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Conserved domains on  [gi|2044745824|ref|WP_213427821|]
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beta-N-acetylhexosaminidase [Paenibacillus dendritiformis]

Protein Classification

glycoside hydrolase family 3 protein( domain architecture ID 11444753)

glycoside hydrolase family 3 (GH3) protein catalyzes the hydrolytic removal of nonreducing glycosyl end residues from a broad range of beta-D-glycans and beta-D-glycosides

CAZY:  GH3
EC:  3.2.1.-
Gene Ontology:  GO:0004553|GO:0005975
SCOP:  4003202|4003716

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BglX COG1472
Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism];
6-481 3.47e-127

Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism];


:

Pssm-ID: 441081 [Multi-domain]  Cd Length: 463  Bit Score: 379.82  E-value: 3.47e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824   6 LTLEQKIGQMVMCGFHGPVvndniRTLIEKHHVGGIIYFrrnvqSKEQVCGLSRELQLISRkhTDIPLFICIDQEGGMVA 85
Cdd:COG1472     1 MTLEEKIGQLFQVGVTGEG-----AELIREGHVGGVILF-----DPAQWAELTNELQRATR--LGIPLLIGTDAEHGVAN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  86 RiDWDDITLIPGNMAIGAARSAEDAYEAARICGEELLHMGINMNFAPSVDVNNNalnPVIG--VRSYGERPDLVAELGAA 163
Cdd:COG1472    69 R-PAGGATVFPQAIALAATWDPELAERVGRAIAREARALGINWNLAPVVDINRD---PRWGrnFESFGEDPYLVGRMAAA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 164 QIRGLQEANVAATAKHFPGHGDTAVDSHHGlaAVNHDEERLLAIELAPFIRAIREGVDLIMTAHVMFpafepNPIPATLS 243
Cdd:COG1472   145 YVRGLQGNGVAATAKHFAGHGDEETGRHTG--PVDVSERELREIYLPPFEAAIKAGVASVMTAYNAL-----NGVPATLS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 244 RNVLTNLLRKRLGYNGVIVTDCLEMHAISKEFGIPEGAVRSVEAGADLVLVSHTyeeqvAAIAALVEAVRSGRIPESQID 323
Cdd:COG1472   218 KWLLTDLLRGEWGFDGLVVSDWGAMGGLAEHYDPAEAAVLALNAGLDLEMPGGK-----AFIAALLEAVESGELSEERID 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 324 ESVDRLLSLKAKRSMDALPEVTP-RFAALFGSDASKAVVDRICENSITLVKNEGGSIPLRKEEPTLVIWPEVRQRTEVDE 402
Cdd:COG1472   293 EAVRRILRLKFRLGLFDDPYVDPeRAAEVVGSPEHRALAREAARESIVLLKNDNGLLPLAALAAGGALAADAAAAAAAAA 372
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044745824 403 PIEQSYTLATALSPYVDHVEKWRIGTYPEADEVKATLEKAASFKQIVVLTYNAVSTLHPGQVEIVQGLIGRPDAQVIVA 481
Cdd:COG1472   373 AAAAAAAAAAAAAAAAALLEAAAGADAALALAAAAAALLLVAAAALVAVVALAAALAVLLLLVLGVAVGVGAVLLAGGG 451
 
Name Accession Description Interval E-value
BglX COG1472
Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism];
6-481 3.47e-127

Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism];


