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Conserved domains on  [gi|1063708312|ref|NP_001319763|]
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Amidohydrolase family [Arabidopsis thaliana]

Protein Classification

amidohydrolase( domain architecture ID 10101347)

metal-dependent amidohydrolase similar to Bacillus subtilis YtcJ and Arthrobacter pascens N-substituted formamide deformylase that catalyzes the hydrolysis of N-benzylformamide (an N-substituted formamide) to benzylamine and formate

CATH:  3.20.20.140
EC:  3.5.-.-
Gene Ontology:  GO:0046872|GO:0016810
PubMed:  9144792
SCOP:  3000176

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 1-432 3.44e-159

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


:

Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 459.08  E-value: 3.44e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312   1 MAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGG-ELPSASWIDEISPRNPVWLIRMDGHMALANSLALK 79
Cdd:cd01300    54 LLWLDLSGVTSKEEALARIREDAAAAPPGEWILGFGWDESLLGEgRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALR 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  80 IAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGttde 159
Cdd:cd01300   134 LAGITRDTPDPPGGEIVRDADGEPTGVLVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAAD---- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 160 lswkDFQDVYLYADSSK-KMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPN 238
Cdd:cd01300   210 ----DIEAYRRLAAAGElTLRVRVALYVSPLAEDLLEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPG 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 239 NYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVA 318
Cdd:cd01300   286 TGGLLLISPEELEELVRAADEAGLQVAIHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIA 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 319 SVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISF 398
Cdd:cd01300   366 SVQPNHLYSDGDAAEDRRLGEERAKRSYPFRSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSL 445

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1063708312 399 TDALIAQTISAARAAFLDHHLGSLSPGKLADFVI 432
Cdd:cd01300   446 EEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 406-460 2.69e-04

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 PRK07228:

Pssm-ID: 469705 [Multi-domain]  Cd Length: 445  Bit Score: 43.06  E-value: 2.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708312 406 TISAARAAFLDHHLGSLSPGKLADFVILSTN--------SWDEFSKDVSAS----VLATYVGGKQLY 460
Cdd:PRK07228  347 TLGGAKAAGFEDEIGSLEEGKKADLAILDLDglhatpshGVDVLSHLVYAAhgsdVETTMVDGKIVM 413
 
Name Accession Description Interval E-value
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 1-432 3.44e-159

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 459.08  E-value: 3.44e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312   1 MAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGG-ELPSASWIDEISPRNPVWLIRMDGHMALANSLALK 79
Cdd:cd01300    54 LLWLDLSGVTSKEEALARIREDAAAAPPGEWILGFGWDESLLGEgRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALR 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  80 IAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGttde 159
Cdd:cd01300   134 LAGITRDTPDPPGGEIVRDADGEPTGVLVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAAD---- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 160 lswkDFQDVYLYADSSK-KMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPN 238
Cdd:cd01300   210 ----DIEAYRRLAAAGElTLRVRVALYVSPLAEDLLEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPG 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 239 NYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVA 318
Cdd:cd01300   286 TGGLLLISPEELEELVRAADEAGLQVAIHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIA 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 319 SVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISF 398
Cdd:cd01300   366 SVQPNHLYSDGDAAEDRRLGEERAKRSYPFRSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSL 445

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1063708312 399 TDALIAQTISAARAAFLDHHLGSLSPGKLADFVI 432
Cdd:cd01300   446 EEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
1-460 1.24e-155

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 451.95  E-value: 1.24e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312   1 MAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWG-GELPSASWIDEISPRNPVWLIRMDGHMALANSLALK 79
Cdd:COG1574    82 LLGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPeGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALE 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  80 IAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGryfpgttde 159
Cdd:COG1574   162 LAGITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAG--------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 160 LSWKDFqDVYLYADSSKKMMIRTCLFFPITT--WSRLLDLKLQKGSVlSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTP 237
Cdd:COG1574   233 LGPDDL-AAYRELAAAGELPLRVVLYLGADDedLEELLALGLRTGYG-DDRLRVGGVKLFADGSLGSRTAALLEPYADDP 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 238 NNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIV 317
Cdd:COG1574   311 GNRGLLLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVI 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 318 ASVQPDHLLDDADSVAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKwDHAWIPSERIS 397
Cdd:COG1574   391 ASMQPTHATSDGDWAEDRLGPERA-ARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPS-GRGLGPEERLT 468

