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Conserved domains on  [gi|74145312|dbj|BAE22274|]
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unnamed protein product [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 ...
 321-515 1.19e-125

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: 372.41  E-value: 1.19e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLKSVSGKPlpCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDI 400
Cdd:cd23281   1 VAYGSQVTLRNTHGSP--CWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 401 VQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSG 480
Cdd:cd23281  79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 74145312 481 AHLPDWGFRQLEVVGEKlsPGYHESMVWNVEEHRY 515
Cdd:cd23281 159 KQLPDWGFGQLEVATDR--AGNQSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 54-289 1.11e-70

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: 231.05  E-value: 1.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312    54 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSgPPFGHMLLALGGWLGGFDGNFLWNRIGAEYS-SNVPIWSLRLLPAL 132
Cdd:pfam02366  13 WNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   133 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFnsqTHSPFSVHWWLWL 212
Cdd:pfam02366  92 LGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---RKAPFSRKWWLWL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74145312   213 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 289
Cdd:pfam02366 169 LLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 544-738 2.35e-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: 190.83  E-value: 2.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   544 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 622
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   623 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 699
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 74145312   700 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 738
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 ...
 321-515 1.19e-125

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: 372.41  E-value: 1.19e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLKSVSGKPlpCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDI 400
Cdd:cd23281   1 VAYGSQVTLRNTHGSP--CWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 401 VQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSG 480
Cdd:cd23281  79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 74145312 481 AHLPDWGFRQLEVVGEKlsPGYHESMVWNVEEHRY 515
Cdd:cd23281 159 KQLPDWGFGQLEVATDR--AGNQSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 54-289 1.11e-70

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: 231.05  E-value: 1.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312    54 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSgPPFGHMLLALGGWLGGFDGNFLWNRIGAEYS-SNVPIWSLRLLPAL 132
Cdd:pfam02366  13 WNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   133 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFnsqTHSPFSVHWWLWL 212
Cdd:pfam02366  92 LGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---RKAPFSRKWWLWL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74145312   213 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 289
Cdd:pfam02366 169 LLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 544-738 2.35e-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: 190.83  E-value: 2.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   544 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 622
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   623 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 699
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 74145312   700 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 738
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 54-279 5.87e-16

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 81.48  E-value: 5.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312  54 WQLSYPRAVVFDEVYYG----QYISFYMKRIFFLDDSG----PPFGHMLLAlggwlggfdgnflwnrIGAEYSSNVPIWS 125
Cdd:COG1928  38 WGLGRPNTLVFDETYYVkdawSLLTNGYERNWPDPGPFfvvhPPLGKWLIA----------------LGEWLFGYVNPFG 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 126 LRLLPALAGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVL--------------S 191
Cdd:COG1928 102 WRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGcllldrdqvrrrlaA 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 192 YLKFFNSQTHSPFSVHWWLWLLLTGVSCSCAVGIKYMGIFtYLLVLGIAAVhAWNLIGDQTLSNMRVLSHLLAR-----I 266
Cdd:COG1928 182 AVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTV-AWDAGARRAAGVRRPWLGALLRdgipaF 259

                       250
                ....*....|...
gi 74145312 267 VALLVVPVFLYLL 279
Cdd:COG1928 260 FALVIVPLLTYLA 272
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 342-494 1.95e-13

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: 69.31  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   342 HSHKNTYPMIYENGRGsSHQQQVTCYPFKDINN----WWIVkdpgrhqLVVNNPP---RPVRHGDIVQLVHGMTTRLLNT 414
Cdd:pfam02815  13 HSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLRHLTTGRYLHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   415 HDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWKLDIVNRESN----RDTWKTILSEVRFVHVNTSAILKLSGAHLPDW 486
Cdd:pfam02815  85 HEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKKSTtgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW 161

                         170
                  ....*....|
gi 74145312   487 GFR--QLEVV 494
Cdd:pfam02815 162 GFGpeQQKVT 171
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 548-740 2.73e-09

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 60.29  E-value: 2.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 548 ELQWKMLTL-KNEDLEHQYSSTPLEWLTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWTSASLATVVytlLFF 615
Cdd:COG1928 309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPALLW---LLW 385

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 616 WYLLRRRrsicdlpedaWsrwvLAGALCTgGWALNYLPFFL-MERVLFLYHYLPALTFQILLLPIVLQHASDHLcRSQLQ 694
Cdd:COG1928 386 RWIARRD----------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLILGPA-RASER 449

