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Conserved domains on  [gi|1239920855|ref|XP_022279400|]
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protein O-mannosyl-transferase 1 isoform X1 [Canis lupus familiaris]

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 ...
 315-509 1.34e-126

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: 375.49  E-value: 1.34e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKNVFGkpVPCWLHSHQSTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPGRHQLVVNNPPRPVRHGDV 394
Cdd:cd23281     1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 395 VQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYVDYNISMPSQNLWRLDIVNRESDTEVWKTILSEVRLVHVNTSAVLKLSG 474
Cdd:cd23281    79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1239920855 475 AHLPDWGFQQLEVVGEKLSRgyHESMVWNVEEHRY 509
Cdd:cd23281   159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-283 4.62e-66

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: 219.49  E-value: 4.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  20 VALTAVGLLSRLWHLAYPRAVVrddcwqyygavplwltFDEVYYGQYISFYMKRIFFLDGSgPPFGHMLLALGGYLGGFD 99
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVV----------------FDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 100 GNFLWNRIGAEYS-SNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFF 178
Cdd:pfam02366  64 GNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFF 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 179 NLLAVLSYLKFsnsQKHRPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLA 258
Cdd:pfam02366 144 TTLSMYCFWKF---ERKAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFA 220

                         250       260
                  ....*....|....*....|....*
gi 1239920855 259 RAAALLVIPTLMYLLFFYVHLILVY 283
Cdd:pfam02366 221 RLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 538-762 1.07e-53

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: 183.90  E-value: 1.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 538 ARFLELQWRMLTAKSD-DSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQIHLLGNIVIWASASLAMVVYVLLFFWYLLRRR 616
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 617 RSICDIPEETkccrciptlleassgkckdqagiavtpgySWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALTF 696
Cdd:pfam16192  81 RGYYDLSDDW-----------------------------TRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYF 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239920855 697 QILLLPVVLQHVSDHLCR--SQLLRSLFSALVVAWYSCACHVFNTLRPLTYGDKSLSpSELKALRWKD 762
Cdd:pfam16192 132 AILALGALLDFLLSLFRRlpRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-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 ...
 315-509 1.34e-126

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: 375.49  E-value: 1.34e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKNVFGkpVPCWLHSHQSTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPGRHQLVVNNPPRPVRHGDV 394
Cdd:cd23281     1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 395 VQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYVDYNISMPSQNLWRLDIVNRESDTEVWKTILSEVRLVHVNTSAVLKLSG 474
Cdd:cd23281    79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1239920855 475 AHLPDWGFQQLEVVGEKLSRgyHESMVWNVEEHRY 509
Cdd:cd23281   159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-283 4.62e-66

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: 219.49  E-value: 4.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  20 VALTAVGLLSRLWHLAYPRAVVrddcwqyygavplwltFDEVYYGQYISFYMKRIFFLDGSgPPFGHMLLALGGYLGGFD 99
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVV----------------FDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 100 GNFLWNRIGAEYS-SNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFF 178
Cdd:pfam02366  64 GNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFF 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 179 NLLAVLSYLKFsnsQKHRPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLA 258
Cdd:pfam02366 144 TTLSMYCFWKF---ERKAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFA 220

                         250       260
                  ....*....|....*....|....*
gi 1239920855 259 RAAALLVIPTLMYLLFFYVHLILVY 283
Cdd:pfam02366 221 RLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 538-762 1.07e-53

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: 183.90  E-value: 1.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 538 ARFLELQWRMLTAKSD-DSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQIHLLGNIVIWASASLAMVVYVLLFFWYLLRRR 616
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 617 RSICDIPEETkccrciptlleassgkckdqagiavtpgySWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALTF 696
Cdd:pfam16192  81 RGYYDLSDDW-----------------------------TRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYF 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239920855 697 QILLLPVVLQHVSDHLCR--SQLLRSLFSALVVAWYSCACHVFNTLRPLTYGDKSLSpSELKALRWKD 762
Cdd:pfam16192 132 AILALGALLDFLLSLFRRlpRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 326-488 5.45e-17

