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Conserved domains on  [gi|1539618801|emb|VEC79247|]
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mannose-1-phosphate guanylyltransferase [Escherichia coli]

Protein Classification

mannose-1-phosphate guanyltransferase( domain architecture ID 11487805)

mannose-1-phosphate guanyltransferase is involved in the biosynthesis of the capsular polysaccharide colanic acid

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-478 0e+00

mannose-1-phosphate guanyltransferase; Provisional


:

Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 1085.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKGVECESPVVICNEQHRFIVAEQLRQLNKLTE 80
Cdd:PRK15460    1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  81 NIILEPAGRNTAPAIALAALAATRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGY 160
Cdd:PRK15460   81 NIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 161 ILRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLD 240
Cdd:PRK15460  161 IRRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 241 FIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLV 320
Cdd:PRK15460  241 FIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 321 TTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSV 400
Cdd:PRK15460  321 TTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSV 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539618801 401 QMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV 478
Cdd:PRK15460  401 QMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV 478
 
Name Accession Description Interval E-value
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-478 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 1085.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKGVECESPVVICNEQHRFIVAEQLRQLNKLTE 80
Cdd:PRK15460    1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  81 NIILEPAGRNTAPAIALAALAATRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGY 160
Cdd:PRK15460   81 NIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 161 ILRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLD 240
Cdd:PRK15460  161 IRRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 241 FIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLV 320
Cdd:PRK15460  241 FIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 321 TTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSV 400
Cdd:PRK15460  321 TTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSV 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539618801 401 QMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV 478
Cdd:PRK15460  401 QMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV 478
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 6-477 0e+00

mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273648 [Multi-domain]  Cd Length: 468  Bit Score: 902.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   6 LYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILE 85
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  86 PAGRNTAPAIALAALAATRHSpESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYILRGE 165
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARRN-GEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 166 VSAGEqdtVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFIRVD 245
Cdd:TIGR01479 160 PLAGE---DVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLD 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 246 EEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGV 325
Cdd:TIGR01479 237 KEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 326 KDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHH 405
Cdd:TIGR01479 317 EDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHH 396

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539618801 406 RAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGR 477
Cdd:TIGR01479 397 RAEHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
4-357 0e+00

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 553.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   4 SKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKG-VECESPVVICNEQHRFIVAEQLRQLNKltENI 82
Cdd:COG0836     1 SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAGlVPPENILVVTNEEHRFLVAEQLPELGP--ANI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  83 ILEPAGRNTAPAIALAALAATRHSPesDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIL 162
Cdd:COG0836    79 LLEPVGRNTAPAIALAALLIAKRDP--DAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 163 RGEVSAGEQdtvAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDfI 242
Cdd:COG0836   157 AGEALGGAG---AYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLE-V 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 243 RVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTT 322
Cdd:COG0836   233 RLDAEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAV 312

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1539618801 323 VGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKA 357
Cdd:COG0836   313 IGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALKE 347
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 6-286 3.19e-142

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 408.50  E-value: 3.19e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   6 LYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKG-VECESPVVICNEQHRFIVAEQLRQLNKlTENIIL 84
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGlVPPDRILVVTNEEYRFLVREQLPEGLP-EENIIL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  85 EPAGRNTAPAIALAALAATRHSPesDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYILRG 164
Cdd:cd02509    80 EPEGRNTAPAIALAALYLAKRDP--DAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 165 EVSAGEqdtvAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDlDFIRV 244
Cdd:cd02509   158 EKLGGG----VYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTD-DFLRL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1539618801 245 DEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSL 286
Cdd:cd02509   233 LEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 323-473 2.99e-98

Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.