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 74145312 695 RNVFSALVVAWYSSACHVSNMLRPLTYGDTsLSPGELRALRWKDSW 740
Cdd:COG1928 450 RRLGRLVVGLYVGLVVANFAFFYPILTGLP-IPYDEWQARMWFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
321-378 9.15e-08

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 49.26  E-value: 9.15e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312    321 VAFGSQVTLKSVSGkplPCWLHSHKNTYPMIyengrgSSHQQQVTCYPFKDI--NNWWIV 378
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPAIdaNTLWLI 54
 
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 ...
 321-515 1.19e-125

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: 372.41  E-value: 1.19e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLKSVSGKPlpCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDI 400
Cdd:cd23281   1 VAYGSQVTLRNTHGSP--CWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 401 VQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSG 480
Cdd:cd23281  79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 74145312 481 AHLPDWGFRQLEVVGEKlsPGYHESMVWNVEEHRY 515
Cdd:cd23281 159 KQLPDWGFGQLEVATDR--AGNQSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 54-289 1.11e-70

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: 231.05  E-value: 1.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312    54 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSgPPFGHMLLALGGWLGGFDGNFLWNRIGAEYS-SNVPIWSLRLLPAL 132
Cdd:pfam02366  13 WNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   133 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFnsqTHSPFSVHWWLWL 212
Cdd:pfam02366  92 LGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---RKAPFSRKWWLWL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74145312   213 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 289
Cdd:pfam02366 169 LLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 321-513 4.60e-64

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: 211.42  E-value: 4.60e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLKSVSgkPLPCWLHSHKNTYPMIyengrgsSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDI 400
Cdd:cd23276   1 VAYGSQITLRNAN--SGGGYLHSHNHTYPDG-------SKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDPEYVRDGDE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 401 VQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESN--RDTWKTILSEVRFVHVNTSAILKL 478
Cdd:cd23276  72 VRLLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGDDNDLWVVEIVKDEGKleDKRIKPLTTRFRLRNKKTGCYLTS 151

                       170       180       190
                ....*....|....*....|....*....|....*
gi 74145312 479 SGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 513
Cdd:cd23276 152 SGVKLPEWGFRQGEVVCSK-NKESDPSTLWNVEEN 185
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 544-738 2.35e-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: 190.83  E-value: 2.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   544 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 622
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   623 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 699
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 74145312   700 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 738
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 319-513 6.19e-48

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: 167.88  E-value: 6.19e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 319 LEVAFGSQVTLKSVsgKPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNN--PPRPVR 396
Cdd:cd23284   2 LDVAYGSKVTIKNQ--GLGGGLLHSHVQTYP-------EGSNQQQVTCYGHKDSNNEWIFERPRGLPSWDENdtDIEFIK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 397 HGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNlWKLDIVNRESNRDTWK--TILSEVRFVHVNTSA 474
Cdd:cd23284  73 DGDIVRLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDN-WVIEIVKQVGSEDPKKlhTLTTSFRLRHEVLGC 151

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 74145312 475 ILKLSGAHLPDWGFRQLEVVGEKLSPGYHESMVWNVEEH 513
Cdd:cd23284 152 YLAQTGVSLPEWGFKQGEVVCDKSNFKRDKRTWWNIETH 190
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 321-512 2.61e-46

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: 163.23  E-value: 2.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLKSVSGKplpCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKdPGRHQLVVNNPPRPVRHGDI 400
Cdd:cd23285   1 VHYGDVITIKHRDTN---AFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQIL-PTDPIDEHEGTGRPVRNGDL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 401 VQLVHGMTTRLLNTHDVAAPLSPHSQEVSCyIDYNISMPAQN--LWKLDIVNRESNrDTWKTILSEVRFVHVNTSAILKL 478
Cdd:cd23285  77 IRLRHVSTDTYLLTHDVASPLTPTNMEFTT-VSDDDTDERYNetLFRVEIEDTDEG-DVLKTKSSHFRLIHVDTNVALWT 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 74145312 479 SGAHLPDWGFRQLEVVGEKLSPGyhESMVWNVEE 512
Cdd:cd23285 155 HKKPLPDWGFGQQEVNGNKNIKD--KSNIWVVDD 186
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 321-515 9.31e-43

