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Conserved domains on  [gi|145339441|ref|NP_190886|]
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nodulin/glutamine synthase-like protein [Arabidopsis thaliana]

Protein Classification

amidohydrolase family protein( domain architecture ID 10897632)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue, similar to Zn-dependent arginine carboxypeptidase (protein Sgx9359b) derived from a DNA sequence isolated from the Sargasso Sea

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Gln-synt_C pfam00120
Glutamine synthetase, catalytic domain;
515-846 6.09e-127

Glutamine synthetase, catalytic domain;


:

Pssm-ID: 425473 [Multi-domain]  Cd Length: 343  Bit Score: 384.63  E-value: 6.09e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  515 YCPRETLRRVAKVLKDEfDLVMNAGFENEFYLLKNVVREGKEE----------YMPFDFGPYCATSSFDAASPIFHDIVP 584
Cdd:pfam00120   1 RDPRSILKRALARLASL-GLTAYVGPELEFFLFDRVEDGNPNGpfyppdseggYRPADKGGYFDVAPVDSAQDLRREIVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  585 ALESLNIEVEQFHAESGKGQFEVSLGHTIASHAADNLVYTREVIRSVARKQGLLATFVPKYDYCDIGSGSHVHLSLWKNG 664
Cdd:pfam00120  80 ALEAMGIEVEASHHEVAPGQHEIDFRFDDALKAADNAQTFKYVVKNVARKHGLTATFMPKPFFGDNGSGMHVHQSLWKDG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  665 ENVFPASNNssSHGISSVGEEFMAGVLFHLPSILAIIAPLPNSYDRIQPNTWSGAFQCWGKENREAALRAasPPGTPDGl 744
Cdd:pfam00120 160 KNLFADPDG--EYGLSETARHFIAGILKHAPALTALTNPTVNSYKRLVPGYEAPVYLAWGARNRSAALRI--PAGSPKA- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  745 vTNFEIKSFDGSANPHLGLAVIMAAGIDGLRRHLQLPTPIDINPADVAAT----LNRLPETLSEAVEALDKDKVLHDLLG 820
Cdd:pfam00120 235 -RRVEVRSPDPDANPYLAFAALLAAGLDGIENKIDPGEPVDGNLYELTPEerkgIPTLPSSLEEALDALEEDELLKEALG 313
                         330       340
                  ....*....|....*....|....*.
gi 145339441  821 QKLLVAIKGVRKAEVEYYSKNPDAYK 846
Cdd:pfam00120 314 EHFIEAYIAVKRAEWEEFRTAVHPWE 339
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
230-390 1.06e-13

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


The actual alignment was detected with superfamily member pfam04909:

Pssm-ID: 469705 [Multi-domain]  Cd Length: 283  Bit Score: 72.56  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  230 LEVAVRRDLPLQIHTGFGDKDLDLRLSNPLHLRTLLEdkRFGKCRIVLLHAAYP------FSKEASFLSSVYPQVYLDFG 303
Cdd:pfam04909 128 YEALEELGLPVDIHTGFGDRPEDTRAIQPLLLAGVAR--KFPDLKIVLDHGGGPwipeglDDPAALALLARRPNVYVKLS 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  304 LAVPKL---SVHGMVSSVKELLDLASIKKVMFSTDGYASPETYYLGAKKAREVIFLVLSDAcasgdlslmeaiDAAKDIF 380
Cdd:pfam04909 206 GLYRDLyfdAPLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLLLALSD------------EEREKIL 273
                         170
                  ....*....|
gi 145339441  381 SRNSIGFYKL 390
Cdd:pfam04909 274 GGNAARLYGL 283
Gln-synt_N super family cl08409
Glutamine synthetase, beta-Grasp domain;
421-513 6.53e-04

Glutamine synthetase, beta-Grasp domain;


The actual alignment was detected with superfamily member pfam16952:

