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Conserved domains on  [gi|2462539981|ref|XP_054231907|]
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protein O-mannosyl-transferase 2 isoform X11 [Homo sapiens]

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_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 35-221 8.25e-125

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: 359.69  E-value: 8.25e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  35 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 114
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 115 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 194
Cdd:cd23282    78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                         170       180
                  ....*....|....*....|....*..
gi 2462539981 195 WEQLEVTCTPYLKETlNSIWNVEDHIN 221
Cdd:cd23282   158 WEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 240-444 1.76e-63

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: 203.55  E-value: 1.76e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 240 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 319
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 320 GARLPAEVAGLSQvLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGI 399
Cdd:pfam16192  82 GYYDLSDDWTRSR-FYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462539981 400 HVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQdpqspMAGLRWLD 444
Cdd:pfam16192 159 GYAIVVVLLALVIYVFIYFSPLTYGMPGTSEE-----CKKLKWLS 198
 
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 ...
 35-221 8.25e-125

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: 359.69  E-value: 8.25e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  35 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 114
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 115 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 194
Cdd:cd23282    78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                         170       180
                  ....*....|....*....|....*..
gi 2462539981 195 WEQLEVTCTPYLKETlNSIWNVEDHIN 221
Cdd:cd23282   158 WEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 240-444 1.76e-63

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: 203.55  E-value: 1.76e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 240 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 319
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 320 GARLPAEVAGLSQvLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGI 399
Cdd:pfam16192  82 GYYDLSDDWTRSR-FYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462539981 400 HVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQdpqspMAGLRWLD 444
Cdd:pfam16192 159 GYAIVVVLLALVIYVFIYFSPLTYGMPGTSEE-----CKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 54-204 3.23e-21

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: 90.50  E-value: 3.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  54 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHY 125
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRHLTTGRYLHSHE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 126 HEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG-- 194
Cdd:pfam02815  87 EQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGfg 164

                         170
                  ....*....|
gi 2462539981 195 WEQLEVTCTP 204
Cdd:pfam02815 165 PEQQKVTCAK 174
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
102-157 3.62e-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: 3.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462539981  102 EFVRHGDIIRLEHKETSRNLHSHYH-EAPMTRKHYQVTGYGiNGTGDSNDFWRIEVV 157
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEkLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 263-446 8.41e-05

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 44.88  E-value: 8.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 263 SKPWHWPIN-------YQGLRF----SGVNDTDFRVYLLGNPVVWWLNLLSIALyllsgSIIAVAMQRGARLPAevagls 331
Cdd:COG1928   329 SKPWSWPLMlrpvsyyYETGQTgtlgCGAGKCVRAVLAIGNPALWWLGLPALLW-----LLWRWIARRDWRAGA------ 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 332 qvllrgggqVLLGWTLHYFPFFL-MGRVLYFHHYFPAMLFssMLTGILWdTLLRLCAWGLASWPLARGIHVAGILSLLLG 410
Cdd:COG1928   398 ---------VLVGYAAGWLPWFLyLDRTMFFFYAIPFVPF--LVLALAL-VLGLILGPARASERRRLGRLVVGLYVGLVV 465

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462539981 411 TAYSFylFHPLAYGMVGPLAQdPQSPMaglrWLDSW 446
Cdd:COG1928   466 ANFAF--FYPILTGLPIPYDE-WQARM----WFPSW 494
 
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 ...
 35-221 8.25e-125

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: 359.69  E-value: 8.25e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  35 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 114
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 115 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 194
Cdd:cd23282    78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                         170       180
                  ....*....|....*....|....*..
gi 2462539981 195 WEQLEVTCTPYLKETlNSIWNVEDHIN 221
Cdd:cd23282   158 WEQLEVTCNPNVRDK-NSLWNVEDNRN 183
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 35-219 2.48e-79

