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Conserved domains on  [gi|18400721|ref|NP_565585|]
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stromal cell-derived factor 2-like protein precursor [Arabidopsis thaliana]

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_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 37-212 3.05e-119

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: 335.88  E-value: 3.05e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHEKTKFRLHSHDVPYGSGSGQQSVTGFPGVVDSNSYWIVKPVPGTTEKQGDAVKSGATIRLQHMKTRKWL 116
Cdd:cd23294   1 VTCGSVIKLQHERTKFRLHSHEVPYGSGSGQQSVTGFPGVDDSNSYWIVKPANGERCKQGDVIKNGDVIRLQHVSTRKWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 117 HSHLHASPISGNLEVSCFGDDTNSDTGDHWKLIIEGSGKTWKQDQRVRLQHIDTSGYLHSHDKKYQRIAGGQQEVCGIRE 196
Cdd:cd23294  81 HSHLHASPLSGNQEVSCFGGDGNSDTGDNWIVEIEGGGKVWERDQKVRLKHVDTGGYLHSHDKKYGRPIPGQQEVCAVAS 160

                       170
                ....*....|....*.
gi 18400721 197 KKADNIWLAAEGVYLP 212
Cdd:cd23294 161 KNSNTLWLAAEGVYFP 176
 
Name Accession Description Interval E-value
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 37-212 3.05e-119

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: 335.88  E-value: 3.05e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHEKTKFRLHSHDVPYGSGSGQQSVTGFPGVVDSNSYWIVKPVPGTTEKQGDAVKSGATIRLQHMKTRKWL 116
Cdd:cd23294   1 VTCGSVIKLQHERTKFRLHSHEVPYGSGSGQQSVTGFPGVDDSNSYWIVKPANGERCKQGDVIKNGDVIRLQHVSTRKWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 117 HSHLHASPISGNLEVSCFGDDTNSDTGDHWKLIIEGSGKTWKQDQRVRLQHIDTSGYLHSHDKKYQRIAGGQQEVCGIRE 196
Cdd:cd23294  81 HSHLHASPLSGNQEVSCFGGDGNSDTGDNWIVEIEGGGKVWERDQKVRLKHVDTGGYLHSHDKKYGRPIPGQQEVCAVAS 160

                       170
                ....*....|....*.
gi 18400721 197 KKADNIWLAAEGVYLP 212
Cdd:cd23294 161 KNSNTLWLAAEGVYFP 176
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 55-201 1.16e-14

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


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 69.31  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721    55 HSHDVPYGSGSGQQ------SVTGFPGVVDSN---SYWIVKPVPGTTEkQGDAVKSGATIRLQHMKTRKWLHSHLHASPI 125
Cdd:pfam02815  13 HSHQDEYLTGSEQQqkqpflRITLYPHGDANNsarSLWRIEVVRHDAW-RGGLIKWGSPFRLRHLTTGRYLHSHEEQKPP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721   126 -----SGNLEVSCFGDDTNSDTGDHwKLIIE-------GSGKTWKQDQRVRLQHIDTSGYLHSH--DKKYQRIAGGQQEV 191
Cdd:pfam02815  92 lvekeDWQKEVSAYGFRGFPGDNDI-VEIFEkksttgmGSDRIKPGDSYFRLQHVCTGCWLFSHsvKLPKWGFGPEQQKV 170

                         170
                  ....*....|
gi 18400721   192 CGIREKKADN 201
Cdd:pfam02815 171 TCAKEGHMDD 180
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
154-204 1.09e-10

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 55.43  E-value: 1.09e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 18400721    154 GKTWKQDQRVRLQHIDTSGYLHSHDKKYQRIAGGQQEVCGIREKK--ADNIWL 204
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAidANTLWL 53
 
Name Accession Description Interval E-value
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 37-212 3.05e-119

