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Conserved domains on  [gi|306530536|gb|ADN00467|]
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Exo-poly-alpha-D-galacturonosidase precursor [Dickeya dadantii 3937]

Protein Classification

FN3 and Pgu1 domain-containing protein( domain architecture ID 11509404)

FN3 and Pgu1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pgu1 COG5434
Polygalacturonase [Carbohydrate transport and metabolism];
149-562 1.76e-120

Polygalacturonase [Carbohydrate transport and metabolism];


:

Pssm-ID: 444185 [Multi-domain]  Cd Length: 373  Bit Score: 361.45  E-value: 1.76e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 149 PQVINITQYGAKGDGTTLNTTAIQKAIDAC--QTGCRVDIPAGVFKTGALWLKSDMTLNLLQGATLLGSDNAADYPDAYK 226
Cdd:COG5434    7 AKTFNITDFGAKGDGKTLNTAAIQKAIDACaaAGGGTVLVPAGTYLTGPIFLKSNVTLHLEKGATLLGSTDPADYPLVET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 227 IYSYSSQVRPASLINAIDktssavgtFKNIRIIGKGVIDGNGWKRSADAKDelgnslpqyvksdsskvskdgilaknqva 306
Cdd:COG5434   87 RWEGGELKGYSALIYAEN--------AENIAITGEGTIDGNGDAWWPWKKE----------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 307 aAVAKGMDTKTAYSQRRSSLVTLRGVKNVYIADVTIRNPANHGVMFLESQNVVENGVIHQTF-DANNGDGVEFGNSQNIM 385
Cdd:COG5434  130 -ARQSGWVPVGAYDYLRPRLIQLKNCKNVLLEGVTLRNSPFWTIHPLGCENVTVDGVTIDNPaDAPNTDGIDPDSCRNVL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 386 VFNSVFDTGDDSINFAAGMGQDAQSQEPSQNAWLFNNYFRRGHGAVVMGSHTGAGIIDVLAENNVISQNDVGLRAKSAPA 465
Cdd:COG5434  209 IENCYIDTGDDAIAIKSGRDADGRRNRPTENIVIRNCTFRSGHGGIVIGSETSGGVRNVTVENCTFDGTDRGLRIKSRRG 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 466 IGGGAHGIVFRNSAMKNLAKQAVIVTLSYSDSNGTIdytpakvPARFYDFTVKNVTVqdsTGSSPVIEITGDSGKgiWHS 545
Cdd:COG5434  289 RGGVVENITIRNITMRNVKGTPIFINLFYEGDRGGP-------TPTFRNITISNVTA---TGAKSAILIAGLPEA--PIE 356
                        410
                 ....*....|....*..
gi 306530536 546 QFTFSNMKLSGVTPASI 562
Cdd:COG5434  357 NITLENVTIGAAYGFYI 373
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
32-132 2.81e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.87  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  32 APQKLQIPTLSydDHSVALVWDAPEDT-SNITDYQIYqngqliglasqnndknspakpyisafYKNDTGNFHRRVVIQN- 109
Cdd:cd00063    3 PPTNLRVTDVT--STSVTLSWTPPEDDgGPITGYVVE--------------------------YREKGSGDWKEVEVTPg 54
                         90       100
                 ....*....|....*....|....*..
gi 306530536 110 ----AKIDGLKANTDYQFTVRTVYADG 132
Cdd:cd00063   55 setsYTLTGLKPGTEYEFRVRAVNGGG 81
 
Name Accession Description Interval E-value
Pgu1 COG5434
Polygalacturonase [Carbohydrate transport and metabolism];
149-562 1.76e-120

Polygalacturonase [Carbohydrate transport and metabolism];


