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Conserved domains on  [gi|15228197|ref|NP_188262|]
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nitrile specifier protein 4 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02193 PLN02193
nitrile-specifier protein
 150-619 0e+00

nitrile-specifier protein


:

Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 1016.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  150 NAKKLEAKGGDTGDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGY 229
Cdd:PLN02193   1 MAQKLEAKGGETGDVWDDGVYDNVRKVYVGQGQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  230 REKVNGMTSEMITFLSFKTYKGKTSQPIEQRPGIKFVLQGGKIVGFHGRSTDVLDSLGAYISLSPTPNLHGKWTKVDENG 309
Cdd:PLN02193  81 REKVNDMTSEMITFLSFKTYKGKTSHPIEKRPGVKFVLQGGKIVGFHGRSTDVLHSLGAYISLPSTPKLLGKWIKVEQKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  310 DGPGLRCSHDIAQVGNKIYSFGGEFTPNQPIDKHLYVFDIESRTWSISPATGDIPTLSCLGVCMVSIGSTLYVFGGRDAS 389
Cdd:PLN02193 161 EGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDKHLYVFDLETRTWSISPATGDVPHLSCLGVRMVSIGSTLYVFGGRDAS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  390 RQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKWFHCSTPGDSLTARG 469
Cdd:PLN02193 241 RQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIVDKKWFHCSTPGDSFSIRG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  470 GAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAALGKHIVIFGGEIAMDPLAHVGPGQL 549
Cdd:PLN02193 321 GAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAAVGKHIVIFGGEIAMDPLAHVGPGQL 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  550 TDGTFALDTETLQWERLDKFGGEEETPSSRGWTASTTATIGGKKGLVMHGGKAPTNDRFDDLFFYGIDSA 619
Cdd:PLN02193 401 TDGTFALDTETLQWERLDKFGEEEETPSSRGWTASTTGTIDGKKGLVMHGGKAPTNDRFDDLFFYGIDSA 470
Jacalin pfam01419
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ...
 13-142 1.08e-48

Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.


:

Pssm-ID: 396138 [Multi-domain]  Cd Length: 134  Bit Score: 166.30  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197    13 GNQWDDGSeYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGrSFEADPFVINHPEEHLVSVEGRYNP-----E 87
Cdd:pfam01419   1 GASWDDGV-YDGVRKVYVGQGGDGITYIKFEYVKGGGKVEGDEHGKKG-LLGPEEFEIDYPDEYITSVEGTYDKvfgsdS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228197    88 GLILGLTFKSNK-KTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFAP 142
Cdd:pfam01419  79 EVITSLTFKTNKgRTSPFFGTPSGTKFSLEVKGKKIVGFHGRAGNALNALGAYFAP 134
 
Name Accession Description Interval E-value
PLN02193 PLN02193
nitrile-specifier protein
 150-619 0e+00

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 1016.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  150 NAKKLEAKGGDTGDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGY 229
Cdd:PLN02193   1 MAQKLEAKGGETGDVWDDGVYDNVRKVYVGQGQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  230 REKVNGMTSEMITFLSFKTYKGKTSQPIEQRPGIKFVLQGGKIVGFHGRSTDVLDSLGAYISLSPTPNLHGKWTKVDENG 309
Cdd:PLN02193  81 REKVNDMTSEMITFLSFKTYKGKTSHPIEKRPGVKFVLQGGKIVGFHGRSTDVLHSLGAYISLPSTPKLLGKWIKVEQKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  310 DGPGLRCSHDIAQVGNKIYSFGGEFTPNQPIDKHLYVFDIESRTWSISPATGDIPTLSCLGVCMVSIGSTLYVFGGRDAS 389
Cdd:PLN02193 161 EGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDKHLYVFDLETRTWSISPATGDVPHLSCLGVRMVSIGSTLYVFGGRDAS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  390 RQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKWFHCSTPGDSLTARG 469
Cdd:PLN02193 241 RQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIVDKKWFHCSTPGDSFSIRG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  470 GAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAALGKHIVIFGGEIAMDPLAHVGPGQL 549
Cdd:PLN02193 321 GAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAAVGKHIVIFGGEIAMDPLAHVGPGQL 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  550 TDGTFALDTETLQWERLDKFGGEEETPSSRGWTASTTATIGGKKGLVMHGGKAPTNDRFDDLFFYGIDSA 619
Cdd:PLN02193 401 TDGTFALDTETLQWERLDKFGEEEETPSSRGWTASTTGTIDGKKGLVMHGGKAPTNDRFDDLFFYGIDSA 470
Jacalin pfam01419
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ...
 162-291 6.07e-57

Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.


