NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462539975|ref|XP_054231904|]
View 

protein O-mannosyl-transferase 2 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 138-337 2.40e-121

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: 357.00  E-value: 2.40e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 138 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 217
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 218 KEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGC 297
Cdd:cd23282    78 VN-------------TKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGC 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462539975 298 VLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVEDHIN 337
Cdd:cd23282   145 ALHSHGKQLPKWGWEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 356-623 1.27e-52

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: 179.28  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 356 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 435
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 436 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 515
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 516 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 595
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 2462539975 596 LFHPLAYGMVGPLAQdpqspMAGLRWLD 623
Cdd:pfam16192 176 YFSPLTYGMPGTSEE-----CKKLKWLS 198
PMT_2 super family cl21590
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 1-107 9.56e-31

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


The actual alignment was detected with superfamily member pfam02366:

Pssm-ID: 473917 [Multi-domain]  Cd Length: 245  Bit Score: 120.49  E-value: 9.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975   1 MFFIMAAMLSMVKYNscADRPFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHL 80
Cdd:pfam02366 141 LFFTTLSMYCFWKFE--RKAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHL 218

                          90       100
                  ....*....|....*....|....*..
gi 2462539975  81 TARVLCLIVLPLALYTATFAVHFMVLS 107
Cdd:pfam02366 219 FARLFCLIVIPWALYLAQFYVHFWLLF 245
 
Name Accession Description Interval E-value
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 138-337 2.40e-121

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: 357.00  E-value: 2.40e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 138 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 217
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 218 KEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGC 297
Cdd:cd23282    78 VN-------------TKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGC 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462539975 298 VLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVEDHIN 337
Cdd:cd23282   145 ALHSHGKQLPKWGWEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 356-623 1.27e-52

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: 179.28  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 356 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 435
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 436 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 515
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 516 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 595
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 2462539975 596 LFHPLAYGMVGPLAQdpqspMAGLRWLD 623
Cdd:pfam16192 176 YFSPLTYGMPGTSEE-----CKKLKWLS 198
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 1-107 9.56e-31

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: 120.49  E-value: 9.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975   1 MFFIMAAMLSMVKYNscADRPFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHL 80
Cdd:pfam02366 141 LFFTTLSMYCFWKFE--RKAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHL 218

                          90       100
                  ....*....|....*....|....*..
gi 2462539975  81 TARVLCLIVLPLALYTATFAVHFMVLS 107
Cdd:pfam02366 219 FARLFCLIVIPWALYLAQFYVHFWLLF 245
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 157-320 3.21e-18

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: 82.80  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 157 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHkecpLKkiwrw 228
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRH----LT----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 229 eqkeTSRNLHSHYHEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVL 299
Cdd:pfam02815  78 ----TGRYLHSHEEQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWL 151

                         170       180
                  ....*....|....*....|...
gi 2462539975 300 GSSGKVLPKWG--WEQLEVTCTP 320
Cdd:pfam02815 152 FSHSVKLPKWGfgPEQQKVTCAK 174
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
286-335 3.82e-08

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: 3.82e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462539975  286 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 335
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDANTLWLIEPV 57
 
Name Accession Description Interval E-value
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 138-337 2.40e-121

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: 357.00  E-value: 2.40e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 138 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 217
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 218 KEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGC 297
Cdd:cd23282    78 VN-------------TKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGC 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462539975 298 VLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVEDHIN 337
Cdd:cd23282   145 ALHSHGKQLPKWGWEQLEVTCNPNVRDK-NSLWNVEDNRN 183
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 138-335 2.07e-75

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: 238.77  E-value: 2.07e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 138 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGarQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPsfPVEFVRHGDIIRLEH 217
Cdd:cd23276     1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSK--QQQVTGYGHKDENNWWQILKPRGDPSSNPP--DPEYVRDGDEVRLLH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 218 KEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGT-GDSNDFWRIEVVNRKFGN---RIKVLRSRIRFIHL 293
Cdd:cd23276    77 KE-------------TNRYLRTHDAAAPVTSKHKEVSAYPDENEdGDDNDLWVVEIVKDEGKLedkRIKPLTTRFRLRNK 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462539975 294 VTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 335
Cdd:cd23276   144 KTGCYLTSSGVKLPEWGFRQGEVVCSKNKESDPSTLWNVEEN 185
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 135-337 3.89e-68

