NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767980357|ref|XP_011534979|]
View 

protein O-mannosyl-transferase 2 isoform X7 [Homo sapiens]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 11449133)

dolichyl-phosphate-mannose--protein mannosyltransferase is a glycosyltransferase family 39 protein that transfers mannosyl residues to the hydroxyl group of serine or threonine residues, initiating the assembly of O-mannosyl glycans

Graphical summary

 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 ...
 184-370 1.09e-124

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: 366.63  E-value: 1.09e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 184 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 263
Cdd:cd23282    1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 264 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 343
Cdd:cd23282   78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                        170       180
                 ....*....|....*....|....*..
gi 767980357 344 WEQLEVTCTPYLKETlNSIWNVEDHIN 370
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 ...
 389-656 7.84e-54

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: 182.74  E-value: 7.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  389 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 468
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  469 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 548
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  549 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 628
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 767980357  629 LFHPLAYGMVGPLAQdpqspMAGLRWLD 656
Cdd:pfam16192 176 YFSPLTYGMPGTSEE-----CKKLKWLS 198
PMT_2 super family cl21590
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 62-168 1.49e-35

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: 134.36  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357   62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100
                  ....*....|....*....|....*....
gi 767980357  140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSK 168
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGF 109
 
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 ...
 184-370 1.09e-124

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: 366.63  E-value: 1.09e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 184 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 263
Cdd:cd23282    1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 264 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 343
Cdd:cd23282   78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                        170       180
                 ....*....|....*....|....*..
gi 767980357 344 WEQLEVTCTPYLKETlNSIWNVEDHIN 370
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 ...
 389-656 7.84e-54

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: 182.74  E-value: 7.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  389 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 468
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  469 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 548
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  549 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 628
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 767980357  629 LFHPLAYGMVGPLAQdpqspMAGLRWLD 656
Cdd:pfam16192 176 YFSPLTYGMPGTSEE-----CKKLKWLS 198
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 62-168 1.49e-35

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: 134.36  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357   62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100
                  ....*....|....*....|....*....
gi 767980357  140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSK 168
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGF 109
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 203-353 4.11e-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: 91.27  E-value: 4.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  203 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHY 274
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRHLTTGRYLHSHE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  275 HEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG-- 343
Cdd:pfam02815  87 EQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGfg 164

                         170
                  ....*....|
gi 767980357  344 WEQLEVTCTP 353
Cdd:pfam02815 165 PEQQKVTCAK 174
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 37-127 1.60e-12

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 70.31  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  37 AVARSPKRPAWGSRRFEAVGWWALLaLVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINR---------TFFFDVHP 107
Cdd:COG1928    2 TAALPPARLVPPMPGDRLRGWLGTL-LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHP 80

                         90       100
                 ....*....|....*....|
gi 767980357 108 PLGKMLIGLAGYLSGYDGTF 127
Cdd:COG1928   81 PLGKWLIALGEWLFGYVNPF 100
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
251-306 1.96e-10

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 56.58  E-value: 1.96e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767980357   251 EFVRHGDIIRLEHKETSRNLHSHYH-EAPMTRKHYQVTGYGiNGTGDSNDFWRIEVV 306
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEkLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 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 ...
 184-370 1.09e-124

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: 366.63  E-value: 1.09e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 184 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 263
Cdd:cd23282    1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 264 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 343
Cdd:cd23282   78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                        170       180
                 ....*....|....*....|....*..
gi 767980357 344 WEQLEVTCTPYLKETlNSIWNVEDHIN 370
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 ...
 184-368 7.15e-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: 248.79  E-value: 7.15e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 184 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGarQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPsfPVEFVRHGDIIRLEH 263
Cdd:cd23276    1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSK--QQQVTGYGHKDENNWWQILKPRGDPSSNPP--DPEYVRDGDEVRLLH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 264 KETSRNLHSHYHEAPMTRKHYQVTGYGINGT-GDSNDFWRIEVVNRKFGN---RIKVLRSRIRFIHLVTGCVLGSSGKVL 339
Cdd:cd23276   77 KETNRYLRTHDAAAPVTSKHKEVSAYPDENEdGDDNDLWVVEIVKDEGKLedkRIKPLTTRFRLRNKKTGCYLTSSGVKL 156

                        170       180
                 ....*....|....*....|....*....
gi 767980357 340 PKWGWEQLEVTCTPYLKETLNSIWNVEDH 368
Cdd:cd23276  157 PEWGFRQGEVVCSKNKESDPSTLWNVEEN 185
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 182-370 8.80e-71

