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Conserved domains on  [gi|690618410|gb|AIQ19623|]
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hypothetical protein H70357_25105 [Paenibacillus sp. FSL H7-0357]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YddW COG1649
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];
195-552 2.81e-157

Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];


:

Pssm-ID: 441255 [Multi-domain]  Cd Length: 451  Bit Score: 456.86  E-value: 2.81e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 195 MKGAWISTVfnldwpstssANNADKQKKEFNTMLDKLQATGYNAVFVQVRPSGDSLYPSVLVPWSKVLTGTQGKNPGYDP 274
Cdd:COG1649   33 IRGVWLTTV----------DLSVLKQKAELIEILDRLKELGFNAVFFQVRPAGDALYPSAIEPWSEYLTGTQGKDPGYDP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 275 LEYMVSSTHERGMEFHAWFNPFRATTDASTSSLASNHVAKAHPEWIVKAE--NKLYINPGIPEARQHIIDTVMEVVKGYD 352
Cdd:COG1649  103 LAFAIEEAHKRGLEVHAWFNPYRAAPNTDVSPLAPSHIAKKHPEWLTKYRdgGKLWLNPGHPEVRDFILDLVLEVVTRYD 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 353 IDGVHLDDYFYPSGSFADDTAFNTYNA------KAISSKGDWRRDNINEFIRQLGQEIHSAKSDVSYGVSPFGVWRNkka 426
Cdd:COG1649  183 VDGIHFDDYFYPSEFGYDDATYALYGQetgfdnPKDLSWADWRRDNVNRFVRRLYQAIKAVKPDVKFSISPFGIWRN--- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 427 dstgSDTtaGVSAYDDMYADTRTWIKNGWIDYIAPQIYWSLSFSAARYDKLVDWWVNEVKGTGVKLYIGQAAYKVGAsdq 506
Cdd:COG1649  260 ----SPT--GLFAYDDLYQDWRTWVKEGWVDYIVPQLYWPDGNSAADFEKLLDWWAQQAKGRKVPLYIGIGLYKVPP--- 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 690618410 507 kaewqsgEQIINQLKYNEQYDEVAGSIMFRANDIvvRDPFGLSSLL 552
Cdd:COG1649  331 -------EEILRQIQLNRDLPGVAGVVFFSYESL--WNNPGLADAL 367
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
52-142 2.19e-28

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


:

Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 108.46  E-value: 2.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410   52 NVTLVPVAVVSRGLGATVDWNQSSKTATISKGSTVLKLTSGSTTALVDGASISLETSVQSRQGRVMVPLRFVGEQLGLQV 131
Cdd:pfam07833   3 GRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLINGRTYVPLRFVAEALGAKV 82
                          90
                  ....*....|.
gi 690618410  132 AWNKAANNIAL 142
Cdd:pfam07833  83 DWDEATRTVYI 93
 
Name Accession Description Interval E-value
YddW COG1649
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];
195-552 2.81e-157

Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];


Pssm-ID: 441255 [Multi-domain]  Cd Length: 451  Bit Score: 456.86  E-value: 2.81e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 195 MKGAWISTVfnldwpstssANNADKQKKEFNTMLDKLQATGYNAVFVQVRPSGDSLYPSVLVPWSKVLTGTQGKNPGYDP 274
Cdd:COG1649   33 IRGVWLTTV----------DLSVLKQKAELIEILDRLKELGFNAVFFQVRPAGDALYPSAIEPWSEYLTGTQGKDPGYDP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 275 LEYMVSSTHERGMEFHAWFNPFRATTDASTSSLASNHVAKAHPEWIVKAE--NKLYINPGIPEARQHIIDTVMEVVKGYD 352
Cdd:COG1649  103 LAFAIEEAHKRGLEVHAWFNPYRAAPNTDVSPLAPSHIAKKHPEWLTKYRdgGKLWLNPGHPEVRDFILDLVLEVVTRYD 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 353 IDGVHLDDYFYPSGSFADDTAFNTYNA------KAISSKGDWRRDNINEFIRQLGQEIHSAKSDVSYGVSPFGVWRNkka 426
Cdd:COG1649  183 VDGIHFDDYFYPSEFGYDDATYALYGQetgfdnPKDLSWADWRRDNVNRFVRRLYQAIKAVKPDVKFSISPFGIWRN--- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 427 dstgSDTtaGVSAYDDMYADTRTWIKNGWIDYIAPQIYWSLSFSAARYDKLVDWWVNEVKGTGVKLYIGQAAYKVGAsdq 506
Cdd:COG1649  260 ----SPT--GLFAYDDLYQDWRTWVKEGWVDYIVPQLYWPDGNSAADFEKLLDWWAQQAKGRKVPLYIGIGLYKVPP--- 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 690618410 507 kaewqsgEQIINQLKYNEQYDEVAGSIMFRANDIvvRDPFGLSSLL 552
Cdd:COG1649  331 -------EEILRQIQLNRDLPGVAGVVFFSYESL--WNNPGLADAL 367
GHL10 pfam02638
Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins ...
195-512 3.09e-93

Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,.