Pssm-ID: 444185 [Multi-domain]  Cd Length: 373  Bit Score: 361.45  E-value: 1.76e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 149 PQVINITQYGAKGDGTTLNTTAIQKAIDAC--QTGCRVDIPAGVFKTGALWLKSDMTLNLLQGATLLGSDNAADYPDAYK 226
Cdd:COG5434    7 AKTFNITDFGAKGDGKTLNTAAIQKAIDACaaAGGGTVLVPAGTYLTGPIFLKSNVTLHLEKGATLLGSTDPADYPLVET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 227 IYSYSSQVRPASLINAIDktssavgtFKNIRIIGKGVIDGNGWKRSADAKDelgnslpqyvksdsskvskdgilaknqva 306
Cdd:COG5434   87 RWEGGELKGYSALIYAEN--------AENIAITGEGTIDGNGDAWWPWKKE----------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 307 aAVAKGMDTKTAYSQRRSSLVTLRGVKNVYIADVTIRNPANHGVMFLESQNVVENGVIHQTF-DANNGDGVEFGNSQNIM 385
Cdd:COG5434  130 -ARQSGWVPVGAYDYLRPRLIQLKNCKNVLLEGVTLRNSPFWTIHPLGCENVTVDGVTIDNPaDAPNTDGIDPDSCRNVL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 386 VFNSVFDTGDDSINFAAGMGQDAQSQEPSQNAWLFNNYFRRGHGAVVMGSHTGAGIIDVLAENNVISQNDVGLRAKSAPA 465
Cdd:COG5434  209 IENCYIDTGDDAIAIKSGRDADGRRNRPTENIVIRNCTFRSGHGGIVIGSETSGGVRNVTVENCTFDGTDRGLRIKSRRG 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 466 IGGGAHGIVFRNSAMKNLAKQAVIVTLSYSDSNGTIdytpakvPARFYDFTVKNVTVqdsTGSSPVIEITGDSGKgiWHS 545
Cdd:COG5434  289 RGGVVENITIRNITMRNVKGTPIFINLFYEGDRGGP-------TPTFRNITISNVTA---TGAKSAILIAGLPEA--PIE 356
                        410
                 ....*....|....*..
gi 306530536 546 QFTFSNMKLSGVTPASI 562
Cdd:COG5434  357 NITLENVTIGAAYGFYI 373
PLN02218 PLN02218
polygalacturonase ADPG
149-529 2.42e-16

polygalacturonase ADPG


Pssm-ID: 177865 [Multi-domain]  Cd Length: 431  Bit Score: 81.61  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 149 PQVINITQYGAKGDGTTLNTTAIQKAID-ACQTGCRVD--IPAG---VFKTGALWLKSDMTLNLLQGATLLGSDNAADYP 222
Cdd:PLN02218  65 PTTVSVSDFGAKGDGKTDDTQAFVNAWKkACSSNGAVNllVPKGntyLLKSIQLTGPCKSIRTVQIFGTLSASQKRSDYK 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 223 DAYKIYsyssqvrpasLINAIDKTSSAVGtfkniriiGKGVIDGNG---WKrsadakdelgnslpqyvksDSSKVSKdgi 299
Cdd:PLN02218 145 DISKWI----------MFDGVNNLSVDGG--------STGVVDGNGetwWQ-------------------NSCKRNK--- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 300 lAKNQVAAAVAkgmdtktaysqrrsslVTLRGVKNVYIADVTIRNPANHGVMFLESQNV-VENGVIHQTFDANNGDGVEF 378
Cdd:PLN02218 185 -AKPCTKAPTA----------------LTFYNSKSLIVKNLRVRNAQQIQISIEKCSNVqVSNVVVTAPADSPNTDGIHI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 379 GNSQNIMVFNSVFDTGDDSINFAAGmgqdaqsqepSQNAWLFNNYFRRGHGaVVMGS----HTGAGIIDVLAENNVISQN 454
Cdd:PLN02218 248 TNTQNIRVSNSIIGTGDDCISIESG----------SQNVQINDITCGPGHG-ISIGSlgddNSKAFVSGVTVDGAKLSGT 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306530536 455 DVGLRAKSAPAIGGGAHGIVFRNSAMKNLaKQAVIVTLSYSDSNGTIDYTPAkvparfydFTVKNVTVQDSTGSS 529
Cdd:PLN02218 317 DNGVRIKTYQGGSGTASNIIFQNIQMENV-KNPIIIDQDYCDKSKCTSQQSA--------VQVKNVVYRNISGTS 382
Glyco_hydro_28 pfam00295
Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2. ...
252-556 4.26e-16

Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism.