Pssm-ID: 396138 [Multi-domain]  Cd Length: 134  Bit Score: 188.25  E-value: 6.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197   162 GDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEID-ADDYIVYVEGYREKVNGMTSEM 240
Cdd:pfam01419   1 GASWDDGVYDGVRKVYVGQGGDGITYIKFEYVKGGGKVEGDEHGKKGLLGPEEFEIDyPDEYITSVEGTYDKVFGSDSEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15228197   241 ITFLSFKTYKGKTSQPIEQRPGIKFVL--QGGKIVGFHGRSTDVLDSLGAYIS 291
Cdd:pfam01419  81 ITSLTFKTNKGRTSPFFGTPSGTKFSLevKGKKIVGFHGRAGNALNALGAYFA 133
Jacalin pfam01419
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ...
 13-142 1.08e-48

Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.


Pssm-ID: 396138 [Multi-domain]  Cd Length: 134  Bit Score: 166.30  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197    13 GNQWDDGSeYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGrSFEADPFVINHPEEHLVSVEGRYNP-----E 87
Cdd:pfam01419   1 GASWDDGV-YDGVRKVYVGQGGDGITYIKFEYVKGGGKVEGDEHGKKG-LLGPEEFEIDYPDEYITSVEGTYDKvfgsdS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228197    88 GLILGLTFKSNK-KTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFAP 142
Cdd:pfam01419  79 EVITSLTFKTNKgRTSPFFGTPSGTKFSLEVKGKKIVGFHGRAGNALNALGAYFAP 134
Jacalin cd09612
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ...
 13-141 2.13e-42

Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.


Pssm-ID: 187708 [Multi-domain]  Cd Length: 130  Bit Score: 148.87  E-value: 2.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  13 GNQWDDGSEYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGRsfEADPFVINHPEEHLVSVEGRYNP---EGL 89
Cdd:cd09612   1 GSAWDDGVFPDGLRKITVRSGENGIDSIKFEYDKDGQHVVGPWHGGGGG--TPEEIVLDYPDEYITSVSGTYGPvsgSNV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15228197  90 ILGLTFKSNKKTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFA 141
Cdd:cd09612  79 ITSLTFKTNKRTYGPFGVESGTPFSLPVEGGKIVGFHGRSGDYLDAIGVYVS 130
Jacalin smart00915
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ...
 162-291 9.76e-42

Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.


Pssm-ID: 214909 [Multi-domain]  Cd Length: 128  Bit Score: 146.99  E-value: 9.76e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197    162 GDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGsQVVVGDEHGKKTELGvEEFEIDADDYIVYVEGYREKVNGMTSemi 241
Cdd:smart00915   1 GTEWDDGAFDGVRKIYVGQGGEGIKSIQFDYDKG-GKVWGDEHGGKGGTG-EEILLYPGEYITSVEGTYDKSGVITS--- 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15228197    242 tfLSFKTYKGKTSQPIEQRPGIKFVLQ---GGKIVGFHGR-STDVLDSLGAYIS 291
Cdd:smart00915  76 --LTFKTNKGRTSPFGGYEGGTKFVLEskeGKKIVGFHGRsSGDGLDSLGAYFS 127
Jacalin smart00915
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ...
 13-142 4.47e-41

Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.


Pssm-ID: 214909 [Multi-domain]  Cd Length: 128  Bit Score: 145.45  E-value: 4.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197     13 GNQWDDGSeYDAVTKIQVAAGGNGIEYVKFTYVKnGQTEEAPLRGVKGRSFEadpFVINHPEEHLVSVEGRYNPEGLILG 92
Cdd:smart00915   1 GTEWDDGA-FDGVRKIYVGQGGEGIKSIQFDYDK-GGKVWGDEHGGKGGTGE---EILLYPGEYITSVEGTYDKSGVITS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15228197     93 LTFKSNK-KTSDLIGYEDGTPFTLQ-VQDKKIVGFYG-FAGNNLHSLGAYFAP 142
Cdd:smart00915  76 LTFKTNKgRTSPFGGYEGGTKFVLEsKEGKKIVGFHGrSSGDGLDSLGAYFSP 128
Jacalin cd09612
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ...
 162-291 1.02e-33

Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.