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708312 398 FTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTnswDEFSKDVSA----SVLATYVGGKQLY 460
Cdd:COG1574   469 VEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR---DPLTVPPEEikdiKVLLTVVGGRVVY 532
Amidohydro_3 pfam07969
Amidohydrolase family;
19-460 3.32e-69

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 227.41  E-value: 3.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  19 VKDAVQNAKEGSWILGGGWN--NDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIM 96
Cdd:pfam07969  42 VKGQAGRTPKGRWLVGEGWDeaQFAETRFPYALADLDEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  97 RMPSGE-PTGLLIDAAMELVTPWVKEisvdERREALFRASKYALTRGVTTVIDLGRYfpgttdelsWKDFQDVYLYADSS 175
Cdd:pfam07969 122 RDANGEgLTGLLREGAYALPPLLARE----AEAAAVAAALAALPGFGITSVDGGGGN---------VHSLDDYEPLRELT 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 176 KKMMIrtclffpittwSRLLDLKLQKGSVLS-EWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNyGLEVMDPEKLSNFT 254
Cdd:pfam07969 189 AAEKL-----------KELLDAPERLGLPHSiYELRIGAMKLFADGVLGSRTAALTEPYFDAPGT-GWPDFEDEALAELV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 255 MAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRfRIEHAQHLAPGS---ANRFGQLHIVASVQPDHLLDDADS 331
Cdd:pfam07969 257 AAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGNQGRV-RIEHAQGVVPYTysqIERVAALGGAAGVQPVFDPLWGDW 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 332 VAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAAR 411
Cdd:pfam07969 336 LQDRLGAERA-RGLTPVKELLNAGVKVALGSDAPVGPFDPWPRIGAAVMRQTAGGGEVLGPDEELSLEEALALYTSGPAK 414

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063708312 412 AAFLDHHLGSLSPGKLADFVILSTNSWD-EFSKDVSASVLATYVGGKQLY 460
Cdd:pfam07969 415 ALGLEDRKGTLGVGKDADLVVLDDDPLTvDPPAIADIRVRLTVVDGRVVY 464
PRK08204 PRK08204
hypothetical protein; Provisional
 386-437 1.65e-05

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 46.92  E-value: 1.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063708312 386 WDHAWIPSERISFT--DALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNS 437
Cdd:PRK08204  330 LREGGMPPPRLTLTarQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATD 383
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
406-460 2.69e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 43.06  E-value: 2.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708312 406 TISAARAAFLDHHLGSLSPGKLADFVILSTN--------SWDEFSKDVSAS----VLATYVGGKQLY 460
Cdd:PRK07228  347 TLGGAKAAGFEDEIGSLEEGKKADLAILDLDglhatpshGVDVLSHLVYAAhgsdVETTMVDGKIVM 413
 
Name Accession Description Interval E-value
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 1-432 3.44e-159

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 459.08  E-value: 3.44e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312   1 MAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGG-ELPSASWIDEISPRNPVWLIRMDGHMALANSLALK 79
Cdd:cd01300    54 LLWLDLSGVTSKEEALARIREDAAAAPPGEWILGFGWDESLLGEgRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALR 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  80 IAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGttde 159
Cdd:cd01300   134 LAGITRDTPDPPGGEIVRDADGEPTGVLVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAAD---- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 160 lswkDFQDVYLYADSSK-KMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPN 238
Cdd:cd01300   210 ----DIEAYRRLAAAGElTLRVRVALYVSPLAEDLLEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPG 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 239 NYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVA 318
Cdd:cd01300   286 TGGLLLISPEELEELVRAADEAGLQVAIHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIA 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 319 SVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISF 398
Cdd:cd01300   366 SVQPNHLYSDGDAAEDRRLGEERAKRSYPFRSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSL 445