Pssm-ID: 441081 [Multi-domain]  Cd Length: 463  Bit Score: 379.82  E-value: 3.47e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824   6 LTLEQKIGQMVMCGFHGPVvndniRTLIEKHHVGGIIYFrrnvqSKEQVCGLSRELQLISRkhTDIPLFICIDQEGGMVA 85
Cdd:COG1472     1 MTLEEKIGQLFQVGVTGEG-----AELIREGHVGGVILF-----DPAQWAELTNELQRATR--LGIPLLIGTDAEHGVAN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  86 RiDWDDITLIPGNMAIGAARSAEDAYEAARICGEELLHMGINMNFAPSVDVNNNalnPVIG--VRSYGERPDLVAELGAA 163
Cdd:COG1472    69 R-PAGGATVFPQAIALAATWDPELAERVGRAIAREARALGINWNLAPVVDINRD---PRWGrnFESFGEDPYLVGRMAAA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 164 QIRGLQEANVAATAKHFPGHGDTAVDSHHGlaAVNHDEERLLAIELAPFIRAIREGVDLIMTAHVMFpafepNPIPATLS 243
Cdd:COG1472   145 YVRGLQGNGVAATAKHFAGHGDEETGRHTG--PVDVSERELREIYLPPFEAAIKAGVASVMTAYNAL-----NGVPATLS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 244 RNVLTNLLRKRLGYNGVIVTDCLEMHAISKEFGIPEGAVRSVEAGADLVLVSHTyeeqvAAIAALVEAVRSGRIPESQID 323
Cdd:COG1472   218 KWLLTDLLRGEWGFDGLVVSDWGAMGGLAEHYDPAEAAVLALNAGLDLEMPGGK-----AFIAALLEAVESGELSEERID 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 324 ESVDRLLSLKAKRSMDALPEVTP-RFAALFGSDASKAVVDRICENSITLVKNEGGSIPLRKEEPTLVIWPEVRQRTEVDE 402
Cdd:COG1472   293 EAVRRILRLKFRLGLFDDPYVDPeRAAEVVGSPEHRALAREAARESIVLLKNDNGLLPLAALAAGGALAADAAAAAAAAA 372
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044745824 403 PIEQSYTLATALSPYVDHVEKWRIGTYPEADEVKATLEKAASFKQIVVLTYNAVSTLHPGQVEIVQGLIGRPDAQVIVA 481
Cdd:COG1472   373 AAAAAAAAAAAAAAAAALLEAAAGADAALALAAAAAALLLVAAAALVAVVALAAALAVLLLLVLGVAVGVGAVLLAGGG 451
Glyco_hydro_3 pfam00933
Glycosyl hydrolase family 3 N terminal domain;
7-332 2.63e-101

Glycosyl hydrolase family 3 N terminal domain;


Pssm-ID: 395747 [Multi-domain]  Cd Length: 316  Bit Score: 308.18  E-value: 2.63e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824   7 TLEQKIGQMVMCGFHGPVVNDNIRTLIEKHHVGGIIYFRRNVQSKEQVCGLSR-ELQLISRKHTDIPLFICIDQEGGMVA 85
Cdd:pfam00933   1 TLDEKIGQLLQVEVGEGKPSHEEAELLKDYHVGGIILFGGNLEDWVQLSDLIRyQRQAVEESRLGIPLLVAVDQEGGRVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  86 RIDwdDITLIPGNMAIGAARSAEDAYEAARICGEELLHMGINMNFAPSVDVNNNALNPvIGVRSYGERPDLVAELGAAQI 165
Cdd:pfam00933  81 RFG--EGTMFPSAIALAATSDPDLAKQMGWAMAREMRALGIDWDFAPVVDVARDPRWG-IGERSFSEDPQLVSALAGAMI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 166 RGLQEANVAATAKHFPGHGDTAVDSHHGLAAVNHDEERLLAIELAPFIRAIREGVDLIMTAHVMFPAFepNPIPATLSRN 245
Cdd:pfam00933 158 EGLQGAGVLATVKHFPGHGHGATDSHKETPTTPRPEQRLRTVDLLPFQAAIEAGVDAVMAAHVIYSSL--DGTPATGSKY 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 246 VLTNLLRKRLGYNGVIVTDCLEMHAISKEFGIPEGAVRSVEAGADLVLVSHTYEEqvaaiaALVEAVRSGRIPESQIDES 325
Cdd:pfam00933 236 LLTDVLRKKWGFDGIVVSDDLSMKGIADHGGPAEAVRRALEAGVDIALVPEERTK------YLKKVVKNGKLPMARIDAA 309

                  ....*..
gi 2044745824 326 VDRLLSL 332
Cdd:pfam00933 310 VRRVLRL 316
PRK05337 PRK05337
beta-hexosaminidase; Provisional
15-350 5.17e-64