Pssm-ID: 187708 [Multi-domain]  Cd Length: 130  Bit Score: 124.99  E-value: 1.02e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 162 GDIWDDGVY-DNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTElGVEEFEIDA-DDYIVYVEGYREKVNGmtSE 239
Cdd:cd09612   1 GSAWDDGVFpDGLRKITVRSGENGIDSIKFEYDKDGQHVVGPWHGGGGG-TPEEIVLDYpDEYITSVSGTYGPVSG--SN 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15228197 240 MITFLSFKTYKgKTSQPIEQRPGIKFVLQ--GGKIVGFHGRSTDVLDSLGAYIS 291
Cdd:cd09612  78 VITSLTFKTNK-RTYGPFGVESGTPFSLPveGGKIVGFHGRSGDYLDAIGVYVS 130
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
302-592 7.57e-29

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 116.02  E-value: 7.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 302 WTKVdenGDGPGLRCSHDIAQVGNKIYSFGGeFTPNQPIDKhLYVFDIESRTWSispATGDIPTLSCLGVCMVSIGSTLY 381
Cdd:COG3055   3 WSSL---PDLPTPRSEAAAALLDGKVYVAGG-LSGGSASNS-FEVYDPATNTWS---ELAPLPGPPRHHAAAVAQDGKLY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 382 VFGGRDA----SRQYNGFYSFDTTTNEWKLLTPVeegPTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKWfh 457
Cdd:COG3055  75 VFGGFTGanpsSTPLNDVYVYDPATNTWTKLAPM---PTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTW-- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 458 cSTPGDSLTARGG-AGLEVVQGKVWVVYGFNGcevddvhyyDPVQDKWTQVETFgvrPSERSVFASAALGKHIVIFGGEi 536
Cdd:COG3055 150 -TQLAPLPTPRDHlAAAVLPDGKILVIGGRNG---------SGFSNTWTTLAPL---PTARAGHAAAVLGGKILVFGGE- 215

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228197 537 amdplahvgpGQLTDGTFALDTETLQWERLDkfggeeETPSSRGWTAstTATIGGK 592
Cdd:COG3055 216 ----------SGFSDEVEAYDPATNTWTALG------ELPTPRHGHA--AVLTDGK 253
 
Name Accession Description Interval E-value
PLN02193 PLN02193
nitrile-specifier protein
 150-619 0e+00

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 1016.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  150 NAKKLEAKGGDTGDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGY 229
Cdd:PLN02193   1 MAQKLEAKGGETGDVWDDGVYDNVRKVYVGQGQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  230 REKVNGMTSEMITFLSFKTYKGKTSQPIEQRPGIKFVLQGGKIVGFHGRSTDVLDSLGAYISLSPTPNLHGKWTKVDENG 309
Cdd:PLN02193  81 REKVNDMTSEMITFLSFKTYKGKTSHPIEKRPGVKFVLQGGKIVGFHGRSTDVLHSLGAYISLPSTPKLLGKWIKVEQKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  310 DGPGLRCSHDIAQVGNKIYSFGGEFTPNQPIDKHLYVFDIESRTWSISPATGDIPTLSCLGVCMVSIGSTLYVFGGRDAS 389
Cdd:PLN02193 161 EGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDKHLYVFDLETRTWSISPATGDVPHLSCLGVRMVSIGSTLYVFGGRDAS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  390 RQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKWFHCSTPGDSLTARG 469
Cdd:PLN02193 241 RQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIVDKKWFHCSTPGDSFSIRG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  470 GAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAALGKHIVIFGGEIAMDPLAHVGPGQL 549
Cdd:PLN02193 321 GAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAAVGKHIVIFGGEIAMDPLAHVGPGQL 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  550 TDGTFALDTETLQWERLDKFGGEEETPSSRGWTASTTATIGGKKGLVMHGGKAPTNDRFDDLFFYGIDSA 619
Cdd:PLN02193 401 TDGTFALDTETLQWERLDKFGEEEETPSSRGWTASTTGTIDGKKGLVMHGGKAPTNDRFDDLFFYGIDSA 470
PLN02153 PLN02153
epithiospecifier protein
 296-619 1.31e-142

