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Conserved domains on  [gi|226958312|ref|NP_001099273|]
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stromal cell-derived factor 2 precursor [Rattus norvegicus]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 1001097)

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

EC:  2.4.1.109
Gene Ontology:  GO:0000030|GO:0016740|GO:0016757|GO:0005789
PubMed:  31285605|20378538|15809069

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 32-206 2.51e-133

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: 371.60  E-value: 2.51e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  32 VTCGSVVKLLNIRHNVRLHSHDVRYGSGSGQQSVTGVTSVDDSNSYWRIRGKTATVCERGTPIKCGQPIRLTHINTGRNL 111
Cdd:cd23293    1 VTCGSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTGKNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 112 HSHHFTSPLSGNQEVSAFGEEGEGDYLDDWTVLCNGPYWVRDGEVRFKHSSTDVLLSVTGEQYGRPISGQKEVHGMAQPS 191
Cdd:cd23293   81 HSHHFQSPLSGNQEVSAFGEDGEGDTGDNWTVVCSGTYWERDEAVRLKHVDTEVYLHVTGEQYGRPIHGQREVSGMSSPS 160

                        170
                 ....*....|....*
gi 226958312 192 QNNYWKAMEGIFMKP 206
Cdd:cd23293  161 QANYWKAMEGIFIKP 175
 
Name Accession Description Interval E-value
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 32-206 2.51e-133

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: 371.60  E-value: 2.51e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  32 VTCGSVVKLLNIRHNVRLHSHDVRYGSGSGQQSVTGVTSVDDSNSYWRIRGKTATVCERGTPIKCGQPIRLTHINTGRNL 111
Cdd:cd23293    1 VTCGSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTGKNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 112 HSHHFTSPLSGNQEVSAFGEEGEGDYLDDWTVLCNGPYWVRDGEVRFKHSSTDVLLSVTGEQYGRPISGQKEVHGMAQPS 191
Cdd:cd23293   81 HSHHFQSPLSGNQEVSAFGEDGEGDTGDNWTVVCSGTYWERDEAVRLKHVDTEVYLHVTGEQYGRPIHGQREVSGMSSPS 160

                        170
                 ....*....|....*
gi 226958312 192 QNNYWKAMEGIFMKP 206
Cdd:cd23293  161 QANYWKAMEGIFIKP 175
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 41-140 1.03e-12

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: 63.92  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312   41 LNIRHNVRL-HSHDVRYGSGSGQQ------SVTGVTSVDDSN---SYWRIRGKTATVCeRGTPIKCGQPIRLTHINTGRN 110
Cdd:pfam02815   3 LKGGDVVRLfHSHQDEYLTGSEQQqkqpflRITLYPHGDANNsarSLWRIEVVRHDAW-RGGLIKWGSPFRLRHLTTGRY 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 226958312  111 LHSH-HFTSPLS----GNQEVSAFGEEGEGDYLDD 140
Cdd:pfam02815  82 LHSHeEQKPPLVekedWQKEVSAYGFRGFPGDNDI 116
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
91-146 1.42e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 57.74  E-value: 1.42e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 226958312    91 GTPIKCGQPIRLTHINTGRNLHSHHFTSPL--SGNQEVSAFGeEGEGDYLDDWTVLCN 146
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPwgDGQQEVTGYG-NPAIDANTLWLIEPV 57
 
Name Accession Description Interval E-value
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 32-206 2.51e-133

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: 371.60  E-value: 2.51e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  32 VTCGSVVKLLNIRHNVRLHSHDVRYGSGSGQQSVTGVTSVDDSNSYWRIRGKTATVCERGTPIKCGQPIRLTHINTGRNL 111
Cdd:cd23293    1 VTCGSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTGKNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 112 HSHHFTSPLSGNQEVSAFGEEGEGDYLDDWTVLCNGPYWVRDGEVRFKHSSTDVLLSVTGEQYGRPISGQKEVHGMAQPS 191
Cdd:cd23293   81 HSHHFQSPLSGNQEVSAFGEDGEGDTGDNWTVVCSGTYWERDEAVRLKHVDTEVYLHVTGEQYGRPIHGQREVSGMSSPS 160

