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Conserved domains on  [gi|1910257199|ref|WP_191078693|]
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bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase [Stenotrophomonas sp. Br8]

Protein Classification

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase( domain architecture ID 1002182)

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase adenylates and deadenylates glutamate-ammonia ligase; the two activities are functionally the reverse of one another and must be controlled by the organism to prevent futile cycling

CATH:  1.10.4050.10|1.20.120.330
EC:  2.7.7.-
Gene Ontology:  GO:0008882
PubMed:  11585846|20026075
SCOP:  4002593|4002381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlnE1 COG1391
Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, ...
 5-914 0e+00

Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441001 [Multi-domain]  Cd Length: 948  Bit Score: 1033.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199   5 PAELPAPLQPLVDRALARLAQAVPDPIPA--ELQPMLVQLAVSSDFAMDTLVRQPGLLAQLSAPGCPPLP---------- 72
Cdd:COG1391     2 TAPLPAALQAALERLLARLLEALAALLALdpALRALLAAVLAASPFLARLLRRDPELLARLLASGPLPRPldaadllarl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  73 -APVLDPLQPSDWPAQLRRWRTAMSTRLIWRDLAGLDDVPQTLAGATALAEDCLRLALDALQQEFAQRHGVIADDNGRPQ 151
Cdd:COG1391    82 aAALAAAADEAALMRALRRFRRREMLRIAWRDLAGLADLEEVTAALSALAEAAIQAALDWLYRELAARYGTPLDADGEPQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 152 QLVVFglgklgggelNFSSDVDLVYAYVQGGESDGPRALAAEEYFARLGQRLAKLLDETTVDGFSHRVDLRLRPFGSAGR 231
Cdd:COG1391   162 GLVVLgmgklggrelNFSSDIDLIFAYPEDGETDGRRSLSNQEFFTRLGQRLIKLLDERTADGFVFRVDMRLRPDGDSGP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 232 VALSFAAMDQYFQREGRDWERYAWLKARAVAGDIAAGEAWLQTLRPFVYRRYLDFTALDGLREMKAAITAEVARREMHDD 311
Cdd:COG1391   242 LALSFAALEDYYQSQGREWERYAMIKARPVAGDLEAGEELLALLRPFVYRRYLDFGAIESLREMKRQIRAEVRRRGLGDN 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 312 IKRGAGGIREIEFLCQALQLIRGGREPVLRERRLLVALEALVAAGQIARDDGAALREAYLFLRRLENRLQMLRDAQTHVL 391
Cdd:COG1391   322 IKLGRGGIREIEFIVQTFQLIRGGREPELRQRSTLEALDALAELGLLPAEAADELAEAYRFLRRVEHRLQMLDDQQTHTL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 392 PSDVLDRERIAVGLGYADWDALRAALTVQQQRVSTEFGALLAPRKGQAAPD-ALANYWR-SLPEGSNAPLLAEAGFLDAN 469
Cdd:COG1391   402 PEDEEDRARLARAMGFADWAAFLAALDAHRQRVHRHFAALFGDPEELSSEDgPLNLLWTgDLDDEETLETLAQLGFEDPE 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 470 GADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLALLDEQPSALARLVDV 549
Cdd:COG1391   482 AAAERLRAWRHGRRVRTLSERARERLDRLMPRLLEALAETPDPDEALLRFLDLLEAIPRRTAYLALLAENPAALKRLARL 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 550 LARSALLAERLAAYPLLLDELLDVRVSGPMPDAAGMLAECQQVL---TVEDPESALRWLNETRLALSFRMAMATLDGRQG 626
Cdd:COG1391   562 CGASPWLAEYLARHPILLDELLDPRFLYEPPDRAALRAELRQRLaraPEDDEEQQLDALRQFKQAQVFRIAAADLAGALP 641

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 627 AVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIA---GGRFAIIGYGSLGGLELGFGSDLDLVFLHDHPAGVEASDGAR 703
Cdd:COG1391   642 VMKVSDHLTALAEAILEAVLRLAWQELAARHGRPRhreGPGFAVIGYGKLGGKELGYGSDLDLVFLYDDDDEAAETDGER 721

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 704 PLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGVAGDASLL 783
Cdd:COG1391   722 PIDASQFYARLAQRLIHALTTRTAAGILYEVDMRLRPSGNSGLLVTSLDAFEDYQRNEAWTWEHQALTRARVVAGDPALG 801

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 784 QDFEQVRAQTLGRERDRATLYADVVKMRGRMRTELDRSDAARLDLKQGSGGVVDLEFLLQSGVLARSAQTPALLQPRATP 863
Cdd:COG1391   802 ARFEAIRREVLTRPRDPAKLREEVREMREKMRAELGSKSAGRFDLKQDRGGIVDIEFIVQYLVLAHAHEHPELLRNSDNI 881

                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1910257199 864 ALIDALAAAGFLPEATAQTLHGAHATLLEVGLACTLDRRPRLAPTTPAIEE 914
Cdd:COG1391   882 RLLEALAEAGLLPAEDAEALADAYRLLRRLQHRLRLQEQPARVPPDELEAE 932
 
Name Accession Description Interval E-value
GlnE1 COG1391
Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, ...
 5-914 0e+00

Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441001 [Multi-domain]  Cd Length: 948  Bit Score: 1033.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199   5 PAELPAPLQPLVDRALARLAQAVPDPIPA--ELQPMLVQLAVSSDFAMDTLVRQPGLLAQLSAPGCPPLP---------- 72
Cdd:COG1391     2 TAPLPAALQAALERLLARLLEALAALLALdpALRALLAAVLAASPFLARLLRRDPELLARLLASGPLPRPldaadllarl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  73 -APVLDPLQPSDWPAQLRRWRTAMSTRLIWRDLAGLDDVPQTLAGATALAEDCLRLALDALQQEFAQRHGVIADDNGRPQ 151
Cdd:COG1391    82 aAALAAAADEAALMRALRRFRRREMLRIAWRDLAGLADLEEVTAALSALAEAAIQAALDWLYRELAARYGTPLDADGEPQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 152 QLVVFglgklgggelNFSSDVDLVYAYVQGGESDGPRALAAEEYFARLGQRLAKLLDETTVDGFSHRVDLRLRPFGSAGR 231
Cdd:COG1391   162 GLVVLgmgklggrelNFSSDIDLIFAYPEDGETDGRRSLSNQEFFTRLGQRLIKLLDERTADGFVFRVDMRLRPDGDSGP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 232 VALSFAAMDQYFQREGRDWERYAWLKARAVAGDIAAGEAWLQTLRPFVYRRYLDFTALDGLREMKAAITAEVARREMHDD 311
Cdd:COG1391   242 LALSFAALEDYYQSQGREWERYAMIKARPVAGDLEAGEELLALLRPFVYRRYLDFGAIESLREMKRQIRAEVRRRGLGDN 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 312 IKRGAGGIREIEFLCQALQLIRGGREPVLRERRLLVALEALVAAGQIARDDGAALREAYLFLRRLENRLQMLRDAQTHVL 391
Cdd:COG1391   322 IKLGRGGIREIEFIVQTFQLIRGGREPELRQRSTLEALDALAELGLLPAEAADELAEAYRFLRRVEHRLQMLDDQQTHTL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 392 PSDVLDRERIAVGLGYADWDALRAALTVQQQRVSTEFGALLAPRKGQAAPD-ALANYWR-SLPEGSNAPLLAEAGFLDAN 469
Cdd:COG1391   402 PEDEEDRARLARAMGFADWAAFLAALDAHRQRVHRHFAALFGDPEELSSEDgPLNLLWTgDLDDEETLETLAQLGFEDPE 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 470 GADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLALLDEQPSALARLVDV 549
Cdd:COG1391   482 AAAERLRAWRHGRRVRTLSERARERLDRLMPRLLEALAETPDPDEALLRFLDLLEAIPRRTAYLALLAENPAALKRLARL 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 550 LARSALLAERLAAYPLLLDELLDVRVSGPMPDAAGMLAECQQVL---TVEDPESALRWLNETRLALSFRMAMATLDGRQG 626
Cdd:COG1391   562 CGASPWLAEYLARHPILLDELLDPRFLYEPPDRAALRAELRQRLaraPEDDEEQQLDALRQFKQAQVFRIAAADLAGALP 641