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: 219.88  E-value: 3.89e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 135 PEHLAYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIKK-HNTNSDPLDPSfPVEFVRHGDII 213
Cdd:cd23284     1 PLDVAYGSKVTIKNQGLGGGLLHSHVQTYPEG--SNQQQVTCYGHKDSNNEWIFERpRGLPSWDENDT-DIEFIKDGDIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 214 RLEHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVV---NRKFGNRIKVLRSRIRF 290
Cdd:cd23284    78 RLVHKQ-------------TGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDNWVIEIVkqvGSEDPKKLHTLTTSFRL 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462539975 291 IHLVTGCVLGSSGKVLPKWGWEQLEVTCTP-YLKETLNSIWNVEDHIN 337
Cdd:cd23284   145 RHEVLGCYLAQTGVSLPEWGFKQGEVVCDKsNFKRDKRTWWNIETHTN 192
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 139-334 6.96e-61

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: 200.99  E-value: 6.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 139 AYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIkkHNTNSDPLDPSFPVEFVRHGDIIRLEHK 218
Cdd:cd23283     2 AYGSTIRIRHLNTRGGYLHSHPHNYPAG--SKQQQITLYPHRDENNDWLV--ELANAPEEWSPTTFENLKDGDVVRLEHV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 219 EcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQ--VTGYGING-TGDSNDFWRIEVVNRKF-----GNRIKVLRSRIRF 290
Cdd:cd23283    78 A-------------TGRRLHSHDHRPPVSDNDWQneVSAYGYEGfEGDANDDWRVEILKDDSrpgesKERVRAIDTKFRL 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462539975 291 IHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVED 334
Cdd:cd23283   145 VHVMTGCYLFSHGVKLPEWGFEQQEVTCAKSGLLE-LSLWYIET 187
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 356-623 1.27e-52

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: 179.28  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 356 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 435
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 436 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 515
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 516 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 595
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 2462539975 596 LFHPLAYGMVGPLAQdpqspMAGLRWLD 623
Cdd:pfam16192 176 YFSPLTYGMPGTSEE-----CKKLKWLS 198
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 138-337 3.32e-47

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: 164.40  E-value: 3.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 138 LAYGSVITVKNLRMAIGYLHSHRHLYP----EGIG-ARQQQVTTYLHKDYNNLWIIKKHNTNSDPldPSFPVEFVRHGDI 212
Cdd:cd23281     1 VAYGSQVTLRNTHGSPCWLHSHKHRYPikypDGRGsSHQQQVTCYPFKDVNNWWIIKDPGRQDLA--VDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 213 IRLEHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGY-GINGTGDSNDFWRIEVVNRKF-GNRIKVLRSRIRF 290
Cdd:cd23281    79 IQLVHGK-------------TGRFLNSHDVAAPLSPTHQEVSCYiDYNISMPAQNLWRIEIVNRDSeGDTWKAIKSQFRL 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462539975 291 IHLVTGCVLGSSGKVLPKWGWEQLEVTcTPYLKETLNSIWNVEDHIN 337
Cdd:cd23281   146 IHVNTSAALKLSGKQLPDWGFGQLEVA-TDRAGNQSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 138-333 5.65e-31

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: 119.46  E-value: 5.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 138 LAYGSVITVKNLRMAIGYLHSHRHLYPegIGARQQQVTTY-LHKDYNNLWII-KKHNTNSDPLDPSFpvEFVRHGDIIRL 215
Cdd:cd23286     1 LLYGSTVTIRHLESLGGYLHSHDLTYP--SGSNEQQVTLYdFEDDANNEWIIeTKTKEQMDKFPGQF--REVRDGDVIRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 216 EHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRK--HYQVTGYG-INGTGDSNDFWRIEVVNRK-------FGNRIKVLR 285
Cdd:cd23286    77 RHVV-------------TGKLLRASNARPPVSEQeyNNEVSCTGnANYSGDMDENWRIDVKGDEshaelklPNIKIKSTE 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462539975 286 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTC--TPYLKETLnsiWNVE 333
Cdd:cd23286   144 SVFQLYNRGTGCTLLSHDTRLPDWAFHQQEVLCvnSPTIPNTL---FYVE 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 1-107 9.56e-31

