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Conserved domains on  [gi|1848567235|gb|QKH11699|]
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type I glutamate--ammonia ligase [Bacillus cereus]

Protein Classification

glutamine synthetase family protein( domain architecture ID 11415048)

glutamine synthetase family protein such as glutamine synthetase that catalyzes the condensation of glutamate and ammonia to form glutamine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GlnA COG0174
Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of ...
1-442 0e+00

Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of the Pathway/BioSystem: Glutamine biosynthesis


:

Pssm-ID: 439944 [Multi-domain]  Cd Length: 440  Bit Score: 737.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235   1 MSRYTKEDIFRLAKEENVKYIRLQFTDLLGVIKNVEIPVRQLTKALDNKMMFDGSSIEGFVRIEESDMYLYPDLDTWVIF 80
Cdd:COG0174     1 MSKLTVEEVLAFLKERGVKFVDLQFTDINGVLRGKRVPASELEKALEEGIGFDGSSIEGFVEIGESDMVLVPDPSTLRIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  81 PWTAEKgkVARLICDIYNADGTPFDGDPRNNLKRVLKEMEALGFSdFNLGPEPEFFLFKVDE--KGNPTLELNDNGGYFD 158
Cdd:COG0174    81 PWRPEP--TARVICDVYDPDGEPYEGDPRNVLKRVLARLAETGLT-PYVGPELEFFLFDDDSdeKGNRGLRPRDKGGYYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 159 LAPMDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIARKHGLHATFMPKPLYG 238
Cdd:COG0174   158 LAPLDRFEDFRREIVLALEAMGIPVETSHHEVAPGQHEINLRYADALTAADRVVLFKYVVKEVARRHGLTATFMPKPFAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 239 VNGSGMHCNLSLFK-NGENVFFDANGDLQLSDDARHFIAGILKHAPAFTAIANPTVNSYKRLVPGYEAPCYVAWSAQNRS 317
Cdd:COG0174   238 DNGSGMHVHQSLWDaDGKNLFADPDGYAGLSELARHFIGGLLKHAPALTAFTAPTVNSYKRLVPGYEAPVNIAWGYDNRS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 318 PLVRIPASRGISTRVEVRSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNIYVMTKEEReeAGIVDLPATLAQALV 397
Cdd:COG0174   318 AAIRIPGGSPKATRIEYRVPDADANPYLAFAALLAAGLDGIENKLEPGEPVDGNAYELSPEER--AGIPRLPRSLEEALD 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1848567235 398 TLQSNEVVCGALGEHLLEHFIEAKEIEWDIFRTQVHQWERDQYMS 442
Cdd:COG0174   396 ALEADEFLREVLGEDFVDHYIALKRAEWEEFRRRVTPWERERYLE 440
 
Name Accession Description Interval E-value
GlnA COG0174
Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of ...
1-442 0e+00

Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439944 [Multi-domain]  Cd Length: 440  Bit Score: 737.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235   1 MSRYTKEDIFRLAKEENVKYIRLQFTDLLGVIKNVEIPVRQLTKALDNKMMFDGSSIEGFVRIEESDMYLYPDLDTWVIF 80
Cdd:COG0174     1 MSKLTVEEVLAFLKERGVKFVDLQFTDINGVLRGKRVPASELEKALEEGIGFDGSSIEGFVEIGESDMVLVPDPSTLRIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  81 PWTAEKgkVARLICDIYNADGTPFDGDPRNNLKRVLKEMEALGFSdFNLGPEPEFFLFKVDE--KGNPTLELNDNGGYFD 158
Cdd:COG0174    81 PWRPEP--TARVICDVYDPDGEPYEGDPRNVLKRVLARLAETGLT-PYVGPELEFFLFDDDSdeKGNRGLRPRDKGGYYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 159 LAPMDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIARKHGLHATFMPKPLYG 238
Cdd:COG0174   158 LAPLDRFEDFRREIVLALEAMGIPVETSHHEVAPGQHEINLRYADALTAADRVVLFKYVVKEVARRHGLTATFMPKPFAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 239 VNGSGMHCNLSLFK-NGENVFFDANGDLQLSDDARHFIAGILKHAPAFTAIANPTVNSYKRLVPGYEAPCYVAWSAQNRS 317
Cdd:COG0174   238 DNGSGMHVHQSLWDaDGKNLFADPDGYAGLSELARHFIGGLLKHAPALTAFTAPTVNSYKRLVPGYEAPVNIAWGYDNRS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 318 PLVRIPASRGISTRVEVRSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNIYVMTKEEReeAGIVDLPATLAQALV 397
Cdd:COG0174   318 AAIRIPGGSPKATRIEYRVPDADANPYLAFAALLAAGLDGIENKLEPGEPVDGNAYELSPEER--AGIPRLPRSLEEALD 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1848567235 398 TLQSNEVVCGALGEHLLEHFIEAKEIEWDIFRTQVHQWERDQYMS 442
Cdd:COG0174   396 ALEADEFLREVLGEDFVDHYIALKRAEWEEFRRRVTPWERERYLE 440
GlnA TIGR00653
glutamine synthetase, type I; Alternate name: glutamate--ammonia ligase. This model represents ...
7-442 0e+00