Pssm-ID: 447627  Cd Length: 112  Bit Score: 40.07  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  421 FVRIIWVDTSGQQRCRAVQAQRFNRSVKkNGVGLTFASMGMTSFtDGPAEESKLTGVGEIRLVPDLSTKQTIPW-----T 495
Cdd:pfam16952  17 LIRFLTADHAGIIRGKALPLARLAEQLA-SGCGHTPAMMALNML-DLIDESEPLGPHGDLRLLPDPASFVALEQapdaaA 94
                          90
                  ....*....|....*...
gi 145339441  496 KQESMVLADMQLKPGEAW 513
Cdd:pfam16952  95 PALDYLHGDLRETDGSPW 112
 
Name Accession Description Interval E-value
Gln-synt_C pfam00120
Glutamine synthetase, catalytic domain;
515-846 6.09e-127

Glutamine synthetase, catalytic domain;


Pssm-ID: 425473 [Multi-domain]  Cd Length: 343  Bit Score: 384.63  E-value: 6.09e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  515 YCPRETLRRVAKVLKDEfDLVMNAGFENEFYLLKNVVREGKEE----------YMPFDFGPYCATSSFDAASPIFHDIVP 584
Cdd:pfam00120   1 RDPRSILKRALARLASL-GLTAYVGPELEFFLFDRVEDGNPNGpfyppdseggYRPADKGGYFDVAPVDSAQDLRREIVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  585 ALESLNIEVEQFHAESGKGQFEVSLGHTIASHAADNLVYTREVIRSVARKQGLLATFVPKYDYCDIGSGSHVHLSLWKNG 664
Cdd:pfam00120  80 ALEAMGIEVEASHHEVAPGQHEIDFRFDDALKAADNAQTFKYVVKNVARKHGLTATFMPKPFFGDNGSGMHVHQSLWKDG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  665 ENVFPASNNssSHGISSVGEEFMAGVLFHLPSILAIIAPLPNSYDRIQPNTWSGAFQCWGKENREAALRAasPPGTPDGl 744
Cdd:pfam00120 160 KNLFADPDG--EYGLSETARHFIAGILKHAPALTALTNPTVNSYKRLVPGYEAPVYLAWGARNRSAALRI--PAGSPKA- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  745 vTNFEIKSFDGSANPHLGLAVIMAAGIDGLRRHLQLPTPIDINPADVAAT----LNRLPETLSEAVEALDKDKVLHDLLG 820
Cdd:pfam00120 235 -RRVEVRSPDPDANPYLAFAALLAAGLDGIENKIDPGEPVDGNLYELTPEerkgIPTLPSSLEEALDALEEDELLKEALG 313
                         330       340
                  ....*....|....*....|....*.
gi 145339441  821 QKLLVAIKGVRKAEVEYYSKNPDAYK 846
Cdd:pfam00120 314 EHFIEAYIAVKRAEWEEFRTAVHPWE 339
GlnA COG0174
Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of ...
409-852 2.27e-110

