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Conserved domains on  [gi|2111843731|gb|KAH0994712|]
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hypothetical protein GBA52_018576 [Prunus armeniaca]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 288-533 1.27e-179

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


:

Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 513.99  E-value: 1.27e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 288 MHMQLLRTNMVIMFDRTDYGPSNISLPDRQCRHDPNDTLLKVDCTAHSILYDIGTNTLRPLTVQTDTWCSSGAVFPDGTL 367
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 368 VQTGGYNDGDHVVRTFTPCTGDNCDWLEFPNYLVQRRWYASNQILPDGRIIIVGGRRQFNYEFYPRNFQNPPRTFWLDIL 447
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEGQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 448 RQTKDQDENNLYPFLHLLPDGNLFIFANTKSILFNYNQNVVVREFPEIPGGePRNYPSTGSSVLLPLDENKPAnvNIEAE 527
Cdd:pfam07250 161 RETNDPQENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLPGG-PRNYPSSGSSVLLPLDLNNDG--FIEAE 237


                  ....*.
gi 2111843731 528 IMVCGG 533
Cdd:pfam07250 238 VLVCGG 243
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 687-791 1.00e-27

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


:

Pssm-ID: 199882  Cd Length: 103  Bit Score: 107.71  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 687 VRPRIVSVKEVLGYRQFFSVAFAVPEllsVSVLSVRLVAPSFTTHSFAMNQRMIVMKligVTRVAPeTYEISLVGPSTGE 766
Cdd:cd02851     5 PRPTITSAPKTVGYGQTFTVTVSGPG---GGIVRVTLVRPGFVTHSFNMGQRLVKLP---VTGSGG-DYTVTVTAPPNAN 77

                          90       100
                  ....*....|....*....|....*.
gi 2111843731 767 IAPPGYYLLFVVHAD-IPSSAAWVKL 791
Cdd:cd02851    78 VAPPGYYMLFVVNADgVPSVAKWVRV 103
WGG pfam10273
Pre-rRNA-processing protein TSR2; This entry represents the central conserved section of a ...
 15-62 1.15e-17

Pre-rRNA-processing protein TSR2; This entry represents the central conserved section of a family of proteins described as pre-rRNA-processing protein TSR2. The region has a distinctive WGG motif but the function is unknown.


:

Pssm-ID: 463040  Cd Length: 80  Bit Score: 77.97  E-value: 1.15e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2111843731  15 FREGVALVLSRWSALQLAVDNEWGGRDSRRKSEQLAADVFSWFTQSKE 62
Cdd:pfam10273   1 FEEGVSLILSNWTALRLAVENGWGGPDSAEKRDWLAGAVVDLFNENPD 48
NanM super family cl34543
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
568-660 9.87e-03

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG3055:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 38.60  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 568 MEEMPVPRVMADMLLlptgdvviINGAALGTAGWEYGRdPVTKPVIYRPSENpnrRFSVMAGSQRPRLYHSAAVLvPDGR 647
Cdd:COG3055   105 LAPMPTPRGGATALL--------LDGKIYVVGGWDDGG-NVAWVEVYDPATG---TWTQLAPLPTPRDHLAAAVL-PDGK 171

                          90
                  ....*....|....
gi 2111843731 648 VLV-GGSNPHVYYN 660
Cdd:COG3055   172 ILViGGRNGSGFSN 185
 
Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 288-533 1.27e-179

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 513.99  E-value: 1.27e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 288 MHMQLLRTNMVIMFDRTDYGPSNISLPDRQCRHDPNDTLLKVDCTAHSILYDIGTNTLRPLTVQTDTWCSSGAVFPDGTL 367
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 368 VQTGGYNDGDHVVRTFTPCTGDNCDWLEFPNYLVQRRWYASNQILPDGRIIIVGGRRQFNYEFYPRNFQNPPRTFWLDIL 447
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEGQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 448 RQTKDQDENNLYPFLHLLPDGNLFIFANTKSILFNYNQNVVVREFPEIPGGePRNYPSTGSSVLLPLDENKPAnvNIEAE 527
Cdd:pfam07250 161 RETNDPQENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLPGG-PRNYPSSGSSVLLPLDLNNDG--FIEAE 237