Pssm-ID: 425588 [Multi-domain]  Cd Length: 319  Bit Score: 79.73  E-value: 4.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  252 TFKNIRI--IGKGVIDGNG--WKRSADAKDELGNSLPQYV---KSDSSKVSKDGIL-AKNQVaaavakgmdtktaysqrr 323
Cdd:pfam00295  47 SGSSITVtgASGGTIDGQGqrWWDGKGTKKNGGKKKPKFIyihKVKNSKITGLNIKnSPVFH------------------ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  324 sslVTLRGVKNVYIADVTIRNPANhgvmflesqnvvengvihqTFDANNGDGVEFGNSQNIMVFNSVFDTGDDSINFAAG 403
Cdd:pfam00295 109 ---FSVQSGTDLTISDITIDNSAG-------------------DSNGHNTDGFDVGSSSGVTISNTNIYNQDDCIAINSG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  404 MgqdaqsqepsqNAWLFNNYFRRGHGAVV--MGSHTGAGIIDVLAENNVISQNDVGLRAKSAPAIGGGAHGIVFRNSAMK 481
Cdd:pfam00295 167 S-----------NISITNVTCGGGHGISIgsVGGRSDNTVKNVTVKDSTVVNSDNGVRIKTISGATGTVSNITYENIVLS 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 306530536  482 NLAKQAVIVTLSYSDSNGTIDYTPAkvparfydFTVKNVTVQDSTGSS----PVIEITGDSGKGiwhSQFTFSNMKLSG 556
Cdd:pfam00295 236 NISKYGIVIDQDYENGEPTGKPTSG--------VKISDITFKNVTGTVassaTAVYLLCGDGSC---SGWTWSGVNITG 303
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
32-132 2.81e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.87  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  32 APQKLQIPTLSydDHSVALVWDAPEDT-SNITDYQIYqngqliglasqnndknspakpyisafYKNDTGNFHRRVVIQN- 109
Cdd:cd00063    3 PPTNLRVTDVT--STSVTLSWTPPEDDgGPITGYVVE--------------------------YREKGSGDWKEVEVTPg 54
                         90       100
                 ....*....|....*....|....*..
gi 306530536 110 ----AKIDGLKANTDYQFTVRTVYADG 132
Cdd:cd00063   55 setsYTLTGLKPGTEYEFRVRAVNGGG 81
GH55_beta13glucanase-like cd23668
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
150-190 2.93e-05

fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.


Pssm-ID: 467840 [Multi-domain]  Cd Length: 623  Bit Score: 47.12  E-value: 2.93e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 306530536 150 QVINITQYGAKGDGTTLNTTAIQKAIDACQTGCRVDIPAGV 190
Cdd:cd23668  302 QFVNVKDYGAKGDGVTDDTAALQAILNTAAGGKIVYFPAGT 342
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
32-133 7.33e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.75  E-value: 7.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536    32 APQKLQIPTLSydDHSVALVWDAPEDtSNITDYQIYqngqliglasqnndknspakpYISAfYKNDTGNFHRRVVIQN-- 109
Cdd:smart00060   3 PPSNLRVTDVT--STSVTLSWEPPPD-DGITGYIVG---------------------YRVE-YREEGSEWKEVNVTPSst 57
                           90       100
                   ....*....|....*....|....*
gi 306530536   110 -AKIDGLKANTDYQFTVRTVYADGS 133
Cdd:smart00060  58 sYTLTGLKPGTEYEFRVRAVNGAGE 82
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
40-127 5.48e-03

