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Conserved domains on  [gi|2217325200|ref|XP_047299026|]
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polypeptide N-acetylgalactosaminyltransferase 5 isoform X3 [Homo sapiens]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551826)

polypeptide N-acetylgalactosaminyltransferase catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor

CAZY:  GT2
EC:  2.4.1.41
Gene Ontology:  GO:0004653|GO:0030246|GO:0046872
PubMed:  12634319|12691742|9445404|8844840
SCOP:  3000077|3000678

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-299 1.51e-178

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


:

Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 500.96  E-value: 1.51e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   1 MCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQNAT 79
Cdd:cd02510     4 IIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGARAAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  80 GDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKNRIK 159
Cdd:cd02510    84 GDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RRRES 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 160 ETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKDrMK 238
Cdd:cd02510   162 PTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG-SG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217325200 239 TVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 299
Cdd:cd02510   241 TVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 305-453 9.93e-80

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


:

Pssm-ID: 467314  Cd Length: 132  Bit Score: 243.16  E-value: 9.93e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 305 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 384
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217325200 385 STSVFhPELlsnsacgsfpallslqVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 453
Cdd:cd23436    81 SLIAF-PEL----------------MDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-299 1.51e-178

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 500.96  E-value: 1.51e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   1 MCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQNAT 79
Cdd:cd02510     4 IIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGARAAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  80 GDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKNRIK 159
Cdd:cd02510    84 GDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RRRES 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 160 ETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKDrMK 238
Cdd:cd02510   162 PTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG-SG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217325200 239 TVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 299
Cdd:cd02510   241 TVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 305-453 9.93e-80

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467314  Cd Length: 132  Bit Score: 243.16  E-value: 9.93e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 305 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 384
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217325200 385 STSVFhPELlsnsacgsfpallslqVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 453
Cdd:cd23436    81 SLIAF-PEL----------------MDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 8-178 1.29e-32

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 121.35  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   8 WSTLLRSVHSVINRspPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 87
Cdd:pfam00535  10 EKYLLETLESLLNQ--TYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGDYIAFLD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  88 SHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYmtvdnfqrgifvWPMNFGWRTIPPDVIAKNRIKETDTIRCP 167
Cdd:pfam00535  87 ADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRLLGLNLPFLIG 154

                         170
                  ....*....|.
gi 2217325200 168 VMAGGLFSIDK 178
Cdd:pfam00535 155 GFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
309-447 7.95e-15

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 71.02  E-value: 7.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 309 ASGVLINVALGKCISIE-----NTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIA--PIPDKGAVRLHPCDNRNKGL 379
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDvgSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217325200 380 KWLHKSTSvfhpellsnsacgsfpallslqvNHIVfeNNQQLLCLEGNFSQKILK---VAACDPVKPYQKW 447
Cdd:pfam00652  81 RWRYDEDG-----------------------TQIR--NPQSGKCLDVSGAGTSNGkviLWTCDSGNPNQQW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-253 1.53e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 69.25  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   8 WSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 87
Cdd:COG1216    15 PELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLGLRAAGGDYLLFLD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  88 SHVECNVGWLEPLLErvylsrkkVACpvievindkdmsymtvdnfqrgifvwpmnfgwrtippdviaknriketdtircp 167
Cdd:COG1216    90 DDTVVEPDWLERLLA--------AAC------------------------------------------------------ 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 168 vmagglFSIDKSYFFELGTYDPGLDVWGGEnMELSFKVWMCGGEIEIIPCSRVGHIFRNDnpySFPKDRMKTVERNLVRV 247
Cdd:COG1216   108 ------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SGPLLRAYYLGRNRLLF 177


                  ....*.
gi 2217325200 248 AEVWLD 253
Cdd:COG1216   178 LRKHGP 183
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 314-450 3.53e-12

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 62.91  E-value: 3.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  314 INVALGKCISI--ENTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIAPIPDKGA-VRLHPCDNRNKGLKWLHKSTSv 388
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDG- 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217325200  389 fhpeLLSNSACGsfpalLSLQVNhivfennqqllclEGNFSQKILkVAACDPvKPYQKWKFE 450
Cdd:smart00458  81 ----TIRNPDSG-----KCLDVK-------------DGNTGTKVI-LWTCSG-NPNQKWIFE 118
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 29-87 9.00e-06