Pssm-ID: 426015 [Multi-domain]  Cd Length: 151  Bit Score: 292.01  E-value: 2.99e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 323 VGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQM 402
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539618801 403 HHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFAD 473
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVRFED 151
 
Name Accession Description Interval E-value
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-478 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 1085.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKGVECESPVVICNEQHRFIVAEQLRQLNKLTE 80
Cdd:PRK15460    1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  81 NIILEPAGRNTAPAIALAALAATRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGY 160
Cdd:PRK15460   81 NIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 161 ILRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLD 240
Cdd:PRK15460  161 IRRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 241 FIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLV 320
Cdd:PRK15460  241 FIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 321 TTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSV 400
Cdd:PRK15460  321 TTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSV 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539618801 401 QMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV 478
Cdd:PRK15460  401 QMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV 478
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 6-477 0e+00

mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273648 [Multi-domain]  Cd Length: 468  Bit Score: 902.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   6 LYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILE 85
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  86 PAGRNTAPAIALAALAATRHSpESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYILRGE 165
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARRN-GEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 166 VSAGEqdtVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFIRVD 245
Cdd:TIGR01479 160 PLAGE---DVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLD 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 246 EEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGV 325
Cdd:TIGR01479 237 KEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 326 KDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHH 405
Cdd:TIGR01479 317 EDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHH 396

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539618801 406 RAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGR 477
Cdd:TIGR01479 397 RAEHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
4-357 0e+00

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 553.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   4 SKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKG-VECESPVVICNEQHRFIVAEQLRQLNKltENI 82
Cdd:COG0836     1 SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAGlVPPENILVVTNEEHRFLVAEQLPELGP--ANI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  83 ILEPAGRNTAPAIALAALAATRHSPesDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIL 162
Cdd:COG0836    79 LLEPVGRNTAPAIALAALLIAKRDP--DAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 163 RGEVSAGEQdtvAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDfI 242
Cdd:COG0836   157 AGEALGGAG---AYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLE-V 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 243 RVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTT 322
Cdd:COG0836   233 RLDAEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAV 312

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1539618801 323 VGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKA 357
Cdd:COG0836   313 IGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALKE 347
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 6-286 3.19e-142

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 408.50  E-value: 3.19e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   6 LYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLKG-VECESPVVICNEQHRFIVAEQLRQLNKlTENIIL 84
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGlVPPDRILVVTNEEYRFLVREQLPEGLP-EENIIL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  85 EPAGRNTAPAIALAALAATRHSPesDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYILRG 164
Cdd:cd02509    80 EPEGRNTAPAIALAALYLAKRDP--DAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 165 EVSAGEqdtvAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDlDFIRV 244
Cdd:cd02509   158 EKLGGG----VYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTD-DFLRL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1539618801 245 DEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSL 286
Cdd:cd02509   233 LEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 323-473 2.99e-98

Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.


Pssm-ID: 426015 [Multi-domain]  Cd Length: 151  Bit Score: 292.01  E-value: 2.99e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 323 VGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQM 402
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539618801 403 HHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFAD 473
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVRFED 151
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 8-294 1.38e-80

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 250.25  E-value: 1.38e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   8 PVVMAGGSGSRLWPLSRVLYPKQFLCLKGDlTMLQTTICRLKGVECESPVVICNEQHRFIVAEQLRQLNKL--TENIILE 85
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKY-PLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFgvQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  86 PAGRNTAPAIALAALAATRHSPEsdplMLVLAADHVIadEDAFRAAVRNAMPYAeAGKLVTFGIVPDLPETGYGYILRGE 165
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSD----VLVLGGDHIY--RMDLEQAVKFHIEKA-ADATVTFGIVPVEPPTGYGVVEFDD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 166 vsageqdtvAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAgRYLEELKKYRPDILDACEKAMSAVDPDLDFIRVD 245
Cdd:pfam00483 154 ---------NGRVIRFVEKPKLPKASNYASMGIYIFNSGVLDFLA-KYLEELKRGEDEITDILPKALEDGKLAYAFIFKG 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1539618801 246 EEaflacpeesvdyavmertadavvvpmdagWSDVGSWSSLWEISAHTA 294
Cdd:pfam00483 224 YA-----------------------------WLDVGTWDSLWEANLFLL 243
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 345-471 1.97e-69