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 36.62  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536   40 TLSYDDHSVALVWDAPEDTsniTDYQIYqngqlIGLASQNNDKNSPAKPYISAFYKNDTGNFHRrvviqnAKIDGLKANT 119
Cdd:pfam16656   7 SLTGDSTSMTVSWVTPSAV---TSPVVQ-----YGTSSSALTSTATATSSTYTTGDGGTGYIHR------ATLTGLEPGT 72

                  ....*...
gi 306530536  120 DYQFTVRT 127
Cdd:pfam16656  73 TYYYRVGD 80
 
Name Accession Description Interval E-value
Pgu1 COG5434
Polygalacturonase [Carbohydrate transport and metabolism];
149-562 1.76e-120

Polygalacturonase [Carbohydrate transport and metabolism];


Pssm-ID: 444185 [Multi-domain]  Cd Length: 373  Bit Score: 361.45  E-value: 1.76e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 149 PQVINITQYGAKGDGTTLNTTAIQKAIDAC--QTGCRVDIPAGVFKTGALWLKSDMTLNLLQGATLLGSDNAADYPDAYK 226
Cdd:COG5434    7 AKTFNITDFGAKGDGKTLNTAAIQKAIDACaaAGGGTVLVPAGTYLTGPIFLKSNVTLHLEKGATLLGSTDPADYPLVET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 227 IYSYSSQVRPASLINAIDktssavgtFKNIRIIGKGVIDGNGWKRSADAKDelgnslpqyvksdsskvskdgilaknqva 306
Cdd:COG5434   87 RWEGGELKGYSALIYAEN--------AENIAITGEGTIDGNGDAWWPWKKE----------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 307 aAVAKGMDTKTAYSQRRSSLVTLRGVKNVYIADVTIRNPANHGVMFLESQNVVENGVIHQTF-DANNGDGVEFGNSQNIM 385
Cdd:COG5434  130 -ARQSGWVPVGAYDYLRPRLIQLKNCKNVLLEGVTLRNSPFWTIHPLGCENVTVDGVTIDNPaDAPNTDGIDPDSCRNVL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 386 VFNSVFDTGDDSINFAAGMGQDAQSQEPSQNAWLFNNYFRRGHGAVVMGSHTGAGIIDVLAENNVISQNDVGLRAKSAPA 465
Cdd:COG5434  209 IENCYIDTGDDAIAIKSGRDADGRRNRPTENIVIRNCTFRSGHGGIVIGSETSGGVRNVTVENCTFDGTDRGLRIKSRRG 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 466 IGGGAHGIVFRNSAMKNLAKQAVIVTLSYSDSNGTIdytpakvPARFYDFTVKNVTVqdsTGSSPVIEITGDSGKgiWHS 545
Cdd:COG5434  289 RGGVVENITIRNITMRNVKGTPIFINLFYEGDRGGP-------TPTFRNITISNVTA---TGAKSAILIAGLPEA--PIE 356
                        410
                 ....*....|....*..
gi 306530536 546 QFTFSNMKLSGVTPASI 562
Cdd:COG5434  357 NITLENVTIGAAYGFYI 373
PLN02218 PLN02218
polygalacturonase ADPG
149-529 2.42e-16