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 417.47  E-value: 1.31e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  296 PNLHGKWTKVDENG-DGPGLRCSHDIAQVGNKIYSFGGEFTPNQPIDKHLYVFDIESRTWSISPATGDIPTLSCLGVCMV 374
Cdd:PLN02153   3 PTLQGGWIKVEQKGgKGPGPRCSHGIAVVGDKLYSFGGELKPNEHIDKDLYVFDFNTHTWSIAPANGDVPRISCLGVRMV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  375 SIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVEE--GPTPRSFHSMAADEENVYVFGGVS------ATARLNTLD 446
Cdd:PLN02153  83 AVGTKLYIFGGRDEKREFSDFYSYDTVKNEWTFLTKLDEegGPEARTFHSMASDENHVYVFGGVSkgglmkTPERFRTIE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  447 SYNIVDKKWFHCSTPGDSLTARGGAGLEVVQGKVWVVYGF---------NGCEVDDVHYYDPVQDKWTQVETFGVRPSER 517
Cdd:PLN02153 163 AYNIADGKWVQLPDPGENFEKRGGAGFAVVQGKIWVVYGFatsilpggkSDYESNAVQFFDPASGKWTEVETTGAKPSAR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  518 SVFASAALGKHIVIFGGEIAMDPLAHVGPGQLTDGTFALDTETLQWErldKFGGEEETPSSRGWTASTTATIGGKKGLVM 597
Cdd:PLN02153 243 SVFAHAVVGKYIIIFGGEVWPDLKGHLGPGTLSNEGYALDTETLVWE---KLGECGEPAMPRGWTAYTTATVYGKNGLLM 319

                        330       340
                 ....*....|....*....|..
gi 15228197  598 HGGKAPTNDRFDDLFFYGIDSA 619
Cdd:PLN02153 320 HGGKLPTNERTDDLYFYAVNSA 341
Jacalin pfam01419
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ...
 162-291 6.07e-57

Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.


Pssm-ID: 396138 [Multi-domain]  Cd Length: 134  Bit Score: 188.25  E-value: 6.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197   162 GDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEID-ADDYIVYVEGYREKVNGMTSEM 240
Cdd:pfam01419   1 GASWDDGVYDGVRKVYVGQGGDGITYIKFEYVKGGGKVEGDEHGKKGLLGPEEFEIDyPDEYITSVEGTYDKVFGSDSEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15228197   241 ITFLSFKTYKGKTSQPIEQRPGIKFVL--QGGKIVGFHGRSTDVLDSLGAYIS 291
Cdd:pfam01419  81 ITSLTFKTNKGRTSPFFGTPSGTKFSLevKGKKIVGFHGRAGNALNALGAYFA 133
Jacalin pfam01419
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ...
 13-142 1.08e-48

Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.


Pssm-ID: 396138 [Multi-domain]  Cd Length: 134  Bit Score: 166.30  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197    13 GNQWDDGSeYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGrSFEADPFVINHPEEHLVSVEGRYNP-----E 87
Cdd:pfam01419   1 GASWDDGV-YDGVRKVYVGQGGDGITYIKFEYVKGGGKVEGDEHGKKG-LLGPEEFEIDYPDEYITSVEGTYDKvfgsdS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228197    88 GLILGLTFKSNK-KTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFAP 142
Cdd:pfam01419  79 EVITSLTFKTNKgRTSPFFGTPSGTKFSLEVKGKKIVGFHGRAGNALNALGAYFAP 134
Jacalin cd09612
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ...
 13-141 2.13e-42

Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.


Pssm-ID: 187708 [Multi-domain]  Cd Length: 130  Bit Score: 148.87  E-value: 2.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  13 GNQWDDGSEYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGRsfEADPFVINHPEEHLVSVEGRYNP---EGL 89
Cdd:cd09612   1 GSAWDDGVFPDGLRKITVRSGENGIDSIKFEYDKDGQHVVGPWHGGGGG--TPEEIVLDYPDEYITSVSGTYGPvsgSNV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15228197  90 ILGLTFKSNKKTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFA 141
Cdd:cd09612  79 ITSLTFKTNKRTYGPFGVESGTPFSLPVEGGKIVGFHGRSGDYLDAIGVYVS 130
Jacalin smart00915
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ...
 162-291 9.76e-42

Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.