                        170
                 ....*....|....*
gi 226958312 192 QNNYWKAMEGIFMKP 206
Cdd:cd23293  161 QANYWKAMEGIFIKP 175
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 32-204 4.59e-75

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: 224.18  E-value: 4.59e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  32 VTCGSVVKLLNIRHNVRLHSHDVRYGSGSGQQSVTGVTSVDDSNSYWRIRGKTATVCERGTPIKCGQPIRLTHINTGRNL 111
Cdd:cd23294    1 VTCGSVIKLQHERTKFRLHSHEVPYGSGSGQQSVTGFPGVDDSNSYWIVKPANGERCKQGDVIKNGDVIRLQHVSTRKWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 112 HSHHFTSPLSGNQEVSAFGEEGEGDYLDDWTVLCNG--PYWVRDGEVRFKHSSTDVLLSVTGEQYGRPISGQKEVHGMAQ 189
Cdd:cd23294   81 HSHLHASPLSGNQEVSCFGGDGNSDTGDNWIVEIEGggKVWERDQKVRLKHVDTGGYLHSHDKKYGRPIPGQQEVCAVAS 160

                        170
                 ....*....|....*
gi 226958312 190 PSQNNYWKAMEGIFM 204
Cdd:cd23294  161 KNSNTLWLAAEGVYF 175
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 34-201 2.99e-68

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: 206.77  E-value: 2.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  34 CGSVVKLLNIRHNVRLHSHDVRYGSGSGQQSVTGVTSVDDSNSYWRIRGK-TATVCERGTPIKCGQPIRLTHINTGRNLH 112
Cdd:cd23279    1 YGSAIKLKHVNSGYRLHSHEVSYGSGSGQQSVTAVPSADDANSLWTVLPGlGEPCQEQGKPVKCGDIIRLQHVNTRKNLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 113 SHHFTSPLSGNQEVSAFGEEGEGDyLDDWTVLCNGP---YWVRDGEVRFKHSSTDVLLSVTGEQYGR--PISGQKEVHGM 187
Cdd:cd23279   81 SHNHSSPLSGNQEVSAFGGGDEDS-GDNWIVECEGKkakFWKRGEPVRLKHVDTGKYLSASKTHKFTqqPIAGQLEVSAA 159

                        170
                 ....*....|....
gi 226958312 188 AQPSQNNYWKAMEG 201
Cdd:cd23279  160 SSKDSDSQWKAVEG 173
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 35-198 8.05e-27

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: 100.92  E-value: 8.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  35 GSVVKLLNIRHNVRLHSHDVRYGSGSGQQSVTGVTSVD--DSNSYWRIRGKTATVcerGTPIKCGQPIRLTHINTGRNLH 112
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTFESSSRkgDTNGLWIIESENGKQ---GGPVKWGDKIRLRHLSTGKYLS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 113 SH-HFTSPLSGNQEVSAFGEegEGDYLDDWTVLC------NGPYWVRDGEVRFKHSSTDVLLSVTGEQYGRPISGQKEV- 184
Cdd:cd23263   78 SEeGKKSPKSNHQEVLCLTD--NPDKSSLFKFEPigstkyKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNINNKTQQEVi 155

                        170
                 ....*....|....*
gi 226958312 185 -HGmAQPSQNNYWKA 198
Cdd:cd23263  156 cHG-EREEVFKLWKA 169
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 35-184 1.17e-19

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: 82.35  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  35 GSVVKLLNIR-HNVRLHSHDVRY--GSGSGQQSVTGVTSVDDSNsYWRIR--GKTATVCERGTPIKCGQPIRLTHINTGR 109
Cdd:cd23282    4 GSVITLKNHRtGGGYLHSHWHLYpeGVGARQQQVTTYSHKDDNN-LWLIKkhNQSSDLSDPVEYVRHGDLIRLEHVNTKR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 110 NLHSHHFTSPLSGN-QEVSAFGEEGEGDYLDDWTV-LCNGpywvRDGEV--------RFKHSSTDVLLSVTGEQYGRPIS 179
Cdd:cd23282   83 NLHSHKEKAPLTKKhYQVTGYGENGTGDANDVWRVeVVGG----REGDPvktvrskfRLVHYNTGCALHSHGKQLPKWGW 158


