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Conserved domains on  [gi|1907144097|ref|XP_036018638|]
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protein O-mannosyl-transferase 1 isoform X2 [Mus musculus]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 11449133)

dolichyl-phosphate-mannose--protein mannosyltransferase is a glycosyltransferase family 39 protein that transfers mannosyl residues to the hydroxyl group of serine or threonine residues, initiating the assembly of O-mannosyl glycans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 323-486 4.82e-98

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar proteins; POMT1 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 1, belongs to the glycosyltransferase 39 family. It transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins, but not of cadherins and protocaherins. POMT1 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


:

Pssm-ID: 467752 [Multi-domain]  Cd Length: 191  Bit Score: 300.38  E-value: 4.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLKSVSGKPlpCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKDPGR----------------- 385
Cdd:cd23281     1 VAYGSQVTLRNTHGSP--CWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRqdlavddpprpvrhgdi 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 386 --------------HDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSG 451
Cdd:cd23281    79 iqlvhgktgrflnsHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907144097 452 AHLPDWGFRQLEVVGEKlsPGYHESMVWNVEEHRY 486
Cdd:cd23281   159 KQLPDWGFGQLEVATDR--AGNQSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 56-291 1.05e-69

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


:

Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 227.96  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097  56 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSgPPFGHMLLALGGWLGGFDGNFLWNRIGAEYS-SNVPIWSLRLLPAL 134
Cdd:pfam02366  13 WNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 135 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFnsqTHSPFSVHWWLWL 214
Cdd:pfam02366  92 LGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---RKAPFSRKWWLWL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907144097 215 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 291
Cdd:pfam02366 169 LLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 515-709 6.62e-56

C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.


:

Pssm-ID: 465056  Cd Length: 198  Bit Score: 189.29  E-value: 6.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 515 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 593
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 594 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 670
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907144097 671 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 709
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
 
Name Accession Description Interval E-value
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 323-486 4.82e-98

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar proteins; POMT1 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 1, belongs to the glycosyltransferase 39 family. It transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins, but not of cadherins and protocaherins. POMT1 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467752 [Multi-domain]  Cd Length: 191  Bit Score: 300.38  E-value: 4.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLKSVSGKPlpCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKDPGR----------------- 385
Cdd:cd23281     1 VAYGSQVTLRNTHGSP--CWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRqdlavddpprpvrhgdi 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 386 --------------HDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSG 451
Cdd:cd23281    79 iqlvhgktgrflnsHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907144097 452 AHLPDWGFRQLEVVGEKlsPGYHESMVWNVEEHRY 486
Cdd:cd23281   159 KQLPDWGFGQLEVATDR--AGNQSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 56-291 1.05e-69

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 227.96  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097  56 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSgPPFGHMLLALGGWLGGFDGNFLWNRIGAEYS-SNVPIWSLRLLPAL 134
Cdd:pfam02366  13 WNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 135 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFnsqTHSPFSVHWWLWL 214
Cdd:pfam02366  92 LGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---RKAPFSRKWWLWL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907144097 215 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 291
Cdd:pfam02366 169 LLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 515-709 6.62e-56

C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.


Pssm-ID: 465056  Cd Length: 198  Bit Score: 189.29  E-value: 6.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 515 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 593
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 594 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 670
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907144097 671 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 709
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 56-281 8.53e-16

Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 80.71  E-value: 8.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097  56 WQLSYPRAVVFDEVYYG----QYISFYMKRIFFLDDSG----PPFGHMLLAlggwlggfdgnflwnrIGAEYSSNVPIWS 127
Cdd:COG1928    38 WGLGRPNTLVFDETYYVkdawSLLTNGYERNWPDPGPFfvvhPPLGKWLIA----------------LGEWLFGYVNPFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 128 LRLLPALAGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVL--------------S 193
Cdd:COG1928   102 WRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGcllldrdqvrrrlaA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 194 YLKFFNSQTHSPFSVHWWLWLLLTGVSCSCAVGIKYMGIFtYLLVLGIAAVhAWNLIGDQTLSNMRVLSHLLAR-----I 268
Cdd:COG1928   182 AVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTV-AWDAGARRAAGVRRPWLGALLRdgipaF 259