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: 345.16  E-value: 2.27e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 409 IKEPDVQedsssFVRIIWVDTSGQQRCRAVQAQRFnRSVKKNGVGLtfasmgmtsftDGpaeeSKLTGVGEI-----RLV 483
Cdd:COG0174   13 LKERGVK-----FVDLQFTDINGVLRGKRVPASEL-EKALEEGIGF-----------DG----SSIEGFVEIgesdmVLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 484 PDLSTKQTIPWTKQES-MVLADMQLKPGEAWGYCPRETLRRVAKVLKDEfDLVMNAGFENEFYLLKNVVRE-GKEEYMPF 561
Cdd:COG0174   72 PDPSTLRILPWRPEPTaRVICDVYDPDGEPYEGDPRNVLKRVLARLAET-GLTPYVGPELEFFLFDDDSDEkGNRGLRPR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 562 DFGPYCATSSFDAASPIFHDIVPALESLNIEVEQFHAESGKGQFEVSLGHTIASHAADNLVYTREVIRSVARKQGLLATF 641
Cdd:COG0174  151 DKGGYYDLAPLDRFEDFRREIVLALEAMGIPVETSHHEVAPGQHEINLRYADALTAADRVVLFKYVVKEVARRHGLTATF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 642 VPKYDYCDIGSGSHVHLSLWK-NGENVFpaSNNSSSHGISSVGEEFMAGVLFHLPSILAIIAPLPNSYDRIQPNTWSGAF 720
Cdd:COG0174  231 MPKPFAGDNGSGMHVHQSLWDaDGKNLF--ADPDGYAGLSELARHFIGGLLKHAPALTAFTAPTVNSYKRLVPGYEAPVN 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 721 QCWGKENREAALRAasPPGTPDGlvTNFEIKSFDGSANPHLGLAVIMAAGIDGLRRHLQLPTPIDIN----PADVAATLN 796
Cdd:COG0174  309 IAWGYDNRSAAIRI--PGGSPKA--TRIEYRVPDADANPYLAFAALLAAGLDGIENKLEPGEPVDGNayelSPEERAGIP 384
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145339441 797 RLPETLSEAVEALDKDKVLHDLLGQKLLVAIKGVRKAEVEYYSKNPDAYKqlIHRY 852
Cdd:COG0174  385 RLPRSLEEALDALEADEFLREVLGEDFVDHYIALKRAEWEEFRRRVTPWE--RERY 438
glnA PRK09469
glutamate--ammonia ligase;
482-813 4.81e-27

glutamate--ammonia ligase;


Pssm-ID: 181884 [Multi-domain]  Cd Length: 469  Bit Score: 115.63  E-value: 4.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 482 LVPDLSTKQTIPWTKQESMVLADMQLKPGEAWGYC--PRETLRRVAKVLKDE--FDLVMnAGFENEFYLLKNV------- 550
Cdd:PRK09469  68 LMPDASTAVLDPFFEDSTLIIRCDILEPGTMQGYDrdPRSIAKRAEDYLRSTgiADTVL-FGPEPEFFLFDDIrfgssis 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 551 ------------------VREGKEEYMPFDFGPYCATSSFDAASPIFHDIVPALESLNIEVEQFHAESGK-GQFEVSLGH 611
Cdd:PRK09469 147 gshvaiddieaawnsgtkYEGGNKGHRPGVKGGYFPVPPVDSSQDIRSAMCLVMEEMGLVVEAHHHEVATaGQNEVATRF 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 612 TIASHAADNLVYTREVIRSVARKQGLLATFVPKYDYCDIGSGSHVHLSLWKNGENVFPASNNSsshGISSVGEEFMAGVL 691
Cdd:PRK09469 227 NTMTKKADEIQIYKYVVHNVAHAFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLFAGDKYA---GLSEQALYYIGGII 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 692 FHLPSILAIIAPLPNSYDRIQPNTWSGAFQCWGKENREAALRAaspPGTPDGLVTNFEIKSFDGSANPHLGLAVIMAAGI 771
Cdd:PRK09469 304 KHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRI---PVVASPKARRIEVRFPDPAANPYLCFAALLMAGL 380
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 145339441 772 DGLRRHLQLPTPIDIN----PADVAATLNRLPETLSEAVEALDKDK 813
Cdd:PRK09469 381 DGIKNKIHPGEAMDKNlydlPPEEAAEIPQVAGSLEEALNALDADR 426
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
230-390 1.06e-13

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 72.56  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  230 LEVAVRRDLPLQIHTGFGDKDLDLRLSNPLHLRTLLEdkRFGKCRIVLLHAAYP------FSKEASFLSSVYPQVYLDFG 303
Cdd:pfam04909 128 YEALEELGLPVDIHTGFGDRPEDTRAIQPLLLAGVAR--KFPDLKIVLDHGGGPwipeglDDPAALALLARRPNVYVKLS 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  304 LAVPKL---SVHGMVSSVKELLDLASIKKVMFSTDGYASPETYYLGAKKAREVIFLVLSDAcasgdlslmeaiDAAKDIF 380
Cdd:pfam04909 206 GLYRDLyfdAPLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLLLALSD------------EEREKIL 273
                         170
                  ....*....|
gi 145339441  381 SRNSIGFYKL 390
Cdd:pfam04909 274 GGNAARLYGL 283
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
230-390 3.14e-12