                 ....*
gi 226958312 180 GQKEV 184
Cdd:cd23282  159 EQLEV 163
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 35-143 9.36e-19

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: 80.42  E-value: 9.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  35 GSVVKllnIRH-NVR---LHSHDVRYGSGSGQQSVTGVTSVDDsNSYWRIRGKTATVCERGTP---IKCGQPIRLTHINT 107
Cdd:cd23283    4 GSTIR---IRHlNTRggyLHSHPHNYPAGSKQQQITLYPHRDE-NNDWLVELANAPEEWSPTTfenLKDGDVVRLEHVAT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 226958312 108 GRNLHSHHFTSPLSGN---QEVSAFGEEG-EGDYLDDWTV 143
Cdd:cd23283   80 GRRLHSHDHRPPVSDNdwqNEVSAYGYEGfEGDANDDWRV 119
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 49-195 1.43e-18

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: 80.06  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  49 LHSHDVRYGSGSGQQSVTGVtSVDDSNSYW---RIRGKTATVcERGTP---IKCGQPIRLTHINTGRNLHSHHFTSPLS- 121
Cdd:cd23284   22 LHSHVQTYPEGSNQQQVTCY-GHKDSNNEWifeRPRGLPSWD-ENDTDiefIKDGDIVRLVHKQTGRNLHSHPVPAPISk 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 122 GNQEVSAFGEEGEGDYLDDWTVLCNGPYWVRDGE--------VRFKHSSTDVLLSVTGEQYgrPISG--QKEVHGMAQPS 191
Cdd:cd23284  100 SDYEVSGYGDLTVGDEKDNWVIEIVKQVGSEDPKklhtlttsFRLRHEVLGCYLAQTGVSL--PEWGfkQGEVVCDKSNF 177


                 ....
gi 226958312 192 QNNY 195
Cdd:cd23284  178 KRDK 181
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 32-184 3.79e-17

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: 75.83  E-value: 3.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  32 VTCGSVVKLLNIRHNV-RLHSHDVRYGSGSGQQSVTGVTSvDDSNSYWRI---RGKTATVCERGTPIKCGQPIRLTHINT 107
Cdd:cd23276    1 VAYGSQITLRNANSGGgYLHSHNHTYPDGSKQQQVTGYGH-KDENNWWQIlkpRGDPSSNPPDPEYVRDGDEVRLLHKET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 108 GRNLHSHHFTSPLSGN-QEVSAFG-EEGEGDYLDDWTV--------LCNGPYWVRDGEVRFKHSSTDVLLSVTGEQYgrP 177
Cdd:cd23276   80 NRYLRTHDAAAPVTSKhKEVSAYPdENEDGDDNDLWVVeivkdegkLEDKRIKPLTTRFRLRNKKTGCYLTSSGVKL--P 157


                 ....*....
gi 226958312 178 ISG--QKEV 184
Cdd:cd23276  158 EWGfrQGEV 166
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 35-173 1.52e-15

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: 71.96  E-value: 1.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  35 GSVVKLLNI-RHNVRLHSHDVRY--------GSgSGQQSVTGVTSVDDSNSYWRIR-GKTATVCERGT-PIKCGQPIRLT 103
Cdd:cd23281    4 GSQVTLRNThGSPCWLHSHKHRYpikypdgrGS-SHQQQVTCYPFKDVNNWWIIKDpGRQDLAVDDPPrPVRHGDIIQLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 104 HINTGRNLHSHHFTSPLS-GNQEVSAFgeegeGDY------LDDWTVLCNGPYWVRD------GEVRFKHSSTDVLLSVT 170
Cdd:cd23281   83 HGKTGRFLNSHDVAAPLSpTHQEVSCY-----IDYnismpaQNLWRIEIVNRDSEGDtwkaikSQFRLIHVNTSAALKLS 157


                 ...
gi 226958312 171 GEQ 173
Cdd:cd23281  158 GKQ 160
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 43-200 6.74e-14