Pssm-ID: 214909 [Multi-domain]  Cd Length: 128  Bit Score: 146.99  E-value: 9.76e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197    162 GDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGsQVVVGDEHGKKTELGvEEFEIDADDYIVYVEGYREKVNGMTSemi 241
Cdd:smart00915   1 GTEWDDGAFDGVRKIYVGQGGEGIKSIQFDYDKG-GKVWGDEHGGKGGTG-EEILLYPGEYITSVEGTYDKSGVITS--- 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15228197    242 tfLSFKTYKGKTSQPIEQRPGIKFVLQ---GGKIVGFHGR-STDVLDSLGAYIS 291
Cdd:smart00915  76 --LTFKTNKGRTSPFGGYEGGTKFVLEskeGKKIVGFHGRsSGDGLDSLGAYFS 127
Jacalin smart00915
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ...
 13-142 4.47e-41

Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.


Pssm-ID: 214909 [Multi-domain]  Cd Length: 128  Bit Score: 145.45  E-value: 4.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197     13 GNQWDDGSeYDAVTKIQVAAGGNGIEYVKFTYVKnGQTEEAPLRGVKGRSFEadpFVINHPEEHLVSVEGRYNPEGLILG 92
Cdd:smart00915   1 GTEWDDGA-FDGVRKIYVGQGGEGIKSIQFDYDK-GGKVWGDEHGGKGGTGE---EILLYPGEYITSVEGTYDKSGVITS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15228197     93 LTFKSNK-KTSDLIGYEDGTPFTLQ-VQDKKIVGFYG-FAGNNLHSLGAYFAP 142
Cdd:smart00915  76 LTFKTNKgRTSPFGGYEGGTKFVLEsKEGKKIVGFHGrSSGDGLDSLGAYFSP 128
Jacalin cd09612
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ...
 162-291 1.02e-33

Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.


Pssm-ID: 187708 [Multi-domain]  Cd Length: 130  Bit Score: 124.99  E-value: 1.02e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 162 GDIWDDGVY-DNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTElGVEEFEIDA-DDYIVYVEGYREKVNGmtSE 239
Cdd:cd09612   1 GSAWDDGVFpDGLRKITVRSGENGIDSIKFEYDKDGQHVVGPWHGGGGG-TPEEIVLDYpDEYITSVSGTYGPVSG--SN 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15228197 240 MITFLSFKTYKgKTSQPIEQRPGIKFVLQ--GGKIVGFHGRSTDVLDSLGAYIS 291
Cdd:cd09612  78 VITSLTFKTNK-RTYGPFGVESGTPFSLPveGGKIVGFHGRSGDYLDAIGVYVS 130
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
302-592 7.57e-29

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 116.02  E-value: 7.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 302 WTKVdenGDGPGLRCSHDIAQVGNKIYSFGGeFTPNQPIDKhLYVFDIESRTWSispATGDIPTLSCLGVCMVSIGSTLY 381
Cdd:COG3055   3 WSSL---PDLPTPRSEAAAALLDGKVYVAGG-LSGGSASNS-FEVYDPATNTWS---ELAPLPGPPRHHAAAVAQDGKLY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 382 VFGGRDA----SRQYNGFYSFDTTTNEWKLLTPVeegPTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKWfh 457
Cdd:COG3055  75 VFGGFTGanpsSTPLNDVYVYDPATNTWTKLAPM---PTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTW-- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 458 cSTPGDSLTARGG-AGLEVVQGKVWVVYGFNGcevddvhyyDPVQDKWTQVETFgvrPSERSVFASAALGKHIVIFGGEi 536
Cdd:COG3055 150 -TQLAPLPTPRDHlAAAVLPDGKILVIGGRNG---------SGFSNTWTTLAPL---PTARAGHAAAVLGGKILVFGGE- 215

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228197 537 amdplahvgpGQLTDGTFALDTETLQWERLDkfggeeETPSSRGWTAstTATIGGK 592
Cdd:COG3055 216 ----------SGFSDEVEAYDPATNTWTALG------ELPTPRHGHA--AVLTDGK 253
PHA03098 PHA03098
kelch-like protein; Provisional
 315-455 7.18e-10

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 61.71  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  315 RCSHDIAQVGNKIYSFGGEFTpNQPIDKHLYVFDIESRTWSISPATgdipTLSCLGVCMVSIGSTLYVFGGR---DASRQ 391
Cdd:PHA03098 380 RYNPCVVNVNNLIYVIGGISK-NDELLKTVECFSLNTNKWSKGSPL----PISHYGGCAIYHDGKIYVIGGIsyiDNIKV 454

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228197  392 YNGFYSFDTTTNEWKLLTPVEegpTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKW 455
Cdd:PHA03098 455 YNIVESYNPVTNKWTELSSLN---FPRINASLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTW 515
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
266-452 2.66e-09