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 627 AVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIA---GGRFAIIGYGSLGGLELGFGSDLDLVFLHDHPAGVEASDGAR 703
Cdd:COG1391   642 VMKVSDHLTALAEAILEAVLRLAWQELAARHGRPRhreGPGFAVIGYGKLGGKELGYGSDLDLVFLYDDDDEAAETDGER 721

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 704 PLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGVAGDASLL 783
Cdd:COG1391   722 PIDASQFYARLAQRLIHALTTRTAAGILYEVDMRLRPSGNSGLLVTSLDAFEDYQRNEAWTWEHQALTRARVVAGDPALG 801

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 784 QDFEQVRAQTLGRERDRATLYADVVKMRGRMRTELDRSDAARLDLKQGSGGVVDLEFLLQSGVLARSAQTPALLQPRATP 863
Cdd:COG1391   802 ARFEAIRREVLTRPRDPAKLREEVREMREKMRAELGSKSAGRFDLKQDRGGIVDIEFIVQYLVLAHAHEHPELLRNSDNI 881

                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1910257199 864 ALIDALAAAGFLPEATAQTLHGAHATLLEVGLACTLDRRPRLAPTTPAIEE 914
Cdd:COG1391   882 RLLEALAEAGLLPAEDAEALADAYRLLRRLQHRLRLQEQPARVPPDELEAE 932
PRK11072 PRK11072
bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/ ...
 9-890 0e+00

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase;


Pssm-ID: 236836 [Multi-domain]  Cd Length: 943  Bit Score: 833.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199   9 PAPLQPLVDRALARLAQAVPDP-IPAELQPMLVQLAVSSDFAMDTLVRQPGLLAQLSAPgcppLPAPvLDPLQPSDWPAQ 87
Cdd:PRK11072    1 MLPLSSPLQQYWQTLVERLPEPlAPESLSAQLKSVLALSDFVARQLQAHPELLEELAAQ----LPQP-LERQAYAAWLQE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  88 --------------LRRWRTAMSTRLIWRDLAGLDDVPQTLAGATALAEDCLRLALDALQQEFAQRHGVIADDNGRPQQL 153
Cdd:PRK11072   76 llaavadedalmraLRQFRRRVMVRIAWRDLLGLADLEEVLGQLSDLAEALIIAARDWLYAALCAEYGTPCGAQGEPQPL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 154 VVFGLGKLGGGELNFSSDVDLVYAYVQGGE-SDGPRALAAEEYFARLGQRLAKLLDETTVDGFSHRVDLRLRPFGSAGRV 232
Cdd:PRK11072  156 LILGMGKLGGRELNFSSDIDLIFTYPEHGEtQGGRRSIDNQQFFTRLGQRLIKALDQVTADGFVFRVDMRLRPFGDSGPL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 233 ALSFAAMDQYFQREGRDWERYAWLKARAV-AGDIAAGEAWLQTLRPFVYRRYLDFTALDGLREMKAAITAEVARREMHDD 311
Cdd:PRK11072  236 VLSFAALEDYYQEQGRDWERYAMIKARVMgDPDDAYAQELRAMLRPFVFRRYLDFSAIQALRNMKGMIRREVRRRGLADN 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 312 IKRGAGGIREIEFLCQALQLIRGGREPVLRERRLLVALEALVAAGQIARDDGAALREAYLFLRRLENRLQMLRDAQTHVL 391
Cdd:PRK11072  316 IKLGAGGIREIEFIVQVFQLIRGGREPSLQQRSLLEVLDALAELGLLPEEQVAELRDAYLFLRRLEHLLQAINDQQTQTL 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 392 PSDVLDRERIAVGLGYADWDALRAALTVQQQRVSTEFGALLAPRKGQAAPDALANYWRSL-----PEGSNAPLLAEAGFL 466
Cdd:PRK11072  396 PDDPLDRARLAWAMGFADWAALLDVLDAHRANVRRVFNQLIGDDEEETEEEAASEQWRELwqdalDEEDATPLLAELGFD 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 467 DANGADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLALLDEQPSALARL 546
Cdd:PRK11072  476 DPAQVLARLAAFRHSLRKRTLGPRGRERLDALMPRLLEAACAREDADVTLERLLDLLEAISRRTTYLELLSENPGALKRL 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 547 VDVLARSALLAERLAAYPLLLDELLDVRVSGPMPDAAGMLAECQQVLT---VEDPESALRWLNETRLALSFRMAMATLDG 623
Cdd:PRK11072  556 ISLCAASPWIAEQLARYPLLLDELLDPRALYQPTDWDAYRDELRQYLLrvpEDDEEQQMEALRQFKQAQVLRIAAADIAG 635

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 624 RQGAVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIA-----GGRFAIIGYGSLGGLELGFGSDLDLVFLHDHPAGVEa 698
Cdd:PRK11072  636 VLPVMKVSDHLTYLAEAILDAVVQQAWQQMVKRHGEPPhlegrERGFAVIGYGKLGGKELGYASDLDLVFLHDCPEDAM- 714

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 699 SDGARPLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGVAG 778
Cdd:PRK11072  715 TDGDKSIDGRQFYLRLAQRIIHLFSTRTSSGILYEVDMRLRPSGAAGLLVSSLEAFERYQLNEAWTWEHQALVRARFVAG 794

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 779 DASLLQDFEQVRAQTLGRERDRATLYADVVKMRGRMRTELDRSDAARLDLKQGSGGVVDLEFLLQSGVLARSAQTPALLQ 858
Cdd:PRK11072  795 DPQLGAAFEAIRREVLTQPRDLATLRTEVREMREKMRDHLGNKTRDRFDLKQDRGGIVDIEFIAQYLVLAHAHEHPELTR 874

                         890       900       910
                  ....*....|....*....|....*....|..
gi 1910257199 859 PRATPALIDALAAAGFLPEATAQTLHGAHATL 890
Cdd:PRK11072  875 WSDNVRILELLAELGLMSEEEAEALTDAYRTL 906
GlnE pfam03710
Glutamate-ammonia ligase adenylyltransferase; Conserved repeated domain found in GlnE proteins. ...
 543-788 7.65e-56

Glutamate-ammonia ligase adenylyltransferase; Conserved repeated domain found in GlnE proteins. These proteins adenylate and deadenylate glutamine synthases: ATP + {L-Glutamate:ammonia ligase (ADP-forming)} = Diphosphate + Adenylyl-{L-Glutamate:Ammonia ligase (ADP-forming)}. The family is related to the pfam01909 domain.