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: 79.72  E-value: 5.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 326 VFGKPVPCWLHSHQSTYPMIYENGRGSsHQQQVTCYPFKDVNN----WWIVkdpgrhqLVVNNPP---RPVRHGDVVQLV 398
Cdd:pfam02815   3 LKGGDVVRLFHSHQDEYLTGSEQQQKQ-PFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 399 HGMTTRFLNTHDV-AAPLSPHS---QEVSCYvDYNISM----PSQNLWRLDIVNRESDTEvwKTILSEVRLVHVNTSAVL 470
Cdd:pfam02815  75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGFPgdndIVEIFEKKSTTGMGSDRI--KPGDSYFRLQHVCTGCWL 151

                         170       180
                  ....*....|....*....|
gi 1239920855 471 KLSGAHLPDWGF--QQLEVV 488
Cdd:pfam02815 152 FSHSVKLPKWGFgpEQQKVT 171
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 20-239 4.37e-13

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 72.23  E-value: 4.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  20 VALTAVGLLSRLWHLAYPRAVVrddcwqyygavplwltFDEVYYG----QYISFYMKRIFFLDGSG----PPFGHMLLAl 91
Cdd:COG1928    26 LLVTLLAGVLRFWGLGRPNTLV----------------FDETYYVkdawSLLTNGYERNWPDPGPFfvvhPPLGKWLIA- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  92 ggylggfdgnflwnrIGAEYSSNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLL 171
Cdd:COG1928    89 ---------------LGEWLFGYVNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 172 ESVLIFFNLLAVLSYLKFSNSQKHR--------------PFSLSWWFWLMLTGVACSCAVGVKYMGIFtYLLVLAVASVh 237
Cdd:COG1928   154 DIFLMFFVLAAFGCLLLDRDQVRRRlaaavaagrapsrwGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTV- 231


                  ..
gi 1239920855 238 AW 239
Cdd:COG1928   232 AW 233
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 540-764 1.16e-08

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 58.36  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 540 FLELQWRMLT-AKSDDSEHKYSSSPLDWVTLDTSIAYWLH-----------PRTSAQIHLLGNIVIWASASLAMVVyvlL 607
Cdd:COG1928   307 LWHYHQQILSfHTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPALLW---L 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 608 FFWYLLRRrrsicdipeetkccrciptlleassgkckdqagiavtpgySWlrwvLAGALCAgGWAVNYLPFFM-MEKTLF 686
Cdd:COG1928   384 LWRWIARR----------------------------------------DW----RAGAVLV-GYAAGWLPWFLyLDRTMF 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 687 LYHYLPALTFQILLLPVVLQHV---SDHLCRSQLLR---SLFSALVVAwyscachVFNTLRPLTYGDkSLSPSELKALRW 760
Cdd:COG1928   419 FFYAIPFVPFLVLALALVLGLIlgpARASERRRLGRlvvGLYVGLVVA-------NFAFFYPILTGL-PIPYDEWQARMW 490


                  ....
gi 1239920855 761 KDSW 764
Cdd:COG1928   491 FPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
315-372 8.34e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.57  E-value: 8.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  315 VAYGSQVTLKNVFGkpvPCWLHSHQSTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 372
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 ...
 315-509 1.34e-126

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: 375.49  E-value: 1.34e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKNVFGkpVPCWLHSHQSTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPGRHQLVVNNPPRPVRHGDV 394
Cdd:cd23281     1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 395 VQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYVDYNISMPSQNLWRLDIVNRESDTEVWKTILSEVRLVHVNTSAVLKLSG 474
Cdd:cd23281    79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1239920855 475 AHLPDWGFQQLEVVGEKLSRgyHESMVWNVEEHRY 509
Cdd:cd23281   159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 315-507 2.33e-66