beta-hexosaminidase; Provisional


Pssm-ID: 235417 [Multi-domain]  Cd Length: 337  Bit Score: 212.32  E-value: 5.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  15 MVMCGFHGPVVNDNIRTLIEKHHVGGIIYFRRNVQSKEQVCGLSRELQLISRKhtdiPLFICIDQEGGMVARIDwDDITL 94
Cdd:PRK05337    3 PLMLDVAGTELTAEERERLQHPLVGGVILFARNFEDPAQLRELTAAIRAAVRP----PLLIAVDQEGGRVQRFR-EGFTR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  95 IPGNMAIGAA--RSAEDAYEAARICGE----ELLHMGINMNFAPSVDVNNNalNPVIGVRSYGERPDLVAELGAAQIRGL 168
Cdd:PRK05337   78 LPAMQSFGALwdRDPLEALKLAEEAGWlmaaELRACGIDLSFAPVLDLDGI--SAVIGDRAFHRDPQVVAALASAFIDGM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 169 QEANVAATAKHFPGHGDTAVDSHHGLAAVNHDEERLLAIELAPFIRAIREGVDLIMTAHVMFPAFEPNpiPATLSRNVLT 248
Cdd:PRK05337  156 HAAGMAATGKHFPGHGAVEADSHVETPVDERPLEEIRAEDMAPFRALIAAGLDAVMPAHVIYPQVDPR--PAGFSRYWLQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 249 NLLRKRLGYNGVIVTDCLEMHAISKEFGIPEGAVRSVEAGADLVLVSHTYEEQVAAIAALveavrsgripesQIDESVDR 328
Cdd:PRK05337  234 DILRQELGFDGVIFSDDLSMEGAAVAGDYAERAQAALDAGCDMVLVCNNRDGAVSVLDNL------------SPPISAER 301
                         330       340
                  ....*....|....*....|....
gi 2044745824 329 LLSLKAKR--SMDALpEVTPRFAA 350
Cdd:PRK05337  302 LTRLYGRGafSWQEL-MASPRWKA 324
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
299-335 3.46e-03

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 35.78  E-value: 3.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2044745824  299 EEQVAAIAALVEAVRSGRIPESQIDESVDRLLSLKAK 335
Cdd:smart00991   1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQ 37
 
Name Accession Description Interval E-value
BglX COG1472
Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism];
6-481 3.47e-127

Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism];


Pssm-ID: 441081 [Multi-domain]  Cd Length: 463  Bit Score: 379.82  E-value: 3.47e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824   6 LTLEQKIGQMVMCGFHGPVvndniRTLIEKHHVGGIIYFrrnvqSKEQVCGLSRELQLISRkhTDIPLFICIDQEGGMVA 85
Cdd:COG1472     1 MTLEEKIGQLFQVGVTGEG-----AELIREGHVGGVILF-----DPAQWAELTNELQRATR--LGIPLLIGTDAEHGVAN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  86 RiDWDDITLIPGNMAIGAARSAEDAYEAARICGEELLHMGINMNFAPSVDVNNNalnPVIG--VRSYGERPDLVAELGAA 163
Cdd:COG1472    69 R-PAGGATVFPQAIALAATWDPELAERVGRAIAREARALGINWNLAPVVDINRD---PRWGrnFESFGEDPYLVGRMAAA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 164 QIRGLQEANVAATAKHFPGHGDTAVDSHHGlaAVNHDEERLLAIELAPFIRAIREGVDLIMTAHVMFpafepNPIPATLS 243
Cdd:COG1472   145 YVRGLQGNGVAATAKHFAGHGDEETGRHTG--PVDVSERELREIYLPPFEAAIKAGVASVMTAYNAL-----NGVPATLS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 244 RNVLTNLLRKRLGYNGVIVTDCLEMHAISKEFGIPEGAVRSVEAGADLVLVSHTyeeqvAAIAALVEAVRSGRIPESQID 323
Cdd:COG1472   218 KWLLTDLLRGEWGFDGLVVSDWGAMGGLAEHYDPAEAAVLALNAGLDLEMPGGK-----AFIAALLEAVESGELSEERID 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 324 ESVDRLLSLKAKRSMDALPEVTP-RFAALFGSDASKAVVDRICENSITLVKNEGGSIPLRKEEPTLVIWPEVRQRTEVDE 402
Cdd:COG1472   293 EAVRRILRLKFRLGLFDDPYVDPeRAAEVVGSPEHRALAREAARESIVLLKNDNGLLPLAALAAGGALAADAAAAAAAAA 372
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044745824 403 PIEQSYTLATALSPYVDHVEKWRIGTYPEADEVKATLEKAASFKQIVVLTYNAVSTLHPGQVEIVQGLIGRPDAQVIVA 481
Cdd:COG1472   373 AAAAAAAAAAAAAAAAALLEAAAGADAALALAAAAAALLLVAAAALVAVVALAAALAVLLLLVLGVAVGVGAVLLAGGG 451
Glyco_hydro_3 pfam00933
Glycosyl hydrolase family 3 N terminal domain;
7-332 2.63e-101