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1063708312 399 TDALIAQTISAARAAFLDHHLGSLSPGKLADFVI 432
Cdd:cd01300   446 EEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
1-460 1.24e-155

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 451.95  E-value: 1.24e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312   1 MAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWG-GELPSASWIDEISPRNPVWLIRMDGHMALANSLALK 79
Cdd:COG1574    82 LLGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPeGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALE 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  80 IAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGryfpgttde 159
Cdd:COG1574   162 LAGITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAG--------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 160 LSWKDFqDVYLYADSSKKMMIRTCLFFPITT--WSRLLDLKLQKGSVlSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTP 237
Cdd:COG1574   233 LGPDDL-AAYRELAAAGELPLRVVLYLGADDedLEELLALGLRTGYG-DDRLRVGGVKLFADGSLGSRTAALLEPYADDP 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 238 NNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIV 317
Cdd:COG1574   311 GNRGLLLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVI 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 318 ASVQPDHLLDDADSVAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKwDHAWIPSERIS 397
Cdd:COG1574   391 ASMQPTHATSDGDWAEDRLGPERA-ARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPS-GRGLGPEERLT 468

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708312 398 FTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTnswDEFSKDVSA----SVLATYVGGKQLY 460
Cdd:COG1574   469 VEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR---DPLTVPPEEikdiKVLLTVVGGRVVY 532
Amidohydro_3 pfam07969
Amidohydrolase family;
19-460 3.32e-69

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 227.41  E-value: 3.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  19 VKDAVQNAKEGSWILGGGWN--NDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIM 96
Cdd:pfam07969  42 VKGQAGRTPKGRWLVGEGWDeaQFAETRFPYALADLDEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312  97 RMPSGE-PTGLLIDAAMELVTPWVKEisvdERREALFRASKYALTRGVTTVIDLGRYfpgttdelsWKDFQDVYLYADSS 175
Cdd:pfam07969 122 RDANGEgLTGLLREGAYALPPLLARE----AEAAAVAAALAALPGFGITSVDGGGGN---------VHSLDDYEPLRELT 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 176 KKMMIrtclffpittwSRLLDLKLQKGSVLS-EWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNyGLEVMDPEKLSNFT 254
Cdd:pfam07969 189 AAEKL-----------KELLDAPERLGLPHSiYELRIGAMKLFADGVLGSRTAALTEPYFDAPGT-GWPDFEDEALAELV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 255 MAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRfRIEHAQHLAPGS---ANRFGQLHIVASVQPDHLLDDADS 331
Cdd:pfam07969 257 AAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGNQGRV-RIEHAQGVVPYTysqIERVAALGGAAGVQPVFDPLWGDW 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 332 VAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAAR 411
Cdd:pfam07969 336 LQDRLGAERA-RGLTPVKELLNAGVKVALGSDAPVGPFDPWPRIGAAVMRQTAGGGEVLGPDEELSLEEALALYTSGPAK 414

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063708312 412 AAFLDHHLGSLSPGKLADFVILSTNSWD-EFSKDVSASVLATYVGGKQLY 460
Cdd:pfam07969 415 ALGLEDRKGTLGVGKDADLVVLDDDPLTvDPPAIADIRVRLTVVDGRVVY 464
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 118-412 2.80e-09

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.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 57.73  E-value: 2.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 118 WVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDelsWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDl 197
Cdd:cd01292    24 EAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTT---KAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDED- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 198 klqKGSVLSEWLyLGGVKAFIDGslgsnsALFYEEYIDTPNNyglevmdPEKLSNFTMAADKSGLQVAIHAIGDKANDMi 277
Cdd:cd01292   100 ---AEALLLELL-RRGLELGAVG------LKLAGPYTATGLS-------DESLRRVLEEARKLGLPVVIHAGELPDPTR- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 278 ldMYESVAAANGDrDRRFRIEHAQHLAPGSANRFGQL--HIVASVQPDHLLDDADSVAKKLGSERAVKESYLFqsllngn 355
Cdd:cd01292   162 --ALEDLVALLRL-GGRVVIGHVSHLDPELLELLKEAgvSLEVCPLSNYLLGRDGEGAEALRRLLELGIRVTL------- 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063708312 356 allalGSDWPVA--DINPLHSIRTAVKRIPPKWDHAwipserisftDALIAQTISAARA 412
Cdd:cd01292   232 -----GTDGPPHplGTDLLALLRLLLKVLRLGLSLE----------EALRLATINPARA 275
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 256-459 6.45e-08