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 67.31  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 230 LEVAVRRDLPLQIHTG---FGDKDLDLRLSNPLHLRTLLEdkRFGKCRIVLLHAAYPFSKEA-SFLSSVYPQVYLDFGla 305
Cdd:COG2159  112 YEAAAELGLPVLVHPGtppGPPPGLDLYYAAPLILSGVAE--RFPDLKFILAHGGGPWLPELlGRLLKRLPNVYFDTS-- 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 306 vpklSVHGMVSSVKELLDLASIKKVMFSTDgyaSPetyYLGAKKAREVIflvlsdaCASGDLSlmeaiDAAKD-IFSRNS 384
Cdd:COG2159  188 ----GVFPRPEALRELLETLGADRILFGSD---YP---HWDPPEALEAL-------EELPGLS-----EEDREkILGGNA 245

                 ....*.
gi 145339441 385 IGFYKL 390
Cdd:COG2159  246 ARLLGL 251
Gln-synt_N_2 pfam16952
Glutamine synthetase N-terminal domain;
421-513 6.53e-04

Glutamine synthetase N-terminal domain;


Pssm-ID: 407170  Cd Length: 112  Bit Score: 40.07  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  421 FVRIIWVDTSGQQRCRAVQAQRFNRSVKkNGVGLTFASMGMTSFtDGPAEESKLTGVGEIRLVPDLSTKQTIPW-----T 495
Cdd:pfam16952  17 LIRFLTADHAGIIRGKALPLARLAEQLA-SGCGHTPAMMALNML-DLIDESEPLGPHGDLRLLPDPASFVALEQapdaaA 94
                          90
                  ....*....|....*...
gi 145339441  496 KQESMVLADMQLKPGEAW 513
Cdd:pfam16952  95 PALDYLHGDLRETDGSPW 112
 
Name Accession Description Interval E-value
Gln-synt_C pfam00120
Glutamine synthetase, catalytic domain;
515-846 6.09e-127

Glutamine synthetase, catalytic domain;


Pssm-ID: 425473 [Multi-domain]  Cd Length: 343  Bit Score: 384.63  E-value: 6.09e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  515 YCPRETLRRVAKVLKDEfDLVMNAGFENEFYLLKNVVREGKEE----------YMPFDFGPYCATSSFDAASPIFHDIVP 584
Cdd:pfam00120   1 RDPRSILKRALARLASL-GLTAYVGPELEFFLFDRVEDGNPNGpfyppdseggYRPADKGGYFDVAPVDSAQDLRREIVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  585 ALESLNIEVEQFHAESGKGQFEVSLGHTIASHAADNLVYTREVIRSVARKQGLLATFVPKYDYCDIGSGSHVHLSLWKNG 664
Cdd:pfam00120  80 ALEAMGIEVEASHHEVAPGQHEIDFRFDDALKAADNAQTFKYVVKNVARKHGLTATFMPKPFFGDNGSGMHVHQSLWKDG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  665 ENVFPASNNssSHGISSVGEEFMAGVLFHLPSILAIIAPLPNSYDRIQPNTWSGAFQCWGKENREAALRAasPPGTPDGl 744
Cdd:pfam00120 160 KNLFADPDG--EYGLSETARHFIAGILKHAPALTALTNPTVNSYKRLVPGYEAPVYLAWGARNRSAALRI--PAGSPKA- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  745 vTNFEIKSFDGSANPHLGLAVIMAAGIDGLRRHLQLPTPIDINPADVAAT----LNRLPETLSEAVEALDKDKVLHDLLG 820
Cdd:pfam00120 235 -RRVEVRSPDPDANPYLAFAALLAAGLDGIENKIDPGEPVDGNLYELTPEerkgIPTLPSSLEEALDALEEDELLKEALG 313
                         330       340
                  ....*....|....*....|....*.
gi 145339441  821 QKLLVAIKGVRKAEVEYYSKNPDAYK 846
Cdd:pfam00120 314 EHFIEAYIAVKRAEWEEFRTAVHPWE 339
GlnA COG0174
Glutamine synthetase [Amino acid transport and metabolism]; Glutamine synthetase is part of ...
409-852 2.27e-110