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: 153.23  E-value: 9.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLK-SVSGKPLpcwLHSHKNTYPmiyeNGRGSsHQQQVTCYPFKDINNWWIVKDPGRHQLVvNNPPRPVRHGD 399
Cdd:cd23282   1 VAYGSVITLKnHRTGGGY---LHSHWHLYP----EGVGA-RQQQVTTYSHKDDNNLWLIKKHNQSSDL-SDPVEYVRHGD 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 400 IVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDyNISMPAQNLWKLDIVNRESNrDTWKTILSEVRFVHVNTSAILKLS 479
Cdd:cd23282  72 LIRLEHVNTKRNLHSHKEKAPLTKKHYQVTGYGE-NGTGDANDVWRVEVVGGREG-DPVKTVRSKFRLVHYNTGCALHSH 149

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 74145312 480 GAHLPDWGFRQLEVVgekLSPGYHE-SMVWNVEEHRY 515
Cdd:cd23282 150 GKQLPKWGWEQLEVT---CNPNVRDkNSLWNVEDNRN 183
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 321-512 3.44e-42

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: 151.68  E-value: 3.44e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLKSVSgkPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDI 400
Cdd:cd23283   1 VAYGSTIRIRHLN--TRGGYLHSHPHNYP-------AGSKQQQITLYPHRDENNDWLVELANAPEEWSPTTFENLKDGDV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 401 VQLVHGMTTRLLNTHDVAAPLS--PHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRD----TWKTILSEVRFVHVNTSA 474
Cdd:cd23283  72 VRLEHVATGRRLHSHDHRPPVSdnDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGeskeRVRAIDTKFRLVHVMTGC 151

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 74145312 475 ILKLSGAHLPDWGFRQLEVVGEKlSPGYHESmVWNVEE 512
Cdd:cd23283 152 YLFSHGVKLPEWGFEQQEVTCAK-SGLLELS-LWYIET 187
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 321-494 3.63e-28

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: 112.14  E-value: 3.63e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLKSVSGkpLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFK-DINNWWIVKDPGRHQLV-VNNPPRPVRHG 398
Cdd:cd23286   1 LLYGSTVTIRHLES--LGGYLHSHDLTYP-------SGSNEQQVTLYDFEdDANNEWIIETKTKEQMDkFPGQFREVRDG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 399 DIVQLVHGMTTRLLNTHDVAAPLSPH--SQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTW------KTILSEVRFVHV 470
Cdd:cd23286  72 DVIRLRHVVTGKLLRASNARPPVSEQeyNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKlpnikiKSTESVFQLYNR 151

                       170       180
                ....*....|....*....|....
gi 74145312 471 NTSAILKLSGAHLPDWGFRQLEVV 494
Cdd:cd23286 152 GTGCTLLSHDTRLPDWAFHQQEVL 175
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 323-496 4.88e-21

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: 90.82  E-value: 4.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 323 FGSQVTLKSVSGKplpCWLHSHKNTYpmiyenGRGSShQQQVTCYP-FKDINNWWIVK----DPGRHQlvvnnpPRPVRH 397
Cdd:cd23279   1 YGSAIKLKHVNSG---YRLHSHEVSY------GSGSG-QQSVTAVPsADDANSLWTVLpglgEPCQEQ------GKPVKC 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 398 GDIVQLVHGMTTRLLNTHDVAAPLSPHsQEVSCY--IDYNISmpaqNLWKLDIVNreSNRDTWKtILSEVRFVHVNTSAI 475
Cdd:cd23279  65 GDIIRLQHVNTRKNLHSHNHSSPLSGN-QEVSAFggGDEDSG----DNWIVECEG--KKAKFWK-RGEPVRLKHVDTGKY 136

                       170       180
                ....*....|....*....|.
gi 74145312 476 LKLSGAHLpdwgFRQLEVVGE 496
Cdd:cd23279 137 LSASKTHK----FTQQPIAGQ 153
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 321-476 1.20e-16

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: 78.19  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 321 VAFGSQVTLKSVSGKplpCWLHSHKNTYpmiyenGRGSShQQQVTCYPFK-DINNWWIVKDPGRHQLVvnnPPRPVRHGD 399
Cdd:cd23294   1 VTCGSVIKLQHERTK---FRLHSHEVPY------GSGSG-QQSVTGFPGVdDSNSYWIVKPANGERCK---QGDVIKNGD 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74145312 400 IVQLVHGMTTRLLNTHDVAAPLSpHSQEVSCYIDYNISMPAQNlWKLDIvnrESNRDTWKtiLSE-VRFVHVNTSAIL 476
Cdd:cd23294  68 VIRLQHVSTRKWLHSHLHASPLS-GNQEVSCFGGDGNSDTGDN-WIVEI---EGGGKVWE--RDQkVRLKHVDTGGYL 138
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 54-279 5.87e-16