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 54.04  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 256 AADKSGLQVAIHAIGDKA----------NDMILDMYESVAAANGD-RDRRFRIEHAQHLAPGSANRFGQLHIVASVqpDH 324
Cdd:pfam01979 135 EAKKYGLPVAIHALETKGevedaiaafgGGIEHGTHLEVAESGGLlDIIKLILAHGVHLSPTEANLLAEHLKGAGV--AH 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 325 LLDDADSVAKKLGSERAVKESYLFQSLLngnallalgSDWPVADINP--LHSIRTAVKRippkwdhAWIPSERISFTDAL 402
Cdd:pfam01979 213 CPFSNSKLRSGRIALRKALEDGVKVGLG---------TDGAGSGNSLnmLEELRLALEL-------QFDPEGGLSPLEAL 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063708312 403 IAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSKD-VSASVLATYVGGKQL 459
Cdd:pfam01979 277 RMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLkPDGNVKKVIVKGKIV 334
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 232-460 4.32e-07

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 51.89  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 232 EYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMildmyesvAAANGdrdrrFR-IEHAQHLAPGSANR 310
Cdd:COG1228   176 DYIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHAHQADDIRL--------AVEAG-----VDsIEHGTYLDDEVADL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 311 FGQLHIVAsVQPDHLLDDADSVAKKLGSERAVKESY-----------------LFQSllngnallalgsDWPVADI---N 370
Cdd:COG1228   243 LAEAGTVV-LVPTLSLFLALLEGAAAPVAAKARKVReaalanarrlhdagvpvALGT------------DAGVGVPpgrS 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 371 PLHSIRTAVKrippkwdhawipsERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSkdVSASVL 450
Cdd:COG1228   310 LHRELALAVE-------------AGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIA--YLEDVR 374

                         250
                  ....*....|
gi 1063708312 451 ATYVGGKQLY 460
Cdd:COG1228   375 AVMKDGRVVD 384
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 368-460 2.48e-06

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 49.44  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 368 DINPLHSIRTAVK--RippkwdHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNS------WD 439
Cdd:COG0402   316 SLDMFEEMRLAALlqR------LRGGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAphlaplHD 389

                          90       100
                  ....*....|....*....|....*
gi 1063708312 440 EFSKDV----SASVLATYVGGKQLY 460
Cdd:COG0402   390 PLSALVyaadGRDVRTVWVAGRVVV 414
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 397-460 7.22e-06

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 48.08  E-value: 7.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063708312 397 SFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVIlstnsWDEFSKDVSASVLATYVGGKQLY 460
Cdd:cd01309   301 SYEEALKAITINPAKILGIEDRVGSLEPGKDADLVV-----WNGDPLEPTSKPEQVYIDGRLVY 359
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
396-457 1.01e-05

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 47.40  E-value: 1.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063708312 396 ISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILStnswDEFskdvsaSVLATYVGGK 457
Cdd:COG1820   322 LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLD----DDL------NVRATWVGGE 373
PRK08204 PRK08204
hypothetical protein; Provisional
 386-437 1.65e-05

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 46.92  E-value: 1.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063708312 386 WDHAWIPSERISFT--DALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNS 437
Cdd:PRK08204  330 LREGGMPPPRLTLTarQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATD 383
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 395-441 3.37e-05