glutamine synthetase, type I; Alternate name: glutamate--ammonia ligase. This model represents the dodecameric form, which can be subdivided into 1-alpha and 1-beta forms. The phylogeny of the 1-alpha and 1-beta forms appears polyphyletic. E. coli, Synechocystis PCC6803, Aquifex aeolicus, and the crenarcheon Sulfolobus acidocaldarius have form 1-beta, while Bacillus subtilis, Thermotoga maritima, and various euryarchaea has form 1-alpha. The 1-beta dodecamer from the crenarcheon Sulfolobus acidocaldarius differs from that in E. coli in that it is not regulated by adenylylation. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273198 [Multi-domain]  Cd Length: 459  Bit Score: 665.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235   7 EDIFRLAKEENVKYIRLQFTDLLGVIKNVEIPVRQLTK-ALDNKMMFDGSSIEGFVRIEESDMYLYPDLDTWVIFPWTAE 85
Cdd:TIGR00653   1 EEVFKLIKEENVKFVDLRFTDIKGKPQHVEIPASALDKeAFEEGIMFDGSSIRGFQGIEESDMLLKPDPSTAVIDPWRAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  86 KgkVARLICDIYNA-DGTPFDGDPRNNLKRVLKEMEALGFSDFNLGPEPEFFLFKVDEKG-------------------- 144
Cdd:TIGR00653  81 K--TLRVICDVYEPfTGEPYERDPRSIAKRAEEYLKSGIGDTAYFGPEPEFFLFDSVEFGslangsfyevdseegrwnee 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 145 --NPTLELNDNGGYFDLAPMDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIA 222
Cdd:TIGR00653 159 sgNRGYKPRDKGGYFPVAPTDTAVDIRREMVLYLEQLGFDVEVHHHEVATGQHEIDFKFDTLLKTADDIQTYKYVVKNVA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 223 RKHGLHATFMPKPLYGVNGSGMHCNLSLFKNGENVFFDaNGDLQLSDDARHFIAGILKHAPAFTAIANPTVNSYKRLVPG 302
Cdd:TIGR00653 239 RKHGKTATFMPKPLFGDNGSGMHCHQSLWKDGENLFAG-EEYAGLSETALYYIGGILKHAKALAAFTNPTVNSYKRLVPG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 303 YEAPCYVAWSAQNRSPLVRIPASR-GISTRVEVRSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNIYVMTKEERE 381
Cdd:TIGR00653 318 YEAPVYLAYSARNRSALIRIPASGnPKAKRIEFRFPDPSANPYLAFAAMLMAGLDGIKNKIDPGEPVDKNLYELSPEELR 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1848567235 382 EAGIVDLPATLAQALVTLQS-NEVVCGALGEHLLEHFIEAKEIEWDIFRTQVHQWERDQYMS 442
Cdd:TIGR00653 398 EKGIPQLPGSLEEALDELESdHLVEGGVFGEEFIEAFIELKRKEWDPYRLRPHPWEFELYYD 459
Gln-synt_C pfam00120
Glutamine synthetase, catalytic domain;
106-440 0e+00

Glutamine synthetase, catalytic domain;