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: 335.88  E-value: 3.05e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHEKTKFRLHSHDVPYGSGSGQQSVTGFPGVVDSNSYWIVKPVPGTTEKQGDAVKSGATIRLQHMKTRKWL 116
Cdd:cd23294   1 VTCGSVIKLQHERTKFRLHSHEVPYGSGSGQQSVTGFPGVDDSNSYWIVKPANGERCKQGDVIKNGDVIRLQHVSTRKWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 117 HSHLHASPISGNLEVSCFGDDTNSDTGDHWKLIIEGSGKTWKQDQRVRLQHIDTSGYLHSHDKKYQRIAGGQQEVCGIRE 196
Cdd:cd23294  81 HSHLHASPLSGNQEVSCFGGDGNSDTGDNWIVEIEGGGKVWERDQKVRLKHVDTGGYLHSHDKKYGRPIPGQQEVCAVAS 160

                       170
                ....*....|....*.
gi 18400721 197 KKADNIWLAAEGVYLP 212
Cdd:cd23294 161 KNSNTLWLAAEGVYFP 176
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 39-208 9.90e-82

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: 241.05  E-value: 9.90e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  39 YGSAIKLMHEKTKFRLHSHDVPYGSGSGQQSVTGFPGVVDSNSYWIVKPVPG-TTEKQGDAVKSGATIRLQHMKTRKWLH 117
Cdd:cd23279   1 YGSAIKLKHVNSGYRLHSHEVSYGSGSGQQSVTAVPSADDANSLWTVLPGLGePCQEQGKPVKCGDIIRLQHVNTRKNLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 118 SHLHASPISGNLEVSCFGDDtNSDTGDHWKLIIEGSG-KTWKQDQRVRLQHIDTSGYLHSHDKKY--QRIAGGQQEVCGI 194
Cdd:cd23279  81 SHNHSSPLSGNQEVSAFGGG-DEDSGDNWIVECEGKKaKFWKRGEPVRLKHVDTGKYLSASKTHKftQQPIAGQLEVSAA 159

                       170
                ....*....|....
gi 18400721 195 REKKADNIWLAAEG 208
Cdd:cd23279 160 SSKDSDSQWKAVEG 173
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 37-211 2.61e-77

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: 229.85  E-value: 2.61e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHEKTKFRLHSHDVPYGSGSGQQSVTGFPGVVDSNSYWIVKPVPGTTEKQGDAVKSGATIRLQHMKTRKWL 116
Cdd:cd23293   1 VTCGSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTGKNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 117 HSHLHASPISGNLEVSCFGDDTNSDTGDHWKLIIegSGKTWKQDQRVRLQHIDTSGYLHSHDKKYQRIAGGQQEVCGIRE 196
Cdd:cd23293  81 HSHHFQSPLSGNQEVSAFGEDGEGDTGDNWTVVC--SGTYWERDEAVRLKHVDTEVYLHVTGEQYGRPIHGQREVSGMSS 158

                       170
                ....*....|....*
gi 18400721 197 KKADNIWLAAEGVYL 211
Cdd:cd23293 159 PSQANYWKAMEGIFI 173
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 40-205 6.29e-46

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: 149.84  E-value: 6.29e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  40 GSAIKLMHEKTKFRLHSHDVPYGSGSGQQSVTGFPGV--VDSNSYWIVKPVPGtteKQGDAVKSGATIRLQHMKTRKWLH 117
Cdd:cd23263   1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTFESSSrkGDTNGLWIIESENG---KQGGPVKWGDKIRLRHLSTGKYLS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 118 SHLHA-SPISGNLEVSCFGDdtNSDTGDHWKLIIEGSG----KTWKQDQRVRLQHIDTSGYLHSHDKKYQRIAGGQQEVC 192
Cdd:cd23263  78 SEEGKkSPKSNHQEVLCLTD--NPDKSSLFKFEPIGSTkykqKYVKKDSYFRLKHVNTNFWLHSHEKKFNINNKTQQEVI 155

                       170
                ....*....|....
gi 18400721 193 GIREKKADN-IWLA 205
Cdd:cd23263 156 CHGEREEVFkLWKA 169
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 37-203 2.60e-34