polygalacturonase ADPG


Pssm-ID: 177865 [Multi-domain]  Cd Length: 431  Bit Score: 81.61  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 149 PQVINITQYGAKGDGTTLNTTAIQKAID-ACQTGCRVD--IPAG---VFKTGALWLKSDMTLNLLQGATLLGSDNAADYP 222
Cdd:PLN02218  65 PTTVSVSDFGAKGDGKTDDTQAFVNAWKkACSSNGAVNllVPKGntyLLKSIQLTGPCKSIRTVQIFGTLSASQKRSDYK 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 223 DAYKIYsyssqvrpasLINAIDKTSSAVGtfkniriiGKGVIDGNG---WKrsadakdelgnslpqyvksDSSKVSKdgi 299
Cdd:PLN02218 145 DISKWI----------MFDGVNNLSVDGG--------STGVVDGNGetwWQ-------------------NSCKRNK--- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 300 lAKNQVAAAVAkgmdtktaysqrrsslVTLRGVKNVYIADVTIRNPANHGVMFLESQNV-VENGVIHQTFDANNGDGVEF 378
Cdd:PLN02218 185 -AKPCTKAPTA----------------LTFYNSKSLIVKNLRVRNAQQIQISIEKCSNVqVSNVVVTAPADSPNTDGIHI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 379 GNSQNIMVFNSVFDTGDDSINFAAGmgqdaqsqepSQNAWLFNNYFRRGHGaVVMGS----HTGAGIIDVLAENNVISQN 454
Cdd:PLN02218 248 TNTQNIRVSNSIIGTGDDCISIESG----------SQNVQINDITCGPGHG-ISIGSlgddNSKAFVSGVTVDGAKLSGT 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306530536 455 DVGLRAKSAPAIGGGAHGIVFRNSAMKNLaKQAVIVTLSYSDSNGTIDYTPAkvparfydFTVKNVTVQDSTGSS 529
Cdd:PLN02218 317 DNGVRIKTYQGGSGTASNIIFQNIQMENV-KNPIIIDQDYCDKSKCTSQQSA--------VQVKNVVYRNISGTS 382
Glyco_hydro_28 pfam00295
Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2. ...
252-556 4.26e-16

Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism.


Pssm-ID: 425588 [Multi-domain]  Cd Length: 319  Bit Score: 79.73  E-value: 4.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  252 TFKNIRI--IGKGVIDGNG--WKRSADAKDELGNSLPQYV---KSDSSKVSKDGIL-AKNQVaaavakgmdtktaysqrr 323
Cdd:pfam00295  47 SGSSITVtgASGGTIDGQGqrWWDGKGTKKNGGKKKPKFIyihKVKNSKITGLNIKnSPVFH------------------ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  324 sslVTLRGVKNVYIADVTIRNPANhgvmflesqnvvengvihqTFDANNGDGVEFGNSQNIMVFNSVFDTGDDSINFAAG 403
Cdd:pfam00295 109 ---FSVQSGTDLTISDITIDNSAG-------------------DSNGHNTDGFDVGSSSGVTISNTNIYNQDDCIAINSG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  404 MgqdaqsqepsqNAWLFNNYFRRGHGAVV--MGSHTGAGIIDVLAENNVISQNDVGLRAKSAPAIGGGAHGIVFRNSAMK 481
Cdd:pfam00295 167 S-----------NISITNVTCGGGHGISIgsVGGRSDNTVKNVTVKDSTVVNSDNGVRIKTISGATGTVSNITYENIVLS 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 306530536  482 NLAKQAVIVTLSYSDSNGTIDYTPAkvparfydFTVKNVTVQDSTGSS----PVIEITGDSGKGiwhSQFTFSNMKLSG 556
Cdd:pfam00295 236 NISKYGIVIDQDYENGEPTGKPTSG--------VKISDITFKNVTGTVassaTAVYLLCGDGSC---SGWTWSGVNITG 303
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
327-458 8.18e-07

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 51.46  E-value: 8.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 327 VTLRGVKNVYIADVTIRNPAnHGVMFLES-QNVVENGVIH--QTFDANNGDGVEFGNSQNIMVFNSVFDTGDDSINFaag 403
Cdd:COG3420  101 IYVRGADNAVIENNRIENNL-FGIYLEGSdNNVIRNNTISgnRDLRADRGNGIHLWNSPGNVIEGNTISGGRDGIYL--- 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 306530536 404 mgqdaqsqEPSQNAWLFNNYFRRGHGAV-VMGSHtgagiiDVLAENNVISQNDVGL 458
Cdd:COG3420  177 --------EFSDNNVIRNNTIRNLRYGIhYMYSN------DNLVEGNTFRDNGAGI 218
PLN02793 PLN02793
Probable polygalacturonase
150-497 1.38e-05