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 217.04  E-value: 1.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 345 VQDVKKVVEQIKADGRHEHrvHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGD 424
Cdd:cd02213     2 SQRVKEIVEELKKRGRSEE--HRTVYRPWGSYEVLDEGEGYKVKRLTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTLDGK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1539618801 425 IKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRF 471
Cdd:cd02213    80 EKLLKEGESIYIPKGTKHRLENPGKIPLEIIEVQTGEYLGEDDIVRL 126
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
371-470 1.58e-36

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 130.65  E-value: 1.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 371 RPWGKYDSI-DAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGK 449
Cdd:COG0662    12 IGWGSYEVLgEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGD 91

                          90       100
                  ....*....|....*....|.
gi 1539618801 450 IPLDLIEVRSGSYLEEDDVVR 470
Cdd:COG0662    92 EPLELLEVQAPAYLGEDDIVR 112
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 367-466 5.80e-12

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 61.76  E-value: 5.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 367 REVYRPwgkydSIDAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLEN 446
Cdd:cd02214     6 RELLHP-----DNDGDPRYSLAHARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIEN 80

                          90       100
                  ....*....|....*....|
gi 1539618801 447 PGKIPLDLIEVRSGSYLEED 466
Cdd:cd02214    81 TGEEDLVFLCICSPAWSPED 100
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 389-457 5.36e-10

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 55.34  E-value: 5.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539618801 389 RITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEV 457
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 380-455 1.62e-09

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 54.76  E-value: 1.62e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539618801 380 DAGDRYQVKRITVKPGeGLSvQMHHHRAEHWV-VVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLI 455
Cdd:cd02222    12 DGAPNFAMRYFEIEPG-GHT-PLHTHPWEHEVyVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPLGFL 86
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
379-457 2.39e-09

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 54.47  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 379 IDAGDRYQVKRITVKPGEglSVQMHHHRA-EHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEV 457
Cdd:COG1917    17 ADGEDELEVVRVTFEPGA--RTPWHSHPGeELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVV 94
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
382-473 1.66e-08

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 52.71  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 382 GDRYQVKRITVKPGEGlSVQMHHHRA--EHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVrs 459
Cdd:COG3837    25 LTRLGVNLITLPPGAS-SSPYHAHSAeeEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVV-- 101

                          90
                  ....*....|....
gi 1539618801 460 GSYLEEDDVVRFAD 473
Cdd:COG3837   102 GTRAPYPDSFDYWD 115
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 382-454 6.80e-08

Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold.


Pssm-ID: 380352 [Multi-domain]  Cd Length: 98  Bit Score: 50.24  E-value: 6.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539618801 382 GDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDL 454
Cdd:cd02223     8 GKNLQLVLMSIPPGEDIGLEVHDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWHNVINTGNEPLKL 80
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 390-455 2.70e-07

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 48.83  E-value: 2.70e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539618801 390 ITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLI 455
Cdd:cd06991    24 LTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARLV 89
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 389-458 2.85e-07

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 47.86  E-value: 2.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539618801 389 RITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIK-LLGENESIYIPLGATHCLENPGKIPLDLIEVR 458
Cdd:cd02208     3 VVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGETvELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 390-452 3.43e-07

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 47.62  E-value: 3.43e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539618801 390 ITVKPGEGlSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPL 452
Cdd:cd06988     7 CVVRPGTT-STPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVKNDGDEDF 68
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 389-455 4.69e-07

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.