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: 120.86  E-value: 2.60e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHEKTKF-RLHSHDVPYGSGSGQQSVTGFPgVVDSNSYWIVKPVPGTTEKQGDA---VKSGATIRLQHMKT 112
Cdd:cd23283   1 VAYGSTIRIRHLNTRGgYLHSHPHNYPAGSKQQQITLYP-HRDENNDWLVELANAPEEWSPTTfenLKDGDVVRLEHVAT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 113 RKWLHSHLHASPISGN---LEVSCFGDDTN-SDTGDHWKLII-------EGSGKTWKQ-DQRVRLQHIDTSGYLHSHDKK 180
Cdd:cd23283  80 GRRLHSHDHRPPVSDNdwqNEVSAYGYEGFeGDANDDWRVEIlkddsrpGESKERVRAiDTKFRLVHVMTGCYLFSHGVK 159

                       170       180
                ....*....|....*....|....
gi 18400721 181 YQRIAGGQQEV-CGIREKKADNIW 203
Cdd:cd23283 160 LPEWGFEQQEVtCAKSGLLELSLW 183
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 37-203 2.30e-29

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: 107.80  E-value: 2.30e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHEKTKF-RLHSHDVPYGSGSGQQSVTGFpGVVDSNSYWIVKPVPGTTEK---QGDAVKSGATIRLQHMKT 112
Cdd:cd23276   1 VAYGSQITLRNANSGGgYLHSHNHTYPDGSKQQQVTGY-GHKDENNWWQILKPRGDPSSnppDPEYVRDGDEVRLLHKET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 113 RKWLHSH-LHASPISGNLEVSCFGDDTNSDTGDH-WKLIIEGSGKTWKQDQ------RVRLQHIDTSGYLHSHDKKYQRI 184
Cdd:cd23276  80 NRYLRTHdAAAPVTSKHKEVSAYPDENEDGDDNDlWVVEIVKDEGKLEDKRikplttRFRLRNKKTGCYLTSSGVKLPEW 159

                       170       180
                ....*....|....*....|.
gi 18400721 185 AGGQQEVCGIREKKAD--NIW 203
Cdd:cd23276 160 GFRQGEVVCSKNKESDpsTLW 180
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 37-207 6.86e-27

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: 101.60  E-value: 6.86e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHEKTKFRLHSHDVPYG--------SGSGQQsVTGFPGVvDSNSYWIVKPV--PGTTEKQGDAVKSGATIR 106
Cdd:cd23285   1 VHYGDVITIKHRDTNAFLHSHPERYPlryedgriSSQGQQ-VTGYPHK-DANNQWQILPTdpIDEHEGTGRPVRNGDLIR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 107 LQHMKTRKWLHSHLHASPI-SGNLEVSCF-GDDTNSDTGDH-WKLIIE--GSGKTWK-QDQRVRLQHIDTSGYLHSHDKK 180
Cdd:cd23285  79 LRHVSTDTYLLTHDVASPLtPTNMEFTTVsDDDTDERYNETlFRVEIEdtDEGDVLKtKSSHFRLIHVDTNVALWTHKKP 158

                       170       180
                ....*....|....*....|....*...
gi 18400721 181 YQRIAGGQQEVCGIREKK-ADNIWLAAE 207
Cdd:cd23285 159 LPDWGFGQQEVNGNKNIKdKSNIWVVDD 186
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 37-203 4.24e-25

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: 96.60  E-value: 4.24e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHEKTKFR-LHSHDV--PYGSGSGQQSVTGFpGVVDSNSYWIVKPvPGTTEKQGDA---VKSGATIRLQHM 110
Cdd:cd23282   1 VAYGSVITLKNHRTGGGyLHSHWHlyPEGVGARQQQVTTY-SHKDDNNLWLIKK-HNQSSDLSDPveyVRHGDLIRLEHV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 111 KTRKWLHSHLHASPISGN-LEVSCFGDDTNSDTGDHWKLIIEGsGKTWKQDQRV----RLQHIDTSGYLHSHDKKYQRIA 185
Cdd:cd23282  79 NTKRNLHSHKEKAPLTKKhYQVTGYGENGTGDANDVWRVEVVG-GREGDPVKTVrskfRLVHYNTGCALHSHGKQLPKWG 157