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: 217.97  E-value: 2.33e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKNVfgKPVPCWLHSHQSTYPMIyengrgsSHQQQVTCYPFKDVNNWWIVKDPGRHQLVVNNPPRPVRHGDV 394
Cdd:cd23276     1 VAYGSQITLRNA--NSGGGYLHSHNHTYPDG-------SKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDPEYVRDGDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 395 VQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYVDYNISMPSQNLWRLDIVNRESDTE--VWKTILSEVRLVHVNTSAVLKL 472
Cdd:cd23276    72 VRLLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGDDNDLWVVEIVKDEGKLEdkRIKPLTTRFRLRNKKTGCYLTS 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1239920855 473 SGAHLPDWGFQQLEVVGEKLSRGyHESMVWNVEEH 507
Cdd:cd23276   152 SGVKLPEWGFRQGEVVCSKNKES-DPSTLWNVEEN 185
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-283 4.62e-66

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: 219.49  E-value: 4.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  20 VALTAVGLLSRLWHLAYPRAVVrddcwqyygavplwltFDEVYYGQYISFYMKRIFFLDGSgPPFGHMLLALGGYLGGFD 99
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVV----------------FDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 100 GNFLWNRIGAEYS-SNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFF 178
Cdd:pfam02366  64 GNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFF 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 179 NLLAVLSYLKFsnsQKHRPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLA 258
Cdd:pfam02366 144 TTLSMYCFWKF---ERKAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFA 220

                         250       260
                  ....*....|....*....|....*
gi 1239920855 259 RAAALLVIPTLMYLLFFYVHLILVY 283
Cdd:pfam02366 221 RLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 538-762 1.07e-53

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: 183.90  E-value: 1.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 538 ARFLELQWRMLTAKSD-DSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQIHLLGNIVIWASASLAMVVYVLLFFWYLLRRR 616
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 617 RSICDIPEETkccrciptlleassgkckdqagiavtpgySWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALTF 696
Cdd:pfam16192  81 RGYYDLSDDW-----------------------------TRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYF 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239920855 697 QILLLPVVLQHVSDHLCR--SQLLRSLFSALVVAWYSCACHVFNTLRPLTYGDKSLSpSELKALRWKD 762
Cdd:pfam16192 132 AILALGALLDFLLSLFRRlpRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 315-506 3.11e-50

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: 174.02  E-value: 3.11e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKNVFGKpvpCWLHSHQSTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKdPGRHQLVVNNPPRPVRHGDV 394
Cdd:cd23285     1 VHYGDVITIKHRDTN---AFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQIL-PTDPIDEHEGTGRPVRNGDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 395 VQLVHGMTTRFLNTHDVAAPLSPHSQEVSC------YVDYNISmpsqnLWRLDIVNREsDTEVWKTILSEVRLVHVNTSA 468
Cdd:cd23285    77 IRLRHVSTDTYLLTHDVASPLTPTNMEFTTvsdddtDERYNET-----LFRVEIEDTD-EGDVLKTKSSHFRLIHVDTNV 150

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1239920855 469 VLKLSGAHLPDWGFQQLEVVGEKlsRGYHESMVWNVEE 506
Cdd:cd23285   151 ALWTHKKPLPDWGFGQQEVNGNK--NIKDKSNIWVVDD 186
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 312-507 1.47e-49

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: 172.50  E-value: 1.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 312 PLEVAYGSQVTLKNVfgKPVPCWLHSHQSTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKDPGRHQLVVNN--PPRPV 389
Cdd:cd23284     1 PLDVAYGSKVTIKNQ--GLGGGLLHSHVQTYP-------EGSNQQQVTCYGHKDSNNEWIFERPRGLPSWDENdtDIEFI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 390 RHGDVVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYVDYNISMPSQNlWRLDIVNRES--DTEVWKTILSEVRLVHVNTS 467
Cdd:cd23284    72 KDGDIVRLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDN-WVIEIVKQVGseDPKKLHTLTTSFRLRHEVLG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1239920855 468 AVLKLSGAHLPDWGFQQLEVVGEKLSRGYHESMVWNVEEH 507
Cdd:cd23284   151 CYLAQTGVSLPEWGFKQGEVVCDKSNFKRDKRTWWNIETH 190
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 315-506 1.68e-46