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: 243.78  E-value: 2.48e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  35 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGarQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPsfPVEFVRHGDIIRLEH 114
Cdd:cd23276     1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSK--QQQVTGYGHKDENNWWQILKPRGDPSSNPP--DPEYVRDGDEVRLLH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 115 KETSRNLHSHYHEAPMTRKHYQVTGYGINGT-GDSNDFWRIEVVNRKFGN---RIKVLRSRIRFIHLVTGCVLGSSGKVL 190
Cdd:cd23276    77 KETNRYLRTHDAAAPVTSKHKEVSAYPDENEdGDDNDLWVVEIVKDEGKLedkRIKPLTTRFRLRNKKTGCYLTSSGVKL 156

                         170       180
                  ....*....|....*....|....*....
gi 2462539981 191 PKWGWEQLEVTCTPYLKETLNSIWNVEDH 219
Cdd:cd23276   157 PEWGFRQGEVVCSKNKESDPSTLWNVEEN 185
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 32-221 5.45e-72

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: 225.28  E-value: 5.45e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  32 PEHLAYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIKK-HNTNSDPLDPSfPVEFVRHGDII 110
Cdd:cd23284     1 PLDVAYGSKVTIKNQGLGGGLLHSHVQTYPEG--SNQQQVTCYGHKDSNNEWIFERpRGLPSWDENDT-DIEFIKDGDIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 111 RLEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVV---NRKFGNRIKVLRSRIRFIHLVTGCVLGSSG 187
Cdd:cd23284    78 RLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDNWVIEIVkqvGSEDPKKLHTLTTSFRLRHEVLGCYLAQTG 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462539981 188 KVLPKWGWEQLEVTCTP-YLKETLNSIWNVEDHIN 221
Cdd:cd23284   158 VSLPEWGFKQGEVVCDKsNFKRDKRTWWNIETHTN 192
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 36-218 2.75e-64

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: 205.22  E-value: 2.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  36 AYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIkkHNTNSDPLDPSFPVEFVRHGDIIRLEHK 115
Cdd:cd23283     2 AYGSTIRIRHLNTRGGYLHSHPHNYPAG--SKQQQITLYPHRDENNDWLV--ELANAPEEWSPTTFENLKDGDVVRLEHV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 116 ETSRNLHSHYHEAPMTRKHYQ--VTGYGING-TGDSNDFWRIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSG 187
Cdd:cd23283    78 ATGRRLHSHDHRPPVSDNDWQneVSAYGYEGfEGDANDDWRVEILKDDSrpgesKERVRAIDTKFRLVHVMTGCYLFSHG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462539981 188 KVLPKWGWEQLEVTCTPYLKETlNSIWNVED 218
Cdd:cd23283   158 VKLPEWGFEQQEVTCAKSGLLE-LSLWYIET 187
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 240-444 1.76e-63

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: 203.55  E-value: 1.76e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 240 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 319
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 320 GARLPAEVAGLSQvLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGI 399
Cdd:pfam16192  82 GYYDLSDDWTRSR-FYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462539981 400 HVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQdpqspMAGLRWLD 444
Cdd:pfam16192 159 GYAIVVVLLALVIYVFIYFSPLTYGMPGTSEE-----CKKLKWLS 198
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 35-221 2.58e-51

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: 171.72  E-value: 2.58e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  35 LAYGSVITVKNLRMAIGYLHSHRHLYP----EGIG-ARQQQVTTYLHKDYNNLWIIKKHNTNSDPldPSFPVEFVRHGDI 109
Cdd:cd23281     1 VAYGSQVTLRNTHGSPCWLHSHKHRYPikypDGRGsSHQQQVTCYPFKDVNNWWIIKDPGRQDLA--VDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 110 IRLEHKETSRNLHSHYHEAPMTRKHYQVTGY-GINGTGDSNDFWRIEVVNRKF-GNRIKVLRSRIRFIHLVTGCVLGSSG 187
Cdd:cd23281    79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYiDYNISMPAQNLWRIEIVNRDSeGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462539981 188 KVLPKWGWEQLEVTcTPYLKETLNSIWNVEDHIN 221
Cdd:cd23281   159 KQLPDWGFGQLEVA-TDRAGNQSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 35-217 9.48e-34