Pssm-ID: 251441 [Multi-domain]  Cd Length: 311  Bit Score: 287.96  E-value: 3.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  195 MKGAWISTVFNLDWPstssannADKQKKEfntMLDKLQATGYNAVFVQVRPSGDSLYPSVLVPWSKVLTGTQGKNPGYDP 274
Cdd:pfam02638   2 IRGVWLTNVDSNDWP-------DPVQLQE---AIALLDDLNFNTVYPQVWNDGHALYPSAVAPWSGLKTGEKGGDPGYDP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  275 LEYMVSSTHERGMEFHAWFN-PFRATTDASTSSLASNHVAKAHPEWIVKAE----NKLYINPGIPEARQHIIDTVMEVVK 349
Cdd:pfam02638  72 LAFMIDEAHKRNLRVHPWFEfGFNAPALSDLVKAHPAWLTTQHRDWTITSEggtgPRVWLNPGHPEVQDFITALVVDVVR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  350 GYDIDGVHLDDYFYPSGSFADD----------TAFNTYNAKAISSKGDWRRDNINEFIRQLGQEIHSAKSDVSYGVSPFG 419
Cdd:pfam02638 152 RYDVDGVQFDDHFYYPYSFGYDpitvalyrqeTKQEPFSNPEDDLNTDWRRDKISQLVQQLNPTIKAAKPNVTFSISPAG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  420 VWRnkkadstgsdttagvSAYDDMYADTRTWIKNGWIDYIAPQIYW-SLSFSAARYDKLVDWWVNEVKGTGVKLYIGQAA 498
Cdd:pfam02638 232 VWN---------------FAYNCFLADWRTWIEAGVIDEIAPQVYReKQAAFTAEYQVLAVWWSKQVIPTVVGILIGLAN 296
                         330
                  ....*....|....*
gi 690618410  499 YKVG-ASDQKAEWQS 512
Cdd:pfam02638 297 YKIPsPIKQDPQWVD 311
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
52-142 2.19e-28

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 108.46  E-value: 2.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410   52 NVTLVPVAVVSRGLGATVDWNQSSKTATISKGSTVLKLTSGSTTALVDGASISLETSVQSRQGRVMVPLRFVGEQLGLQV 131
Cdd:pfam07833   3 GRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLINGRTYVPLRFVAEALGAKV 82
                          90
                  ....*....|.
gi 690618410  132 AWNKAANNIAL 142
Cdd:pfam07833  83 DWDEATRTVYI 93
GH36 cd14791
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
275-377 1.74e-11

glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269892 [Multi-domain]  Cd Length: 299  Bit Score: 65.32  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 275 LEYMVSSTHERGMEFHAWFNPFRATTDAstsslasnHVAKAHPEWIVKAENK--------LYINPGIPEARQHIIDTVME 346
Cdd:cd14791   67 LKALADRIHALGMKFGLWLEPEMVGPDS--------ELYREHPDWLLKDPGGppvtgrnqYVLDLSNPEVRDYLREVIDR 138
                         90       100       110
                 ....*....|....*....|....*....|...
gi 690618410 347 VVKGYDIDGVHLD--DYFYPSGSFADDTAFNTY 377
Cdd:cd14791  139 LLREWGIDYLKWDfnRAGAEGGSRALDSQGEGL 171
tynA PRK14696
primary-amine oxidase;
55-129 1.92e-06

primary-amine oxidase;


Pssm-ID: 184793 [Multi-domain]  Cd Length: 721  Bit Score: 50.59  E-value: 1.92e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 690618410  55 LVPVAVVSRGLGATVDWNQSSKTATISKGSTVLKLTSGSTTALVDGASISLETSVQSRQGRVMVPLRFVGE--QLGL 129
Cdd:PRK14696   1 MVPLDKTLKEFGADVQWDDYAQTFTIIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDGKAWVSDTFINDvfQSGL 77
 
Name Accession Description Interval E-value
YddW COG1649
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];
195-552 2.81e-157

Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown];