Glycosyl hydrolase family 3 N terminal domain;


Pssm-ID: 395747 [Multi-domain]  Cd Length: 316  Bit Score: 308.18  E-value: 2.63e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824   7 TLEQKIGQMVMCGFHGPVVNDNIRTLIEKHHVGGIIYFRRNVQSKEQVCGLSR-ELQLISRKHTDIPLFICIDQEGGMVA 85
Cdd:pfam00933   1 TLDEKIGQLLQVEVGEGKPSHEEAELLKDYHVGGIILFGGNLEDWVQLSDLIRyQRQAVEESRLGIPLLVAVDQEGGRVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  86 RIDwdDITLIPGNMAIGAARSAEDAYEAARICGEELLHMGINMNFAPSVDVNNNALNPvIGVRSYGERPDLVAELGAAQI 165
Cdd:pfam00933  81 RFG--EGTMFPSAIALAATSDPDLAKQMGWAMAREMRALGIDWDFAPVVDVARDPRWG-IGERSFSEDPQLVSALAGAMI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 166 RGLQEANVAATAKHFPGHGDTAVDSHHGLAAVNHDEERLLAIELAPFIRAIREGVDLIMTAHVMFPAFepNPIPATLSRN 245
Cdd:pfam00933 158 EGLQGAGVLATVKHFPGHGHGATDSHKETPTTPRPEQRLRTVDLLPFQAAIEAGVDAVMAAHVIYSSL--DGTPATGSKY 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 246 VLTNLLRKRLGYNGVIVTDCLEMHAISKEFGIPEGAVRSVEAGADLVLVSHTYEEqvaaiaALVEAVRSGRIPESQIDES 325
Cdd:pfam00933 236 LLTDVLRKKWGFDGIVVSDDLSMKGIADHGGPAEAVRRALEAGVDIALVPEERTK------YLKKVVKNGKLPMARIDAA 309

                  ....*..
gi 2044745824 326 VDRLLSL 332
Cdd:pfam00933 310 VRRVLRL 316
PRK05337 PRK05337
beta-hexosaminidase; Provisional
15-350 5.17e-64

beta-hexosaminidase; Provisional


Pssm-ID: 235417 [Multi-domain]  Cd Length: 337  Bit Score: 212.32  E-value: 5.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  15 MVMCGFHGPVVNDNIRTLIEKHHVGGIIYFRRNVQSKEQVCGLSRELQLISRKhtdiPLFICIDQEGGMVARIDwDDITL 94
Cdd:PRK05337    3 PLMLDVAGTELTAEERERLQHPLVGGVILFARNFEDPAQLRELTAAIRAAVRP----PLLIAVDQEGGRVQRFR-EGFTR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  95 IPGNMAIGAA--RSAEDAYEAARICGE----ELLHMGINMNFAPSVDVNNNalNPVIGVRSYGERPDLVAELGAAQIRGL 168
Cdd:PRK05337   78 LPAMQSFGALwdRDPLEALKLAEEAGWlmaaELRACGIDLSFAPVLDLDGI--SAVIGDRAFHRDPQVVAALASAFIDGM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 169 QEANVAATAKHFPGHGDTAVDSHHGLAAVNHDEERLLAIELAPFIRAIREGVDLIMTAHVMFPAFEPNpiPATLSRNVLT 248
Cdd:PRK05337  156 HAAGMAATGKHFPGHGAVEADSHVETPVDERPLEEIRAEDMAPFRALIAAGLDAVMPAHVIYPQVDPR--PAGFSRYWLQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 249 NLLRKRLGYNGVIVTDCLEMHAISKEFGIPEGAVRSVEAGADLVLVSHTYEEQVAAIAALveavrsgripesQIDESVDR 328
Cdd:PRK05337  234 DILRQELGFDGVIFSDDLSMEGAAVAGDYAERAQAALDAGCDMVLVCNNRDGAVSVLDNL------------SPPISAER 301
                         330       340
                  ....*....|....*....|....
gi 2044745824 329 LLSLKAKR--SMDALpEVTPRFAA 350
Cdd:PRK05337  302 LTRLYGRGafSWQEL-MASPRWKA 324
PRK15098 PRK15098
beta-glucosidase BglX;
4-392 1.75e-24

beta-glucosidase BglX;