                       170
                ....*....|....*....
gi 18400721 186 GGQQEV-CGIREKKADNIW 203
Cdd:cd23282 158 WEQLEVtCNPNVRDKNSLW 176
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 35-203 9.34e-24

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: 93.54  E-value: 9.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  35 VEITYGS--AIKLMHEKTKFrLHSHDVPYGSGSGQQSVTGFpGVVDSNSYWIVKPVPGTTEKQGD-----AVKSGATIRL 107
Cdd:cd23284   2 LDVAYGSkvTIKNQGLGGGL-LHSHVQTYPEGSNQQQVTCY-GHKDSNNEWIFERPRGLPSWDENdtdieFIKDGDIVRL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 108 QHMKTRKWLHSHLHASPIS-GNLEVSCFGDDTNSDTGDHWKLIIEgsgktwKQDQ------------RVRLQHIDTSGYL 174
Cdd:cd23284  80 VHKQTGRNLHSHPVPAPISkSDYEVSGYGDLTVGDEKDNWVIEIV------KQVGsedpkklhtlttSFRLRHEVLGCYL 153

                       170       180       190
                ....*....|....*....|....*....|.
gi 18400721 175 HSHDKKYQRIAGGQQEVCGIRE--KKADNIW 203
Cdd:cd23284 154 AQTGVSLPEWGFKQGEVVCDKSnfKRDKRTW 184
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 37-210 6.55e-21

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: 85.82  E-value: 6.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMHekTKFR---LHSHDVPY--------GSgSGQQSVTGFPgVVDSNSYWIVKPvPGTTEKQGDA----VKS 101
Cdd:cd23281   1 VAYGSQVTLRN--THGSpcwLHSHKHRYpikypdgrGS-SHQQQVTCYP-FKDVNNWWIIKD-PGRQDLAVDDpprpVRH 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 102 GATIRLQHMKTRKWLHSHLHASPISGNL-EVSCFGDDTNSDTG-DHWKLIIEGS---GKTWKQDQ-RVRLQHIDTSGYLH 175
Cdd:cd23281  76 GDIIQLVHGKTGRFLNSHDVAAPLSPTHqEVSCYIDYNISMPAqNLWRIEIVNRdseGDTWKAIKsQFRLIHVNTSAALK 155

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 18400721 176 SHDKKYQRIAGGQQEVCGIREKK-ADNIWLAAEGVY 210
Cdd:cd23281 156 LSGKQLPDWGFGQLEVATDRAGNqSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 37-191 4.96e-20

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: 83.64  E-value: 4.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  37 ITYGSAIKLMH-EKTKFRLHSHDVPYGSGSGQQSVTGFPGVVDSNSYWIVKPV----PGTTEKQGDAVKSGATIRLQHMK 111
Cdd:cd23286   1 LLYGSTVTIRHlESLGGYLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKtkeqMDKFPGQFREVRDGDVIRLRHVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721 112 TRKWLHSHLHASPISG---NLEVSCFGDDTNS-DTGDHWKLIIEG----------SGKTWKQDQRVRLQHIDTSGYLHSH 177
Cdd:cd23286  81 TGKLLRASNARPPVSEqeyNNEVSCTGNANYSgDMDENWRIDVKGdeshaelklpNIKIKSTESVFQLYNRGTGCTLLSH 160

                       170
                ....*....|....
gi 18400721 178 DKKYQRIAGGQQEV 191
Cdd:cd23286 161 DTRLPDWAFHQQEV 174
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 55-201 1.16e-14