                         250
                  ....*....|...
gi 1907144097 269 VALLVVPVFLYLL 281
Cdd:COG1928   260 FALVIVPLLTYLA 272
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
323-380 5.76e-08

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 49.65  E-value: 5.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097  323 VAFGSQVTLKSVSGkplPCWLHSHKNTYPMIyengrgSSHQQQVTCYPFKDI--NNWWIV 380
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPAIdaNTLWLI 54
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 344-465 6.56e-07

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 50.05  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 344 HSHKNTYPMIYENGRGsSHQQQVTCYPFKDINN----WWIV----KDP-------------------GR----HDV-AAP 391
Cdd:pfam02815  13 HSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRIevvrHDAwrgglikwgspfrlrhlttGRylhsHEEqKPP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 392 LSPHS---QEVSCYiDYNISmpAQNLWKLDIVNRESN----RDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFR--QL 462
Cdd:pfam02815  92 LVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKKSTtgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpeQQ 168


                  ...
gi 1907144097 463 EVV 465
Cdd:pfam02815 169 KVT 171
 
Name Accession Description Interval E-value
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 323-486 4.82e-98

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar proteins; POMT1 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 1, belongs to the glycosyltransferase 39 family. It transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins, but not of cadherins and protocaherins. POMT1 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467752 [Multi-domain]  Cd Length: 191  Bit Score: 300.38  E-value: 4.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLKSVSGKPlpCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKDPGR----------------- 385
Cdd:cd23281     1 VAYGSQVTLRNTHGSP--CWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRqdlavddpprpvrhgdi 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 386 --------------HDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSG 451
Cdd:cd23281    79 iqlvhgktgrflnsHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907144097 452 AHLPDWGFRQLEVVGEKlsPGYHESMVWNVEEHRY 486
Cdd:cd23281   159 KQLPDWGFGQLEVATDR--AGNQSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 56-291 1.05e-69

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 227.96  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097  56 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSgPPFGHMLLALGGWLGGFDGNFLWNRIGAEYS-SNVPIWSLRLLPAL 134
Cdd:pfam02366  13 WNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 135 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFnsqTHSPFSVHWWLWL 214
Cdd:pfam02366  92 LGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---RKAPFSRKWWLWL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907144097 215 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 291
Cdd:pfam02366 169 LLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 515-709 6.62e-56

C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.


Pssm-ID: 465056  Cd Length: 198  Bit Score: 189.29  E-value: 6.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 515 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 593
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 594 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 670
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907144097 671 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 709
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 323-484 5.83e-47

MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein mannosyltransferase (PMT); The PMT (EC 2.4.1.109) family includes mammalian protein O-mannosyl-transferases (POMT1 and POMT2) and yeast PMT1-7. PMTs are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467747 [Multi-domain]  Cd Length: 185  Bit Score: 164.43  E-value: 5.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLKSVSgkPLPCWLHSHKNTYPMIyengrgsSHQQQVTCYPFKDINNWWIVKDPGR----------------- 385
Cdd:cd23276     1 VAYGSQITLRNAN--SGGGYLHSHNHTYPDG-------SKQQQVTGYGHKDENNWWQILKPRGdpssnppdpeyvrdgde 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 386 --------------HDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESN--RDTWKTILSEVRFVHVNTSAILKL 449
Cdd:cd23276    72 vrllhketnrylrtHDAAAPVTSKHKEVSAYPDENEDGDDNDLWVVEIVKDEGKleDKRIKPLTTRFRLRNKKTGCYLTS 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907144097 450 SGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 484
Cdd:cd23276   152 SGVKLPEWGFRQGEVVCSK-NKESDPSTLWNVEEN 185
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 320-484 7.71e-36