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 47.35  E-value: 9.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217325200  29 EILLVDDFSTkDYLKDNLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 87
Cdd:PRK10073   37 EIIIVNDGST-DNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 1-299 1.51e-178

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 500.96  E-value: 1.51e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   1 MCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLD-KYMSQFPKVRILRLKERHGLIRARLAGAQNAT 79
Cdd:cd02510     4 IIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGARAAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  80 GDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDViaKNRIK 159
Cdd:cd02510    84 GDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RRRES 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 160 ETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKDrMK 238
Cdd:cd02510   162 PTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG-SG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217325200 239 TVERNLVRVAEVWLDEYKELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLENVF 299
Cdd:cd02510   241 TVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 305-453 9.93e-80

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467314  Cd Length: 132  Bit Score: 243.16  E-value: 9.93e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 305 PIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHK 384
Cdd:cd23436     1 PLVKASGLLVNVALRKCIAIENTTLTLQDCDLNNKSQHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217325200 385 STSVFhPELlsnsacgsfpallslqVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYY 453
Cdd:cd23436    81 SLIAF-PEL----------------MDHIMLEHQSQPTCLEADPSQKILRLNACDSFKRYQKWRFGHYY 132
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 8-178 1.29e-32

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 121.35  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   8 WSTLLRSVHSVINRspPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 87
Cdd:pfam00535  10 EKYLLETLESLLNQ--TYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGDYIAFLD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  88 SHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYmtvdnfqrgifvWPMNFGWRTIPPDVIAKNRIKETDTIRCP 167
Cdd:pfam00535  87 ADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRLLGLNLPFLIG 154

                         170
                  ....*....|.
gi 2217325200 168 VMAGGLFSIDK 178
Cdd:pfam00535 155 GFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
309-447 7.95e-15

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 71.02  E-value: 7.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 309 ASGVLINVALGKCISIE-----NTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIA--PIPDKGAVRLHPCDNRNKGL 379
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCLDvgSTADGAKVVLWPCHPGNGNQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217325200 380 KWLHKSTSvfhpellsnsacgsfpallslqvNHIVfeNNQQLLCLEGNFSQKILK---VAACDPVKPYQKW 447
Cdd:pfam00652  81 RWRYDEDG-----------------------TQIR--NPQSGKCLDVSGAGTSNGkviLWTCDSGNPNQQW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-253 1.53e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 69.25  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   8 WSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 87
Cdd:COG1216    15 PELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLGLRAAGGDYLLFLD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  88 SHVECNVGWLEPLLErvylsrkkVACpvievindkdmsymtvdnfqrgifvwpmnfgwrtippdviaknriketdtircp 167
Cdd:COG1216    90 DDTVVEPDWLERLLA--------AAC------------------------------------------------------ 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 168 vmagglFSIDKSYFFELGTYDPGLDVWGGEnMELSFKVWMCGGEIEIIPCSRVGHIFRNDnpySFPKDRMKTVERNLVRV 247
Cdd:COG1216   108 ------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SGPLLRAYYLGRNRLLF 177


                  ....*.
gi 2217325200 248 AEVWLD 253
Cdd:COG1216   178 LRKHGP 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 10-103 6.78e-13

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 67.42  E-value: 6.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  10 TLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSH 89
Cdd:COG0463    16 YLEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARGDYIAFLDAD 92

                          90
                  ....*....|....
gi 2217325200  90 VECNVGWLEPLLER 103
Cdd:COG0463    93 DQLDPEKLEELVAA 106
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 9-113 1.03e-12

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 65.61  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   9 STLLRSVHSVINRSPPHLikEILLVDDFSTKDYLKDnLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDS 88
Cdd:cd00761    10 PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYILFLDA 86

                          90       100
                  ....*....|....*....|....*
gi 2217325200  89 HVECNVGWLEPLLERVYLSRKKVAC 113
Cdd:cd00761    87 DDLLLPDWLERLVAELLADPEADAV 111
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 314-450 3.53e-12

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 62.91  E-value: 3.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  314 INVALGKCISI--ENTTVILEDCDGSKELQQFNYTWLRLIKC--GEWCIAPIPDKGA-VRLHPCDNRNKGLKWLHKSTSv 388
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDG- 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217325200  389 fhpeLLSNSACGsfpalLSLQVNhivfennqqllclEGNFSQKILkVAACDPvKPYQKWKFE 450
Cdd:smart00458  81 ----TIRNPDSG-----KCLDVK-------------DGNTGTKVI-LWTCSG-NPNQKWIFE 118
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 10-227 2.57e-11

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 64.38  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  10 TLLRSVHSVINRSPPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSH 89
Cdd:COG1215    43 VIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDAD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  90 VECNVGWLEPLLErvYLSRKKVACPvievindkdmsymtvdnfqrgifvwpmnfgwrtippdviaknriketdtircpvm 169
Cdd:COG1215   122 TVLDPDWLRRLVA--AFADPGVGAS------------------------------------------------------- 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217325200 170 aGGLFSIDKSYFFELGTYDPGLdvwGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND 227
Cdd:COG1215   145 -GANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPET 198
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 307-449 3.83e-10

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 57.31  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 307 VRASGVLINVALGKCI----SIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGlKWL 382
Cdd:cd23437     2 NLAWGEIRNLGTGLCLdtmgHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETG-KWE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217325200 383 HKSTSvfhpELLSNSACGsfpallslqvnhivfennqqlLCLEGNFSQKILKVAACDPVKPYQKWKF 449
Cdd:cd23437    81 YDEAT----GQIRHKGTG---------------------KCLDLNEGTNKLILQPCDSSSPSQKWEF 122
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 4-88 3.20e-08

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 53.75  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   4 VDEVWstLLRSVHSVINRSPPHLikEILLVDDFSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVL 83
Cdd:cd04184    12 TPEKY--LREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALELATGEFV 87


                  ....*
gi 2217325200  84 TFLDS 88
Cdd:cd04184    88 ALLDH 92
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 309-450 3.32e-08

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 51.98  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 309 ASGVLINVALGKCIS------IENTTVILEDCDGSKELQQFNYTWLRLIKCGEWC--IAPIPDKgaVRLHPCDNRNKGLK 380
Cdd:cd23462     4 AYGEIRNLAGKLCLDapgrkkELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCldYAGGSGD--VTLYPCHGMKGNQF 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 381 WLHKSTSvfhpellsnsacgsfpallslqvNHIVFENNQqlLCLEGNFSQKILKVAACDPVKPYQKWKFE 450
Cdd:cd23462    82 WIYDEET-----------------------KQIVHGTSK--KCLELSDDSSKLVMEPCNGSSPRQQWEFE 126
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 11-88 3.80e-07

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 50.26  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  11 LLRSVHSVINRSPPHlikEILLVDDFSTkdylkDN----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFL 86
Cdd:cd04179    15 LVERLLAVLEEGYDY---EIIVVDDGST-----DGtaeiARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTM 86


                  ..
gi 2217325200  87 DS 88
Cdd:cd04179    87 DA 88
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 309-449 4.64e-07

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 48.49  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 309 ASGVLINVALGKCI----SIENTTVILEDC--DGSKELQQFNYTW---LRlIKCGEWCI-APIPDKGA-VRLHPCDNR-- 375
Cdd:cd23439     1 ASGEIRNVGSGLCIdtkhGGENDEVRLSKCvkDGGGGEQQFELTWhedIR-PKKRKVCFdVSSHTPGApVILYACHGMkg 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217325200 376 NKGLKWLHKSTSVFHPEllSNsacgsfpallslqvnhivfennqqlLCLEGNFSQKILKVAACDPVKPYQKWKF 449
Cdd:cd23439    80 NQLWKYRPNTKQLYHPV--SG-------------------------LCLDADPGSGKVFMNHCDESSDTQKWTW 126
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 11-88 4.68e-06

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 46.70  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  11 LLRSVHSVINRSPPHLikEILLVDDFSTkdylkDN----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFL 86
Cdd:cd04187    15 LYERLKAVLESLGYDY--EIIFVDDGST-----DRtleiLRELAARDPRVKVIRLSRNFGQQAALLAGLDHARGDAVITM 87


                  ..
gi 2217325200  87 DS 88
Cdd:cd04187    88 DA 89
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 29-87 9.00e-06