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


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 69.31  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721    55 HSHDVPYGSGSGQQ------SVTGFPGVVDSN---SYWIVKPVPGTTEkQGDAVKSGATIRLQHMKTRKWLHSHLHASPI 125
Cdd:pfam02815  13 HSHQDEYLTGSEQQqkqpflRITLYPHGDANNsarSLWRIEVVRHDAW-RGGLIKWGSPFRLRHLTTGRYLHSHEEQKPP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721   126 -----SGNLEVSCFGDDTNSDTGDHwKLIIE-------GSGKTWKQDQRVRLQHIDTSGYLHSH--DKKYQRIAGGQQEV 191
Cdd:pfam02815  92 lvekeDWQKEVSAYGFRGFPGDNDI-VEIFEkksttgmGSDRIKPGDSYFRLQHVCTGCWLFSHsvKLPKWGFGPEQQKV 170

                         170
                  ....*....|
gi 18400721   192 CGIREKKADN 201
Cdd:pfam02815 171 TCAKEGHMDD 180
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
154-204 1.09e-10

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 55.43  E-value: 1.09e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 18400721    154 GKTWKQDQRVRLQHIDTSGYLHSHDKKYQRIAGGQQEVCGIREKK--ADNIWL 204
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAidANTLWL 53
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
37-88 2.82e-08

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 2.82e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 18400721     37 ITYGSAIKLMHEKTKFRLHSHDVPYG-SGSGQQSVTGFP-GVVDSNSYWIVKPV 88
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLPpWGDGQQEVTGYGnPAIDANTLWLIEPV 57
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 21-119 1.65e-06

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: 46.59  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721    21 GYTSASAAASGK-------------EGVEITYGSAIKLMHEKTKFRLHSHDVP----YGSGSGQQSVT-----GFPGVVD 78
Cdd:pfam02815  36 LYPHGDANNSARslwrievvrhdawRGGLIKWGSPFRLRHLTTGRYLHSHEEQkpplVEKEDWQKEVSaygfrGFPGDND 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18400721    79 SNSYWIVKPVPGttEKQGDAVKSGATIRLQHMKTRKWLHSH 119
Cdd:pfam02815 116 IVEIFEKKSTTG--MGSDRIKPGDSYFRLQHVCTGCWLFSH 154
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 77-183 2.02e-06

MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate receptor Itr-1 and similar proteins; Itr-1, also called IP3 receptor, or IP3R, or InsP3R, or LET-23 fertility effector 1, is a receptor for inositol 1,4,5-trisphosphate, a second messenger that regulates intracellular calcium homeostasis. It binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity. It can also bind inositol 1,3,4,5-tetrakisphosphate (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with lower affinity. Itr-1 acts as a timekeeper/rhythm generator via calcium signaling, affecting the defecation cycle and pharyngeal pumping. It affects normal hermaphrodite and male fertility as a participant in intracellular signaling by acting downstream of let-23/lin-3 which regulates ovulation, spermathecal valve dilation and male mating behavior. It plays an important role in early embryonic development. It controls epidermal cell migration and may also regulate filopodial protrusive activity during epithelial morphogenesis. Itr-1 functions as a component of inositol trisphosphate (IP3)-mediated downstream signaling pathways that controls amphid sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde, but no other ASH-mediated responses. Itr-1 contains an N-terminal 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: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 46.61  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400721  77 VDSNSYWIVKPVpgTTEKQGDAVKSGATIRLQHMKTRKWLHshlhASPISGNLEVSCFGDDTNSDTgdHWKLI--IEGSG 154
Cdd:cd23280  58 TSGDTFWQIEKE--DTPLKGGVIKWGDQCRLRHLPTGKYLA----VDDKTGNGKVVLTSDPSDPST--VFRLHpvTKETS 129

                        90       100
                ....*....|....*....|....*....
gi 18400721 155 KTWKQDQRVRLQHIDTSGYLHSHDKKYQR 183
Cdd:cd23280 130 EEVKFGSYVRIEHVATGTWLHAETDEELR 158
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
96-147 1.03e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.56  E-value: 1.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 18400721     96 GDAVKSGATIRLQHMKTRKWLHSHLHASP--ISGNLEVSCFGDDTNSDTgDHWK 147
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPpwGDGQQEVTGYGNPAIDAN-TLWL 53
 
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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