Pssm-ID: 380350 [Multi-domain]  Cd Length: 93  Bit Score: 47.85  E-value: 4.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539618801 389 RITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLI 455
Cdd:cd02221    23 RVTLPPGSSIGYHQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 389-451 8.09e-07

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 47.12  E-value: 8.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539618801 389 RITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIP 451
Cdd:cd02209    20 LVTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEP 82
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 9-281 1.68e-06

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 48.73  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   9 VVMAGGSGSRLWPLSRVLyPKQFLCLkGDLTMLQTTICRLKGVECESPVVICNEQHRFIVaEQLRQLNKLTENI--ILEP 86
Cdd:cd04181     2 VILAAGKGTRLRPLTDTR-PKPLLPI-AGKPILEYIIERLARAGIDEIILVVGYLGEQIE-EYFGDGSKFGVNIeyVVQE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  87 AGRNTapaiaLAALAATRHSPESDPLmLVLAADhVIADEDaFRAAVRNAMpyaEAGKLVTFGIVPDLPETGYGYILRGEV 166
Cdd:cd04181    79 EPLGT-----AGAVRNAEDFLGDDDF-LVVNGD-VLTDLD-LSELLRFHR---EKGADATIAVKEVEDPSRYGVVELDDD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 167 SageqdtvafEVAQFVEKPNLETAqayvasgeYYWNSGMFLFragryleelkkyRPDILDACekamsavdPDLDFIRVDE 246
Cdd:cd04181   148 G---------RVTRFVEKPTLPES--------NLANAGIYIF------------EPEILDYI--------PEILPRGEDE 190

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1539618801 247 EAFLacpeesvdYAVMERTADAVVVPMDAGWSDVG 281
Cdd:cd04181   191 LTDA--------IPLLIEEGKVYGYPVDGYWLDIG 217
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 9-298 1.03e-05

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 46.68  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801   9 VVMAGGSGSRLWPLSRVLyPKQFLCLkGDLTMLQTTICRLK--GVEcespvvicneqhRFIV-----AEQLR-------- 73
Cdd:COG1208     3 VILAGGLGTRLRPLTDTR-PKPLLPV-GGKPLLEHILERLAaaGIT------------EIVInvgylAEQIEeyfgdgsr 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801  74 ---QLNKLTENIILEPAGRntapaialaaLAATRHSPESDPLmLVLAADhVIADEDaFRAAVRNampYAEAGKLVTFGIV 150
Cdd:COG1208    69 fgvRITYVDEGEPLGTGGA----------LKRALPLLGDEPF-LVLNGD-ILTDLD-LAALLAF---HREKGADATLALV 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 151 PDLPETGYGYIlrgEVSAGEQdtvafeVAQFVEKPNlETAQAYVasgeyywNSGMFLFragryleelkkyRPDILDACEK 230
Cdd:COG1208   133 PVPDPSRYGVV---ELDGDGR------VTRFVEKPE-EPPSNLI-------NAGIYVL------------EPEIFDYIPE 183

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539618801 231 amsavDPDLDFirvdEEAFlacpeesvdyavmERTADA---VVVPMDAGWSDVGSWSSLWEISAHTAEGNV 298
Cdd:COG1208   184 -----GEPFDL----EDLL-------------PRLIAEgrvYGYVHDGYWLDIGTPEDLLEANALLLSGKA 232
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 388-462 1.36e-04

Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380367 [Multi-domain]  Cd Length: 145  Bit Score: 42.08  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 388 KRITVKPGeGLSvQMHHHRAEH-W-VVVAGTAKVTI---DG--DIKLLGENESIYIPLGATHCLENPGKIPLDLIEV-RS 459
Cdd:cd02240    30 ALVRVAPG-AMR-ELHWHPNTAeWqYVISGSARVTVfdeDGrfETFNLGAGDVGYVPSGSGHHIENIGDEDAEFLLIfDD 107


                  ...
gi 1539618801 460 GSY 462
Cdd:cd02240   108 GTF 110
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
390-451 1.57e-04

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 43.27  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539618801 390 ITVKPGEGLSVQMHHHRAEHWV-VVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIP 451
Cdd:COG3257    64 VEVAPGGGSDRPEPDPGAETFLfVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEP 126
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 380-446 2.27e-04

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.