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: 120.49  E-value: 9.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975   1 MFFIMAAMLSMVKYNscADRPFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHL 80
Cdd:pfam02366 141 LFFTTLSMYCFWKFE--RKAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHL 218

                          90       100
                  ....*....|....*....|....*..
gi 2462539975  81 TARVLCLIVLPLALYTATFAVHFMVLS 107
Cdd:pfam02366 219 FARLFCLIVIPWALYLAQFYVHFWLLF 245
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 140-334 7.40e-28

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: 110.46  E-value: 7.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 140 YGSVITVKNlRMAIGYLHSHRHLYP----EG-IGARQQQVTTYLHKDYNNLWIIKkhntnsdPLDPSFPVE----FVRHG 210
Cdd:cd23285     3 YGDVITIKH-RDTNAFLHSHPERYPlryeDGrISSQGQQVTGYPHKDANNQWQIL-------PTDPIDEHEgtgrPVRNG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 211 DIIRLEHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTgygingTGDSNDF--------WRIEVVNRKFGNRIK 282
Cdd:cd23285    75 DLIRLRHVS-------------TDTYLLTHDVASPLTPTNMEFT------TVSDDDTderynetlFRVEIEDTDEGDVLK 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462539975 283 VLRSRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVED 334
Cdd:cd23285   136 TKSSHFRLIHVDTNVALWTHKKPLPDWGFGQQEVNGNKNIKDK-SNIWVVDD 186
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 140-332 1.13e-22

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: 95.44  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 140 YGSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLH-KDYNNLWIIKKHNtNSDPLDPSFPVefvRHGDIIRLEHK 218
Cdd:cd23279     1 YGSAIKLKHVNSGY-RLHSHEVSY--GSGSGQQSVTAVPSaDDANSLWTVLPGL-GEPCQEQGKPV---KCGDIIRLQHV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 219 EcplkkiwrweqkeTSRNLHSHYHEAPMTRkHYQVTGYGiNGTGDSNDFWRIEVVNRKFGNrIKVlRSRIRFIHLVTGCV 298
Cdd:cd23279    74 N-------------TRKNLHSHNHSSPLSG-NQEVSAFG-GGDEDSGDNWIVECEGKKAKF-WKR-GEPVRLKHVDTGKY 136

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462539975 299 LGSSGKVL----PKWGweQLEVTCTPYLKEtlNSIWNV 332
Cdd:cd23279   137 LSASKTHKftqqPIAG--QLEVSAASSKDS--DSQWKA 170
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 140-330 8.08e-21

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: 90.13  E-value: 8.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 140 YGSVITVKNLRMAIgYLHSHrhLYPEGIGARQQQVTTYLHK-DYNNLWIIKKHNTNSDPldpsfPVEFVRHGDIIRLEHK 218
Cdd:cd23294     3 CGSVIKLQHERTKF-RLHSH--EVPYGSGSGQQSVTGFPGVdDSNSYWIVKPANGERCK-----QGDVIKNGDVIRLQHV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 219 EcplkkiwrweqkeTSRNLHSHYHEAPMTRKHyQVTGYGINGTGDSNDFWRIEVVNrkfGNRIKVLRSRIRFIHLVTGCV 298
Cdd:cd23294    75 S-------------TRKWLHSHLHASPLSGNQ-EVSCFGGDGNSDTGDNWIVEIEG---GGKVWERDQKVRLKHVDTGGY 137

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462539975 299 LGSSGKvlpKWGWE---QLEVTCTPylKETLNSIW 330
Cdd:cd23294   138 LHSHDK---KYGRPipgQQEVCAVA--SKNSNTLW 167
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 141-334 1.25e-19