Pssm-ID: 441255 [Multi-domain]  Cd Length: 451  Bit Score: 456.86  E-value: 2.81e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 195 MKGAWISTVfnldwpstssANNADKQKKEFNTMLDKLQATGYNAVFVQVRPSGDSLYPSVLVPWSKVLTGTQGKNPGYDP 274
Cdd:COG1649   33 IRGVWLTTV----------DLSVLKQKAELIEILDRLKELGFNAVFFQVRPAGDALYPSAIEPWSEYLTGTQGKDPGYDP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 275 LEYMVSSTHERGMEFHAWFNPFRATTDASTSSLASNHVAKAHPEWIVKAE--NKLYINPGIPEARQHIIDTVMEVVKGYD 352
Cdd:COG1649  103 LAFAIEEAHKRGLEVHAWFNPYRAAPNTDVSPLAPSHIAKKHPEWLTKYRdgGKLWLNPGHPEVRDFILDLVLEVVTRYD 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 353 IDGVHLDDYFYPSGSFADDTAFNTYNA------KAISSKGDWRRDNINEFIRQLGQEIHSAKSDVSYGVSPFGVWRNkka 426
Cdd:COG1649  183 VDGIHFDDYFYPSEFGYDDATYALYGQetgfdnPKDLSWADWRRDNVNRFVRRLYQAIKAVKPDVKFSISPFGIWRN--- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 427 dstgSDTtaGVSAYDDMYADTRTWIKNGWIDYIAPQIYWSLSFSAARYDKLVDWWVNEVKGTGVKLYIGQAAYKVGAsdq 506
Cdd:COG1649  260 ----SPT--GLFAYDDLYQDWRTWVKEGWVDYIVPQLYWPDGNSAADFEKLLDWWAQQAKGRKVPLYIGIGLYKVPP--- 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 690618410 507 kaewqsgEQIINQLKYNEQYDEVAGSIMFRANDIvvRDPFGLSSLL 552
Cdd:COG1649  331 -------EEILRQIQLNRDLPGVAGVVFFSYESL--WNNPGLADAL 367
GHL10 pfam02638
Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins ...
195-512 3.09e-93

Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,.


Pssm-ID: 251441 [Multi-domain]  Cd Length: 311  Bit Score: 287.96  E-value: 3.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  195 MKGAWISTVFNLDWPstssannADKQKKEfntMLDKLQATGYNAVFVQVRPSGDSLYPSVLVPWSKVLTGTQGKNPGYDP 274
Cdd:pfam02638   2 IRGVWLTNVDSNDWP-------DPVQLQE---AIALLDDLNFNTVYPQVWNDGHALYPSAVAPWSGLKTGEKGGDPGYDP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  275 LEYMVSSTHERGMEFHAWFN-PFRATTDASTSSLASNHVAKAHPEWIVKAE----NKLYINPGIPEARQHIIDTVMEVVK 349
Cdd:pfam02638  72 LAFMIDEAHKRNLRVHPWFEfGFNAPALSDLVKAHPAWLTTQHRDWTITSEggtgPRVWLNPGHPEVQDFITALVVDVVR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  350 GYDIDGVHLDDYFYPSGSFADD----------TAFNTYNAKAISSKGDWRRDNINEFIRQLGQEIHSAKSDVSYGVSPFG 419
Cdd:pfam02638 152 RYDVDGVQFDDHFYYPYSFGYDpitvalyrqeTKQEPFSNPEDDLNTDWRRDKISQLVQQLNPTIKAAKPNVTFSISPAG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  420 VWRnkkadstgsdttagvSAYDDMYADTRTWIKNGWIDYIAPQIYW-SLSFSAARYDKLVDWWVNEVKGTGVKLYIGQAA 498
Cdd:pfam02638 232 VWN---------------FAYNCFLADWRTWIEAGVIDEIAPQVYReKQAAFTAEYQVLAVWWSKQVIPTVVGILIGLAN 296
                         330
                  ....*....|....*
gi 690618410  499 YKVG-ASDQKAEWQS 512
Cdd:pfam02638 297 YKIPsPIKQDPQWVD 311
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
52-142 2.19e-28