                  ....*.
gi 2111843731 528 IMVCGG 533
Cdd:pfam07250 238 VLVCGG 243
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 687-791 1.00e-27

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199882  Cd Length: 103  Bit Score: 107.71  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 687 VRPRIVSVKEVLGYRQFFSVAFAVPEllsVSVLSVRLVAPSFTTHSFAMNQRMIVMKligVTRVAPeTYEISLVGPSTGE 766
Cdd:cd02851     5 PRPTITSAPKTVGYGQTFTVTVSGPG---GGIVRVTLVRPGFVTHSFNMGQRLVKLP---VTGSGG-DYTVTVTAPPNAN 77

                          90       100
                  ....*....|....*....|....*.
gi 2111843731 767 IAPPGYYLLFVVHAD-IPSSAAWVKL 791
Cdd:cd02851    78 VAPPGYYMLFVVNADgVPSVAKWVRV 103
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 695-791 3.28e-27

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


Pssm-ID: 462683  Cd Length: 91  Bit Score: 105.73  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 695 KEVLGYRQFFSVAFAVPellsvSVLSVRLVAPSFTTHSFAMNQRMIVMKligVTRVAPETYEISLVGPSTGEIAPPGYYL 774
Cdd:pfam09118   3 PTTLSYGGTFTVTFGVA-----GNVKVSLIRPGFVTHSVNMGQRLVFLD---VTSTGGTGYTVTVTAPPNPNIAPPGYYM 74

                          90
                  ....*....|....*..
gi 2111843731 775 LFVVHADIPSSAAWVKL 791
Cdd:pfam09118  75 LFVVDNGVPSVGKWVRV 91
WGG pfam10273
Pre-rRNA-processing protein TSR2; This entry represents the central conserved section of a ...
 15-62 1.15e-17

Pre-rRNA-processing protein TSR2; This entry represents the central conserved section of a family of proteins described as pre-rRNA-processing protein TSR2. The region has a distinctive WGG motif but the function is unknown.


Pssm-ID: 463040  Cd Length: 80  Bit Score: 77.97  E-value: 1.15e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2111843731  15 FREGVALVLSRWSALQLAVDNEWGGRDSRRKSEQLAADVFSWFTQSKE 62
Cdd:pfam10273   1 FEEGVSLILSNWTALRLAVENGWGGPDSAEKRDWLAGAVVDLFNENPD 48
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
332-439 1.28e-06

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 50.92  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 332 TAHSILYDIGTNTLRPLTVQTDTWCSSGAVFPDGTLVQTGGYNDGDHV--VRTFTPCTGdncDWLEFPNYLVQRRWYASn 409
Cdd:COG3055    89 LNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVawVEVYDPATG---TWTQLAPLPTPRDHLAA- 164

                          90       100       110
                  ....*....|....*....|....*....|
gi 2111843731 410 QILPDGRIIIVGGRrqfNYEFYPRNFQNPP 439
Cdd:COG3055   165 AVLPDGKILVIGGR---NGSGFSNTWTTLA 191
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
568-660 9.87e-03

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 38.60  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 568 MEEMPVPRVMADMLLlptgdvviINGAALGTAGWEYGRdPVTKPVIYRPSENpnrRFSVMAGSQRPRLYHSAAVLvPDGR 647
Cdd:COG3055   105 LAPMPTPRGGATALL--------LDGKIYVVGGWDDGG-NVAWVEVYDPATG---TWTQLAPLPTPRDHLAAAVL-PDGK 171

                          90
                  ....*....|....
gi 2111843731 648 VLV-GGSNPHVYYN 660
Cdd:COG3055   172 ILViGGRNGSGFSN 185
 
Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 288-533 1.27e-179

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 513.99  E-value: 1.27e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 288 MHMQLLRTNMVIMFDRTDYGPSNISLPDRQCRHDPNDTLLKVDCTAHSILYDIGTNTLRPLTVQTDTWCSSGAVFPDGTL 367
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 368 VQTGGYNDGDHVVRTFTPCTGDNCDWLEFPNYLVQRRWYASNQILPDGRIIIVGGRRQFNYEFYPRNFQNPPRTFWLDIL 447
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEGQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 448 RQTKDQDENNLYPFLHLLPDGNLFIFANTKSILFNYNQNVVVREFPEIPGGePRNYPSTGSSVLLPLDENKPAnvNIEAE 527
Cdd:pfam07250 161 RETNDPQENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLPGG-PRNYPSSGSSVLLPLDLNNDG--FIEAE 237