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: 125.24  E-value: 9.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  35 LAYGSVITVKNLRMAIGYLHSHRHLYPegIGARQQQVTTY-LHKDYNNLWII-KKHNTNSDPLDPSFpvEFVRHGDIIRL 112
Cdd:cd23286     1 LLYGSTVTIRHLESLGGYLHSHDLTYP--SGSNEQQVTLYdFEDDANNEWIIeTKTKEQMDKFPGQF--REVRDGDVIRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 113 EHKETSRNLHSHYHEAPMTRK--HYQVTGYG-INGTGDSNDFWRIEVVNRK-------FGNRIKVLRSRIRFIHLVTGCV 182
Cdd:cd23286    77 RHVVTGKLLRASNARPPVSEQeyNNEVSCTGnANYSGDMDENWRIDVKGDEshaelklPNIKIKSTESVFQLYNRGTGCT 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462539981 183 LGSSGKVLPKWGWEQLEVTC--TPYLKETLnsiWNVE 217
Cdd:cd23286   157 LLSHDTRLPDWAFHQQEVLCvnSPTIPNTL---FYVE 190
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 37-218 5.48e-31

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: 117.78  E-value: 5.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  37 YGSVITVKNlRMAIGYLHSHRHLYP----EG-IGARQQQVTTYLHKDYNNLWIIKkhntnsdPLDPSFPVE----FVRHG 107
Cdd:cd23285     3 YGDVITIKH-RDTNAFLHSHPERYPlryeDGrISSQGQQVTGYPHKDANNQWQIL-------PTDPIDEHEgtgrPVRNG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 108 DIIRLEHKETSRNLHSHYHEAPMTRKHYQVTgygingTGDSNDF--------WRIEVVNRKFGNRIKVLRSRIRFIHLVT 179
Cdd:cd23285    75 DLIRLRHVSTDTYLLTHDVASPLTPTNMEFT------TVSDDDTderynetlFRVEIEDTDEGDVLKTKSSHFRLIHVDT 148

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462539981 180 GCVLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVED 218
Cdd:cd23285   149 NVALWTHKKPLPDWGFGQQEVNGNKNIKDK-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 ...
 37-216 1.75e-25

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: 101.99  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  37 YGSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLH-KDYNNLWIIKKHNtNSDPLDPSFPVefvRHGDIIRLEHK 115
Cdd:cd23279     1 YGSAIKLKHVNSGY-RLHSHEVSY--GSGSGQQSVTAVPSaDDANSLWTVLPGL-GEPCQEQGKPV---KCGDIIRLQHV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 116 ETSRNLHSHYHEAPMTRkHYQVTGYGiNGTGDSNDFWRIEVVNRKFGNrIKVlRSRIRFIHLVTGCVLGSSGKVL----P 191
Cdd:cd23279    74 NTRKNLHSHNHSSPLSG-NQEVSAFG-GGDEDSGDNWIVECEGKKAKF-WKR-GEPVRLKHVDTGKYLSASKTHKftqqP 149

                         170       180
                  ....*....|....*....|....*
gi 2462539981 192 KWGweQLEVTCTPYLKEtlNSIWNV 216
Cdd:cd23279   150 IAG--QLEVSAASSKDS--DSQWKA 170
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 37-214 9.77e-24