Pssm-ID: 380384 [Multi-domain]  Cd Length: 93  Bit Score: 40.14  E-value: 2.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539618801 380 DAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVV-AGTAKVTIDGDIKLLGENESIYIPLGATHCLEN 446
Cdd:cd06979    12 GTADRFDLFEFEVSPNAGMPPPHYHEDWEETIYGlEGSVTLTLPGKTVEVGPGDSIFIPRGEVHGFVN 79
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 382-445 2.94e-04

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 40.15  E-value: 2.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539618801 382 GDRYQVKRITVKPGEglSVQMHHHRAEHWV-VVAGTAKVTIDGDIKLLGENESIYIPLGATH---CLE 445
Cdd:cd02238    24 GEKLMLVEVRFEKGA--VVPLHSHPHEQIGyVLSGRFEFTIGGETRILKPGDSYYIPPNVPHgaeALE 89
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 390-451 5.18e-04

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.


Pssm-ID: 380341 [Multi-domain]  Cd Length: 117  Bit Score: 39.81  E-value: 5.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539618801 390 ITVKPGEGLSVQMHHHRAEHWV-VVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIP 451
Cdd:cd02211    30 VEVEPGGGSTAPEGGEGIERFLyVLEGEVELTVGGETHTLTAGGYAYLPPGTKHSLRNAGDEP 92
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 384-473 7.91e-04

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380353 [Multi-domain]  Cd Length: 105  Bit Score: 39.01  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 384 RYQVKRITVKPGeGLSVQMHHHRA--EHWVVVAGTAKVTIDGDIKLLGENESIYIP--LGATHCLENPGKIPLDLIEVRS 459
Cdd:cd02224    16 QLGVNLERLPPG-ARSSPRHWHSAeeEFVYVLSGEGTLRLDGEEVLPRPGDFVGFPagTGVAHQLINRSDEPLVYLVVGT 94

                          90
                  ....*....|....
gi 1539618801 460 GsylEEDDVVRFAD 473
Cdd:cd02224    95 R---LPDDVCTYPD 105
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 9-49 1.75e-03

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 39.80  E-value: 1.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1539618801   9 VVMAGGSGSRLWPLSRVLyPKQFLCLkGDLTMLQTTICRLK 49
Cdd:cd06426     2 VIMAGGKGTRLRPLTENT-PKPMLKV-GGKPILETIIDRFI 40
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 403-473 3.26e-03

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 37.25  E-value: 3.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539618801 403 HHHRAEHWVVVAGTAKVTI---DGDIKL--LGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFAD 473
Cdd:COG2140    21 HPNAAEWYYVLSGEARMTVqdpPGRARTvdVGPGDVVYVPPGYGHYIINTGDEPLVFLAVFDDDAGSDYGTISLSG 96
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 9-76 6.65e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 38.19  E-value: 6.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539618801   9 VVMAGGSGSRLwplsRVLYPKQFLCLKGdLTMLQTTICRLKGVECESPVVI-CNEQHRFIVAEQLRQLN 76
Cdd:COG1211     1 IIPAAGSGSRM----GAGIPKQFLPLGG-KPVLEHTLEAFLAHPRIDEIVVvVPPDDIEYFEELLAKYG 64
cupin_YP766765-like cd20299
Rhizobium leguminosarum YP_766765.1 and related proteins, cupin domain; This family includes ...
 411-448 7.93e-03

Rhizobium leguminosarum YP_766765.1 and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to Rhizobium leguminosarum YP_766765.1, a protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380433 [Multi-domain]  Cd Length: 90  Bit Score: 35.72  E-value: 7.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1539618801 411 VVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPG 448
Cdd:cd20299    42 VVLEGELTVTTDGEEVVLGPGDSCYIPPGETRSIDNRT 79
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
 393-452 8.06e-03

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin (cupa is the Latin term for small barrel).


Pssm-ID: 380377 [Multi-domain]  Cd Length: 102  Bit Score: 36.00  E-value: 8.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539618801 393 KPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPL 452
Cdd:cd06122    35 EPGQSQKVHAHAGSDKVYFVLEGEGRFTVGDEERELGAGEAVLAPAGVPHGVRNTGAERL 94
 
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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