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 108.46  E-value: 2.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410   52 NVTLVPVAVVSRGLGATVDWNQSSKTATISKGSTVLKLTSGSTTALVDGASISLETSVQSRQGRVMVPLRFVGEQLGLQV 131
Cdd:pfam07833   3 GRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNGQEITLDVPPVLINGRTYVPLRFVAEALGAKV 82
                          90
                  ....*....|.
gi 690618410  132 AWNKAANNIAL 142
Cdd:pfam07833  83 DWDEATRTVYI 93
GH36 cd14791
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
275-377 1.74e-11

glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269892 [Multi-domain]  Cd Length: 299  Bit Score: 65.32  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 275 LEYMVSSTHERGMEFHAWFNPFRATTDAstsslasnHVAKAHPEWIVKAENK--------LYINPGIPEARQHIIDTVME 346
Cdd:cd14791   67 LKALADRIHALGMKFGLWLEPEMVGPDS--------ELYREHPDWLLKDPGGppvtgrnqYVLDLSNPEVRDYLREVIDR 138
                         90       100       110
                 ....*....|....*....|....*....|...
gi 690618410 347 VVKGYDIDGVHLD--DYFYPSGSFADDTAFNTY 377
Cdd:cd14791  139 LLREWGIDYLKWDfnRAGAEGGSRALDSQGEGL 171
GalA COG3345
Alpha-galactosidase [Carbohydrate transport and metabolism];
273-360 2.78e-11

Alpha-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442574 [Multi-domain]  Cd Length: 219  Bit Score: 63.46  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410 273 DPLEYMVSSTHERGMEFHAWFNPFRATTDAstsslasnHVAKAHPEWIVKAENK--------LYINPGIPEARQHIIDTV 344
Cdd:COG3345   97 NGLKPLADRIHALGMKFGLWVEPEMVNPDS--------DLYREHPDWVLKDPDGepvegrnqYVLDLSNPEVRDYLFEVL 168
                         90
                 ....*....|....*.
gi 690618410 345 MEVVKGYDIDGVHLDD 360
Cdd:COG3345  169 DRLLAEWGIDYIKWDF 184
Melibiase pfam02065
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
273-359 3.32e-07

Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.


Pssm-ID: 307952  Cd Length: 347  Bit Score: 52.40  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  273 DPLEYMVSSTHERGMEFHAWFNPFRATTDAStsslasnhVAKAHPEWIVKAE--------NKLYINPGIPEARQHIIDTV 344
Cdd:pfam02065 104 NGLDPLAKQVHALGMQFGLWFEPEMVNPNSD--------LYRQHPDWVLHVPgrprtegrNQLVLDLSRPDVVDYIIETL 175
                          90
                  ....*....|....*
gi 690618410  345 MEVVKGYDIDGVHLD 359
Cdd:pfam02065 176 DNLLQEAPIDYVKWD 190
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
32-80 8.82e-07

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 47.21  E-value: 8.82e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 690618410   32 TIELDGKLLSSDVPPYITaSNVTLVPVAVVSRGLGATVDWNQSSKTATI 80
Cdd:pfam07833  46 TATVNGQEITLDVPPVLI-NGRTYVPLRFVAEALGAKVDWDEATRTVYI 93
tynA PRK14696
primary-amine oxidase;
55-129 1.92e-06

primary-amine oxidase;


Pssm-ID: 184793 [Multi-domain]  Cd Length: 721  Bit Score: 50.59  E-value: 1.92e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 690618410  55 LVPVAVVSRGLGATVDWNQSSKTATISKGSTVLKLTSGSTTALVDGASISLETSVQSRQGRVMVPLRFVGE--QLGL 129
Cdd:PRK14696   1 MVPLDKTLKEFGADVQWDDYAQTFTIIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDGKAWVSDTFINDvfQSGL 77
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
113-149 1.02e-04

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 41.43  E-value: 1.02e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 690618410  113 QGRVMVPLRFVGEQLGLQVAWNKAANNIAL-YSNTEII 149
Cdd:pfam07833   2 NGRTLVPLRAIAEALGAKVDWDGKTKTVTItKGGTTIK 39
GHL6 pfam14871
Hypothetical glycosyl hydrolase 6; GHL6 is a family of hypothetical glycoside hydrolases.
226-359 6.95e-04

Hypothetical glycosyl hydrolase 6; GHL6 is a family of hypothetical glycoside hydrolases.


Pssm-ID: 405546 [Multi-domain]  Cd Length: 135  Bit Score: 40.09  E-value: 6.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690618410  226 TMLDKLQATGYNAVFVQVR-PSGDSLYPSvlvpwsKVLTGTQGKNPGYDPLEYMVSSTHERGMEFHAWFnpfrattdasT 304
Cdd:pfam14871   4 ELAELAKEAGANTLVIFARdAGGVVWYRT------KLPFFPEHPYLTRDLLKEAVKACHRRGIKVVVRV----------D 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 690618410  305 SSLASNHVAKAHPEWIVKAENK---------LYINPGIP---EARQHIIDTVMEVVKGYDIDGVHLD 359
Cdd:pfam14871  68 FSKADHRIYEQHPDWAAVDPNGeppggeppgYPGWPTLCinsGYQEFLAPVLEEALKRYPLDGIFLD 134
 
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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