Pssm-ID: 397667 [Multi-domain]  Cd Length: 249  Bit Score: 193.30  E-value: 7.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 543 LARLVDVLARSALLAERLAAYPLLLDELLDvRVSGPMPDAAGMLAECQQVLTVEDPESALRWLNETRLALSFRMAMATLD 622
Cdd:pfam03710   1 LEQLREVLAASPFVAEQLARYPILLDELLD-PLGNPKDLAAYPAELADALAAVPDEEQAMDALRQFRRAELLRIAAADLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 623 GRQGAVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIAGGR------FAIIGYGSLGGLELGFGSDLDLVFLHDHPAGV 696
Cdd:pfam03710  80 GLLTVEEVSDALSQLAEAVIDAALDWAWRQVCSRGGTPVHLQsgepqgFAVIGMGKLGGFELGYSSDLDLIFLYDPDGET 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 697 EasDGARPLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGV 776
Cdd:pfam03710 160 Q--GARRSIDAAQFYTRLAQRLISALSAPTGDGFLYEVDMRLRPSGDSGPLVLSFAAFEDYYEEQAWTWERQALIRARVV 237

                         250
                  ....*....|..
gi 1910257199 777 AGDASLLQDFEQ 788
Cdd:pfam03710 238 GGDAELGAAFLR 249
NT_GlnE_GlnD_like cd05401
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ...
 607-793 2.49e-27

Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143391 [Multi-domain]  Cd Length: 172  Bit Score: 109.35  E-value: 2.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 607 ETRLALSFRMAMATLDGRQGAVDSTRQLAELAQAVVVTVLAMAEADMQAAhgvIAGGRFAIIGYGSLGGLELGFGSDLDL 686
Cdd:cd05401     1 RAKLRQLRRILRRDLLGGASIRAISRALSDLADALLRRALELALAELGKG---PPPVPFALLALGSYGRGELNPSSDQDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 687 VFLHDHPAGVEAsdgarplepgRWYARLAQKVMALLAAvtAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWE 766
Cdd:cd05401    78 LLLYDDDGDEVA----------AYFEELAERLIKILSE--AGGPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEPGRLWE 145

                         170       180
                  ....*....|....*....|....*..
gi 1910257199 767 HQALVRARGVAGDASLLQDFEQVRAQT 793
Cdd:cd05401   146 RTALLDARPVAGDRALAEELRRRIRER 172
 
Name Accession Description Interval E-value
GlnE1 COG1391
Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, ...
 5-914 0e+00

Glutamine synthetase adenylyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441001 [Multi-domain]  Cd Length: 948  Bit Score: 1033.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199   5 PAELPAPLQPLVDRALARLAQAVPDPIPA--ELQPMLVQLAVSSDFAMDTLVRQPGLLAQLSAPGCPPLP---------- 72
Cdd:COG1391     2 TAPLPAALQAALERLLARLLEALAALLALdpALRALLAAVLAASPFLARLLRRDPELLARLLASGPLPRPldaadllarl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  73 -APVLDPLQPSDWPAQLRRWRTAMSTRLIWRDLAGLDDVPQTLAGATALAEDCLRLALDALQQEFAQRHGVIADDNGRPQ 151
Cdd:COG1391    82 aAALAAAADEAALMRALRRFRRREMLRIAWRDLAGLADLEEVTAALSALAEAAIQAALDWLYRELAARYGTPLDADGEPQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 152 QLVVFglgklgggelNFSSDVDLVYAYVQGGESDGPRALAAEEYFARLGQRLAKLLDETTVDGFSHRVDLRLRPFGSAGR 231
Cdd:COG1391   162 GLVVLgmgklggrelNFSSDIDLIFAYPEDGETDGRRSLSNQEFFTRLGQRLIKLLDERTADGFVFRVDMRLRPDGDSGP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 232 VALSFAAMDQYFQREGRDWERYAWLKARAVAGDIAAGEAWLQTLRPFVYRRYLDFTALDGLREMKAAITAEVARREMHDD 311
Cdd:COG1391   242 LALSFAALEDYYQSQGREWERYAMIKARPVAGDLEAGEELLALLRPFVYRRYLDFGAIESLREMKRQIRAEVRRRGLGDN 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 312 IKRGAGGIREIEFLCQALQLIRGGREPVLRERRLLVALEALVAAGQIARDDGAALREAYLFLRRLENRLQMLRDAQTHVL 391
Cdd:COG1391   322 IKLGRGGIREIEFIVQTFQLIRGGREPELRQRSTLEALDALAELGLLPAEAADELAEAYRFLRRVEHRLQMLDDQQTHTL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 392 PSDVLDRERIAVGLGYADWDALRAALTVQQQRVSTEFGALLAPRKGQAAPD-ALANYWR-SLPEGSNAPLLAEAGFLDAN 469
Cdd:COG1391   402 PEDEEDRARLARAMGFADWAAFLAALDAHRQRVHRHFAALFGDPEELSSEDgPLNLLWTgDLDDEETLETLAQLGFEDPE 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 470 GADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLALLDEQPSALARLVDV 549
Cdd:COG1391   482 AAAERLRAWRHGRRVRTLSERARERLDRLMPRLLEALAETPDPDEALLRFLDLLEAIPRRTAYLALLAENPAALKRLARL 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 550 LARSALLAERLAAYPLLLDELLDVRVSGPMPDAAGMLAECQQVL---TVEDPESALRWLNETRLALSFRMAMATLDGRQG 626
Cdd:COG1391   562 CGASPWLAEYLARHPILLDELLDPRFLYEPPDRAALRAELRQRLaraPEDDEEQQLDALRQFKQAQVFRIAAADLAGALP 641

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 627 AVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIA---GGRFAIIGYGSLGGLELGFGSDLDLVFLHDHPAGVEASDGAR 703
Cdd:COG1391   642 VMKVSDHLTALAEAILEAVLRLAWQELAARHGRPRhreGPGFAVIGYGKLGGKELGYGSDLDLVFLYDDDDEAAETDGER 721

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 704 PLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGVAGDASLL 783
Cdd:COG1391   722 PIDASQFYARLAQRLIHALTTRTAAGILYEVDMRLRPSGNSGLLVTSLDAFEDYQRNEAWTWEHQALTRARVVAGDPALG 801