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: 164.01  E-value: 1.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKNVfgKPVPCWLHSHQSTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKDPGRHQLVVNNPPRPVRHGDV 394
Cdd:cd23283     1 VAYGSTIRIRHL--NTRGGYLHSHPHNYP-------AGSKQQQITLYPHRDENNDWLVELANAPEEWSPTTFENLKDGDV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 395 VQLVHGMTTRFLNTHDVAAPLS--PHSQEVSCYVDYNISMPSQNLWRLDIVNRESDTEV----WKTILSEVRLVHVNTSA 468
Cdd:cd23283    72 VRLEHVATGRRLHSHDHRPPVSdnDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGEskerVRAIDTKFRLVHVMTGC 151

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1239920855 469 VLKLSGAHLPDWGFQQLEVVGEKlsRGYHESMVWNVEE 506
Cdd:cd23283   152 YLFSHGVKLPEWGFEQQEVTCAK--SGLLELSLWYIET 187
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 315-509 2.49e-44

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: 157.47  E-value: 2.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKN--VFGKpvpcWLHSHQSTYPmiyeNGRGSsHQQQVTCYPFKDVNNWWIVKDPGRHQLVvNNPPRPVRHG 392
Cdd:cd23282     1 VAYGSVITLKNhrTGGG----YLHSHWHLYP----EGVGA-RQQQVTTYSHKDDNNLWLIKKHNQSSDL-SDPVEYVRHG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 393 DVVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYV-----DYNismpsqNLWRLDIVNRESDtEVWKTILSEVRLVHVNTS 467
Cdd:cd23282    71 DLIRLEHVNTKRNLHSHKEKAPLTKKHYQVTGYGengtgDAN------DVWRVEVVGGREG-DPVKTVRSKFRLVHYNTG 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1239920855 468 AVLKLSGAHLPDWGFQQLEVVGEKLSRgyHESMVWNVEEHRY 509
Cdd:cd23282   144 CALHSHGKQLPKWGWEQLEVTCNPNVR--DKNSLWNVEDNRN 183
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 315-488 1.25e-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: 113.30  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKNVFGkpVPCWLHSHQSTYPmiyengrGSSHQQQVTCYPFK-DVNNWWIVKDPGRHQLV-VNNPPRPVRHG 392
Cdd:cd23286     1 LLYGSTVTIRHLES--LGGYLHSHDLTYP-------SGSNEQQVTLYDFEdDANNEWIIETKTKEQMDkFPGQFREVRDG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 393 DVVQLVHGMTTRFLNTHDVAAPLSPH--SQEVSCYVDYNISMPSQNLWRLDIVNRESDTEVW------KTILSEVRLVHV 464
Cdd:cd23286    72 DVIRLRHVVTGKLLRASNARPPVSEQeyNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKlpnikiKSTESVFQLYNR 151

                         170       180
                  ....*....|....*....|....
gi 1239920855 465 NTSAVLKLSGAHLPDWGFQQLEVV 488
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 ...
 317-490 1.38e-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: 92.36  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 317 YGSQVTLKNVFGKpvpCWLHSHQSTYpmiyenGRGSShQQQVTCYP-FKDVNNWWIVK----DPGRHQlvvnnpPRPVRH 391
Cdd:cd23279     1 YGSAIKLKHVNSG---YRLHSHEVSY------GSGSG-QQSVTAVPsADDANSLWTVLpglgEPCQEQ------GKPVKC 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 392 GDVVQLVHGMTTRFLNTHDVAAPLSPHsQEVSCYVDynISMPSQNLWRLDIVNreSDTEVWKtILSEVRLVHVNTSAVLK 471
Cdd:cd23279    65 GDIIRLQHVNTRKNLHSHNHSSPLSGN-QEVSAFGG--GDEDSGDNWIVECEG--KKAKFWK-RGEPVRLKHVDTGKYLS 138

                         170
                  ....*....|....*....
gi 1239920855 472 LSGAHLpdwgFQQLEVVGE 490
Cdd:cd23279   139 ASKTHK----FTQQPIAGQ 153
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 315-509 7.12e-19

