPDATVLEVRAADRPGLLARLARALERAGVDVRWARVA 741

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2277095423 279 TAGDRAYLEFYIRHTDGTPISsePERQRVIQCLQA 313
Cdd:PRK03381  742 TLGADVVDVFYVTGAAGGPLA--DARAAVEQAVLA 774
glnD PRK00275
PII uridylyl-transferase; Provisional
 50-195 3.64e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 234709 [Multi-domain]  Cd Length: 895  Bit Score: 52.75  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423  50 VQVLTDLNLSIKKAYI-SSDGRWFMDVFHVTDLNGNKLTDESV-INYIEQSLG-----------TIH------------P 104
Cdd:PRK00275  722 VAAMDQLNLNIHDARIiTSSSQFTLDTYIVLDDDGEPIGDNPArIEQIREGLTealrnpddyptIIQrrvprqlkhfafP 801

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 105 GKTTGSN----GLTALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDCNsGSPIEDTQhidrIEAR 180
Cdd:PRK00275  802 TQVTISNdaqrPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDAD-NQPLSDPQ----LCSR 876

                         170
                  ....*....|....*
gi 2277095423 181 LRNVLKGDNDIRSAK 195
Cdd:PRK00275  877 LQDAICEQLDARNEK 891
PRK04374 PRK04374
[protein-PII] uridylyltransferase;
247-388 4.95e-07

[protein-PII] uridylyltransferase;


Pssm-ID: 179839 [Multi-domain]  Cd Length: 869  Bit Score: 52.28  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 247 VNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTA-------------------GDRAYLEFYIRHT-DGTPISSEPERQR 306
Cdd:PRK04374  693 VFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAphdaifdvfevlpqdtyadGDPQRLAAALRQVlAGDLQKVRPARRA 772

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 307 VIQCLQ-----AAVERRASEG---VRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGNPadp 378
Cdd:PRK04374  773 VPRQLRhfrfaPRVEFSESAGgrrTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRP--- 849

                         170
                  ....*....|
gi 2277095423 379 kLIESVRQKI 388
Cdd:PRK04374  850 -LSESARQAL 858
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 64-190 6.47e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 51.79  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423  64 YISSDGRwFMDVFHVTDLNGNKLTDESVINY----IEQSL-GTI---------HPGKT---------------TGSNGLT 114
Cdd:PRK05092  766 FTTTDGR-ALDTFWIQDAFGRDEDEPRRLARlakaIEDALsGEVrlpealakrTKPKKrarafhvpprvtidnEASNRFT 844

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2277095423 115 ALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDcNSGSPIEDTQHIDRIEARLRNVLKGDND 190
Cdd:PRK05092  845 VIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTD-LFGLKITNEARQAAIRRALLAALAEGEA 919
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 325-377 8.85e-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: 45.75  E-value: 8.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2277095423 325 LELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDM-ALNVFYVTDAVGNPAD 377
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGgEADIFIVVDGDGDLEK 54
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 46-101 2.44e-06

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


Pssm-ID: 153171 [Multi-domain]  Cd Length: 70  Bit Score: 44.75  E-value: 2.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2277095423  46 LLEAV-QVLTDLNLSIKKAYISSDGRWFMDVFHVTDLNGNKLTDESvINYIEQSLGT 101
Cdd:cd04899    13 LLADVtRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPER-QEALRAALGE 68
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 323-389 3.30e-06

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


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 44.61  E-value: 3.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2277095423 323 VRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMAlNVFYVTDAVGNPADPKLIESVRQKIG 389
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKG-GIVFVVIVVDEEDLEEVLEALKKLEG 66
ACT_ACR-UUR-like_2 cd04899
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ...
 245-309 3.33e-06

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


Pssm-ID: 153171 [Multi-domain]  Cd Length: 70  Bit Score: 44.37  E-value: 3.33e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277095423 245 SVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDGTPISsePERQRVIQ 309
Cdd:cd04899     1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLD--PERQEALR 63
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 297-382 5.85e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 48.83  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 297 PISSEPERQRVIQCLQAAVERRASE--GVRLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGN 374
Cdd:PRK03381  572 PEPLDPAQLALAADGGVHVEIAPADphMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSHDGVAVLEFVVSPRFGS 651


                  ....*...
gi 2277095423 375 PADPKLIE 382
Cdd:PRK03381  652 PPDAALLR 659
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 116-182 6.18e-06