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 81.48  E-value: 5.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312  54 WQLSYPRAVVFDEVYYG----QYISFYMKRIFFLDDSG----PPFGHMLLAlggwlggfdgnflwnrIGAEYSSNVPIWS 125
Cdd:COG1928  38 WGLGRPNTLVFDETYYVkdawSLLTNGYERNWPDPGPFfvvhPPLGKWLIA----------------LGEWLFGYVNPFG 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 126 LRLLPALAGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVL--------------S 191
Cdd:COG1928 102 WRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGcllldrdqvrrrlaA 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 192 YLKFFNSQTHSPFSVHWWLWLLLTGVSCSCAVGIKYMGIFtYLLVLGIAAVhAWNLIGDQTLSNMRVLSHLLAR-----I 266
Cdd:COG1928 182 AVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTV-AWDAGARRAAGVRRPWLGALLRdgipaF 259

                       250
                ....*....|...
gi 74145312 267 VALLVVPVFLYLL 279
Cdd:COG1928 260 FALVIVPLLTYLA 272
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 324-497 2.81e-14

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: 71.26  E-value: 2.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 324 GSQVTLK-SVSGKplpcWLHSHKNTYPMiyengrgSSHQQQVTCY---PFKDINNWWIVkdpgrhQLVVNNPPRPVRHGD 399
Cdd:cd23263   1 GDVIWLKhSETGK----YLHSHRKNYPT-------GSGQQEVTFEsssRKGDTNGLWII------ESENGKQGGPVKWGD 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 400 IVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNISmpaQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLS 479
Cdd:cd23263  64 KIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDK---SSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSH 140

                       170
                ....*....|....*...
gi 74145312 480 GAHLPDWGFRQLEVVGEK 497
Cdd:cd23263 141 EKKFNINNKTQQEVICHG 158
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 342-494 1.95e-13

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: 69.31  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   342 HSHKNTYPMIYENGRGsSHQQQVTCYPFKDINN----WWIVkdpgrhqLVVNNPP---RPVRHGDIVQLVHGMTTRLLNT 414
Cdd:pfam02815  13 HSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLRHLTTGRYLHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   415 HDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWKLDIVNRESN----RDTWKTILSEVRFVHVNTSAILKLSGAHLPDW 486
Cdd:pfam02815  85 HEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKKSTtgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW 161

                         170
                  ....*....|
gi 74145312   487 GFR--QLEVV 494
Cdd:pfam02815 162 GFGpeQQKVT 171
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 341-495 3.21e-13

MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 (SDF-2); The metazoan SDF-2 family includes SDF-2 and SDF2-like protein 1 (SDF2L1). 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. 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: 467764 [Multi-domain]  Cd Length: 175  Bit Score: 68.45  E-value: 3.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 341 LHSHKNTYpmiyenGRGSShQQQVTCYPFK-DINNWWIVKdpGRHQLVVNNPpRPVRHGDIVQLVHGMTTRLLNTHDVAA 419
Cdd:cd23293  18 LHSHDVKY------GSGSG-QQSVTGVESSdDSNSYWQIR--GPTGADCERG-TPIKCGQTIRLTHLNTGKNLHSHHFQS 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74145312 420 PLSpHSQEVSCYIDYNISMPAQNlWKLDIVNRESNRDtwktilSEVRFVHVNTSAILKLSGAHL--PDWGfrQLEVVG 495
Cdd:cd23293  88 PLS-GNQEVSAFGEDGEGDTGDN-WTVVCSGTYWERD------EAVRLKHVDTEVYLHVTGEQYgrPIHG--QREVSG 155
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 121-288 1.02e-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: 66.57  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 121 VPIWSLRLLPALAGALSVPMAYQIVLELhFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQT 200
Cdd:COG1807  81 VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRALERRR 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 201 hspfsvhwWLWLLLTGVSCSCAVGIKYMGIFTYLLVLGIAAvhawnLIGDQTLSNMRVLSHLLARIVALLVV-------- 272
Cdd:COG1807 160 --------LRWLLLAGLALGLGFLTKGPVALLLPGLALLLY-----LLLTRRWRRLRRLRLLLGLLLALLLAlpwyiand 226

                       170       180
                ....*....|....*....|
gi 74145312 273 ----PVFLYLLFFYVHLMLL 288
Cdd:COG1807 227 watgPAFLEYFFGYENLVPL 246
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 548-740 2.73e-09

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 60.29  E-value: 2.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 548 ELQWKMLTL-KNEDLEHQYSSTPLEWLTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWTSASLATVVytlLFF 615
Cdd:COG1928 309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPALLW---LLW 385