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: 345.16  E-value: 2.27e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 409 IKEPDVQedsssFVRIIWVDTSGQQRCRAVQAQRFnRSVKKNGVGLtfasmgmtsftDGpaeeSKLTGVGEI-----RLV 483
Cdd:COG0174   13 LKERGVK-----FVDLQFTDINGVLRGKRVPASEL-EKALEEGIGF-----------DG----SSIEGFVEIgesdmVLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 484 PDLSTKQTIPWTKQES-MVLADMQLKPGEAWGYCPRETLRRVAKVLKDEfDLVMNAGFENEFYLLKNVVRE-GKEEYMPF 561
Cdd:COG0174   72 PDPSTLRILPWRPEPTaRVICDVYDPDGEPYEGDPRNVLKRVLARLAET-GLTPYVGPELEFFLFDDDSDEkGNRGLRPR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 562 DFGPYCATSSFDAASPIFHDIVPALESLNIEVEQFHAESGKGQFEVSLGHTIASHAADNLVYTREVIRSVARKQGLLATF 641
Cdd:COG0174  151 DKGGYYDLAPLDRFEDFRREIVLALEAMGIPVETSHHEVAPGQHEINLRYADALTAADRVVLFKYVVKEVARRHGLTATF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 642 VPKYDYCDIGSGSHVHLSLWK-NGENVFpaSNNSSSHGISSVGEEFMAGVLFHLPSILAIIAPLPNSYDRIQPNTWSGAF 720
Cdd:COG0174  231 MPKPFAGDNGSGMHVHQSLWDaDGKNLF--ADPDGYAGLSELARHFIGGLLKHAPALTAFTAPTVNSYKRLVPGYEAPVN 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 721 QCWGKENREAALRAasPPGTPDGlvTNFEIKSFDGSANPHLGLAVIMAAGIDGLRRHLQLPTPIDIN----PADVAATLN 796
Cdd:COG0174  309 IAWGYDNRSAAIRI--PGGSPKA--TRIEYRVPDADANPYLAFAALLAAGLDGIENKLEPGEPVDGNayelSPEERAGIP 384
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145339441 797 RLPETLSEAVEALDKDKVLHDLLGQKLLVAIKGVRKAEVEYYSKNPDAYKqlIHRY 852
Cdd:COG0174  385 RLPRSLEEALDALEADEFLREVLGEDFVDHYIALKRAEWEEFRRRVTPWE--RERY 438
glnA PRK09469
glutamate--ammonia ligase;
482-813 4.81e-27

glutamate--ammonia ligase;