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 784 QDFEQVRAQTLGRERDRATLYADVVKMRGRMRTELDRSDAARLDLKQGSGGVVDLEFLLQSGVLARSAQTPALLQPRATP 863
Cdd:COG1391   802 ARFEAIRREVLTRPRDPAKLREEVREMREKMRAELGSKSAGRFDLKQDRGGIVDIEFIVQYLVLAHAHEHPELLRNSDNI 881

                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1910257199 864 ALIDALAAAGFLPEATAQTLHGAHATLLEVGLACTLDRRPRLAPTTPAIEE 914
Cdd:COG1391   882 RLLEALAEAGLLPAEDAEALADAYRLLRRLQHRLRLQEQPARVPPDELEAE 932
PRK11072 PRK11072
bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/ ...
 9-890 0e+00

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase;


Pssm-ID: 236836 [Multi-domain]  Cd Length: 943  Bit Score: 833.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199   9 PAPLQPLVDRALARLAQAVPDP-IPAELQPMLVQLAVSSDFAMDTLVRQPGLLAQLSAPgcppLPAPvLDPLQPSDWPAQ 87
Cdd:PRK11072    1 MLPLSSPLQQYWQTLVERLPEPlAPESLSAQLKSVLALSDFVARQLQAHPELLEELAAQ----LPQP-LERQAYAAWLQE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  88 --------------LRRWRTAMSTRLIWRDLAGLDDVPQTLAGATALAEDCLRLALDALQQEFAQRHGVIADDNGRPQQL 153
Cdd:PRK11072   76 llaavadedalmraLRQFRRRVMVRIAWRDLLGLADLEEVLGQLSDLAEALIIAARDWLYAALCAEYGTPCGAQGEPQPL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 154 VVFGLGKLGGGELNFSSDVDLVYAYVQGGE-SDGPRALAAEEYFARLGQRLAKLLDETTVDGFSHRVDLRLRPFGSAGRV 232
Cdd:PRK11072  156 LILGMGKLGGRELNFSSDIDLIFTYPEHGEtQGGRRSIDNQQFFTRLGQRLIKALDQVTADGFVFRVDMRLRPFGDSGPL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 233 ALSFAAMDQYFQREGRDWERYAWLKARAV-AGDIAAGEAWLQTLRPFVYRRYLDFTALDGLREMKAAITAEVARREMHDD 311
Cdd:PRK11072  236 VLSFAALEDYYQEQGRDWERYAMIKARVMgDPDDAYAQELRAMLRPFVFRRYLDFSAIQALRNMKGMIRREVRRRGLADN 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 312 IKRGAGGIREIEFLCQALQLIRGGREPVLRERRLLVALEALVAAGQIARDDGAALREAYLFLRRLENRLQMLRDAQTHVL 391
Cdd:PRK11072  316 IKLGAGGIREIEFIVQVFQLIRGGREPSLQQRSLLEVLDALAELGLLPEEQVAELRDAYLFLRRLEHLLQAINDQQTQTL 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 392 PSDVLDRERIAVGLGYADWDALRAALTVQQQRVSTEFGALLAPRKGQAAPDALANYWRSL-----PEGSNAPLLAEAGFL 466
Cdd:PRK11072  396 PDDPLDRARLAWAMGFADWAALLDVLDAHRANVRRVFNQLIGDDEEETEEEAASEQWRELwqdalDEEDATPLLAELGFD 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 467 DANGADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLALLDEQPSALARL 546
Cdd:PRK11072  476 DPAQVLARLAAFRHSLRKRTLGPRGRERLDALMPRLLEAACAREDADVTLERLLDLLEAISRRTTYLELLSENPGALKRL 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 547 VDVLARSALLAERLAAYPLLLDELLDVRVSGPMPDAAGMLAECQQVLT---VEDPESALRWLNETRLALSFRMAMATLDG 623
Cdd:PRK11072  556 ISLCAASPWIAEQLARYPLLLDELLDPRALYQPTDWDAYRDELRQYLLrvpEDDEEQQMEALRQFKQAQVLRIAAADIAG 635

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 624 RQGAVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIA-----GGRFAIIGYGSLGGLELGFGSDLDLVFLHDHPAGVEa 698
Cdd:PRK11072  636 VLPVMKVSDHLTYLAEAILDAVVQQAWQQMVKRHGEPPhlegrERGFAVIGYGKLGGKELGYASDLDLVFLHDCPEDAM- 714

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 699 SDGARPLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGVAG 778
Cdd:PRK11072  715 TDGDKSIDGRQFYLRLAQRIIHLFSTRTSSGILYEVDMRLRPSGAAGLLVSSLEAFERYQLNEAWTWEHQALVRARFVAG 794

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 779 DASLLQDFEQVRAQTLGRERDRATLYADVVKMRGRMRTELDRSDAARLDLKQGSGGVVDLEFLLQSGVLARSAQTPALLQ 858
Cdd:PRK11072  795 DPQLGAAFEAIRREVLTQPRDLATLRTEVREMREKMRDHLGNKTRDRFDLKQDRGGIVDIEFIAQYLVLAHAHEHPELTR 874

                         890       900       910
                  ....*....|....*....|....*....|..
gi 1910257199 859 PRATPALIDALAAAGFLPEATAQTLHGAHATL 890
Cdd:PRK11072  875 WSDNVRILELLAELGLMSEEEAEALTDAYRTL 906
PRK14108 PRK14108
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 3-888 3.64e-167

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237612 [Multi-domain]  Cd Length: 986  Bit Score: 513.39  E-value: 3.64e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199   3 LAPAELPAPLQPLVDRALARLAQAVPDPIPAE--LQPMLVQLAVSSDFAMDTLVRQPG-LLAQLSAPGCPPL-------- 71
Cdd:PRK14108   23 LDPEEAKARLADLLADARPEELAALAALLAREpkARDFLSAIAELSPFLRDLLRADPArLLRLLSADPEARLaaliaear 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  72 PAPVLDPLQPSDWPAQLRRWRTAMSTRLIWRDLAGLDDVPQTLAGATALAEDCLRLALDALQQEFAQRHGVIADDNGRPQ 151
Cdd:PRK14108  103 AAAVAAAPSEAEVMAALRRLKREAALLIALADLGGVFPVEQTTAWLTDLAEAAVGAALRFLLRDAHAAGKLNLPDRDAPE 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 152 Q---LVVFGLGKLGGGELNFSSDVDLVYAYVQGGESDGPRaLAAEEYFARLGQRLAKLLDETTVDGFSHRVDLRLRPFGS 228
Cdd:PRK14108  183 KgsgLIVLGMGKLGAGELNYSSDIDLIVFFDETAPILGDP-IEAQPFFVRLTRRLVRILQERTGDGYVFRVDLRLRPDPG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 229 AGRVALSFAAMDQYFQREGRDWERYAWLKARAVAGDIAAGEAWLQTLRPFVYRRYLDFTALDGLREMKAAITA-----EV 303
Cdd:PRK14108  262 STPLAIPVEAALHYYEGRGQNWERAAMIKARPVAGDLAAGEAFLAELSPFVWRKYLDYAAIADVHSIKRQIHAhkghgEI 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 304 ARrEMHDdIKRGAGGIREIEFLCQALQLIRGGREPVLRERRLLVALEALVAAGQIARDDGAALREAYLFLRRLENRLQML 383
Cdd:PRK14108  342 AV-EGHN-VKLGRGGIREIEFFVQTQQLIAGGRFPELRGRQTLEALAELAERGWITAQARDELTEAYWFLRDVEHRIQMV 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 384 RDAQTHVLPSDVLDRERIAVGLGYADWDALRAALTVQQQRVSTEFGALL--APRKGQAAPDALanywrsLPEGSNAPLLA 461
Cdd:PRK14108  420 ADEQTHLLPEDDEALERFARMMGYEDRASFAEDLLAVLKVVEGHYAALFeqEPELSAELGNLV------FTGDPDDPDTL 493