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: 86.67  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 141 GSVITVKNLRMAiGYLHSHRHLYPEGIGarQQQVTTYLHK---DYNNLWIIKKHNTNSDpldpsfpvEFVRHGDIIRLEH 217
Cdd:cd23263     1 GDVIWLKHSETG-KYLHSHRKNYPTGSG--QQEVTFESSSrkgDTNGLWIIESENGKQG--------GPVKWGDKIRLRH 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 218 kecplkkiwrweqKETSRNLHSHYHEAPMTRKHYQVTGYGINgtGDSNDFWRIEVVN-RKFGNRIKVLRSRIRFIHLVTG 296
Cdd:cd23263    70 -------------LSTGKYLSSEEGKKSPKSNHQEVLCLTDN--PDKSSLFKFEPIGsTKYKQKYVKKDSYFRLKHVNTN 134

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462539975 297 CVLGSSGKVLPKWGWEQLEVTCTPyLKETLNSIWNVED 334
Cdd:cd23263   135 FWLHSHEKKFNINNKTQQEVICHG-EREEVFKLWKAEL 171
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 157-320 3.21e-18

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: 82.80  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 157 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHkecpLKkiwrw 228
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRH----LT----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 229 eqkeTSRNLHSHYHEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVL 299
Cdd:pfam02815  78 ----TGRYLHSHEEQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWL 151

                         170       180
                  ....*....|....*....|...
gi 2462539975 300 GSSGKVLPKWG--WEQLEVTCTP 320
Cdd:pfam02815 152 FSHSVKLPKWGfgPEQQKVTCAK 174
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 141-336 1.71e-17

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: 80.39  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 141 GSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLHK-DYNNLWIIK-KHNTNSDPLDPsfpvefVRHGDIIRLEHK 218
Cdd:cd23293     4 GSVVKLLNTRHNV-RLHSHDVKY--GSGSGQQSVTGVESSdDSNSYWQIRgPTGADCERGTP------IKCGQTIRLTHL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 219 EcplkkiwrweqkeTSRNLHSHYHEAPMTRkHYQVTGYGINGTGDSNDFWRIeVVNRKFGNRikvlRSRIRFIHLVTGCV 298
Cdd:cd23293    75 N-------------TGKNLHSHHFQSPLSG-NQEVSAFGEDGEGDTGDNWTV-VCSGTYWER----DEAVRLKHVDTEVY 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462539975 299 LGSSGKVL--PKWGweQLEVTCTPYLkeTLNSIWNVEDHI 336
Cdd:cd23293   136 LHVTGEQYgrPIHG--QREVSGMSSP--SQANYWKAMEGI 171
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 210-346 3.45e-15

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: 73.57  E-value: 3.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975 210 GDIIRLEHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKvLRSRIR 289
Cdd:cd23263     1 GDVIWLKHSE-------------TGKYLHSHRKNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQGGPVK-WGDKIR 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462539975 290 FIHLVTGCVLGSSGKVLPKWGWEQlEVTCTPYLKETlNSIWNVE--DHINPKLPNISLD 346
Cdd:cd23263    67 LRHLSTGKYLSSEEGKKSPKSNHQ-EVLCLTDNPDK-SSLFKFEpiGSTKYKQKYVKKD 123
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
286-335 3.82e-08

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: 3.82e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462539975  286 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 335
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
205-273 4.10e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 47.34  E-value: 4.10e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539975  205 EFVRHGDIIRLEHKEcplkkiwrweqkeTSRNLHSHYH-EAPMTRKHYQVTGYGiNGTGDSNDFWRIEVV 273
Cdd:smart00472   2 GFVRWGDVVRLRHVT-------------TGRYLHSHDEkLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
135-191 1.32e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.80  E-value: 1.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462539975  135 PEHLAYGSVITVKNLRMAiGYLHSHRHLYPEgIGARQQQVTTYLHK--DYNNLWIIKKH 191
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTG-RYLHSHDEKLPP-WGDGQQEVTGYGNPaiDANTLWLIEPV 57
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH