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Conserved domains on  [gi|568942272|ref|XP_006506379|]
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beta-1,4-N-acetylgalactosaminyltransferase 3 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CHGN super family cl47930
Chondroitin N-acetylgalactosaminyltransferase;
654-971 2.69e-25

Chondroitin N-acetylgalactosaminyltransferase;


The actual alignment was detected with superfamily member pfam05679:

Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 111.20  E-value: 2.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  654 PEQEALE-VTRVFLRKL--SQRTRGRY-QLQRIVNVEKRQDRLRGGRYFLELELldgqrlvrlsEYVSTRGWRggdhpgr 729
Cdd:pfam05679 160 ADKEDLDdVINTAMEEInrNYRPRGRVlEFKQLLNGYRRFDPLRGMEYILDLLL----------EYKKYRGRT------- 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  730 edtearnlqglvwSPRNRHRHVLnaqdpepklcwpQGFSWNH---------RAVVHFIVPVKNQARWVQQFIRDMESLSQ 800
Cdd:pfam05679 223 -------------VPVRRRVYLQ------------RPFSKVEiipmpyvteSTRVHIILPLSGRYETFERFLENYERVCL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  801 VTGDAHFSIIITDYSSEDM--DVEMALKrSRLRSYQ---------YLKLSGNFERSAGLQAGIDLVkDPHSIIFLCDLHI 869
Cdd:pfam05679 278 ETGENVVLLLVVLYDPDEGqnDVFAEIK-ELIEELEkkypkakipWISVKGEFSRGKALDLGAKKF-PPDSLLFFCDVDM 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  870 HFPAGIIDTIRKHCVEGKMAFAPMV----------MRLHCGATPQWPE-----GYWEVNGFGLLGIYKSDLDKIGGMNTK 934
Cdd:pfam05679 356 VFTPEFLNRCRMNTIQGKQVYFPIVfsqydpevvyYDKPVPTSDDNFDiskdtGHWRRYGFGIVCFYKSDYMAVGGFRTS 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 568942272  935 eFRDrWGGEDWELLDRILQAGLEVERL---SLRNFFHHFH 971
Cdd:pfam05679 436 -IQG-WGLEDVDLYDKFVKSGLHVFRAvepGLVHRYHPRH 473
PA14 smart00758
domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, ...
140-277 5.08e-17

domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins;


:

Pssm-ID: 214807 [Multi-domain]  Cd Length: 136  Bit Score: 78.60  E-value: 5.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272   140 NNLHFPLYPHIRTTL---------RKLAVSPKWTNYGLRIFGYLHPFTDGKIQFAIAADDNAEFWlsrddqVSGLQLLAS 210
Cdd:smart00758   9 ENEKFSGLPEIIDTDplntfywdsDKFGEGEKADNFSVRWTGYLKPPEDGEYTFSITSDDGARLW------IDGKLVIDN 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942272   211 VGKTGkewtapgefgkFQSQISKPVSLSASLRYYFEVLHKQNDEGTdHVEVAWRRNDpGAKFTIIDS 277
Cdd:smart00758  83 WGKHE-----------ARPSTSSTLYLLAGGTYPIRIEYFEAGTGG-LLKLGWTTPD-AAKEAIDDE 136
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
654-971 2.69e-25

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 111.20  E-value: 2.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  654 PEQEALE-VTRVFLRKL--SQRTRGRY-QLQRIVNVEKRQDRLRGGRYFLELELldgqrlvrlsEYVSTRGWRggdhpgr 729
Cdd:pfam05679 160 ADKEDLDdVINTAMEEInrNYRPRGRVlEFKQLLNGYRRFDPLRGMEYILDLLL----------EYKKYRGRT------- 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  730 edtearnlqglvwSPRNRHRHVLnaqdpepklcwpQGFSWNH---------RAVVHFIVPVKNQARWVQQFIRDMESLSQ 800
Cdd:pfam05679 223 -------------VPVRRRVYLQ------------RPFSKVEiipmpyvteSTRVHIILPLSGRYETFERFLENYERVCL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  801 VTGDAHFSIIITDYSSEDM--DVEMALKrSRLRSYQ---------YLKLSGNFERSAGLQAGIDLVkDPHSIIFLCDLHI 869
Cdd:pfam05679 278 ETGENVVLLLVVLYDPDEGqnDVFAEIK-ELIEELEkkypkakipWISVKGEFSRGKALDLGAKKF-PPDSLLFFCDVDM 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  870 HFPAGIIDTIRKHCVEGKMAFAPMV----------MRLHCGATPQWPE-----GYWEVNGFGLLGIYKSDLDKIGGMNTK 934
Cdd:pfam05679 356 VFTPEFLNRCRMNTIQGKQVYFPIVfsqydpevvyYDKPVPTSDDNFDiskdtGHWRRYGFGIVCFYKSDYMAVGGFRTS 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 568942272  935 eFRDrWGGEDWELLDRILQAGLEVERL---SLRNFFHHFH 971
Cdd:pfam05679 436 -IQG-WGLEDVDLYDKFVKSGLHVFRAvepGLVHRYHPRH 473
PA14 smart00758
domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, ...
140-277 5.08e-17

domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins;


Pssm-ID: 214807 [Multi-domain]  Cd Length: 136  Bit Score: 78.60  E-value: 5.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272   140 NNLHFPLYPHIRTTL---------RKLAVSPKWTNYGLRIFGYLHPFTDGKIQFAIAADDNAEFWlsrddqVSGLQLLAS 210
Cdd:smart00758   9 ENEKFSGLPEIIDTDplntfywdsDKFGEGEKADNFSVRWTGYLKPPEDGEYTFSITSDDGARLW------IDGKLVIDN 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942272   211 VGKTGkewtapgefgkFQSQISKPVSLSASLRYYFEVLHKQNDEGTdHVEVAWRRNDpGAKFTIIDS 277
Cdd:smart00758  83 WGKHE-----------ARPSTSSTLYLLAGGTYPIRIEYFEAGTGG-LLKLGWTTPD-AAKEAIDDE 136
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
775-982 1.43e-07

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 53.07  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 775 VHFIVPVKNQARWVQQFIrdmESLSQVTGDaHFSIIITDYSSEDMDVEMaLKRSRLRSYQYLKLSGNFERSAGLQAGIDL 854
Cdd:COG1216    5 VSVVIPTYNRPELLRRCL---ESLLAQTYP-PFEVIVVDNGSTDGTAEL-LAALAFPRVRVIRNPENLGFAAARNLGLRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 855 VKDPHsIIFLCDlhihfpagiiDTI-RKHCVEGKMAFAPMVMRlhcgatpqwpegywevngfgllgiyKSDLDKIGGMNT 933
Cdd:COG1216   80 AGGDY-LLFLDD----------DTVvEPDWLERLLAAACLLIR-------------------------REVFEEVGGFDE 123
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568942272 934 KEFrdrWGGEDWELLDRILQAGLEVERLSLRNFFHHFHSKRGMWNRRQM 982
Cdd:COG1216  124 RFF---LYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYY 169
PA14 pfam07691
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
140-277 8.15e-05

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.


Pssm-ID: 400161 [Multi-domain]  Cd Length: 141  Bit Score: 43.51  E-value: 8.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  140 NNLHFPLYPHIRTTLRKLAV---------SPKWTNYGLRIFGYLHPFTDGKIQFAIAADDNAEFWLsrDDQvsglqllas 210
Cdd:pfam07691  11 NDADFSGDPVLIDTDPDNTFywdtdvpgfGEAPGDFSARWTGYLLPPESGTYTFGVASDDGARLWI--DGE--------- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942272  211 vgKTGKEWTAPGEFGKFQSqiSKPVSLSASLRYYFEVLHkQNDEGTDHVEVAWRRNDpGAKFTIIDS 277
Cdd:pfam07691  80 --LVIDNWGQHPPDASPEE--SNTLYLVAGKLYPIRIEY-FHAGTGGSVQLSWTSPD-GGGEEIDED 140
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
775-983 5.24e-04

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: 42.99  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 775 VHFIVPVKNQARWVQQFIRDMesLSQVTGDAHFSIIITDYSSED--MDV--EMALKRSRLRSYQYLKLSgnfeRSAGLQA 850
Cdd:cd02525    2 VSIIIPVRNEEKYIEELLESL--LNQSYPKDLIEIIVVDGGSTDgtREIvqEYAAKDPRIRLIDNPKRI----QSAGLNI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 851 GIDLVKdpHSIIFLCDLHIHFPA-------------------GIIDTIRKHCVEGKMAFAPMVMRLHCGA---TPQWPEG 908
Cdd:cd02525   76 GIRNSR--GDIIIRVDAHAVYPKdyilelvealkrtgadnvgGPMETIGESKFQKAIAVAQSSPLGSGGSayrGGAVKIG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 909 YWEVNGFGLLgiYKSDLDKIGGMNTKEFRdrwgGEDWELLDRILQAGLEV-----------ERLSLRNFFHHFHsKRGMW 977
Cdd:cd02525  154 YVDTVHHGAY--RREVFEKVGGFDESLVR----NEDAELNYRLRKAGYKIwlspdirvyyyPRSTLKKLARQYF-RYGKW 226

                 ....*.
gi 568942272 978 NRRQMK 983
Cdd:cd02525  227 RARTLR 232
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
654-971 2.69e-25

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 111.20  E-value: 2.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  654 PEQEALE-VTRVFLRKL--SQRTRGRY-QLQRIVNVEKRQDRLRGGRYFLELELldgqrlvrlsEYVSTRGWRggdhpgr 729
Cdd:pfam05679 160 ADKEDLDdVINTAMEEInrNYRPRGRVlEFKQLLNGYRRFDPLRGMEYILDLLL----------EYKKYRGRT------- 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  730 edtearnlqglvwSPRNRHRHVLnaqdpepklcwpQGFSWNH---------RAVVHFIVPVKNQARWVQQFIRDMESLSQ 800
Cdd:pfam05679 223 -------------VPVRRRVYLQ------------RPFSKVEiipmpyvteSTRVHIILPLSGRYETFERFLENYERVCL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  801 VTGDAHFSIIITDYSSEDM--DVEMALKrSRLRSYQ---------YLKLSGNFERSAGLQAGIDLVkDPHSIIFLCDLHI 869
Cdd:pfam05679 278 ETGENVVLLLVVLYDPDEGqnDVFAEIK-ELIEELEkkypkakipWISVKGEFSRGKALDLGAKKF-PPDSLLFFCDVDM 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  870 HFPAGIIDTIRKHCVEGKMAFAPMV----------MRLHCGATPQWPE-----GYWEVNGFGLLGIYKSDLDKIGGMNTK 934
Cdd:pfam05679 356 VFTPEFLNRCRMNTIQGKQVYFPIVfsqydpevvyYDKPVPTSDDNFDiskdtGHWRRYGFGIVCFYKSDYMAVGGFRTS 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 568942272  935 eFRDrWGGEDWELLDRILQAGLEVERL---SLRNFFHHFH 971
Cdd:pfam05679 436 -IQG-WGLEDVDLYDKFVKSGLHVFRAvepGLVHRYHPRH 473
PA14 smart00758
domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, ...
140-277 5.08e-17

domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins;


Pssm-ID: 214807 [Multi-domain]  Cd Length: 136  Bit Score: 78.60  E-value: 5.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272   140 NNLHFPLYPHIRTTL---------RKLAVSPKWTNYGLRIFGYLHPFTDGKIQFAIAADDNAEFWlsrddqVSGLQLLAS 210
Cdd:smart00758   9 ENEKFSGLPEIIDTDplntfywdsDKFGEGEKADNFSVRWTGYLKPPEDGEYTFSITSDDGARLW------IDGKLVIDN 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942272   211 VGKTGkewtapgefgkFQSQISKPVSLSASLRYYFEVLHKQNDEGTdHVEVAWRRNDpGAKFTIIDS 277
Cdd:smart00758  83 WGKHE-----------ARPSTSSTLYLLAGGTYPIRIEYFEAGTGG-LLKLGWTTPD-AAKEAIDDE 136
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
896-971 1.66e-12

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: 63.78  E-value: 1.66e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568942272  896 RLHCGATPQ-WPEGYWEVNGfGLLGIYKSDLDKIGGMNTKEFRdrWGGEDWELLDRILQAGLEVERLS--LRNFFHHFH 971
Cdd:pfam02709   2 HLSVALDKFgYKLPYKTYFG-GVLALSREDFERINGFSNGFWG--WGGEDDDLYNRLLLAGLEIERPPgdIGRYYMLYH 77
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
775-982 1.43e-07

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 53.07  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 775 VHFIVPVKNQARWVQQFIrdmESLSQVTGDaHFSIIITDYSSEDMDVEMaLKRSRLRSYQYLKLSGNFERSAGLQAGIDL 854
Cdd:COG1216    5 VSVVIPTYNRPELLRRCL---ESLLAQTYP-PFEVIVVDNGSTDGTAEL-LAALAFPRVRVIRNPENLGFAAARNLGLRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 855 VKDPHsIIFLCDlhihfpagiiDTI-RKHCVEGKMAFAPMVMRlhcgatpqwpegywevngfgllgiyKSDLDKIGGMNT 933
Cdd:COG1216   80 AGGDY-LLFLDD----------DTVvEPDWLERLLAAACLLIR-------------------------REVFEEVGGFDE 123
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568942272 934 KEFrdrWGGEDWELLDRILQAGLEVERLSLRNFFHHFHSKRGMWNRRQM 982
Cdd:COG1216  124 RFF---LYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYY 169
PA14 pfam07691
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
140-277 8.15e-05

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.


Pssm-ID: 400161 [Multi-domain]  Cd Length: 141  Bit Score: 43.51  E-value: 8.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272  140 NNLHFPLYPHIRTTLRKLAV---------SPKWTNYGLRIFGYLHPFTDGKIQFAIAADDNAEFWLsrDDQvsglqllas 210
Cdd:pfam07691  11 NDADFSGDPVLIDTDPDNTFywdtdvpgfGEAPGDFSARWTGYLLPPESGTYTFGVASDDGARLWI--DGE--------- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942272  211 vgKTGKEWTAPGEFGKFQSqiSKPVSLSASLRYYFEVLHkQNDEGTDHVEVAWRRNDpGAKFTIIDS 277
Cdd:pfam07691  80 --LVIDNWGQHPPDASPEE--SNTLYLVAGKLYPIRIEY-FHAGTGGSVQLSWTSPD-GGGEEIDED 140
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
778-982 4.38e-04

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 42.77  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 778 IVPVKNQARWVQQFIrdmESLSQVTGdAHFSIIITDYSSED--MDV--EMALKRSRLRsyqYLKLSGNFERSAGLQAGID 853
Cdd:COG0463    7 VIPTYNEEEYLEEAL---ESLLAQTY-PDFEIIVVDDGSTDgtAEIlrELAAKDPRIR---VIRLERNRGKGAARNAGLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 854 LVKDPHsIIFL-CDLhIHFPAGI---IDTIRKHCVEgkMAFAPMVMRLHCGATPQWPEGYWEV---------NGFGLLGI 920
Cdd:COG0463   80 AARGDY-IAFLdADD-QLDPEKLeelVAALEEGPAD--LVYGSRLIREGESDLRRLGSRLFNLvrlltnlpdSTSGFRLF 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568942272 921 YKSDLDKIGgmntkeFRDRWgGEDWELLdRILQAGLEVERLSlrnffHHFHSKRGMWNRRQM 982
Cdd:COG0463  156 RREVLEELG------FDEGF-LEDTELL-RALRHGFRIAEVP-----VRYRAGESKLNLRDL 204
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
775-983 5.24e-04

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: 42.99  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 775 VHFIVPVKNQARWVQQFIRDMesLSQVTGDAHFSIIITDYSSED--MDV--EMALKRSRLRSYQYLKLSgnfeRSAGLQA 850
Cdd:cd02525    2 VSIIIPVRNEEKYIEELLESL--LNQSYPKDLIEIIVVDGGSTDgtREIvqEYAAKDPRIRLIDNPKRI----QSAGLNI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 851 GIDLVKdpHSIIFLCDLHIHFPA-------------------GIIDTIRKHCVEGKMAFAPMVMRLHCGA---TPQWPEG 908
Cdd:cd02525   76 GIRNSR--GDIIIRVDAHAVYPKdyilelvealkrtgadnvgGPMETIGESKFQKAIAVAQSSPLGSGGSayrGGAVKIG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 909 YWEVNGFGLLgiYKSDLDKIGGMNTKEFRdrwgGEDWELLDRILQAGLEV-----------ERLSLRNFFHHFHsKRGMW 977
Cdd:cd02525  154 YVDTVHHGAY--RREVFEKVGGFDESLVR----NEDAELNYRLRKAGYKIwlspdirvyyyPRSTLKKLARQYF-RYGKW 226

                 ....*.
gi 568942272 978 NRRQMK 983
Cdd:cd02525  227 RARTLR 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
775-980 3.62e-03

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: 40.50  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 775 VHFIVPVKNQARWVQQFIRDMesLSQVTGDAHFSIII-----TDYSSEDMDvEMALKRSRLRsyqYLKLSGNFERSAGLQ 849
Cdd:COG1215   31 VSVIIPAYNEEAVIEETLRSL--LAQDYPKEKLEVIVvddgsTDETAEIAR-ELAAEYPRVR---VIERPENGGKAAALN 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942272 850 AGIDLVKdpHSIIFLCDLHIHFPAGIIDTIRKHCVEGKMAFapmvmrlhCGATpqwpegywevngfglLGIYKSDLDKIG 929
Cdd:COG1215  105 AGLKAAR--GDIVVFLDADTVLDPDWLRRLVAAFADPGVGA--------SGAN---------------LAFRREALEEVG 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568942272 930 GmntkeFRDRWGGEDWELLDRILQAGLEVERLSLRNFFHHF-HSKRGMWNRR 980
Cdd:COG1215  160 G-----FDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEApETLRALFRQR 206
 
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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