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 462 EA----GFLDANGADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLALLD 537
Cdd:PRK14108  494 ETlsrlGFERPSDIARVIRTWHAGRYRATQSAEARERLTELTPALLKAFAETRRADEALLRFDRFLQGLPAGIQLFSLLQ 573

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 538 EQPSALARLVDVLARSALLAERLAAYPLLLDELLDVRVSGPMPD----AAGMLAECQQVLTVEDPESALR-WLNETRLAL 612
Cdd:PRK14108  574 SNPDLLSLLVLIMGAAPRLADIIARRPHVFDGLLDPAFFSELPTraylSARLAAFLADAGSYEEVLDRLRiFAQEQRFLI 653

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 613 SFRMAMATLDGRQGAvdstRQLAELAQAVVVTVLAMAEADMQAAHGVIAGGRFAIIGYGSLGGLELGFGSDLDLVFLHDH 692
Cdd:PRK14108  654 GIRILTGTISGQRAG----RAFADLAELIIGAALDAVEEEFARAHGRIKGGRVAILAMGKLGSRELTAGSDVDLILLYDF 729

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 693 PAGVEASDGARPLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVR 772
Cdd:PRK14108  730 DDDAPESDGEKPLDGAQYFARFTQRLIAALSAPTAEGVLYEVDMRLRPSGNKGPVATRIDAFAKYQREEAWTWEHMALTR 809

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 773 ARGVAGDASLLQDFEQVRAQTLGRERDRATLYADVVKMRGRMRTELDRSDaaRLDLKQGSGGVVDLEFLLQSGVLARSAQ 852
Cdd:PRK14108  810 ARVISGDPAFIARIEAIIREVLARPRDIAKIAGDVAEMRRLIAQEKPPRD--IWDLKLAPGGIVDLEFIAQYLQLVHAAK 887

                         890       900       910
                  ....*....|....*....|....*....|....*.
gi 1910257199 853 TPALLqPRATPALIDAlAAAGFLPEATAQTLHGAHA 888
Cdd:PRK14108  888 GPDIL-GVSTAEVLDN-LGRLLLDPADADILREAAR 921
PRK14109 PRK14109
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 18-886 1.74e-81

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237613 [Multi-domain]  Cd Length: 1007  Bit Score: 284.43  E-value: 1.74e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199   18 RALARLAQAVPDPI--------PAELQPMLVQLAVSSDFAMDTLVRQPGLLAQLSAPGC-------------------PP 70
Cdd:PRK14109    61 LALVRLAEALEDWAellaalraDPGLRGRLLAVLGASSALGDHLVAHPEDWRALLRDPValpsaeelraalleavgadPG 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199   71 LPAPVLDPLQPSDWPAQLRRWRTAMsTRLIWRDLAGLD---DVPQTLAGATALAEDCLRLALDALQQEFAQ----RHGVI 143
Cdd:PRK14109   141 APTPVAGVTGAEAVDALRVAYRRQL-LRIAARDLAATDpvlPFPTVAAELADLADAALEAALAVARAEVPGsapvRLAVI 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  144 ADDNGRPQQLvvfglgklgggelNFSSDVDLVYAYVQGGESDGPRALAAEeyfARLGQRLAKLLDETTVDGFSHRVDLRL 223
Cdd:PRK14109   220 AMGKCGAREL-------------NYVSDVDVIFVAEPAEGVDEAAALAVA---TRLASELMRICSAPTAEGALWEVDAAL 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  224 RPFGSAGRVALSFAAMDQYFQREGRDWERYAWLKARAVAGDIAAGEAWLQTLRPFVYR--RYLDFtaLDGLREMKAAITA 301
Cdd:PRK14109   284 RPEGKDGPLVRTLDSHVAYYERWAKTWEFQALLKARPVAGDAELGQRYVDAVAPMVWSaaEREGF--VEDVQAMRRRVED 361

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  302 EVARREMHDDIKRGAGGIREIEFLCQALQLIRGGREPVLRERRLLVALEALVAAGQIARDDGAALREAYLFLRRLENRLQ 381
Cdd:PRK14109   362 LIPAAERDRELKLGPGGLRDVEFAVQLLQLVHGRSDESLRVRSTLDALAALAAGGYVGREDAANLAAAYRFLRLLEHRLQ 441

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  382 MLRDAQTHVLPSDVLDRERIAVGLGYADWDALRAA--LTVQQQRVSTEFGAL--------LAPRKGQAAPDALanywrSL 451
Cdd:PRK14109   442 LQRLRRTHLLPDDEDELRWLARAAGLRPDGRRDAAeeLRAEWRRTRRRVRRLheklfyrpLLEAVARLSAEEA-----RL 516

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  452 PEGSNAPLLAEAGFLDANGADQSLRDFAQGTGvkslsdaARARLDRV-LPALLHAATRSPQPDAalkrvlGLLQavLRRT 530
Cdd:PRK14109   517 SPEAARRRLAALGYADPDGALRHIEALTSGVS-------RRAAIQRTlLPVLLGWLADGPDPDA------GLLA--YRRL 581

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  531 S--------YLALLDEQPSALARLVDVLARSALLAERLAAYP---LLLDELLDVRVSGPMPDAAGMLAecqQVLTVEDPE 599
Cdd:PRK14109   582 SealgttpwYLRLLRDEGAVAERLAHVLGTSRYVADLLMRAPesvAWLGDDAKLLPRSREALARELLA---AASRHDDPE 658

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  600 SALRWLNETRLALSFRMAMATLDGRQGAVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIAGGRFAIIGYGSLGGLELG 679
Cdd:PRK14109   659 RAVAAARALRRRELLRIASADLLGLLDVEEVCRALSDVWDAVLEAALRAAIRAVEAEGGDPAPARIAVIGMGRLGGRELG 738