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: 97.45  E-value: 9.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  37 YGSVITVKNLRMAIgYLHSHrhLYPEGIGARQQQVTTYLHK-DYNNLWIIKKHNTNSDPldpsfPVEFVRHGDIIRLEHK 115
Cdd:cd23294     3 CGSVIKLQHERTKF-RLHSH--EVPYGSGSGQQSVTGFPGVdDSNSYWIVKPANGERCK-----QGDVIKNGDVIRLQHV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 116 ETSRNLHSHYHEAPMTRKHyQVTGYGINGTGDSNDFWRIEVVNrkfGNRIKVLRSRIRFIHLVTGCVLGSSGKvlpKWGW 195
Cdd:cd23294    75 STRKWLHSHLHASPLSGNQ-EVSCFGGDGNSDTGDNWIVEIEG---GGKVWERDQKVRLKHVDTGGYLHSHDK---KYGR 147

                         170       180
                  ....*....|....*....|..
gi 2462539981 196 E---QLEVTCTPylKETLNSIW 214
Cdd:cd23294   148 PipgQQEVCAVA--SKNSNTLW 167
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 38-218 4.18e-22

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: 92.83  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  38 GSVITVKNLRMAiGYLHSHRHLYPEGIGarQQQVTTYLHK---DYNNLWIIKKHNTNSDpldpsfpvEFVRHGDIIRLEH 114
Cdd:cd23263     1 GDVIWLKHSETG-KYLHSHRKNYPTGSG--QQEVTFESSSrkgDTNGLWIIESENGKQG--------GPVKWGDKIRLRH 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 115 KETSRNLHSHYHEAPMTRKHYQVTGYGINgtGDSNDFWRIEVVN-RKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKW 193
Cdd:cd23263    70 LSTGKYLSSEEGKKSPKSNHQEVLCLTDN--PDKSSLFKFEPIGsTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNIN 147

                         170       180
                  ....*....|....*....|....*
gi 2462539981 194 GWEQLEVTCTPyLKETLNSIWNVED 218
Cdd:cd23263   148 NKTQQEVICHG-EREEVFKLWKAEL 171
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 54-204 3.23e-21

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: 90.50  E-value: 3.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  54 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHY 125
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRHLTTGRYLHSHE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 126 HEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG-- 194
Cdd:pfam02815  87 EQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGfg 164

                         170
                  ....*....|
gi 2462539981 195 WEQLEVTCTP 204
Cdd:pfam02815 165 PEQQKVTCAK 174
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 38-220 2.83e-20

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: 87.71  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981  38 GSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLHK-DYNNLWIIK-KHNTNSDPLDPsfpvefVRHGDIIRLEHK 115
Cdd:cd23293     4 GSVVKLLNTRHNV-RLHSHDVKY--GSGSGQQSVTGVESSdDSNSYWQIRgPTGADCERGTP------IKCGQTIRLTHL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 116 ETSRNLHSHYHEAPMTRkHYQVTGYGINGTGDSNDFWRIeVVNRKFGNRikvlRSRIRFIHLVTGCVLGSSGKVL--PKW 193
Cdd:cd23293    75 NTGKNLHSHHFQSPLSG-NQEVSAFGEDGEGDTGDNWTV-VCSGTYWER----DEAVRLKHVDTEVYLHVTGEQYgrPIH 148

                         170       180
                  ....*....|....*....|....*..
gi 2462539981 194 GweQLEVTCTPYLkeTLNSIWNVEDHI 220
Cdd:cd23293   149 G--QREVSGMSSP--SQANYWKAMEGI 171
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 107-230 8.23e-18

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 80.51  E-value: 8.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 107 GDIIRLEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKvLRSRIRFIHLVTGCVLGSS 186
Cdd:cd23263     1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQGGPVK-WGDKIRLRHLSTGKYLSSE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462539981 187 GKVLPKWGWEQlEVTCTPYLKETlNSIWNVE--DHINPKLPNISLD 230
Cdd:cd23263    80 EGKKSPKSNHQ-EVLCLTDNPDK-SSLFKFEpiGSTKYKQKYVKKD 123
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
102-157 3.62e-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: 3.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462539981  102 EFVRHGDIIRLEHKETSRNLHSHYH-EAPMTRKHYQVTGYGiNGTGDSNDFWRIEVV 157
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEkLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
170-219 5.13e-08