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: 43.43  E-value: 6.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2277095423 116 LELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKdcnsgspIEDTQHIDRIEARLR 182
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIV-------VDGDGDLEKLLEALE 60
ACT_ACR_1 cd04895
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 332-392 3.27e-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: 41.67  E-value: 3.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 332 RQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGNP-ADPKLIESVRQKIGVSN 392
Cdd:cd04895    11 KPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKlTDDSLIAYIEKSLGTSR 72
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 45-103 7.12e-05

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


Pssm-ID: 153198  Cd Length: 72  Bit Score: 40.80  E-value: 7.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2277095423  45 ILLEAVQVLTDLNLSIKKAYISSDGRWFMDVFHVTDLNGNKlTDESVINYIEQSLGTIH 103
Cdd:cd04926    14 LLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNP-VDPKTIEAVRQEIGPAC 71
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 122-185 1.30e-04

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


Pssm-ID: 153172 [Multi-domain]  Cd Length: 73  Bit Score: 40.15  E-value: 1.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277095423 122 DRIGLLSEVFAVLADLQCSVVDAKVWT-HNGRIASLMYVKDcNSGSPIEDTQHIDRIEARLRNVL 185
Cdd:cd04900    10 DRPGLFARIAGALDQLGLNILDARIFTtRDGYALDTFVVLD-PDGEPIGERERLARIREALEDAL 73
ACT_ACR-like_1 cd04894
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ...
 330-376 1.70e-04

ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the N-terminal ACT domain of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (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: 153166  Cd Length: 69  Bit Score: 39.81  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2277095423 330 PDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDAVGNPA 376
Cdd:cd04894     8 PDKTGLGCDLCRIILEFGLNITRGDDSTDGRWCYIVFWVVPRPPSIK 54
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
113-195 2.31e-04

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 43.61  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 113 LTALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASL-MYVKdcnsgspIEDTQHIDRIEARLRNVlkgdNDI 191
Cdd:COG0317   646 PVDIRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTATIrFTVE-------VRDLDHLARVLRKLRKV----PGV 714


                  ....
gi 2277095423 192 RSAK 195
Cdd:COG0317   715 ISVR 718
ACT_ACR-like_2 cd04927
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ...
 325-371 2.44e-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: 39.37  E-value: 2.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2277095423 325 LELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGD-MALNVFYVTDA 371
Cdd:cd04927     3 LKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTPDgRVLDLFFITDA 50
ACT_UUR-like_1 cd04900
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ...
 50-99 2.83e-04

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


Pssm-ID: 153172 [Multi-domain]  Cd Length: 73  Bit Score: 39.00  E-value: 2.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2277095423  50 VQVLTDLNLSIKKAYI--SSDGrWFMDVFHVTDLNGNKLTDESVINYIEQSL 99
Cdd:cd04900    19 AGALDQLGLNILDARIftTRDG-YALDTFVVLDPDGEPIGERERLARIREAL 69
ACT_ACR_4 cd04926
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ...
 115-182 4.13e-04

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


Pssm-ID: 153198  Cd Length: 72  Bit Score: 38.87  E-value: 4.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2277095423 115 ALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDCNsGSPIeDTQHIDRIEARLR 182
Cdd:cd04926     3 RLELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDAN-GNPV-DPKTIEAVRQEIG 68
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 114-185 4.14e-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: 38.44  E-value: 4.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 114 TALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHnGRIASLMYVkdcnsgSPIEDTQHIDRIEARLRNVL 185
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTS-EDKGGIVFV------VIVVDEEDLEEVLEALKKLE 65
ACT_GcvR_1 cd04893
ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, ...
 113-181 4.56e-04

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


Pssm-ID: 153165 [Multi-domain]  Cd Length: 77  Bit Score: 38.84  E-value: 4.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2277095423 113 LTALeltGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVkdcnSGSPiedtQHIDRIEARL 181
Cdd:cd04893     4 ISAL---GTDRPGILNELTRAVSESGCNILDSRMAILGTEFALTMLV----EGSW----DAIAKLEAAL 61
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 245-316 5.34e-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: 38.06  E-value: 5.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 245 SVVNVQCKDRTKLLFDVVCTLTDMEYIVFHATINTAGDRAYLEFYIRHTDgtpissEPERQRVIQCLQAAVE 316
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVD------EEDLEEVLEALKKLEG 66
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
 116-184 5.52e-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: 5.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2277095423 116 LELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDcnsgspIEDTQHIDRIEARLRNV 184
Cdd:cd04876     1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDGLATIRLTLE------VRDLEHLARIMRKLRQI 63
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
113-184 1.23e-03