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 2 (PMT2) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called PMTs, are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT2, PMT3 and PMT6. PMT2 forms a heterodimeric complex with PMT1 and more rarely with PMT5. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. It is required for incorporation of proteins in the cell wall. PMT3 form a functional heterodimer with PMT5 and more rarely with PMT1. It may have redundant activity to PMT2. PMT6 may form a heterodimer with PMT4. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467755 [Multi-domain]  Cd Length: 192  Bit Score: 133.60  E-value: 7.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 320 PLEVAFGSQVTLKSVsgKPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDINNWWIV------------------- 380
Cdd:cd23284     1 PLDVAYGSKVTIKNQ--GLGGGLLHSHVQTYP-------EGSNQQQVTCYGHKDSNNEWIFerprglpswdendtdiefi 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 381 ----------KDPGR----HDVAAPLSPHSQEVSCYIDYNISMPAQNlWKLDIVNRESNRDTWK--TILSEVRFVHVNTS 444
Cdd:cd23284    72 kdgdivrlvhKQTGRnlhsHPVPAPISKSDYEVSGYGDLTVGDEKDN-WVIEIVKQVGSEDPKKlhTLTTSFRLRHEVLG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907144097 445 AILKLSGAHLPDWGFRQLEVVGEKLSPGYHESMVWNVEEH 484
Cdd:cd23284   151 CYLAQTGVSLPEWGFKQGEVVCDKSNFKRDKRTWWNIETH 190
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 323-483 8.40e-33

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 4 (PMT4) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called PMTs, are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT4. It forms a functional homodimer and may form a heterodimer with PMT6. PMT4 specifically acts on secretory proteins with an ER-luminally oriented Ser/Thr-rich region flanked by a membrane anchor such as FUS1, AXL2, GAS1, KEX2, MID2, WSC1, WSC2, OPY2, PRM5, RAX2, or YNL176. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467756 [Multi-domain]  Cd Length: 187  Bit Score: 125.10  E-value: 8.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLKSVSGKplpCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKDPG------------------ 384
Cdd:cd23285     1 VHYGDVITIKHRDTN---AFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDpidehegtgrpvrngdli 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 385 ------------RHDVAAPLSPHSQEVSCyIDYNISMPAQN--LWKLDIVNRESNrDTWKTILSEVRFVHVNTSAILKLS 450
Cdd:cd23285    78 rlrhvstdtyllTHDVASPLTPTNMEFTT-VSDDDTDERYNetLFRVEIEDTDEG-DVLKTKSSHFRLIHVDTNVALWTH 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907144097 451 GAHLPDWGFRQLEVVGEKLSPGyhESMVWNVEE 483
Cdd:cd23285   156 KKPLPDWGFGQQEVNGNKNIKD--KSNIWVVDD 186
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 323-483 2.73e-30

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 1 (PMT1) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called PMTs, are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT1 and PMT5. PMT1 forms a heterodimeric complex with PMT2 and more rarely with PMT5. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. It is required for incorporation of proteins in the cell wall. PMT5 form a functional heterodimer with PMT3 and more rarely with PMT1. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467754 [Multi-domain]  Cd Length: 190  Bit Score: 117.78  E-value: 2.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLKSVSgkPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDINNWWIVKDPGR----------------- 385
Cdd:cd23283     1 VAYGSTIRIRHLN--TRGGYLHSHPHNYP-------AGSKQQQITLYPHRDENNDWLVELANApeewspttfenlkdgdv 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 386 --------------HDVAAPLS--PHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRD----TWKTILSEVRFVHVNTSA 445
Cdd:cd23283    72 vrlehvatgrrlhsHDHRPPVSdnDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGeskeRVRAIDTKFRLVHVMTGC 151

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907144097 446 ILKLSGAHLPDWGFRQLEVVGEKlSPGYHESmVWNVEE 483
Cdd:cd23283   152 YLFSHGVKLPEWGFEQQEVTCAK-SGLLELS-LWYIET 187
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 323-486 2.91e-30