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: 84.73  E-value: 7.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 315 VAYGSQVTLKNVfgkPVPCWLHSHQSTYpmiyenGRGSShQQQVTCYPFK-DVNNWWIVKDPGRHQLVvnnPPRPVRHGD 393
Cdd:cd23294     1 VTCGSVIKLQHE---RTKFRLHSHEVPY------GSGSG-QQSVTGFPGVdDSNSYWIVKPANGERCK---QGDVIKNGD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 394 VVQLVHGMTTRFLNTHDVAAPLSpHSQEVSCYVDYNISMPSQNlWRLDIvnrESDTEVWKtiLSE-VRLVHVNTSAVLkl 472
Cdd:cd23294    68 VIRLQHVSTRKWLHSHLHASPLS-GNQEVSCFGGDGNSDTGDN-WIVEI---EGGGKVWE--RDQkVRLKHVDTGGYL-- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1239920855 473 sgaHLPDWGFQ-----QLEVVGeklSRGYHESMVWNVEEHRY 509
Cdd:cd23294   139 ---HSHDKKYGrpipgQQEVCA---VASKNSNTLWLAAEGVY 174
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 318-491 9.98e-18

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: 81.28  E-value: 9.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 318 GSQVTLKNVF-GKpvpcWLHSHQSTYPMiyengrgSSHQQQVTCY---PFKDVNNWWIVkdpgrhQLVVNNPPRPVRHGD 393
Cdd:cd23263     1 GDVIWLKHSEtGK----YLHSHRKNYPT-------GSGQQEVTFEsssRKGDTNGLWII------ESENGKQGGPVKWGD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 394 VVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYVDYNismPSQNLWRLDIVNRESDTEVWKTILSEVRLVHVNTSAVLKLS 473
Cdd:cd23263    64 KIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNP---DKSSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSH 140

                         170
                  ....*....|....*...
gi 1239920855 474 GAHLPDWGFQQLEVVGEK 491
Cdd:cd23263   141 EKKFNINNKTQQEVICHG 158
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 326-488 5.45e-17

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: 79.72  E-value: 5.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 326 VFGKPVPCWLHSHQSTYPMIYENGRGSsHQQQVTCYPFKDVNN----WWIVkdpgrhqLVVNNPP---RPVRHGDVVQLV 398
Cdd:pfam02815   3 LKGGDVVRLFHSHQDEYLTGSEQQQKQ-PFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 399 HGMTTRFLNTHDV-AAPLSPHS---QEVSCYvDYNISM----PSQNLWRLDIVNRESDTEvwKTILSEVRLVHVNTSAVL 470
Cdd:pfam02815  75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGFPgdndIVEIFEKKSTTGMGSDRI--KPGDSYFRLQHVCTGCWL 151

                         170       180
                  ....*....|....*....|
gi 1239920855 471 KLSGAHLPDWGF--QQLEVV 488
Cdd:pfam02815 152 FSHSVKLPKWGFgpEQQKVT 171
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 335-489 5.18e-16

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: 76.54  E-value: 5.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 335 LHSHQSTYpmiyenGRGSShQQQVTCYPFK-DVNNWWIVKdpGRHQLVVNNPpRPVRHGDVVQLVHGMTTRFLNTHDVAA 413
Cdd:cd23293    18 LHSHDVKY------GSGSG-QQSVTGVESSdDSNSYWQIR--GPTGADCERG-TPIKCGQTIRLTHLNTGKNLHSHHFQS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 414 PLSpHSQEVSCYVDynismpsqnlwrldivNRESDT-EVWKTILS--------EVRLVHVNTSAVLKLSGAHL--PDWGf 482
Cdd:cd23293    88 PLS-GNQEVSAFGE----------------DGEGDTgDNWTVVCSgtywerdeAVRLKHVDTEVYLHVTGEQYgrPIHG- 149


                  ....*..
gi 1239920855 483 qQLEVVG 489
Cdd:cd23293   150 -QREVSG 155
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 20-239 4.37e-13