                  ....*.
gi 2111843731 528 IMVCGG 533
Cdd:pfam07250 238 VLVCGG 243
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 687-791 1.00e-27

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199882  Cd Length: 103  Bit Score: 107.71  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 687 VRPRIVSVKEVLGYRQFFSVAFAVPEllsVSVLSVRLVAPSFTTHSFAMNQRMIVMKligVTRVAPeTYEISLVGPSTGE 766
Cdd:cd02851     5 PRPTITSAPKTVGYGQTFTVTVSGPG---GGIVRVTLVRPGFVTHSFNMGQRLVKLP---VTGSGG-DYTVTVTAPPNAN 77

                          90       100
                  ....*....|....*....|....*.
gi 2111843731 767 IAPPGYYLLFVVHAD-IPSSAAWVKL 791
Cdd:cd02851    78 VAPPGYYMLFVVNADgVPSVAKWVRV 103
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 695-791 3.28e-27

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


Pssm-ID: 462683  Cd Length: 91  Bit Score: 105.73  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 695 KEVLGYRQFFSVAFAVPellsvSVLSVRLVAPSFTTHSFAMNQRMIVMKligVTRVAPETYEISLVGPSTGEIAPPGYYL 774
Cdd:pfam09118   3 PTTLSYGGTFTVTFGVA-----GNVKVSLIRPGFVTHSVNMGQRLVFLD---VTSTGGTGYTVTVTAPPNPNIAPPGYYM 74

                          90
                  ....*....|....*..
gi 2111843731 775 LFVVHADIPSSAAWVKL 791
Cdd:pfam09118  75 LFVVDNGVPSVGKWVRV 91
WGG pfam10273
Pre-rRNA-processing protein TSR2; This entry represents the central conserved section of a ...
 15-62 1.15e-17

Pre-rRNA-processing protein TSR2; This entry represents the central conserved section of a family of proteins described as pre-rRNA-processing protein TSR2. The region has a distinctive WGG motif but the function is unknown.


Pssm-ID: 463040  Cd Length: 80  Bit Score: 77.97  E-value: 1.15e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2111843731  15 FREGVALVLSRWSALQLAVDNEWGGRDSRRKSEQLAADVFSWFTQSKE 62
Cdd:pfam10273   1 FEEGVSLILSNWTALRLAVENGWGGPDSAEKRDWLAGAVVDLFNENPD 48
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
332-439 1.28e-06

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 50.92  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 332 TAHSILYDIGTNTLRPLTVQTDTWCSSGAVFPDGTLVQTGGYNDGDHV--VRTFTPCTGdncDWLEFPNYLVQRRWYASn 409
Cdd:COG3055    89 LNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVawVEVYDPATG---TWTQLAPLPTPRDHLAA- 164

                          90       100       110
                  ....*....|....*....|....*....|
gi 2111843731 410 QILPDGRIIIVGGRrqfNYEFYPRNFQNPP 439
Cdd:COG3055   165 AVLPDGKILVIGGR---NGSGFSNTWTTLA 191
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
568-660 9.87e-03

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 38.60  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111843731 568 MEEMPVPRVMADMLLlptgdvviINGAALGTAGWEYGRdPVTKPVIYRPSENpnrRFSVMAGSQRPRLYHSAAVLvPDGR 647
Cdd:COG3055   105 LAPMPTPRGGATALL--------LDGKIYVVGGWDDGG-NVAWVEVYDPATG---TWTQLAPLPTPRDHLAAAVL-PDGK 171

                          90
                  ....*....|....
gi 2111843731 648 VLV-GGSNPHVYYN 660
Cdd:COG3055   172 ILViGGRNGSGFSN 185
 
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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