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar proteins; POMT2 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 2, is a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids. POMT2 transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins. POMT2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467753 [Multi-domain]  Cd Length: 183  Bit Score: 117.79  E-value: 2.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLK-SVSGKPLpcwLHSHKNTYPmiyeNGRGSsHQQQVTCYPFKDINNWWIVKDPGR---------------- 385
Cdd:cd23282     1 VAYGSVITLKnHRTGGGY---LHSHWHLYP----EGVGA-RQQQVTTYSHKDDNNLWLIKKHNQssdlsdpveyvrhgdl 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 386 --------------HDVAAPLSPHSQEVSCYIDyNISMPAQNLWKLDIVNRESNrDTWKTILSEVRFVHVNTSAILKLSG 451
Cdd:cd23282    73 irlehvntkrnlhsHKEKAPLTKKHYQVTGYGE-NGTGDANDVWRVEVVGGREG-DPVKTVRSKFRLVHYNTGCALHSHG 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907144097 452 AHLPDWGFRQLEVVgekLSPGYHE-SMVWNVEEHRY 486
Cdd:cd23282   151 KQLPKWGWEQLEVT---CNPNVRDkNSLWNVEDNRN 183
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 323-465 7.66e-18

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 7 (PMT7) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called PMTs, are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT7. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467757 [Multi-domain]  Cd Length: 192  Bit Score: 82.10  E-value: 7.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLKSVSGkpLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFK-DINNWWIVKDPG----------------- 384
Cdd:cd23286     1 LLYGSTVTIRHLES--LGGYLHSHDLTYP-------SGSNEQQVTLYDFEdDANNEWIIETKTkeqmdkfpgqfrevrdg 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 385 -----RHDVAA----------PLSPH--SQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTW------KTILSEVRFVHV 441
Cdd:cd23286    72 dvirlRHVVTGkllrasnarpPVSEQeyNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKlpnikiKSTESVFQLYNR 151

                         170       180
                  ....*....|....*....|....
gi 1907144097 442 NTSAILKLSGAHLPDWGFRQLEVV 465
Cdd:cd23286   152 GTGCTLLSHDTRLPDWAFHQQEVL 175
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 56-281 8.53e-16

Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 80.71  E-value: 8.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097  56 WQLSYPRAVVFDEVYYG----QYISFYMKRIFFLDDSG----PPFGHMLLAlggwlggfdgnflwnrIGAEYSSNVPIWS 127
Cdd:COG1928    38 WGLGRPNTLVFDETYYVkdawSLLTNGYERNWPDPGPFfvvhPPLGKWLIA----------------LGEWLFGYVNPFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 128 LRLLPALAGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVL--------------S 193
Cdd:COG1928   102 WRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGcllldrdqvrrrlaA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 194 YLKFFNSQTHSPFSVHWWLWLLLTGVSCSCAVGIKYMGIFtYLLVLGIAAVhAWNLIGDQTLSNMRVLSHLLAR-----I 268
Cdd:COG1928   182 AVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTV-AWDAGARRAAGVRRPWLGALLRdgipaF 259

                         250
                  ....*....|...
gi 1907144097 269 VALLVVPVFLYLL 281
Cdd:COG1928   260 FALVIVPLLTYLA 272
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 325-467 1.86e-11

MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The SDF-2 family includes mammalian SDF-2 and SDF2-like protein 1 (SDF2L1) as well as similar proteins from plant, such as Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2). SDF-2 is a secretory protein involved in multiple endoplasmic reticulum (ER) functions, including the misfolded protein catabolic process, protein glycosylation, and ER protein quality control. SDF2L1, also called PWP1-interacting protein 8, is an endoplasmic reticulum (ER)-localized protein that plays a role in ER-associated degradation (ERAD) of misfolded proinsulin in pancreatic beta-cells. It is a component of the endoplasmic reticulum (ER) chaperone complex and interacts with alpha- and beta-defensins. SDF2L1 may also act as a tumor suppressor that play an important role in a variety of cancers, such as breast cancer and ovarian cancer. AtSDF2, also called SDF2-like protein, acts as crucial component of the unfolded protein response (UPR) in Arabidopsis thaliana. It is involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. It may be involved in the quality control of glycoproteins. AtSDF2 forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467750 [Multi-domain]  Cd Length: 173  Bit Score: 63.09  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 325 FGSQVTLKSVSGKplpCWLHSHKNTYpmiyenGRGSShQQQVTCYP-FKDINNWWIVKDPGR------------------ 385
Cdd:cd23279     1 YGSAIKLKHVNSG---YRLHSHEVSY------GSGSG-QQSVTAVPsADDANSLWTVLPGLGepcqeqgkpvkcgdiirl 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 386 -----------HDVAAPLSPHsQEVSCY--IDYNISmpaqNLWKLDIVNreSNRDTWKtILSEVRFVHVNTSAILKLSGA 452
Cdd:cd23279    71 qhvntrknlhsHNHSSPLSGN-QEVSAFggGDEDSG----DNWIVECEG--KKAKFWK-RGEPVRLKHVDTGKYLSASKT 142