Pssm-ID: 425473 [Multi-domain]  Cd Length: 343  Bit Score: 560.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 106 GDPRNNLKRVLKEMEALGFsDFNLGPEPEFFLFKVDEKGNP-----------TLELNDNGGYFDLAPMDLGENCRRDIVL 174
Cdd:pfam00120   1 RDPRSILKRALARLASLGL-TAYVGPELEFFLFDRVEDGNPngpfyppdsegGYRPADKGGYFDVAPVDSAQDLRREIVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 175 ELEEMGFEIEASHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIARKHGLHATFMPKPLYGVNGSGMHCNLSLFKNG 254
Cdd:pfam00120  80 ALEAMGIEVEASHHEVAPGQHEIDFRFDDALKAADNAQTFKYVVKNVARKHGLTATFMPKPFFGDNGSGMHVHQSLWKDG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 255 ENVFFDANGDLQLSDDARHFIAGILKHAPAFTAIANPTVNSYKRLVPGYEAPCYVAWSAQNRSPLVRIPASRGISTRVEV 334
Cdd:pfam00120 160 KNLFADPDGEYGLSETARHFIAGILKHAPALTALTNPTVNSYKRLVPGYEAPVYLAWGARNRSAALRIPAGSPKARRVEV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 335 RSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNIYVMTKEEReeAGIVDLPATLAQALVTLQSNEVVCGALGEHLL 414
Cdd:pfam00120 240 RSPDPDANPYLAFAALLAAGLDGIENKIDPGEPVDGNLYELTPEER--KGIPTLPSSLEEALDALEEDELLKEALGEHFI 317
                         330       340
                  ....*....|....*....|....*.
gi 1848567235 415 EHFIEAKEIEWDIFRTQVHQWERDQY 440
Cdd:pfam00120 318 EAYIAVKRAEWEEFRTAVHPWEFERY 343
glnA PRK09469
glutamate--ammonia ligase;
7-443 9.05e-118

glutamate--ammonia ligase;


Pssm-ID: 181884 [Multi-domain]  Cd Length: 469  Bit Score: 352.53  E-value: 9.05e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235   7 EDIFRLAKEENVKYIRLQFTDLLGVIKNVEIPVRQLTKAL--DNKMmFDGSSIEGFVRIEESDMYLYPDLDTWVIFPWTA 84
Cdd:PRK09469    4 EHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNADFfeEGKM-FDGSSIGGWKGINESDMVLMPDASTAVLDPFFE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  85 EKGKVARliCDIYN-ADGTPFDGDPRNNLKRVLKEMEALGFSDFNL-GPEPEFFLF--------------KVD------- 141
Cdd:PRK09469   83 DSTLIIR--CDILEpGTMQGYDRDPRSIAKRAEDYLRSTGIADTVLfGPEPEFFLFddirfgssisgshvAIDdieaawn 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 142 -----EKGNPTLELNDNGGYFDLAPMDLGENCRRDIVLELEEMGFEIEASHHEVA-PGQHEIDFKYANAIRSCDDIQTFK 215
Cdd:PRK09469  161 sgtkyEGGNKGHRPGVKGGYFPVPPVDSSQDIRSAMCLVMEEMGLVVEAHHHEVAtAGQNEVATRFNTMTKKADEIQIYK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 216 LVVKTIARKHGLHATFMPKPLYGVNGSGMHCNLSLFKNGENVFfdaNGDLQ--LSDDARHFIAGILKHAPAFTAIANPTV 293
Cdd:PRK09469  241 YVVHNVAHAFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLF---AGDKYagLSEQALYYIGGIIKHAKAINALANPTT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 294 NSYKRLVPGYEAPCYVAWSAQNRSPLVRIP-ASRGISTRVEVRSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNI 372
Cdd:PRK09469  318 NSYKRLVPGYEAPVMLAYSARNRSASIRIPvVASPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNL 397
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848567235 373 YVMTKEEREEagIVDLPATLAQALVTLQSNE---VVCGALGEHLLEHFIEAKEIEWDIFRTQVHQWERDQYMSL 443
Cdd:PRK09469  398 YDLPPEEAAE--IPQVAGSLEEALNALDADReflTAGGVFTDDAIDAYIALRREEVDRVRMTPHPVEFELYYSV 469
 
Name Accession Description Interval E-value
GlnA COG0174
Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of ...
1-442 0e+00

Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439944 [Multi-domain]  Cd Length: 440  Bit Score: 737.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235   1 MSRYTKEDIFRLAKEENVKYIRLQFTDLLGVIKNVEIPVRQLTKALDNKMMFDGSSIEGFVRIEESDMYLYPDLDTWVIF 80
Cdd:COG0174     1 MSKLTVEEVLAFLKERGVKFVDLQFTDINGVLRGKRVPASELEKALEEGIGFDGSSIEGFVEIGESDMVLVPDPSTLRIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  81 PWTAEKgkVARLICDIYNADGTPFDGDPRNNLKRVLKEMEALGFSdFNLGPEPEFFLFKVDE--KGNPTLELNDNGGYFD 158
Cdd:COG0174    81 PWRPEP--TARVICDVYDPDGEPYEGDPRNVLKRVLARLAETGLT-PYVGPELEFFLFDDDSdeKGNRGLRPRDKGGYYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 159 LAPMDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIARKHGLHATFMPKPLYG 238
Cdd:COG0174   158 LAPLDRFEDFRREIVLALEAMGIPVETSHHEVAPGQHEINLRYADALTAADRVVLFKYVVKEVARRHGLTATFMPKPFAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 239 VNGSGMHCNLSLFK-NGENVFFDANGDLQLSDDARHFIAGILKHAPAFTAIANPTVNSYKRLVPGYEAPCYVAWSAQNRS 317
Cdd:COG0174   238 DNGSGMHVHQSLWDaDGKNLFADPDGYAGLSELARHFIGGLLKHAPALTAFTAPTVNSYKRLVPGYEAPVNIAWGYDNRS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 318 PLVRIPASRGISTRVEVRSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNIYVMTKEEReeAGIVDLPATLAQALV 397
Cdd:COG0174   318 AAIRIPGGSPKATRIEYRVPDADANPYLAFAALLAAGLDGIENKLEPGEPVDGNAYELSPEER--AGIPRLPRSLEEALD 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1848567235 398 TLQSNEVVCGALGEHLLEHFIEAKEIEWDIFRTQVHQWERDQYMS 442
Cdd:COG0174   396 ALEADEFLREVLGEDFVDHYIALKRAEWEEFRRRVTPWERERYLE 440
GlnA TIGR00653
glutamine synthetase, type I; Alternate name: glutamate--ammonia ligase. This model represents ...
7-442 0e+00

glutamine synthetase, type I; Alternate name: glutamate--ammonia ligase. This model represents the dodecameric form, which can be subdivided into 1-alpha and 1-beta forms. The phylogeny of the 1-alpha and 1-beta forms appears polyphyletic. E. coli, Synechocystis PCC6803, Aquifex aeolicus, and the crenarcheon Sulfolobus acidocaldarius have form 1-beta, while Bacillus subtilis, Thermotoga maritima, and various euryarchaea has form 1-alpha. The 1-beta dodecamer from the crenarcheon Sulfolobus acidocaldarius differs from that in E. coli in that it is not regulated by adenylylation. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273198 [Multi-domain]  Cd Length: 459  Bit Score: 665.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235   7 EDIFRLAKEENVKYIRLQFTDLLGVIKNVEIPVRQLTK-ALDNKMMFDGSSIEGFVRIEESDMYLYPDLDTWVIFPWTAE 85
Cdd:TIGR00653   1 EEVFKLIKEENVKFVDLRFTDIKGKPQHVEIPASALDKeAFEEGIMFDGSSIRGFQGIEESDMLLKPDPSTAVIDPWRAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  86 KgkVARLICDIYNA-DGTPFDGDPRNNLKRVLKEMEALGFSDFNLGPEPEFFLFKVDEKG-------------------- 144
Cdd:TIGR00653  81 K--TLRVICDVYEPfTGEPYERDPRSIAKRAEEYLKSGIGDTAYFGPEPEFFLFDSVEFGslangsfyevdseegrwnee 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 145 --NPTLELNDNGGYFDLAPMDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIA 222
Cdd:TIGR00653 159 sgNRGYKPRDKGGYFPVAPTDTAVDIRREMVLYLEQLGFDVEVHHHEVATGQHEIDFKFDTLLKTADDIQTYKYVVKNVA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 223 RKHGLHATFMPKPLYGVNGSGMHCNLSLFKNGENVFFDaNGDLQLSDDARHFIAGILKHAPAFTAIANPTVNSYKRLVPG 302
Cdd:TIGR00653 239 RKHGKTATFMPKPLFGDNGSGMHCHQSLWKDGENLFAG-EEYAGLSETALYYIGGILKHAKALAAFTNPTVNSYKRLVPG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 303 YEAPCYVAWSAQNRSPLVRIPASR-GISTRVEVRSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNIYVMTKEERE 381
Cdd:TIGR00653 318 YEAPVYLAYSARNRSALIRIPASGnPKAKRIEFRFPDPSANPYLAFAAMLMAGLDGIKNKIDPGEPVDKNLYELSPEELR 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1848567235 382 EAGIVDLPATLAQALVTLQS-NEVVCGALGEHLLEHFIEAKEIEWDIFRTQVHQWERDQYMS 442
Cdd:TIGR00653 398 EKGIPQLPGSLEEALDELESdHLVEGGVFGEEFIEAFIELKRKEWDPYRLRPHPWEFELYYD 459
Gln-synt_C pfam00120
Glutamine synthetase, catalytic domain;
106-440 0e+00