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 47.35  E-value: 9.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217325200  29 EILLVDDFSTkDYLKDNLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 87
Cdd:PRK10073   37 EIIIVNDGST-DNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 17-222 3.50e-05

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 45.30  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  17 SVINRSPPHLIKEILLVDDFSTkDYLKDNLDKYMSQFPKVRILRLKERHgLIRARLAGAQNATGDVLTFLDSHVECNVGW 96
Cdd:cd02525    21 SLLNQSYPKDLIEIIVVDGGST-DGTREIVQEYAAKDPRIRLIDNPKRI-QSAGLNIGIRNSRGDIIIRVDAHAVYPKDY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  97 LEPLLErvYLSRKKVACpVIEVINDKDMSymtvdNFQRGIfVWPMNFGWRTIppdvIAKNRIKETDTIRCPVMAGGLFSi 176
Cdd:cd02525    99 ILELVE--ALKRTGADN-VGGPMETIGES-----KFQKAI-AVAQSSPLGSG----GSAYRGGAVKIGYVDTVHHGAYR- 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217325200 177 dKSYFFELGTYDPGLDVwgGENMELSFKVWMCGGEIEIIPCSRVGH 222
Cdd:cd02525   165 -REVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY 207
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 29-89 3.97e-05

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 44.83  E-value: 3.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217325200  29 EILLVDDfSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD---SH 89
Cdd:cd06442    29 EIIVVDD-NSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDadlSH 91
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 319-449 4.75e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467312 [Multi-domain]  Cd Length: 121  Bit Score: 42.69  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 319 GKCI----SIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPI-PDKGA-VRLHPCDNRNKGLKWLHkstsvfhpe 392
Cdd:cd23434     9 NLCLdtlgHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVVdRAPGSlVTLQPCREDDSNQKWEQ--------- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217325200 393 llsnsacgsfpallslqvnhivFENNQQL------LCLEG-NFSQKILKVAACDPVKPYQKWKF 449
Cdd:cd23434    80 ----------------------IENNSKLrhvgsnLCLDSrNAKSGGLTVETCDPSSGSQQWKF 121
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 305-451 5.04e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNTL6 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467355  Cd Length: 148  Bit Score: 43.39  E-value: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 305 PIVRASGVLINVALGKCISIEN----TTVILEDC--DGSKEL----QQFNYTWLRLIKCGE------WCIAPIPDKGAVR 368
Cdd:cd23477     2 PPPAAWGEIRNVAANLCVDSKHgatgTELRLDICvkDGSERTwsheQLFTFGWREDIRPGEplhtrkFCFDAISHNSPVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 369 LHPCDNRNKGLKWLH-KSTSVFHPelLSNSacgsfpallslqvnhivfennqqllCLEGNFSQKILKVAACDPVKPYQKW 447
Cdd:cd23477    82 LYDCHGMKGNQLWSYrKDKTLFHP--VSNS-------------------------CMDCNPADKKIFMNRCDPLSETQQW 134


                  ....
gi 2217325200 448 KFEK 451
Cdd:cd23477   135 IFEH 138
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 311-449 1.09e-04

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467338 [Multi-domain]  Cd Length: 121  Bit Score: 41.66  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 311 GVLINVALGKCISI---ENT--TVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKgAVRLHPCDNRNKGLKWLHKS 385
Cdd:cd23460     3 GQIKHTESGLCLDWageSNGdkTVALKPCHGGGGNQFWMYTGDGQIRQDHLCLTADEGN-KVTLRECADQLPSQEWSYDE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217325200 386 tsvfhpellsnsacgsfpallslQVNHIVfeNNQQLLCLEGNFSQKILKVAACDPVKPYQKWKF 449
Cdd:cd23460    82 -----------------------KTGTIR--HRSTGLCLTLDANNDVVILKECDSNSLWQKWIF 120
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 170-224 5.15e-04

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 38.75  E-value: 5.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217325200 170 AGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEiIPCSRVGHIF 224
Cdd:pfam02709  20 FGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIE-RPPGDIGRYY 73
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 10-98 9.02e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 40.73  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200  10 TLLRSVHSVINRSPPHLIKEILLVDDFS---TKDYLKDNLDKymsQFPKVRILRLKERH--GLIRARLAGAQNATGDVLT 84
Cdd:cd04192    11 NLPRLLQSLSALDYPKEKFEVILVDDHStdgTVQILEFAAAK---PNFQLKILNNSRVSisGKKNALTTAIKAAKGDWIV 87