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 58.63  E-value: 2.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 266 VLQGGKIVGFHGRStdvldslGAYISLSPTPNLH------GKWTKVdenGDGPGLRCSHDIAQVGNKIYSFGGeFTPNQP 339
Cdd:COG3055  67 VAQDGKLYVFGGFT-------GANPSSTPLNDVYvydpatNTWTKL---APMPTPRGGATALLLDGKIYVVGG-WDDGGN 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197 340 IDKHlYVFDIESRTWSispATGDIPTLSCLGVCMVSIGSTLYVFGGRDASRQYNGF------------------------ 395
Cdd:COG3055 136 VAWV-EVYDPATGTWT---QLAPLPTPRDHLAAAVLPDGKILVIGGRNGSGFSNTWttlaplptaraghaaavlggkilv 211

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228197 396 -----------YSFDTTTNEWKLLTPVeegPTPRSFHSMAADEENVYVFGG-VSATARLNTLDSYNIVD 452
Cdd:COG3055 212 fggesgfsdevEAYDPATNTWTALGEL---PTPRHGHAAVLTDGKVYVIGGeTKPGVRTPLVTSAEVYD 277
PHA03098 PHA03098
kelch-like protein; Provisional
 276-505 3.67e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 59.40  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  276 HGRSTDVLD-SLGAYISLSPTPNLHGKWTKVDENGDgpglRCSHDIAQVGNKIYSFGGEftpNQPIDKHLYVFDIESRTW 354
Cdd:PHA03098 249 FGSIIYIHItMSIFTYNYITNYSPLSEINTIIDIHY----VYCFGSVVLNNVIYFIGGM---NKNNLSVNSVVSYDTKTK 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  355 SISPATGDIPTLSCLGVCMvsIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVEEgptPRSFHSMAADEENVYVFG 434
Cdd:PHA03098 322 SWNKVPELIYPRKNPGVTV--FNNRIYVIGGIYNSISLNTVESWKPGESKWREEPPLIF---PRYNPCVVNVNNLIYVIG 396

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228197  435 GVSAT-ARLNTLDSYNIVDKKWFHCSTPGDSLTargGAGLEVVQGKVWVVYGF----NGCEVDDVHYYDPVQDKWT 505
Cdd:PHA03098 397 GISKNdELLKTVECFSLNTNKWSKGSPLPISHY---GGCAIYHDGKIYVIGGIsyidNIKVYNIVESYNPVTNKWT 469
PHA03098 PHA03098
kelch-like protein; Provisional
 300-504 8.38e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 58.24  E-value: 8.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  300 GKWTKVDENGDGPGLRCSHDIAQVGNKIYSFGGEFTPNQPIDKHLYVF-----DIESRTWSISpatgDIPTLSCLGVcmV 374
Cdd:PHA03098 218 KKKKIVFNKRCIKIIYSKKYNLNKILPRSSTFGSIIYIHITMSIFTYNyitnySPLSEINTII----DIHYVYCFGS--V 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  375 SIGSTLYVFGGRDASRQ-YNGFYSFDTTTNEWKLLTPVEegpTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDK 453
Cdd:PHA03098 292 VLNNVIYFIGGMNKNNLsVNSVVSYDTKTKSWNKVPELI---YPRKNPGVTVFNNRIYVIGGIYNSISLNTVESWKPGES 368

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15228197  454 KWfhcSTPGDSLTARGGAGLEVVQGKVWVVYGF--NGCEVDDVHYYDPVQDKW 504
Cdd:PHA03098 369 KW---REEPPLIFPRYNPCVVNVNNLIYVIGGIskNDELLKTVECFSLNTNKW 418
Kelch_3 pfam13415
Galactose oxidase, central domain;
377-426 8.98e-09

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 51.52  E-value: 8.98e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15228197   377 GSTLYVFGGRDASRQ--YNGFYSFDTTTNEWKlltPVEEGPTPRSFHSMAAD 426
Cdd:pfam13415   1 GDKLYIFGGLGFDGQtrLNDLYVYDLDTNTWT---QIGDLPPPRSGHSATYI 49
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 467-511 1.46e-06

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 45.30  E-value: 1.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 15228197   467 ARGGAGLEVVQGKVWVVYGFNG-CEVDDVHYYDPVQDKWTQVETFG 511
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGnQSLNSVEVYDPETNTWSKLPSMP 46
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 368-410 4.25e-06