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  680 FGSDLDLVFLHDHPAGVEASDGArplepgRWYARLAQKVMALLAAVTAAGRLyDIDVRLRPDGGKGSLVSSLASYTEYQR 759
Cdd:PRK14109   739 YGSDADVMFVHEPAPGADEAEAV------RWATAVAEELRRLLGGPSPDPPL-EVDADLRPEGRNGPLVRTLASYAAYYA 811

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  760 DRAWTWEHQALVRARGVAGDASLLQDF----EQVR--AQTLGRERDRatlyaDVVKMRGRMRTE-LDRSDAARLDLKQGS 832
Cdd:PRK14109   812 RWSQTWEAQALLRARPVAGDAELGERFlaliDPLRypAGGLSEAAVR-----EIRRIKARVEAErLPRGADPARHTKLGR 886

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1910257199  833 GGVVDLEFLLQSGVLARSAQTPALLQPRATPALiDALAAAGFLPEATAQTLHGA 886
Cdd:PRK14109   887 GGLSDVEWTVQLLQLQHAHEVPALRTTSTLEAL-DAAAAAGLLSEEDAELLREA 939
GlnE pfam03710
Glutamate-ammonia ligase adenylyltransferase; Conserved repeated domain found in GlnE proteins. ...
 543-788 7.65e-56

Glutamate-ammonia ligase adenylyltransferase; Conserved repeated domain found in GlnE proteins. These proteins adenylate and deadenylate glutamine synthases: ATP + {L-Glutamate:ammonia ligase (ADP-forming)} = Diphosphate + Adenylyl-{L-Glutamate:Ammonia ligase (ADP-forming)}. The family is related to the pfam01909 domain.


Pssm-ID: 397667 [Multi-domain]  Cd Length: 249  Bit Score: 193.30  E-value: 7.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 543 LARLVDVLARSALLAERLAAYPLLLDELLDvRVSGPMPDAAGMLAECQQVLTVEDPESALRWLNETRLALSFRMAMATLD 622
Cdd:pfam03710   1 LEQLREVLAASPFVAEQLARYPILLDELLD-PLGNPKDLAAYPAELADALAAVPDEEQAMDALRQFRRAELLRIAAADLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 623 GRQGAVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIAGGR------FAIIGYGSLGGLELGFGSDLDLVFLHDHPAGV 696
Cdd:pfam03710  80 GLLTVEEVSDALSQLAEAVIDAALDWAWRQVCSRGGTPVHLQsgepqgFAVIGMGKLGGFELGYSSDLDLIFLYDPDGET 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 697 EasDGARPLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGV 776
Cdd:pfam03710 160 Q--GARRSIDAAQFYTRLAQRLISALSAPTGDGFLYEVDMRLRPSGDSGPLVLSFAAFEDYYEEQAWTWERQALIRARVV 237

                         250
                  ....*....|..
gi 1910257199 777 AGDASLLQDFEQ 788
Cdd:pfam03710 238 GGDAELGAAFLR 249
GlnE pfam03710
Glutamate-ammonia ligase adenylyltransferase; Conserved repeated domain found in GlnE proteins. ...
 39-273 1.08e-47

Glutamate-ammonia ligase adenylyltransferase; Conserved repeated domain found in GlnE proteins. These proteins adenylate and deadenylate glutamine synthases: ATP + {L-Glutamate:ammonia ligase (ADP-forming)} = Diphosphate + Adenylyl-{L-Glutamate:Ammonia ligase (ADP-forming)}. The family is related to the pfam01909 domain.


Pssm-ID: 397667 [Multi-domain]  Cd Length: 249  Bit Score: 170.19  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  39 LVQLAVSSDFAMDTLVRQPGLLAQL-SAPGCPPLPAPVldPLQPSDWPAQ----------LRRWRTAMSTRLIWRDLAGL 107
Cdd:pfam03710   4 LREVLAASPFVAEQLARYPILLDELlDPLGNPKDLAAY--PAELADALAAvpdeeqamdaLRQFRRAELLRIAAADLLGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 108 DDVPQTLAGATALAEDCLRLALDALQQEFAQRHGV-IADDNGRPQQLVVFGLGKLGGGELNFSSDVDLVYAYV-QGGESD 185
Cdd:pfam03710  82 LTVEEVSDALSQLAEAVIDAALDWAWRQVCSRGGTpVHLQSGEPQGFAVIGMGKLGGFELGYSSDLDLIFLYDpDGETQG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 186 GPRALAAEEYFARLGQRLAKLLDETTVDGFSHRVDLRLRPFGSAGRVALSFAAMDQYFQREGRDWERYAWLKARAVAGDI 265
Cdd:pfam03710 162 ARRSIDAAQFYTRLAQRLISALSAPTGDGFLYEVDMRLRPSGDSGPLVLSFAAFEDYYEEQAWTWERQALIRARVVGGDA 241


                  ....*...
gi 1910257199 266 AAGEAWLQ 273
Cdd:pfam03710 242 ELGAAFLR 249
PRK14109 PRK14109
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 455-874 7.23e-36

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237613 [Multi-domain]  Cd Length: 1007  Bit Score: 146.92  E-value: 7.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  455 SNAPLLAEAGFLDANGADQSLRDFAqgtgvkslsdAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLA 534
Cdd:PRK14109     9 SSLPSLARLGFTDPDRAAALLAELG----------LAGVDDDDAHADLLWALSRAADPDLALLALVRLAEALEDWAELLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  535 LLDEQPSALARLVDVLARSALLAERLAAYPLLLDELLDVRVSGPMPDA--AGMLAECQ---------QVLTVEDPESALR 603
Cdd:PRK14109    79 ALRADPGLRGRLLAVLGASSALGDHLVAHPEDWRALLRDPVALPSAEElrAALLEAVGadpgaptpvAGVTGAEAVDALR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  604 WLNETRLAlsfRMAMATLDGRQGAV---DSTRQLAELAQAVVVTVLAMAeadmQAAHGVIAGGRFAIIGYGSLGGLELGF 680
Cdd:PRK14109   159 VAYRRQLL---RIAARDLAATDPVLpfpTVAAELADLADAALEAALAVA----RAEVPGSAPVRLAVIAMGKCGARELNY 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  681 GSDLDLVFLhdhpagVEASDGARPLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRD 760
Cdd:PRK14109   232 VSDVDVIFV------AEPAEGVDEAAALAVATRLASELMRICSAPTAEGALWEVDAALRPEGKDGPLVRTLDSHVAYYER 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  761 RAWTWEHQALVRARGVAGDASLLQDFEQVRAQTLGRERDRATLYADVVKMRGRMRTELDRSDAARlDLKQGSGGVVDLEF 840
Cdd:PRK14109   306 WAKTWEFQALLKARPVAGDAELGQRYVDAVAPMVWSAAEREGFVEDVQAMRRRVEDLIPAAERDR-ELKLGPGGLRDVEF 384

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1910257199  841 ---LLQSgVLARSAQTpalLQPRATPALIDALAAAGF 874
Cdd:PRK14109   385 avqLLQL-VHGRSDES---LRVRSTLDALAALAAGGY 417
GlnD_UR_UTase pfam08335
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ...
 293-432 1.18e-30

GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes/uridylyltransferases (UR/UTases, GlnD) that are responsible for the modification (EC:2.7.7.59) of the regulatory protein P-II, or GlnB (pfam00543). In response to nitrogen limitation, these transferases catalyze the uridylylation of the PII protein, which in turn stimulates deadenylylation of glutamine synthetase (GlnA). Deadenylylated glutamine synthetase is the more active form of the enzyme. Moreover, uridylylated PII can act together with NtrB and NtrC to increase transcription of genes in the sigma54 regulon, which include glnA and other nitrogen-level controlled genes. It has also been suggested that the product of the glnD gene is involved in other physiological functions such as control of iron metabolism in certain species. The region described in this family is found in many of its members to be C-terminal to a nucleotidyltransferase domain (pfam01909), and N-terminal to an HD domain (pfam01966) and two ACT domains (pfam01842).