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 45.71  E-value: 3.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1063708312 395 RISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEF 441
Cdd:cd01296   309 RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHL 355
ureC PRK13308
urease subunit alpha; Reviewed
 391-432 5.51e-05

urease subunit alpha; Reviewed


Pssm-ID: 183965 [Multi-domain]  Cd Length: 569  Bit Score: 45.47  E-value: 5.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1063708312 391 IPSERISFTDAL-----IAQ-TISAARAAFLDHHLGSLSPGKLADFVI 432
Cdd:PRK13308  389 LPEDRGTFADNArikryIAKyTINPAITFGIDDHIGSLEPGKLADIVL 436
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
401-460 1.89e-04

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 43.75  E-value: 1.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 401 ALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNS------WDEFSKDVSAS----VLATYVGGKQLY 460
Cdd:PRK09045  345 ALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLSGletqpvYDPVSQLVYAAgreqVSHVWVAGKQLL 414
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
368-458 2.10e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 43.55  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 368 DINPL---------HSIRTAVKR-IPPkwdhawipserisfTDALIAQTISAARAAFLDHhLGSLSPGKLADFVILStnS 437
Cdd:COG1001   260 DRHPDdlleeghidHVVRRAIELgLDP--------------VTAIQMATLNAAEHFGLKD-LGAIAPGRRADIVLLD--D 322

                          90       100
                  ....*....|....*....|.
gi 1063708312 438 WDEFskdvsaSVLATYVGGKQ 458
Cdd:COG1001   323 LEDF------KVEKVYADGKL 337
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
406-460 2.69e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 43.06  E-value: 2.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708312 406 TISAARAAFLDHHLGSLSPGKLADFVILSTN--------SWDEFSKDVSAS----VLATYVGGKQLY 460
Cdd:PRK07228  347 TLGGAKAAGFEDEIGSLEEGKKADLAILDLDglhatpshGVDVLSHLVYAAhgsdVETTMVDGKIVM 413
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 386-460 2.94e-04

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 42.96  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708312 386 WDHAWIPSErisftDALIAQTISAARAAFLDHhLGSLSPGKLADFVILSTNSWDEFSKD----------VSASVLATYVG 455
Cdd:cd01298   327 GDPTALPAE-----EALEMATIGGAKALGLDE-IGSLEVGKKADLILIDLDGPHLLPVHdpishlvysaNGGDVDTVIVN 400


                  ....*
gi 1063708312 456 GKQLY 460
Cdd:cd01298   401 GRVVM 405
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 396-456 8.03e-04

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 41.41  E-value: 8.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063708312 396 ISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILStNSWDefskdvsasVLATYVGG 456
Cdd:cd00854   324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD-DDLN---------VKATWING 374
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 373-434 2.27e-03

Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.


Pssm-ID: 238620 [Multi-domain]  Cd Length: 422  Bit Score: 40.28  E-value: 2.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063708312 373 HSIRTAVKrippkwdhawipsERISFTDALIAQTISAARAAFLdHHLGSLSPGKLADFVILS 434
Cdd:cd01295   225 YIVRRAIE-------------AGIPPEDAIQMATINPAECYGL-HDLGAIAPGRIADIVILD 272
PRK09228 PRK09228
guanine deaminase; Provisional
 406-460 2.27e-03

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 40.17  E-value: 2.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063708312 406 TISAARAAFLDHHLGSLSPGKLADFVILSTNS------WDEFSKDVS------------ASVLATYVGGKQLY 460
Cdd:PRK09228  358 TLGGARALGLDDRIGNLAPGKEADFVVLDPAAtpllalRTARAESLEellfalmtlgddRAVAETYVAGRPVY 430
ureC PRK13206
urease subunit alpha; Reviewed
 406-439 8.86e-03

urease subunit alpha; Reviewed


Pssm-ID: 237304 [Multi-domain]  Cd Length: 573  Bit Score: 38.54  E-value: 8.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1063708312 406 TISAARAAFLDHHLGSLSPGKLADFVIlstnsWD 439
Cdd:PRK13206  414 TICPAVAHGIDHEIGSVEVGKLADLVL-----WE 442
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 401-436 9.85e-03

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 38.04  E-value: 9.85e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1063708312 401 ALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTN 436
Cdd:cd01299   299 ALRAATANAAELLGLSDELGVIEAGKLADLLVVDGD 334
 
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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