Pssm-ID: 181884 [Multi-domain]  Cd Length: 469  Bit Score: 115.63  E-value: 4.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 482 LVPDLSTKQTIPWTKQESMVLADMQLKPGEAWGYC--PRETLRRVAKVLKDE--FDLVMnAGFENEFYLLKNV------- 550
Cdd:PRK09469  68 LMPDASTAVLDPFFEDSTLIIRCDILEPGTMQGYDrdPRSIAKRAEDYLRSTgiADTVL-FGPEPEFFLFDDIrfgssis 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 551 ------------------VREGKEEYMPFDFGPYCATSSFDAASPIFHDIVPALESLNIEVEQFHAESGK-GQFEVSLGH 611
Cdd:PRK09469 147 gshvaiddieaawnsgtkYEGGNKGHRPGVKGGYFPVPPVDSSQDIRSAMCLVMEEMGLVVEAHHHEVATaGQNEVATRF 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 612 TIASHAADNLVYTREVIRSVARKQGLLATFVPKYDYCDIGSGSHVHLSLWKNGENVFPASNNSsshGISSVGEEFMAGVL 691
Cdd:PRK09469 227 NTMTKKADEIQIYKYVVHNVAHAFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLFAGDKYA---GLSEQALYYIGGII 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 692 FHLPSILAIIAPLPNSYDRIQPNTWSGAFQCWGKENREAALRAaspPGTPDGLVTNFEIKSFDGSANPHLGLAVIMAAGI 771
Cdd:PRK09469 304 KHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRI---PVVASPKARRIEVRFPDPAANPYLCFAALLMAGL 380
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 145339441 772 DGLRRHLQLPTPIDIN----PADVAATLNRLPETLSEAVEALDKDK 813
Cdd:PRK09469 381 DGIKNKIHPGEAMDKNlydlPPEEAAEIPQVAGSLEEALNALDADR 426
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
230-390 1.06e-13

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 72.56  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  230 LEVAVRRDLPLQIHTGFGDKDLDLRLSNPLHLRTLLEdkRFGKCRIVLLHAAYP------FSKEASFLSSVYPQVYLDFG 303
Cdd:pfam04909 128 YEALEELGLPVDIHTGFGDRPEDTRAIQPLLLAGVAR--KFPDLKIVLDHGGGPwipeglDDPAALALLARRPNVYVKLS 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  304 LAVPKL---SVHGMVSSVKELLDLASIKKVMFSTDGYASPETYYLGAKKAREVIFLVLSDAcasgdlslmeaiDAAKDIF 380
Cdd:pfam04909 206 GLYRDLyfdAPLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLLLALSD------------EEREKIL 273
                         170
                  ....*....|
gi 145339441  381 SRNSIGFYKL 390
Cdd:pfam04909 274 GGNAARLYGL 283
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
230-390 3.14e-12

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 67.31  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 230 LEVAVRRDLPLQIHTG---FGDKDLDLRLSNPLHLRTLLEdkRFGKCRIVLLHAAYPFSKEA-SFLSSVYPQVYLDFGla 305
Cdd:COG2159  112 YEAAAELGLPVLVHPGtppGPPPGLDLYYAAPLILSGVAE--RFPDLKFILAHGGGPWLPELlGRLLKRLPNVYFDTS-- 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441 306 vpklSVHGMVSSVKELLDLASIKKVMFSTDgyaSPetyYLGAKKAREVIflvlsdaCASGDLSlmeaiDAAKD-IFSRNS 384
Cdd:COG2159  188 ----GVFPRPEALRELLETLGADRILFGSD---YP---HWDPPEALEAL-------EELPGLS-----EEDREkILGGNA 245

                 ....*.
gi 145339441 385 IGFYKL 390
Cdd:COG2159  246 ARLLGL 251
Gln-synt_N_2 pfam16952
Glutamine synthetase N-terminal domain;
421-513 6.53e-04

Glutamine synthetase N-terminal domain;


Pssm-ID: 407170  Cd Length: 112  Bit Score: 40.07  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339441  421 FVRIIWVDTSGQQRCRAVQAQRFNRSVKkNGVGLTFASMGMTSFtDGPAEESKLTGVGEIRLVPDLSTKQTIPW-----T 495
Cdd:pfam16952  17 LIRFLTADHAGIIRGKALPLARLAEQLA-SGCGHTPAMMALNML-DLIDESEPLGPHGDLRLLPDPASFVALEQapdaaA 94
                          90
                  ....*....|....*...
gi 145339441  496 KQESMVLADMQLKPGEAW 513
Cdd:pfam16952  95 PALDYLHGDLRETDGSPW 112
 
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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