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 72.23  E-value: 4.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  20 VALTAVGLLSRLWHLAYPRAVVrddcwqyygavplwltFDEVYYG----QYISFYMKRIFFLDGSG----PPFGHMLLAl 91
Cdd:COG1928    26 LLVTLLAGVLRFWGLGRPNTLV----------------FDETYYVkdawSLLTNGYERNWPDPGPFfvvhPPLGKWLIA- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  92 ggylggfdgnflwnrIGAEYSSNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLL 171
Cdd:COG1928    89 ---------------LGEWLFGYVNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 172 ESVLIFFNLLAVLSYLKFSNSQKHR--------------PFSLSWWFWLMLTGVACSCAVGVKYMGIFtYLLVLAVASVh 237
Cdd:COG1928   154 DIFLMFFVLAAFGCLLLDRDQVRRRlaaavaagrapsrwGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTV- 231


                  ..
gi 1239920855 238 AW 239
Cdd:COG1928   232 AW 233
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 540-764 1.16e-08

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 58.36  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 540 FLELQWRMLT-AKSDDSEHKYSSSPLDWVTLDTSIAYWLH-----------PRTSAQIHLLGNIVIWASASLAMVVyvlL 607
Cdd:COG1928   307 LWHYHQQILSfHTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPALLW---L 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 608 FFWYLLRRrrsicdipeetkccrciptlleassgkckdqagiavtpgySWlrwvLAGALCAgGWAVNYLPFFM-MEKTLF 686
Cdd:COG1928   384 LWRWIARR----------------------------------------DW----RAGAVLV-GYAAGWLPWFLyLDRTMF 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 687 LYHYLPALTFQILLLPVVLQHV---SDHLCRSQLLR---SLFSALVVAwyscachVFNTLRPLTYGDkSLSPSELKALRW 760
Cdd:COG1928   419 FFYAIPFVPFLVLALALVLGLIlgpARASERRRLGRlvvGLYVGLVVA-------NFAFFYPILTGL-PIPYDEWQARMW 490


                  ....
gi 1239920855 761 KDSW 764
Cdd:COG1928   491 FPSW 494
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 115-234 1.66e-07

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: 53.86  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 115 VPVWSLRLLPALTGAFSIPMAYQILLELgFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFSNSQK 194
Cdd:COG1807    81 VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRALERRR 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1239920855 195 hrpfslswWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVA 234
Cdd:COG1807   160 --------LRWLLLAGLALGLGFLTKGPVALLLPGLALLL 191
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
315-372 8.34e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.57  E-value: 8.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855  315 VAYGSQVTLKNVFGkpvPCWLHSHQSTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 372
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
386-443 2.13e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 2.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1239920855  386 PRPVRHGDVVQLVHGMTTRFLNTHDVA-APLSPHSQEVSCYVDYNISmpSQNLWRLDIV 443
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
457-507 2.91e-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: 2.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1239920855  457 SEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSRGyHESMVWNVEEH 507
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAI-DANTLWLIEPV 57
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 119-236 1.51e-03

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


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 41.96  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 119 SLRLLPALTGAFSIPMAYqiLLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFSNSQKHRpf 198
Cdd:COG4745    87 TARLPVALVGGLLPLLAL--LLRERLGDAEVLALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVRAIDTRRRR-- 162

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1239920855 199 slswwfWLMLTGVACSCAVGVKYMGIFtYLLVLAVASV 236
Cdd:COG4745   163 ------YLYLAAVALALAFATKENAVL-YLLCWLGALL 193
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 118-239 7.59e-03

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: 38.01  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920855 118 WSLRLLPALTGAFSIPMAYQILLELgFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFSNSQKhrp 197
Cdd:pfam13231  22 WAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVVPLFVALSRLFTPDAPLLLFWALALYFLLRALEKGR--- 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1239920855 198 fslswWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAW 239
Cdd:pfam13231  98 -----LKWWLLAGAAAGLGFLSKYTAALLVLAALLYLLISPG 134
 
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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