Pssm-ID: 462432 [Multi-domain]  Cd Length: 140  Bit Score: 117.68  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 293 REMKAAITAEVARREMHD--------DIKRGAGGIREIEFLCQALQLIRGGRepvlrerrllvALEALVAAGQIARDDGA 364
Cdd:pfam08335   1 RFMKAKIEEQVARHGRYGdtaynlepNIKLGPGGLRDIEFIVWIAQLIFTLR-----------ALEELVELGLLTREEAR 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1910257199 365 ALREAYLFLRRLENRLQMLRDAQTHVLPSDvlDRERIAVGLGY--ADWDA---LRAALTVQQQRVSTEFGALL 432
Cdd:pfam08335  70 ELRRAYRFLRRVRHRLHLLADRQTDRLPFD--LQRRLARALGYarDGWLAverFMRRLFRHAHRVSRLFEILL 140
NT_GlnE_GlnD_like cd05401
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ...
 607-793 2.49e-27

Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143391 [Multi-domain]  Cd Length: 172  Bit Score: 109.35  E-value: 2.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 607 ETRLALSFRMAMATLDGRQGAVDSTRQLAELAQAVVVTVLAMAEADMQAAhgvIAGGRFAIIGYGSLGGLELGFGSDLDL 686
Cdd:cd05401     1 RAKLRQLRRILRRDLLGGASIRAISRALSDLADALLRRALELALAELGKG---PPPVPFALLALGSYGRGELNPSSDQDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 687 VFLHDHPAGVEAsdgarplepgRWYARLAQKVMALLAAvtAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWE 766
Cdd:cd05401    78 LLLYDDDGDEVA----------AYFEELAERLIKILSE--AGGPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEPGRLWE 145

                         170       180
                  ....*....|....*....|....*..
gi 1910257199 767 HQALVRARGVAGDASLLQDFEQVRAQT 793
Cdd:cd05401   146 RTALLDARPVAGDRALAEELRRRIRER 172
PRK14109 PRK14109
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 103-412 4.13e-25

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237613 [Multi-domain]  Cd Length: 1007  Bit Score: 112.63  E-value: 4.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  103 DLAGLDDVPQTLAGATALAEDCLRLALDAlqqefAQRHGVIADDNGRPQQLVVFGLGKLGGGELNFSSDVDLVYAYVQGG 182
Cdd:PRK14109   679 DLLGLLDVEEVCRALSDVWDAVLEAALRA-----AIRAVEAEGGDPAPARIAVIGMGRLGGRELGYGSDADVMFVHEPAP 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  183 ESDGPRAL-AAEEYFARLGQRLAKLLDETTVDgfshrVDLRLRPFGSAGRVALSFAAMDQYFQREGRDWERYAWLKARAV 261
Cdd:PRK14109   754 GADEAEAVrWATAVAEELRRLLGGPSPDPPLE-----VDADLRPEGRNGPLVRTLASYAAYYARWSQTWEAQALLRARPV 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  262 AGDIAAGEAWLQTLRPFvyrRY----LDFTALDGLREMKAAITAEV----ARREMHddIKRGAGGIREIEFLCQALQLIR 333
Cdd:PRK14109   829 AGDAELGERFLALIDPL---RYpaggLSEAAVREIRRIKARVEAERlprgADPARH--TKLGRGGLSDVEWTVQLLQLQH 903

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1910257199  334 GGREPVLRERRLLVALEALVAAGQIARDDGAALREAYLFLRRLENRLQMLRDAQTHVLPSDVLDRERIAVGLGYADWDA 412
Cdd:PRK14109   904 AHEVPALRTTSTLEALDAAAAAGLLSEEDAELLREAWLLATRARNALVLVRGRPTDQLPGDGRDLAAVARALGYPPGDG 982
PRK11072 PRK11072
bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/ ...
 118-403 1.06e-22

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase;


Pssm-ID: 236836 [Multi-domain]  Cd Length: 943  Bit Score: 104.53  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 118 TALAEDCLRLALDALQQEFAQRHGVIADDNGRPQQLVVFGLGKLGGGELNFSSDVDLVYAY--VQGGESDGPRALAAEEY 195
Cdd:PRK11072  647 TYLAEAILDAVVQQAWQQMVKRHGEPPHLEGRERGFAVIGYGKLGGKELGYASDLDLVFLHdcPEDAMTDGDKSIDGRQF 726

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 196 FARLGQRLAKLLDETTVDGFSHRVDLRLRPFGSAGRVALSFAAMDQYFQREGRDWERYAWLKARAVAGDIAAGEAWlQTL 275
Cdd:PRK11072  727 YLRLAQRIIHLFSTRTSSGILYEVDMRLRPSGAAGLLVSSLEAFERYQLNEAWTWEHQALVRARFVAGDPQLGAAF-EAI 805

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 276 RPFVYRRYLDFTAL-DGLREMkaaitaevaRREMHD----------DIKRGAGGIREIEFLCQALQLIRGGREPVLRERR 344
Cdd:PRK11072  806 RREVLTQPRDLATLrTEVREM---------REKMRDhlgnktrdrfDLKQDRGGIVDIEFIAQYLVLAHAHEHPELTRWS 876

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 345 LLVA-LEALVAAGQIARDDGAALREAYLFLRRLENRLQMlrDAQTHVLPSDVLDRERIAV 403
Cdd:PRK11072  877 DNVRiLELLAELGLMSEEEAEALTDAYRTLRDEQHRLAL--QEQPGRVPADEFAAERAAV 934
NT_GlnE_GlnD_like cd05401
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ...
 98-278 1.63e-20

Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143391 [Multi-domain]  Cd Length: 172  Bit Score: 89.71  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  98 RLIWRDLAGLDDVPQTLAGATALAEDCLRLALDALQQEFAqrhgviadDNGRPQQLVVFGLGKLGGGELNFSSDVDLVYA 177
Cdd:cd05401     9 RILRRDLLGGASIRAISRALSDLADALLRRALELALAELG--------KGPPPVPFALLALGSYGRGELNPSSDQDLLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 178 YVQGGEsdgpralAAEEYFARLGQRLAKLLDEttVDGFSHRVDLRLRPFGSAGRVALSFAAMDQYFQREGRDWERYAWLK 257
Cdd:cd05401    81 YDDDGD-------EVAAYFEELAERLIKILSE--AGGPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEPGRLWERTALLD 151