                          90
                  ....*....|....*.
gi 2217325200  85 FLDShvECNV--GWLE 98
Cdd:cd04192    88 TTDA--DCVVpsNWLL 101
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 313-381 1.03e-03

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 38.73  E-value: 1.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217325200 313 LINVALGKCISIENTT--VILEDCDGSKELQQFNYTW---LRLIKCGEwCIA--PIPDKGAVRLHPCDNRNKGLKW 381
Cdd:cd23385     5 IYNEDLGKCLAARSSSskVSLSTCNPNSPNQQWKWTSghrLFNVGTGK-CLGvsSSSPSSPLRLFECDSEDELQKW 79
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 305-451 2.60e-03

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467354  Cd Length: 150  Bit Score: 38.40  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 305 PIVRASGVLINVALGKCISIEN----TTVILEDCDGSK------ELQQFNYTWLRLIKCGE------WCIAPIPDKGAVR 368
Cdd:cd23476     2 PPAAAWGEIRNVGTGLCADTKHgalgSPLRLEGCVKGRgeaawnNGQVFTFGWREDIRPGDpqhtkkFCFDAISHNSPVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200 369 LHPCDNRNKGLKWLH-KSTSVFHPelLSNSacgsfpallslqvnhivfennqqllCLEGNFSQKILKVAACDPVKPYQKW 447
Cdd:cd23476    82 LYDCHGMKGNQLWRYrKDKTLYHP--VSNS-------------------------CMDCSESDHRIFMNTCNPSSPTQQW 134


                  ....
gi 2217325200 448 KFEK 451
Cdd:cd23476   135 LFEH 138
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 309-345 3.20e-03

second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. The model corresponds to the second lectin domain.


Pssm-ID: 467378 [Multi-domain]  Cd Length: 128  Bit Score: 37.83  E-value: 3.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217325200 309 ASGVLIN-VALGKCISIE------NTTVILEDCDGSKELQQFNY 345
Cdd:cd23500    45 KKGTIRSaLDGNKCLAIPggntgnHTQLQLADCDASNPAQQFNY 88
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-113 3.61e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 38.31  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325200   8 WSTLLRSVHSVINRSPPHLikEILLVDDFSTkDYLKDNLDKYmsqFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD 87
Cdd:cd04186     9 LEYLKACLDSLLAQTYPDF--EVIVVDNAST-DGSVELLREL---FPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLN 82

                          90       100
                  ....*....|....*....|....*.
gi 2217325200  88 SHVECNVGWLEPLLERvYLSRKKVAC 113
Cdd:cd04186    83 PDTVVEPGALLELLDA-AEQDPDVGI 107
beta-trefoil_Ricin_unchar cd23412
ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose ...
 315-375 5.06e-03

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose receptor (MRC)-like proteins; The subfamily corresponds to a group of uncharacterized ricin B-type lectin beta-trefoil domain-containing proteins from Gnathostomata. They show high sequence similarity with macrophage mannose receptor (MRC) family proteins.


Pssm-ID: 467790  Cd Length: 127  Bit Score: 37.00  E-value: 5.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217325200 315 NVALGKCISI---ENTTVILEDCDGSKELQQFNYT----WLRLIKCGEWCIAP-IPDKGAVRLHPCDNR 375
Cdd:cd23412     9 NVQLEKCIQVdhgESERVSLAECKPHSEHQQWSWDpetrALSSLHTGECLTVLkIQEFGSVRLEPCGSR 77
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 313-381 8.09e-03

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 36.42  E-value: 8.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217325200 313 LINVALGKCISIENT----TVILEDCDGSKELQQF-----NYTWLRLIKCGewciaPIPDKGAVRLHPCDNRNKGLKW 381
Cdd:cd23385    45 LFNVGTGKCLGVSSSspssPLRLFECDSEDELQKWkcskdGLLLLKGLGLL-----LLYDKSGKNVVVSKGSGLSSRW 117
 
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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