                         170
                  ....*....|....*
gi 1907144097 453 HLpdwgFRQLEVVGE 467
Cdd:cd23279   143 HK----FTQQPIAGQ 153
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 123-300 2.69e-11

PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 65.41  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 123 VPIWSLRLLPALAGALSVPMAYQIVLELhFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQT 202
Cdd:COG1807    81 VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRALERRR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 203 hspfsvhwWLWLLLTGVSCSCAVGIKYMGIFTYLLVLGIAAvhawnLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLF 282
Cdd:COG1807   160 --------LRWLLLAGLALGLGFLTKGPVALLLPGLALLLY-----LLLTRRWRRLRRLRLLLGLLLALLLALPWYIAND 226

                         170
                  ....*....|....*...
gi 1907144097 283 FYVHLMLLYRSGPHDQIM 300
Cdd:COG1807   227 WATGPAFLEYFFGYENLV 244
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 323-447 1.56e-09

MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2) and similar proteins; AtSDF2, also called SDF2-like protein, acts as a crucial component of the unfolded protein response (UPR) in Arabidopsis thaliana. It is involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. It may be involved in the quality control of glycoproteins. AtSDF2 forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity. AtSDF2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with 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.


Pssm-ID: 467765 [Multi-domain]  Cd Length: 176  Bit Score: 57.77  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 323 VAFGSQVTLKSVSGKplpCWLHSHKNTYpmiyenGRGSShQQQVTCYPFK-DINNWWIVKDPGR---------------- 385
Cdd:cd23294     1 VTCGSVIKLQHERTK---FRLHSHEVPY------GSGSG-QQSVTGFPGVdDSNSYWIVKPANGerckqgdvikngdvir 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907144097 386 ------------HDVAAPLSpHSQEVSCYIDYNISMPAQNlWKLDIvnrESNRDTWKtiLSE-VRFVHVNTSAIL 447
Cdd:cd23294    71 lqhvstrkwlhsHLHASPLS-GNQEVSCFGGDGNSDTGDN-WIVEI---EGGGKVWE--RDQkVRLKHVDTGGYL 138
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
323-380 5.76e-08

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 49.65  E-value: 5.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097  323 VAFGSQVTLKSVSGkplPCWLHSHKNTYPMIyengrgSSHQQQVTCYPFKDI--NNWWIV 380
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPAIdaNTLWLI 54
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 326-468 7.79e-08

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with 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 MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 52.77  E-value: 7.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 326 GSQVTLK-SVSGKplpcWLHSHKNTYPMiyengrgSSHQQQVTCY---PFKDINNWWIVK----DPG-----------RH 386
Cdd:cd23263     1 GDVIWLKhSETGK----YLHSHRKNYPT-------GSGQQEVTFEsssRKGDTNGLWIIEsengKQGgpvkwgdkirlRH 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 387 -----------DVAAPLSPHsQEVSCYIDYNISmpaQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSGAHLP 455
Cdd:cd23263    70 lstgkylsseeGKKSPKSNH-QEVLCLTDNPDK---SSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKKFN 145

                         170
                  ....*....|...
gi 1907144097 456 DWGFRQLEVVGEK 468
Cdd:cd23263   146 INNKTQQEVICHG 158
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 127-287 3.72e-07

Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General function prediction only];


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 53.52  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 127 SLRLLPALAGALSVPMAYqiVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQThspf 206
Cdd:COG4745    87 TARLPVALVGGLLPLLAL--LLRERLGDAEVLALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVRAIDTRR---- 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 207 svhwWLWLLLTGVSCSCAVGIK-----YMGIF--TYLLVLGIAAVHA-------------WNLIGDQTLSNMRVLSHLLA 266
Cdd:COG4745   161 ----RRYLYLAAVALALAFATKenavlYLLCWlgALLLLLDHRLFRArrrgtsvllvlrrLRRLVRRLRLLLRWWRHLVG 236