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 616 WYLLRRRrsicdlpedaWsrwvLAGALCTgGWALNYLPFFL-MERVLFLYHYLPALTFQILLLPIVLQHASDHLcRSQLQ 694
Cdd:COG1928 386 RWIARRD----------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLILGPA-RASER 449

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 74145312 695 RNVFSALVVAWYSSACHVSNMLRPLTYGDTsLSPGELRALRWKDSW 740
Cdd:COG1928 450 RRLGRLVVGLYVGLVVANFAFFYPILTGLP-IPYDEWQARMWFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
321-378 9.15e-08

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 49.26  E-value: 9.15e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312    321 VAFGSQVTLKSVSGkplPCWLHSHKNTYPMIyengrgSSHQQQVTCYPFKDI--NNWWIV 378
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPAIdaNTLWLI 54
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 125-285 3.09e-07

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


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 53.90  E-value: 3.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 125 SLRLLPALAGALSVPMAYqiVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQThspf 204
Cdd:COG4745  87 TARLPVALVGGLLPLLAL--LLRERLGDAEVLALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVRAIDTRR---- 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 205 svhwWLWLLLTGVSCSCAVGIK-----YMGIF--TYLLVLGIAAVHA-------------WNLIGDQTLSNMRVLSHLLA 264
Cdd:COG4745 161 ----RRYLYLAAVALALAFATKenavlYLLCWlgALLLLLDHRLFRArrrgtsvllvlrrLRRLVRRLRLLLRWWRHLVG 236

                       170       180
                ....*....|....*....|.
gi 74145312 265 RIVALLVVPVFLYLLFFYVHL 285
Cdd:COG4745 237 ALAVFLAVAVFFYAPRGGPGL 257
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 120-274 2.27e-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: 45.33  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312   120 NVPIWSLRLLPALAGALSVPMAYQIVLELhFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQ 199
Cdd:pfam13231  18 GDSEWAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVVPLFVALSRLFTPDAPLLLFWALALYFLLRALEKG 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74145312   200 ThspfsvhwWLWLLLTGVSCSCAVGIKYMGIftyllVLGIAAVhAWNLIGDQTLSNMRVLSHLLARIVALLVVPV 274
Cdd:pfam13231  97 R--------LKWWLLAGAAAGLGFLSKYTAA-----LLVLAAL-LYLLISPGRRRLKSPKPYLGLLLALLLFSPV 157
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
463-513 3.67e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.94  E-value: 3.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 74145312    463 SEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 513
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
COG5305 COG5305
Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT ...
 123-281 1.36e-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: 45.02  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 123 IWSLRLLPALAGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRlmllE----SILIFFNLLAVLSYLKFFNS 198
Cdd:COG5305 107 EWALRSLSALFGLLAIPLIYWLGRELFRSRRVALLAAALMAVSPFHIYYAQ----EarmySLLTLLVLLSLLALLRALRR 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 199 QThspfsvhWWLWLLLTGVscsCAVGIkYMGIFTYLLVLGIAAVHAWNLIGDQTLSnmRVLSHLLARIVALLVVPVFLYL 278
Cdd:COG5305 183 PT-------RRLWLLYALA---NALGL-YTHYFFALVLIAHGLYLLLLAWFRRDRK--TWLRYLLAAAAAVLLFLPWLLV 249


                ...
gi 74145312 279 LFF 281
Cdd:COG5305 250 LLT 252
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
392-449 2.57e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 39.63  E-value: 2.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 74145312    392 PRPVRHGDIVQLVHGMTTRLLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWKLDIV 449
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
 118-281 6.60e-03

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


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 39.78  E-value: 6.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 118 SSNVPIWSLRLLPALAGALSVPMAYQIVLELhFSHGAAIGAALLMLIENALITQSRL-----MLLESILIFFNLLAVLSY 192
Cdd:COG1287 107 SQSSVYTVAAWFPPIFGALTVIPVYLLGRRL-GGRKAGLLAALLLALSPGQLSRSLLgfadhHVAELFFSTLAVLFLVLA 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74145312 193 LKFFNSQTHSPFSVHW-WLWLLLTGVscscAVGIKYMGIFTYLLVLGIAAVHAW-NLIGDqtLSNMRVLSHLLARIVALL 270
Cdd:COG1287 186 LKRAKREKRDLEALKRpLLYAVLAGV----ALGLYLLTWGGYVLFVGILALFALlQLLLD--LLRGRSPEYLAIVGAVSF 259

                       170
                ....*....|.
gi 74145312 271 VVPVFLYLLFF 281
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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