Pssm-ID: 185053 [Multi-domain]  Cd Length: 765  Bit Score: 107.85  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824   4 QQLTLEQKIGQMVMCGFHGPVVNDNIRTLIEKHHVGGI---IYFRRNVQSKEQVCGLSRelqlisrkhTDIPLFICIDQE 80
Cdd:PRK15098   43 KKMTLDEKIGQLRLISVGPDNPKEAIREMIKAGQVGAIfntVTRQDIRAMQDQVMQLSR---------LKIPLFFAYDVV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824  81 GGMvaRidwddiTLIPGNMAIGAARSAEDAYEAARICGEELLHMGINMNFAPSVDVNNNalnPVIGVRS--YGERPDLVA 158
Cdd:PRK15098  114 HGQ--R------TVFPISLGLASSWDLDAVATVGRVSAYEAADDGLNMTWAPMVDISRD---PRWGRASegFGEDTYLTS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 159 ELGAAQIRGLQEANVA------ATAKHFPGHGdtAVDSHHGLAAVNHDEERLLAIELAPFIRAIREGVDLIMTAHVMFpa 232
Cdd:PRK15098  183 IMGKTMVKAMQGKSPAdrysvmTSVKHFALYG--AVEGGRDYNTVDMSPQRMFNDYLPPYKAGLDAGSGGVMVALNSL-- 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 233 fepNPIPATLSRNVLTNLLRKRLGYNGVIVTDclemHAISKEF---GI---PEGAVR-SVEAGADLVLVSHTYEEQvaai 305
Cdd:PRK15098  259 ---NGTPATSDSWLLKDLLRDQWGFKGITVSD----HGAIKELikhGVaadPEDAVRlALKSGIDMSMSDEYYSKY---- 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 306 aaLVEAVRSGRIPESQIDESVDRLLSlkAKRSM----DALPEVTPRFAALFGSDAS----KAVVDRICENSITLVKNEGG 377
Cdd:PRK15098  328 --LPGLVKSGKVTMAELDDAVRHVLN--VKYDMglfnDPYSHLGPKESDPVDTNAEsrlhRKEAREVARESLVLLKNRLE 403
                         410
                  ....*....|....*
gi 2044745824 378 SIPLRKEEPTLVIWP 392
Cdd:PRK15098  404 TLPLKKSGTIAVVGP 418
Glyco_hydro_3_C pfam01915
Glycosyl hydrolase family 3 C-terminal domain; This domain is involved in catalysis and may be ...
369-538 1.23e-05

Glycosyl hydrolase family 3 C-terminal domain; This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933.


Pssm-ID: 396478 [Multi-domain]  Cd Length: 216  Bit Score: 46.54  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 369 ITLVKNEGGSIPLRKEEPTL-VIWPEVRQRTE------VDEPIEQSYTL----ATALSPYVDHVEKWRIGTYPEADEVKA 437
Cdd:pfam01915   1 IVLLKNENGLLPLPKKAKKIaVIGPNADDPPNggggsgTGNPPYLVTPLdgirARAGDLYADGAHLTVILSNGTADDDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044745824 438 TLEKAASFKQ---IVVLTYNAVST-----------LHPGQVEIVQGL--IGRPdaQVIVASTRNPYDLNQFPDAQVylcc 501
Cdd:pfam01915  81 IAEAVAAAKDadvAIVFVGLDPETegegydrtdlaLPGNQDALIKAVaaAGKP--TVVVLHSGGPVEMEPWAEENV---- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044745824 502 yenrPATM----------KALAAVLAGKQEARGKLPVTI---------------SPEYPFGH 538
Cdd:pfam01915 155 ----DAILaawypgqeggNAIADVLFGDVNPSGKLPVTFpksledlpaeggpllPDLYPEGY 212
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
299-335 3.46e-03

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 35.78  E-value: 3.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2044745824  299 EEQVAAIAALVEAVRSGRIPESQIDESVDRLLSLKAK 335
Cdd:smart00991   1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQ 37
 
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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