                         170       180
                  ....*....|....*....|.
gi 1907144097 267 RIVALLVVPVFLYLLFFYVHL 287
Cdd:COG4745   237 ALAVFLAVAVFFYAPRGGPGL 257
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 344-465 6.56e-07

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 50.05  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 344 HSHKNTYPMIYENGRGsSHQQQVTCYPFKDINN----WWIV----KDP-------------------GR----HDV-AAP 391
Cdd:pfam02815  13 HSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRIevvrHDAwrgglikwgspfrlrhlttGRylhsHEEqKPP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 392 LSPHS---QEVSCYiDYNISmpAQNLWKLDIVNRESN----RDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFR--QL 462
Cdd:pfam02815  92 LVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKKSTtgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpeQQ 168


                  ...
gi 1907144097 463 EVV 465
Cdd:pfam02815 169 KVT 171
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
434-484 2.63e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.33  E-value: 2.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907144097  434 SEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 484
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 122-276 4.14e-05

Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are not captured by pfam02366.


Pssm-ID: 433048 [Multi-domain]  Cd Length: 160  Bit Score: 44.56  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 122 NVPIWSLRLLPALAGALSVPMAYQIVLELhFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQ 201
Cdd:pfam13231  18 GDSEWAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVVPLFVALSRLFTPDAPLLLFWALALYFLLRALEKG 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907144097 202 ThspfsvhwWLWLLLTGVSCSCAVGIKYMGIftyllVLGIAAVhAWNLIGDQTLSNMRVLSHLLARIVALLVVPV 276
Cdd:pfam13231  97 R--------LKWWLLAGAAAGLGFLSKYTAA-----LLVLAAL-LYLLISPGRRRLKSPKPYLGLLLALLLFSPV 157
COG5305 COG5305
Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT ...
 125-283 2.50e-04

Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT family [General function prediction only];


Pssm-ID: 444104 [Multi-domain]  Cd Length: 402  Bit Score: 43.86  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 125 IWSLRLLPALAGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRlmllE----SILIFFNLLAVLSYLKFFNS 200
Cdd:COG5305   107 EWALRSLSALFGLLAIPLIYWLGRELFRSRRVALLAAALMAVSPFHIYYAQ----EarmySLLTLLVLLSLLALLRALRR 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 201 QThspfsvhWWLWLLLTGVscsCAVGIkYMGIFTYLLVLGIAAVHAWNLIGDQTLSnmRVLSHLLARIVALLVVPVFLYL 280
Cdd:COG5305   183 PT-------RRLWLLYALA---NALGL-YTHYFFALVLIAHGLYLLLLAWFRRDRK--TWLRYLLAAAAAVLLFLPWLLV 249


                  ...
gi 1907144097 281 LFF 283
Cdd:COG5305   250 LLT 252
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
 120-283 9.88e-03

Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 39.39  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 120 SSNVPIWSLRLLPALAGALSVPMAYQIVLELhFSHGAAIGAALLMLIENALITQSRL-----MLLESILIFFNLLAVLSY 194
Cdd:COG1287   107 SQSSVYTVAAWFPPIFGALTVIPVYLLGRRL-GGRKAGLLAALLLALSPGQLSRSLLgfadhHVAELFFSTLAVLFLVLA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144097 195 LKFFNSQTHSPFSVHW-WLWLLLTGVscscAVGIKYMGIFTYLLVLGIAAVHAW-NLIGDqtLSNMRVLSHLLARIVALL 272
Cdd:COG1287   186 LKRAKREKRDLEALKRpLLYAVLAGV----ALGLYLLTWGGYVLFVGILALFALlQLLLD--LLRGRSPEYLAIVGAVSF 259

                         170
                  ....*....|.
gi 1907144097 273 VVPVFLYLLFF 283
Cdd:COG1287   260 AVAALLVLPFI 270
 
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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