Glutamine synthetase, catalytic domain;


Pssm-ID: 425473 [Multi-domain]  Cd Length: 343  Bit Score: 560.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 106 GDPRNNLKRVLKEMEALGFsDFNLGPEPEFFLFKVDEKGNP-----------TLELNDNGGYFDLAPMDLGENCRRDIVL 174
Cdd:pfam00120   1 RDPRSILKRALARLASLGL-TAYVGPELEFFLFDRVEDGNPngpfyppdsegGYRPADKGGYFDVAPVDSAQDLRREIVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 175 ELEEMGFEIEASHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIARKHGLHATFMPKPLYGVNGSGMHCNLSLFKNG 254
Cdd:pfam00120  80 ALEAMGIEVEASHHEVAPGQHEIDFRFDDALKAADNAQTFKYVVKNVARKHGLTATFMPKPFFGDNGSGMHVHQSLWKDG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 255 ENVFFDANGDLQLSDDARHFIAGILKHAPAFTAIANPTVNSYKRLVPGYEAPCYVAWSAQNRSPLVRIPASRGISTRVEV 334
Cdd:pfam00120 160 KNLFADPDGEYGLSETARHFIAGILKHAPALTALTNPTVNSYKRLVPGYEAPVYLAWGARNRSAALRIPAGSPKARRVEV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 335 RSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNIYVMTKEEReeAGIVDLPATLAQALVTLQSNEVVCGALGEHLL 414
Cdd:pfam00120 240 RSPDPDANPYLAFAALLAAGLDGIENKIDPGEPVDGNLYELTPEER--KGIPTLPSSLEEALDALEEDELLKEALGEHFI 317
                         330       340
                  ....*....|....*....|....*.
gi 1848567235 415 EHFIEAKEIEWDIFRTQVHQWERDQY 440
Cdd:pfam00120 318 EAYIAVKRAEWEEFRTAVHPWEFERY 343
gln_synth_III TIGR03105
glutamine synthetase, type III; This family consists of the type III isozyme of glutamine ...
12-441 2.68e-121

glutamine synthetase, type III; This family consists of the type III isozyme of glutamine synthetase, originally described in Rhizobium meliloti, where types I and II also occur.


Pssm-ID: 274431 [Multi-domain]  Cd Length: 435  Bit Score: 360.14  E-value: 2.68e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  12 LAKEENVKYIRLQFTDLLGVIKNVEIPVRQLTKALDNKMMFDGSSIEGF-VRIEESDMYLYPDLDTWVIFPWtaeKGKVA 90
Cdd:TIGR03105   4 LARDKGIKYFLASFVDLHGVQKAKLVPAEAIDHMATGGAGFAGFAAWGLgQSPADPDLMAIPDLDSLTQLPW---QPGVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  91 RLICDIYnADGTPFDGDPRNNLKRVLKEMEALGFSdFNLGPEPEFFLFKVDEKGNptLELNDNGGYFDLAPMDLGENCRR 170
Cdd:TIGR03105  81 WVAADLH-VNGKPYPQAPRVVLKRQLAEAAELGLT-LNTGVECEFFLLRRDEDGS--LSIADRADTLAKPCYDQRGLMRR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 171 DIVLE-----LEEMGFEIEASHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIARKHGLHATFMPKPLYGVNGSGMH 245
Cdd:TIGR03105 157 YDVLTeisdaMNALGWDPYQNDHEDANGQFEMNFTYADALTTADRHAFFRYMVKEIAEKHGMRATFMPKPFADLTGNGCH 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 246 CNLSLF-KNGENVFFDAN--GDLQLSDDARHFIAGILKHAPAFTAIANPTVNSYKRLVPGYE------APCYVAWSAQNR 316
Cdd:TIGR03105 237 FHLSLWdEDGRNLFADDSdpNGLGLSKLAYHFIGGILHHAPALCAVLAPTVNSYKRLNAPRTtsgatwAPNFISYGGNNR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 317 SPLVRIPAsrgiSTRVEVRSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNIYvmtKEEREEAGIVDLPATLAQAL 396
Cdd:TIGR03105 317 THMVRIPD----PGRFELRLADGAANPYLAQAAILAAGLDGIERKLDPGPPRDINLY---AEELAARGVETLPQNLLEAL 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1848567235 397 VTLQSNEVVCGALGEHLLEHFIEAKEIEWDIFRTQVHQWERDQYM 441
Cdd:TIGR03105 390 RALEADPLLAEALGAEFVDEFLKLKRQEWEEYHRHVSDWEIDRYL 434
glnA PRK09469
glutamate--ammonia ligase;
7-443 9.05e-118