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 49.26  E-value: 5.13e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462539981  170 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 219
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
32-88 1.99e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.64  E-value: 1.99e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462539981   32 PEHLAYGSVITVKNLRMAiGYLHSHRHLYPEgIGARQQQVTTYLHK--DYNNLWIIKKH 88
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTG-RYLHSHDEKLPP-WGDGQQEVTGYGNPaiDANTLWLIEPV 57
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 263-446 8.41e-05

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 44.88  E-value: 8.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 263 SKPWHWPIN-------YQGLRF----SGVNDTDFRVYLLGNPVVWWLNLLSIALyllsgSIIAVAMQRGARLPAevagls 331
Cdd:COG1928   329 SKPWSWPLMlrpvsyyYETGQTgtlgCGAGKCVRAVLAIGNPALWWLGLPALLW-----LLWRWIARRDWRAGA------ 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 332 qvllrgggqVLLGWTLHYFPFFL-MGRVLYFHHYFPAMLFssMLTGILWdTLLRLCAWGLASWPLARGIHVAGILSLLLG 410
Cdd:COG1928   398 ---------VLVGYAAGWLPWFLyLDRTMFFFYAIPFVPF--LVLALAL-VLGLILGPARASERRRLGRLVVGLYVGLVV 465

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462539981 411 TAYSFylFHPLAYGMVGPLAQdPQSPMaglrWLDSW 446
Cdd:COG1928   466 ANFAF--FYPILTGLPIPYDE-WQARM----WFPSW 494
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 104-202 1.94e-04

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: 41.98  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 104 VRHGDIIRLEHKETSRNLHShyHEAPMTRKHYQ--VTGYgiNGTGDSNDFWRIEVVNR---KFGNRIKVlRSRIRFIHLV 178
Cdd:cd23294     1 VTCGSVIKLQHERTKFRLHS--HEVPYGSGSGQqsVTGF--PGVDDSNSYWIVKPANGercKQGDVIKN-GDVIRLQHVS 75

                          90       100
                  ....*....|....*....|....
gi 2462539981 179 TGCVLGSSGKVLPKWGweQLEVTC 202
Cdd:cd23294    76 TRKWLHSHLHASPLSG--NQEVSC 97
OafA COG1835
Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains ...
 285-443 5.55e-04

Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441440  Cd Length: 309  Bit Score: 41.94  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 285 FRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQRGARLPAEVAGLSQVLLrgggqvllgwtlhyfpffLMGRVLYFHHY 364
Cdd:COG1835   140 LALLLTGDPSAAYFLTLTRLWEFLLGALLALLYRRLRRLRRLLALAGLALL------------------LAALLLLDGAP 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 365 FPAMLFSSMLTGILwdtLLRLCA--WGLASWPLARGIHVAGILSlllgtaYSFYLFHPLAYGMVGPLAQDPQSPMAGLRW 442
Cdd:COG1835   202 FPGFGLLPLLAALL---VLAAAAgsGLLSRLLSSRPLVFLGDIS------YSLYLWHWPVLVLLLALLGRLLGPAPLLLL 272


                  .
gi 2462539981 443 L 443
Cdd:COG1835   273 L 273
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 103-183 1.62e-03

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: 39.68  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539981 103 FVRHGDIIRLEHKETSRNLH---SHYHEAPMTRKHYQV------TGYGINGTGDSNDFWRIEVVNRKF-GNRIKvLRSRI 172
Cdd:cd23280     6 FLKGGDVVRLFHKELEAYLSaegSFVDEVLTEDVHLRVrpvddrKPRTLFPPTSGDTFWQIEKEDTPLkGGVIK-WGDQC 84

                          90
                  ....*....|.
gi 2462539981 173 RFIHLVTGCVL 183
Cdd:cd23280    85 RLRHLPTGKYL 95
 
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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