Probable polygalacturonase


Pssm-ID: 215426 [Multi-domain]  Cd Length: 443  Bit Score: 47.95  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 150 QVINITQYGAKGDGTTLNTTAIQKAID-AC--QTGCRVDIPAG-VFKTGALWL----KSDMTLnllqgaTLLGSDNAADY 221
Cdd:PLN02793  51 RVLHVGDFGAKGDGVTDDTQAFKEAWKmACssKVKTRIVIPAGyTFLVRPIDLggpcKAKLTL------QISGTIIAPKD 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 222 PDAYKiysySSQVRPASLINAIdktssavgtfKNIRIIGKGVIDGNGWKRSADakdelgnslpqyvksdSSKVSKDgila 301
Cdd:PLN02793 125 PDVWK----GLNPRKWLYFHGV----------NHLTVEGGGTVNGMGHEWWAQ----------------SCKINHT---- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 302 kNQVAAAvakgmdtKTAysqrrsslVTLRGVKNVYIADVTIRNPANHGVMFLESQNVVENG--VIHQTFDANNgDGVEFG 379
Cdd:PLN02793 171 -NPCRHA-------PTA--------ITFHKCKDLRVENLNVIDSQQMHIAFTNCRRVTISGlkVIAPATSPNT-DGIHIS 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 380 NSQNIMVFNSVFDTGDDSINFAAGmgqdaqsqepSQNAWLFNNYFRRGHGAVV--MG-SHTGAGIIDVLAENNVISQNDV 456
Cdd:PLN02793 234 ASRGVVIKDSIVRTGDDCISIVGN----------SSRIKIRNIACGPGHGISIgsLGkSNSWSEVRDITVDGAFLSNTDN 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 306530536 457 GLRAKSAPAIGGGAHGIVFRNSAMKNLAkQAVIVTLSYSDS 497
Cdd:PLN02793 304 GVRIKTWQGGSGNASKITFQNIFMENVS-NPIIIDQYYCDS 343
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
32-132 2.81e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.87  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  32 APQKLQIPTLSydDHSVALVWDAPEDT-SNITDYQIYqngqliglasqnndknspakpyisafYKNDTGNFHRRVVIQN- 109
Cdd:cd00063    3 PPTNLRVTDVT--STSVTLSWTPPEDDgGPITGYVVE--------------------------YREKGSGDWKEVEVTPg 54
                         90       100
                 ....*....|....*....|....*..
gi 306530536 110 ----AKIDGLKANTDYQFTVRTVYADG 132
Cdd:cd00063   55 setsYTLTGLKPGTEYEFRVRAVNGGG 81
GH55_beta13glucanase-like cd23668
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
150-190 2.93e-05

fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.


Pssm-ID: 467840 [Multi-domain]  Cd Length: 623  Bit Score: 47.12  E-value: 2.93e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 306530536 150 QVINITQYGAKGDGTTLNTTAIQKAIDACQTGCRVDIPAGV 190
Cdd:cd23668  302 QFVNVKDYGAKGDGVTDDTAALQAILNTAAGGKIVYFPAGT 342
Pectate_lyase_3 pfam12708
Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure ...
152-277 4.99e-05

Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.