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 43.75  E-value: 4.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15228197   368 CLGVCMVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTP 410
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
Kelch_6 pfam13964
Kelch motif;
315-355 3.12e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 41.55  E-value: 3.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 15228197   315 RCSHDIAQVGNKIYSFGGEFTPNQPIDKhLYVFDIESRTWS 355
Cdd:pfam13964   2 RTFHSVVSVGGYIYVFGGYTNASPALNK-LEVYNPLTKSWE 41
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 417-455 6.71e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 40.67  E-value: 6.71e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 15228197   417 PRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKW 455
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTW 39
Kelch_6 pfam13964
Kelch motif;
417-459 1.80e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 39.63  E-value: 1.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15228197   417 PRSFHSMAADEENVYVFGG-VSATARLNTLDSYNIVDKKWFHCS 459
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGyTNASPALNKLEVYNPLTKSWEELP 44
Kelch smart00612
Kelch domain;
380-425 2.83e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 38.69  E-value: 2.83e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 15228197    380 LYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVeegPTPRSFHSMAA 425
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKWTPLPSM---PTPRSGHGVAV 44
PRK14131 PRK14131
N-acetylneuraminate epimerase;
373-566 3.12e-04

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 43.47  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  373 MVSIGSTLYVFGG-----RDASRQ-YNGFYSFDTTTNEW-KLLTpveegPTPRSF---HSMAADEENVYVFGGVSatarL 442
Cdd:PRK14131  80 AAFIDGKLYVFGGigktnSEGSPQvFDDVYKYDPKTNSWqKLDT-----RSPVGLaghVAVSLHNGKAYITGGVN----K 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  443 NTLDSY----NIVDKKwfhcSTPGDSLTARggaglevVQGKVWVVYGFNgcevDDVHYYDPVQDKWtqvETFGVRP-SER 517
Cdd:PRK14131 151 NIFDGYfedlAAAGKD----KTPKDKINDA-------YFDKKPEDYFFN----KEVLSYDPSTNQW---KNAGESPfLGT 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15228197  518 SVFASAALGKHIVIFGGEIAmdplahvgPGQLTDGTFALDT--ETLQWERL 566
Cdd:PRK14131 213 AGSAVVIKGNKLWLINGEIK--------PGLRTDAVKQGKFtgNNLKWQKL 255
Kelch_6 pfam13964
Kelch motif;
373-418 5.20e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.09  E-value: 5.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15228197   373 MVSIGSTLYVFGGR-DASRQYNGFYSFDTTTNEWKLLTPVeegPTPR 418
Cdd:pfam13964   7 VVSVGGYIYVFGGYtNASPALNKLEVYNPLTKSWEELPPL---PTPR 50
Kelch_4 pfam13418
Galactose oxidase, central domain;
315-359 6.22e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 37.98  E-value: 6.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 15228197   315 RCSHDIAQVGN-KIYSFGGEFTPNQPIDkHLYVFDIESRTWSISPA 359
Cdd:pfam13418   2 RAYHTSTSIPDdTIYLFGGEGEDGTLLS-DLWVFDLSTNEWTRLGS 46
Jacalin_ZG16_like cd09611
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a ...
 9-139 2.24e-03

Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a conserved secreted vertebrate protein with tissue-specific expression profiles, which might play a role in glycoprotein secretion, perhaps as a linker protein that participates in the formation and/or transport of the zymogen granule. Its paralog ZG16b (PAUF) has been associated with roles in gene regulation and cancer. This domain family also contains mammalian proteins labelled as prostatic spermine-binding protein (SBP) and salivary-gland specific secreted proteins.


Pssm-ID: 187707 [Multi-domain]  Cd Length: 128  Bit Score: 38.46  E-value: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197   9 GGNGGNQWDDGSEYD-AVTKIQVAAGGNGIEYVKFTYVKNgqteEAPLRGvkGRSFEADPFVInHPEEHLVSVEGRYNPe 87
Cdd:cd09611   1 GSGGGKYFSDVGEGGgPITGIRVSVGNNYIKGIQVRYGSN----WSDVYG--GRGGNEQEIVL-EPGESITKVSGSYKI- 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15228197  88 gLILGLTFKSNKKTSDLIGYEDGTPFTLQ--VQDKKIVGFYG-FAGNNLHSLGAY 139
Cdd:cd09611  73 -YLHGLVFTTNKGRYLSFGKLRGRSFNATppPSNYVLRGISGrYGGLGIKSIGFH 126
Kelch_4 pfam13418
Galactose oxidase, central domain;
370-411 2.33e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.44  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15228197   370 GVCMVSIGS-TLYVFGGRDAS-RQYNGFYSFDTTTNEWKLLTPV 411
Cdd:pfam13418   4 YHTSTSIPDdTIYLFGGEGEDgTLLSDLWVFDLSTNEWTRLGSL 47
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 315-358 2.46e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 36.05  E-value: 2.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15228197   315 RCSHDIAQVGNKIYSFGGeFTPNQPIDKhLYVFDIESRTWSISP 358
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGG-FDGNQSLNS-VEVYDPETNTWSKLP 43
Kelch smart00612
Kelch domain;
430-478 3.66e-03