                         170       180
                  ....*....|....*....|.
gi 1910257199 258 ARAVAGDIAAGEAWLQTLRPF 278
Cdd:cd05401   152 ARPVAGDRALAEELRRRIRER 172
PRK14108 PRK14108
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 496-893 2.19e-20

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237612 [Multi-domain]  Cd Length: 986  Bit Score: 97.38  E-value: 2.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 496 DRVLPALLHAATRSPQP--DAALKRVLGLLQAVLR---RTSYLALLDEQPSALARLVDVLARSALLAERLAAYPLLLDEL 570
Cdd:PRK14108    6 EADKASLAARFLAALRPldPEEAKARLADLLADARpeeLAALAALLAREPKARDFLSAIAELSPFLRDLLRADPARLLRL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 571 LDVRvsgPMPDAAGMLAECQQVLTVEDPE--SALRWLNETRLALSFRMAMATLDGRQGAVDSTRQLAELAQAVV---VTV 645
Cdd:PRK14108   86 LSAD---PEARLAALIAEARAAAVAAAPSeaEVMAALRRLKREAALLIALADLGGVFPVEQTTAWLTDLAEAAVgaaLRF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 646 LAMAEAdmqaAHGVIA---------GGRFAIIGYGSLGGLELGFGSDLDLVFLHDHPAGVEASdgarPLEPGRWYARLAQ 716
Cdd:PRK14108  163 LLRDAH----AAGKLNlpdrdapekGSGLIVLGMGKLGAGELNYSSDIDLIVFFDETAPILGD----PIEAQPFFVRLTR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 717 KVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGVAGDASLLQDFEQVRAQTLGR 796
Cdd:PRK14108  235 RLVRILQERTGDGYVFRVDLRLRPDPGSTPLAIPVEAALHYYEGRGQNWERAAMIKARPVAGDLAAGEAFLAELSPFVWR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 797 ER-DRATLyADVVKMRGRMRTELDRSDAARL--DLKQGSGGVVDLEFLLQSGVLARSAQTPALlQPRATPALIDALAAAG 873
Cdd:PRK14108  315 KYlDYAAI-ADVHSIKRQIHAHKGHGEIAVEghNVKLGRGGIREIEFFVQTQQLIAGGRFPEL-RGRQTLEALAELAERG 392

                         410       420
                  ....*....|....*....|
gi 1910257199 874 FLPEATAQTLHGAHATLLEV 893
Cdd:PRK14108  393 WITAQARDELTEAYWFLRDV 412
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 370-894 4.76e-09

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 60.66  E-value: 4.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  370 YLFLRRLEnrlqmLRDAQTHVLPSDVLDRERIAVGLGYADWDALRAALTVQQQRVSTEFGALLAPRKGQAAPDALANYWR 449
Cdd:COG3321    866 YPFQREDA-----AAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  450 SLPEGSNAPLLAEAGFLDANGADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRR 529
Cdd:COG3321    941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  530 TSYLALLDEQPSALARLVDVLARSALLAERLAAYPLLLDELLDVRVSGPMPDAAGMLAECQQVLTVEDPESALRWLNETR 609
Cdd:COG3321   1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  610 LALSFRMAMATLDGRQGAVDSTRQLAELAQAVVVTVLAMAEADMQAAHGVIAGGRFAIIGYGSLGGLELGFGSDLDLVFL 689
Cdd:COG3321   1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALA 1180

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  690 HDHPAGVEASDGARPLEPGRWYARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQA 769
Cdd:COG3321   1181 LAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALA 1260

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  770 LVRARGVAGDASLLQDFEQVRAQTLGRERDRATLYADVVKMRGRMRTELDRSDAARLDLKQGSGGVVDLEFLLQSGVLAR 849
Cdd:COG3321   1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1910257199  850 SAQTPALLQPRATPALIDALAAAGFLPEATAQTLHGAHATLLEVG 894
Cdd:COG3321   1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 391-911 2.25e-08

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 58.35  E-value: 2.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  391 LPSDVLDRERIAVGLgyadwdALRAALTVQQQRVSTEFGALLAPRKGQAAPDALANYWRSLPEGSNAPLLAEAGFLDANG 470
Cdd:COG3321    863 LPTYPFQREDAAAAL------LAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALA 936

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  471 ADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLALLDEQPSALARLVDVL 550
Cdd:COG3321    937 AAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAA 1016

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  551 ARSALLAERLAAYPLLLDELLDVRVSGPMPDAAGMLAECQQVLTVEDPESALRWLNETRLALSFRMAMATLDGRQGAVDS 630
Cdd:COG3321   1017 AAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALA 1096

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  631 TRQLAELAQAVVVTVLAMAEADMQAAHGVIAGGRFAIIGYGSLGGLELGFGSDLDLVFLHDHPAGVEASDGARPLEPGRW 710
Cdd:COG3321   1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLA 1176

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  711 YARLAQKVMALLAAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRDRAWTWEHQALVRARGVAGDASLLQDFEQVR 790
Cdd:COG3321   1177 LALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199  791 AQTLGRERDRATLYADVVKMRGRMRTELDRSDAARLDLKQGSGGVVDLEFLLQSGVLARSAQTPALLQPRATPALIDALA 870
Cdd:COG3321   1257 AALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAA 1336

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1910257199  871 AAGFLPEATAQTLHGAHATLLEVGLACTLDRRPRLAPTTPA 911
Cdd:COG3321   1337 VAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALA 1377
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 651-893 2.46e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 41.52  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 651 ADMQAAHGVIAGGRFAIIGYGSLGGLELGFGSDLDLVFLHDhpaGVEAsDGARPLEPGRWY------ARLAQKVMALLAA 724
Cdd:PRK03381   44 AGLAAEAGIADGSGVALVAVGGLGRRELLPYSDLDLVLLHD---GRPA-DDVAEVADRLWYplwdagIRLDHSVRTVPEA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 725 VTAAGRlyDIDVRLrpdggkgslvsslasyteyqrdrawtwehqALVRARGVAGDASLLQDF-EQVRAQTLGRERDRATL 803
Cdd:PRK03381  120 LKVAGS--DLKAAL------------------------------GLLDARHIAGDADLSALLiGGVRRQWRNGARRRLPE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910257199 804 YADVVKMRGRMRTELdrsdAARL--DLKQGSGGVVDLefllqsgvlarsaqtpallqpratpALIDALAAAGfLPEATAQ 881
Cdd:PRK03381  168 LVELTRARWERSGEI----AHLAepDLKEGRGGLRDV-------------------------QLLRALAAAQ-LADAPGG 217

                         250
                  ....*....|..
gi 1910257199 882 TLHGAHATLLEV 893
Cdd:PRK03381  218 GLDAAHRRLLDV 229
 
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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