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


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 39.43  E-value: 1.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277095423 113 LTALeltGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVkdcnSGSPiedtQHIDRIEARLRNV 184
Cdd:COG2716     6 ITAI---GPDRPGIVAALARAVSEHGCNILDSRMARLGGEFAGILLV----SGPW----DAIAKLEAALPAL 66
PRK03059 PRK03059
PII uridylyl-transferase; Provisional
 324-371 1.56e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235101 [Multi-domain]  Cd Length: 856  Bit Score: 41.04  E-value: 1.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2277095423 324 RLELCTPDRQGLLADVTRTFRENGLNVTRAEISTAGDMALNVFYVTDA 371
Cdd:PRK03059  788 ILSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDGS 835
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
323-390 1.63e-03

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 40.91  E-value: 1.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 323 VRLELCTPDRQGLLADVTRTFRENGLNVTRAEI-STAGDMALNVFYVTdaVGNPAD-PKLIESVRQKIGV 390
Cdd:COG0317   647 VDIRIEALDRPGLLADITSVIAEEKINILSVNTrSRDDGTATIRFTVE--VRDLDHlARVLRKLRKVPGV 714
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 322-350 3.61e-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: 36.08  E-value: 3.61e-03
                          10        20
                  ....*....|....*....|....*....
gi 2277095423 322 GVRLELCTPDRQGLLADVTRTFRENGLNV 350
Cdd:cd04883     1 SSQIEVRVPDRPGQLADIAAIFKDRGVNI 29
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
 118-154 3.70e-03

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


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 36.00  E-value: 3.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2277095423 118 LTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIA 154
Cdd:pfam13740   7 ATGPDRPGLTASLTAVLAEHGCNILDSGQAVIHNRLS 43
PRK05007 PRK05007
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
50-148 4.24e-03

bifunctional uridylyltransferase/uridylyl-removing protein GlnD;


Pssm-ID: 235329 [Multi-domain]  Cd Length: 884  Bit Score: 39.57  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423  50 VQVLTDLNLSIKKAYI--SSDGrWFMDVFHVTDLNGNKLTD---ESVINYIEQSL--GTIHPGKT--------------- 107
Cdd:PRK05007  719 CAELDRRNLSVHDAQIftSRDG-MAMDTFIVLEPDGSPLSQdrhQVIRKALEQALtqSSPQPPKPrrlpaklrhfnvpte 797

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2277095423 108 -----TGSNGLTALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWT 148
Cdd:PRK05007  798 vsflpTHTDRRSYMELIALDQPGLLARVGKIFADLGISLHGARITT 843
PRK05092 PRK05092
PII uridylyl-transferase; Provisional
 326-377 4.57e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235342 [Multi-domain]  Cd Length: 931  Bit Score: 39.47  E-value: 4.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2277095423 326 ELC--TPDRQGLLADVTRTFRENGLNVTRAEISTAGD-MALNVFYVTDAVGNPAD 377
Cdd:PRK05092  734 EVTvlAADHPGLFSRIAGACAAAGANIVDARIFTTTDgRALDTFWIQDAFGRDED 788
PRK08577 PRK08577
hypothetical protein; Provisional
 315-399 5.82e-03

hypothetical protein; Provisional


Pssm-ID: 236301 [Multi-domain]  Cd Length: 136  Bit Score: 36.90  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277095423 315 VERRASEG---VRLELCTPDRQGLLADVTRTFRENGLNV--TRAEISTAGDMALNVFyVTDAVGNPADPKLIESVRQKI- 388
Cdd:PRK08577   46 LEPIALPGkklVEIELVVEDRPGVLAKITGLLAEHGVDIlaTECEELKRGELAECVI-IVDLSKSDIDLEELEEELKKLe 124

                          90
                  ....*....|.
gi 2277095423 389 GVSNLKVKELP 399
Cdd:PRK08577  125 EVKEVEIRQIE 135
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 108-182 9.50e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 38.43  E-value: 9.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277095423 108 TGSNGLTALELTGTDRIGLLSEVFAVLADLQCSVVDAKVWTHNGRIASLMYVKDcNSGSPIEDTQhiDRIEARLR 182
Cdd:PRK03381  702 GASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTG-AAGGPLADAR--AAVEQAVL 773
 
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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