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 35.61  E-value: 3.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 15228197    430 VYVFGGVSATARLNTLDSYNIVDKKWfhcsTPGDSL-TARGGAGLEVVQG 478
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKW----TPLPSMpTPRSGHGVAVING 47
PHA03098 PHA03098
kelch-like protein; Provisional
 400-563 4.80e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 39.75  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  400 TTTNEWKLLTPVEEGPTPRSFHSMAADEeNVYVFGGV-SATARLNTLDSYNIVDKKWFHcsTPgDSLTARGGAGLEVVQG 478
Cdd:PHA03098 268 TNYSPLSEINTIIDIHYVYCFGSVVLNN-VIYFIGGMnKNNLSVNSVVSYDTKTKSWNK--VP-ELIYPRKNPGVTVFNN 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  479 KVWVVYG-FNGCEVDDVHYYDPVQDKWTQvETFGVRPseRSVFASAALGKHIVIFGGEIAMDplahvgpgQLTDGTFALD 557
Cdd:PHA03098 344 RIYVIGGiYNSISLNTVESWKPGESKWRE-EPPLIFP--RYNPCVVNVNNLIYVIGGISKND--------ELLKTVECFS 412


                 ....*.
gi 15228197  558 TETLQW 563
Cdd:PHA03098 413 LNTNKW 418
Kelch_4 pfam13418
Galactose oxidase, central domain;
417-455 5.49e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 35.28  E-value: 5.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 15228197   417 PRSFHSMAADEEN-VYVFGG-VSATARLNTLDSYNIVDKKW 455
Cdd:pfam13418   1 PRAYHTSTSIPDDtIYLFGGeGEDGTLLSDLWVFDLSTNEW 41
PRK14131 PRK14131
N-acetylneuraminate epimerase;
424-534 6.10e-03

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 39.23  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  424 AADEENVYVFGGVSATA--RLNTLDSynivDKKWFHCST-PGdslTARGGAGLEVVQGKVWVVYGFNGCE-------VDD 493
Cdd:PRK14131  35 AIDNNTVYVGLGSAGTSwyKLDLNAP----SKGWTKIAAfPG---GPREQAVAAFIDGKLYVFGGIGKTNsegspqvFDD 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15228197  494 VHYYDPVQDKWTQVETfgVRPSERSVFASAAL-GKHIVIFGG 534
Cdd:PRK14131 108 VYKYDPKTNSWQKLDT--RSPVGLAGHVAVSLhNGKAYITGG 147
griffithsin_like cd09614
Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin ...
 10-141 8.63e-03

Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin isolated from a red alga, which has shown potential as an inhibitor of viral entry, exhibiting antiviral activity against HIV and SARS. The biological functions of griffithsin and griffithsin-like proteins with respect to their source organisms are not known.


Pssm-ID: 187710  Cd Length: 128  Bit Score: 36.99  E-value: 8.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228197  10 GNGGNQWDDgseydaVTKIQVAA----GGNGIEYVKFTYVKNGQTEEAPLRGVKGRSFEADPFvinHPEEHLVSVEGRYN 85
Cdd:cd09614   1 GFGGSPGSD------FDILTVSAiqlrSGSYVDQIITDYQDLNGTQNFHHGGGGGNLSPTLNF---SSGEYITEVTGRSG 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15228197  86 peGLILGLTFKSNKKTSDLI-GYEDGTPFTLQVQDK-KIVGFYGFAGNNLHSLGAYFA 141
Cdd:cd09614  72 --DRVDQVQFTTNYGGRTLPgGGGGGSAFTWTVPDNqKVIGFAGRSGSYLDQLQVYYL 127
 
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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