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: 67.32  E-value: 6.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  43 IRH---NVRLHSHDVRYG--------SGSGQQsVTGVTSvDDSNSYWRI--RGKTATVCERGTPIKCGQPIRLTHINTGR 109
Cdd:cd23285    9 IKHrdtNAFLHSHPERYPlryedgriSSQGQQ-VTGYPH-KDANNQWQIlpTDPIDEHEGTGRPVRNGDLIRLRHVSTDT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312 110 NLHSHHFTSPL-SGNQEVS-AFGEEGEGDYLDD-WTVLC----NGPYWV-RDGEVRFKHSSTDVLLSVTGEQ---YGRpi 178
Cdd:cd23285   87 YLLTHDVASPLtPTNMEFTtVSDDDTDERYNETlFRVEIedtdEGDVLKtKSSHFRLIHVDTNVALWTHKKPlpdWGF-- 164

                        170       180
                 ....*....|....*....|...
gi 226958312 179 sGQKEVHG-MAQPSQNNYWKAME 200
Cdd:cd23285  165 -GQQEVNGnKNIKDKSNIWVVDD 186
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 43-147 3.83e-13

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: 65.15  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  43 IRHNVR----LHSHDVRYGSGSGQQSVTGVTSVDDSNSYWRIRGKT----ATVCERGTPIKCGQPIRLTHINTGRNLHSH 114
Cdd:cd23286    9 IRHLESlggyLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKTkeqmDKFPGQFREVRDGDVIRLRHVVTGKLLRAS 88

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 226958312 115 HFTSPLSG---NQEVSAFGEEG-EGDYLDDWTVLCNG 147
Cdd:cd23286   89 NARPPVSEqeyNNEVSCTGNANySGDMDENWRIDVKG 125
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 41-140 1.03e-12

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: 63.92  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312   41 LNIRHNVRL-HSHDVRYGSGSGQQ------SVTGVTSVDDSN---SYWRIRGKTATVCeRGTPIKCGQPIRLTHINTGRN 110
Cdd:pfam02815   3 LKGGDVVRLfHSHQDEYLTGSEQQqkqpflRITLYPHGDANNsarSLWRIEVVRHDAW-RGGLIKWGSPFRLRHLTTGRY 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 226958312  111 LHSH-HFTSPLS----GNQEVSAFGEEGEGDYLDD 140
Cdd:pfam02815  82 LHSHeEQKPPLVekedWQKEVSAYGFRGFPGDNDI 116
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
91-146 1.42e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 57.74  E-value: 1.42e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 226958312    91 GTPIKCGQPIRLTHINTGRNLHSHHFTSPL--SGNQEVSAFGeEGEGDYLDDWTVLCN 146
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPwgDGQQEVTGYG-NPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
29-80 8.21e-09

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 50.03  E-value: 8.21e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 226958312    29 MAVVTCGSVVKLLNIRHNVRLHSHDVRYG-SGSGQQSVTGVTSVD-DSNSYWRI 80
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPpWGDGQQEVTGYGNPAiDANTLWLI 54
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
148-197 1.31e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.95  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 226958312   148 PYWVRDG-EVRFKHSSTDVLLSVTGEQYGRPISGQKEVHGMAQP--SQNNYWK 197
Cdd:smart00472   1 GGFVRWGdVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPaiDANTLWL 53
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 32-127 2.16e-07

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: 49.22  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958312  32 VTCGSVVKLLNIRHNVRLHSHDVRYG--SGSGQQSVTGV---TSVDDSNSYWRI---RGKTATVCERGTPIKCGQPIRLT 103
Cdd:cd23283   66 LKDGDVVRLEHVATGRRLHSHDHRPPvsDNDWQNEVSAYgyeGFEGDANDDWRVeilKDDSRPGESKERVRAIDTKFRLV 145

                         90       100
                 ....*....|....*....|....*.
gi 226958312 104 HINTGRNLHSHHFTSPLSG--NQEVS 127
Cdd:cd23283  146 HVMTGCYLFSHGVKLPEWGfeQQEVT 171
 
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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