glutamate--ammonia ligase;


Pssm-ID: 181884 [Multi-domain]  Cd Length: 469  Bit Score: 352.53  E-value: 9.05e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235   7 EDIFRLAKEENVKYIRLQFTDLLGVIKNVEIPVRQLTKAL--DNKMmFDGSSIEGFVRIEESDMYLYPDLDTWVIFPWTA 84
Cdd:PRK09469    4 EHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNADFfeEGKM-FDGSSIGGWKGINESDMVLMPDASTAVLDPFFE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  85 EKGKVARliCDIYN-ADGTPFDGDPRNNLKRVLKEMEALGFSDFNL-GPEPEFFLF--------------KVD------- 141
Cdd:PRK09469   83 DSTLIIR--CDILEpGTMQGYDRDPRSIAKRAEDYLRSTGIADTVLfGPEPEFFLFddirfgssisgshvAIDdieaawn 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 142 -----EKGNPTLELNDNGGYFDLAPMDLGENCRRDIVLELEEMGFEIEASHHEVA-PGQHEIDFKYANAIRSCDDIQTFK 215
Cdd:PRK09469  161 sgtkyEGGNKGHRPGVKGGYFPVPPVDSSQDIRSAMCLVMEEMGLVVEAHHHEVAtAGQNEVATRFNTMTKKADEIQIYK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 216 LVVKTIARKHGLHATFMPKPLYGVNGSGMHCNLSLFKNGENVFfdaNGDLQ--LSDDARHFIAGILKHAPAFTAIANPTV 293
Cdd:PRK09469  241 YVVHNVAHAFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLF---AGDKYagLSEQALYYIGGIIKHAKAINALANPTT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 294 NSYKRLVPGYEAPCYVAWSAQNRSPLVRIP-ASRGISTRVEVRSVDPAANPYLVMATLLAAGLDGIKNKLTPPAAVDRNI 372
Cdd:PRK09469  318 NSYKRLVPGYEAPVMLAYSARNRSASIRIPvVASPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNL 397
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848567235 373 YVMTKEEREEagIVDLPATLAQALVTLQSNE---VVCGALGEHLLEHFIEAKEIEWDIFRTQVHQWERDQYMSL 443
Cdd:PRK09469  398 YDLPPEEAAE--IPQVAGSLEEALNALDADReflTAGGVFTDDAIDAYIALRREEVDRVRMTPHPVEFELYYSV 469
Gln-synt_N pfam03951
Glutamine synthetase, beta-Grasp domain;
17-98 5.55e-40

Glutamine synthetase, beta-Grasp domain;


Pssm-ID: 427610 [Multi-domain]  Cd Length: 82  Bit Score: 138.03  E-value: 5.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  17 NVKYIRLQFTDLLGVIKNVEIPVRQLT-KALDNKMMFDGSSIEGFVRIEESDMYLYPDLDTWVIFPWTAEkgKVARLICD 95
Cdd:pfam03951   1 NVKFVDLRFTDILGKLKHVTIPASELDeDAFEEGIGFDGSSIEGFARIEESDMLLKPDPSTAFIDPFRPE--PTARVICD 78

                  ...
gi 1848567235  96 IYN 98
Cdd:pfam03951  79 VYD 81
GlnA3 COG3968
Glutamine synthetase type III [Amino acid transport and metabolism];
116-250 9.17e-12

Glutamine synthetase type III [Amino acid transport and metabolism];