Pssm-ID: 403800 [Multi-domain]  Cd Length: 213  Bit Score: 44.62  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536  152 INITQYGAKGDGTTLNTTAIQKAIDACQ---TGCRVDIPAGVFktgalwLKSDmTLNLLQGATLLGsdNAADYPdaykIY 228
Cdd:pfam12708   2 RNVKDYGAKGDGVTDDTAAIQKAIDDGGattTPAVVYFPPGTY------LVSS-PIILYSGTVLVG--DGNNPP----VL 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 306530536  229 SYSSQVRPASLINAIDKTSS--AVGTFKNIRI-IGKGVIDGNGWKRSADAKD 277
Cdd:pfam12708  69 KAAPNFVGAGLIDGDPYTGGgpGIINTNNFYRqIRNLVIDITGVAPGATGIH 120
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
32-133 7.33e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.75  E-value: 7.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536    32 APQKLQIPTLSydDHSVALVWDAPEDtSNITDYQIYqngqliglasqnndknspakpYISAfYKNDTGNFHRRVVIQN-- 109
Cdd:smart00060   3 PPSNLRVTDVT--STSVTLSWEPPPD-DGITGYIVG---------------------YRVE-YREEGSEWKEVNVTPSst 57
                           90       100
                   ....*....|....*....|....*
gi 306530536   110 -AKIDGLKANTDYQFTVRTVYADGS 133
Cdd:smart00060  58 sYTLTGLKPGTEYEFRVRAVNGAGE 82
GH55_beta13glucanase-like cd23668
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
153-182 2.98e-03

fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.


Pssm-ID: 467840 [Multi-domain]  Cd Length: 623  Bit Score: 40.58  E-value: 2.98e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 306530536 153 NITQYGAKGDGTTLNTTAIQKAIDA---CQTGC 182
Cdd:cd23668   25 NVKDYGAKGDGVTDDTAAINAAISDgnrCGGGC 57
PLN03010 PLN03010
polygalacturonase
150-515 5.22e-03

polygalacturonase


Pssm-ID: 215540 [Multi-domain]  Cd Length: 409  Bit Score: 39.59  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 150 QVINITQYGAKGDGTTLNTTAIQKAIDACQTGcrvdipAGVFKTgaLWLKSDMTLnLLQGATLLGSDNAAdypdAYKIYS 229
Cdd:PLN03010  45 QNYNVLKFGAKGDGQTDDSNAFLQAWNATCGG------EGNINT--LLIPSGKTY-LLQPIEFKGPCKST----SIKVQL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 230 YSSQVRPASLI---NAIDKTSSAVGTFKNIRIIGKGVIDGNG---WkrsadakdelgnslpqyvksDSSKVSKDGILAKN 303
Cdd:PLN03010 112 DGIIVAPSNIVawsNPKSQMWISFSTVSGLMIDGSGTIDGRGssfW--------------------EALHISKCDNLTIN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 304 QVAAavakgMDTKTAYsqrrsslVTLRGVKNVYIADVTIRNPANhgvmflesqnvvengvihqtfdANNGDGVEFGNSQN 383
Cdd:PLN03010 172 GITS-----IDSPKNH-------ISIKTCNYVAISKINILAPET----------------------SPNTDGIDISYSTN 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536 384 IMVFNSVFDTGDDSINFAAGmgqdaqsqepSQNAWLFNNYFRRGHGAVV--MGSH-TGAGIIDVLAENNVISQNDVGLRA 460
Cdd:PLN03010 218 INIFDSTIQTGDDCIAINSG----------SSNINITQINCGPGHGISVgsLGADgANAKVSDVHVTHCTFNQTTNGARI 287
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 306530536 461 KSAPAIGGGAHGIVFRNSAMKNlAKQAVIVTLSYSDS---NGTIDYTPAKVPARFYDF 515
Cdd:PLN03010 288 KTWQGGQGYARNISFENITLIN-TKNPIIIDQQYIDKgklDATKDSAVAISNVKYVGF 344
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
40-127 5.48e-03

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 36.62  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306530536   40 TLSYDDHSVALVWDAPEDTsniTDYQIYqngqlIGLASQNNDKNSPAKPYISAFYKNDTGNFHRrvviqnAKIDGLKANT 119
Cdd:pfam16656   7 SLTGDSTSMTVSWVTPSAV---TSPVVQ-----YGTSSSALTSTATATSSTYTTGDGGTGYIHR------ATLTGLEPGT 72

                  ....*...
gi 306530536  120 DYQFTVRT 127
Cdd:pfam16656  73 TYYYRVGD 80
 
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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