Pssm-ID: 443168 [Multi-domain]  Cd Length: 727  Bit Score: 67.08  E-value: 9.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 116 LKEMEALG---------FSDFN-------LGPEPEFFLfkVDEkgnptlelndnggyfDLApmdlgeNCRRDIVL----- 174
Cdd:COG3968   188 LRSMEALDkaatrvlklFGDKDvkkvtstLGPEQEYFL--VDK---------------ALY------NARPDLVLtgrtl 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 175 ---------ELEE-------------M-GFEIEA---------SHHEVAPGQHEIDFKYANAIRSCDDIQTFKLVVKTIA 222
Cdd:COG3968   245 fgapppkgqQLEDhyfgsipervlafMkDLERELwklgipaktRHNEVAPGQFELAPIFEEANLAVDHNQLLMEVMKKVA 324
                         170       180
                  ....*....|....*....|....*...
gi 1848567235 223 RKHGLHATFMPKPLYGVNGSGMHCNLSL 250
Cdd:COG3968   325 RRHGLVCLLHEKPFAGVNGSGKHNNWSL 352
PLN02284 PLN02284
glutamine synthetase
52-249 6.67e-09

glutamine synthetase


Pssm-ID: 177922 [Multi-domain]  Cd Length: 354  Bit Score: 57.39  E-value: 6.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  52 FDGSSIeGFVRIEESDMYLYPDldtwVIFPWTAEKGKVARLICDIYNADGTPFDGDPRNNLKRVLKEMEALGfSDFNLGP 131
Cdd:PLN02284   55 YDGSST-GQAPGEDSEVILYPQ----AIFKDPFRGGNNILVMCDAYTPAGEPIPTNKRAKAAKIFSHPDVAA-EEPWYGI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 132 EPEFFLFKVDEK---GNPTlelndnGGYfdLAP-------MDLGENCRRDIVlelEEM-------GFEIEASHHEVAPGQ 194
Cdd:PLN02284  129 EQEYTLLQKDVKwplGWPV------GGY--PGPqgpyycgVGADKAFGRDIV---DAHykaclyaGINISGINGEVMPGQ 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1848567235 195 HEIDFKYANAIRSCDDIQTFKLVVKTIARKHGLHATFMPKPLYG-VNGSGMHCNLS 249
Cdd:PLN02284  198 WEFQVGPVVGISAGDQLWVARYILERITEIAGVVVSFDPKPIPGdWNGAGAHTNYS 253
PLN03036 PLN03036
glutamine synthetase; Provisional
49-350 4.85e-08

glutamine synthetase; Provisional


Pssm-ID: 178603 [Multi-domain]  Cd Length: 432  Bit Score: 54.98  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235  49 KMMFDGSSIeGFVRIEESDMYLYPDldtwVIFPWTAEKGKVARLICDIYNADGTPFDGDPRNNLKRVLKEMEALGFSDFn 128
Cdd:PLN03036  112 KWNYDGSST-GQAPGEDSEVILYPQ----AIFKDPFRGGNNILVICDTYTPAGEPIPTNKRHRAAEIFSNKKVVDEVPW- 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 129 LGPEPEFFLFKVDEK---GNPTLEL-NDNGGYFDLAPMDlgENCRRDIVLELEEM----GFEIEASHHEVAPGQHEIDFK 200
Cdd:PLN03036  186 FGIEQEYTLLQQNVKwplGWPVGAYpGPQGPYYCGAGAD--KSFGRDISDAHYKAclyaGINISGTNGEVMPGQWEYQVG 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848567235 201 YANAIRSCDDIQTFKLVVKTIARKHGLHATFMPKPLYG-VNGSGMHCNLSLFKNGENVFFDANGDLQLSDDARHfiagiL 279
Cdd:PLN03036  264 PSVGIDAGDHIWCSRYILERITEQAGVVLTLDPKPIEGdWNGAGCHTNYSTKSMREEGGFEVIKKAILNLSLRH-----K 338
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1848567235 280 KHAPAFTAianptvNSYKRLVPGYEAPCY--VAWSAQNRSPLVRIPASRGISTRVEVRSVDPAAN--PYLVMATL 350
Cdd:PLN03036  339 EHISAYGE------GNERRLTGKHETASIdtFSWGVANRGCSIRVGRDTEKKGKGYLEDRRPASNmdPYIVTSLL 407
 
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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