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: 227.59  E-value: 8.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 182 FDLAYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIKK-HNTNSDPLDPSfPVEFVRHGDIIR 260
Cdd:cd23284    2 LDVAYGSKVTIKNQGLGGGLLHSHVQTYPEG--SNQQQVTCYGHKDSNNEWIFERpRGLPSWDENDT-DIEFIKDGDIVR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 261 LEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVV---NRKFGNRIKVLRSRIRFIHLVTGCVLGSSGK 337
Cdd:cd23284   79 LVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDNWVIEIVkqvGSEDPKKLHTLTTSFRLRHEVLGCYLAQTGV 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767980357 338 VLPKWGWEQLEVTCTP-YLKETLNSIWNVEDHIN 370
Cdd:cd23284  159 SLPEWGFKQGEVVCDKsNFKRDKRTWWNIETHTN 192
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 185-367 1.09e-63

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: 209.08  E-value: 1.09e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 185 AYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIkkHNTNSDPLDPSFPVEFVRHGDIIRLEHK 264
Cdd:cd23283    2 AYGSTIRIRHLNTRGGYLHSHPHNYPAG--SKQQQITLYPHRDENNDWLV--ELANAPEEWSPTTFENLKDGDVVRLEHV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 265 ETSRNLHSHYHEAPMTRKHYQ--VTGYGING-TGDSNDFWRIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSG 336
Cdd:cd23283   78 ATGRRLHSHDHRPPVSDNDWQneVSAYGYEGfEGDANDDWRVEILKDDSrpgesKERVRAIDTKFRLVHVMTGCYLFSHG 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767980357 337 KVLPKWGWEQLEVTCTPYLKETlNSIWNVED 367
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 ...
 389-656 7.84e-54

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: 182.74  E-value: 7.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  389 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 468
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  469 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 548
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  549 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 628
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 767980357  629 LFHPLAYGMVGPLAQdpqspMAGLRWLD 656
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 ...
 184-370 9.98e-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: 174.42  E-value: 9.98e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 184 LAYGSVITVKNLRMAIGYLHSHRHLYP----EGIG-ARQQQVTTYLHKDYNNLWIIKKHNTNSDPldPSFPVEFVRHGDI 258
Cdd:cd23281    1 VAYGSQVTLRNTHGSPCWLHSHKHRYPikypDGRGsSHQQQVTCYPFKDVNNWWIIKDPGRQDLA--VDDPPRPVRHGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 259 IRLEHKETSRNLHSHYHEAPMTRKHYQVTGY-GINGTGDSNDFWRIEVVNRKF-GNRIKVLRSRIRFIHLVTGCVLGSSG 336
Cdd:cd23281   79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYiDYNISMPAQNLWRIEIVNRDSeGDTWKAIKSQFRLIHVNTSAALKLSG 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767980357 337 KVLPKWGWEQLEVTcTPYLKETLNSIWNVEDHIN 370
Cdd:cd23281  159 KQLPDWGFGQLEVA-TDRAGNQSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 62-168 1.49e-35

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: 134.36  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357   62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100
                  ....*....|....*....|....*....
gi 767980357  140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSK 168
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGF 109
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 184-366 2.37e-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: 129.48  E-value: 2.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 184 LAYGSVITVKNLRMAIGYLHSHRHLYPegIGARQQQVTTY-LHKDYNNLWII-KKHNTNSDPLDPSFpvEFVRHGDIIRL 261
Cdd:cd23286    1 LLYGSTVTIRHLESLGGYLHSHDLTYP--SGSNEQQVTLYdFEDDANNEWIIeTKTKEQMDKFPGQF--REVRDGDVIRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 262 EHKETSRNLHSHYHEAPMTRK--HYQVTGYG-INGTGDSNDFWRIEVVNRK-------FGNRIKVLRSRIRFIHLVTGCV 331
Cdd:cd23286   77 RHVVTGKLLRASNARPPVSEQeyNNEVSCTGnANYSGDMDENWRIDVKGDEshaelklPNIKIKSTESVFQLYNRGTGCT 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767980357 332 LGSSGKVLPKWGWEQLEVTC--TPYLKETLnsiWNVE 366
Cdd:cd23286  157 LLSHDTRLPDWAFHQQEVLCvnSPTIPNTL---FYVE 190
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 186-367 3.77e-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: 120.09  E-value: 3.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 186 YGSVITVKNlRMAIGYLHSHRHLYP----EG-IGARQQQVTTYLHKDYNNLWIIKkhntnsdPLDPSFPVE----FVRHG 256
Cdd:cd23285    3 YGDVITIKH-RDTNAFLHSHPERYPlryeDGrISSQGQQVTGYPHKDANNQWQIL-------PTDPIDEHEgtgrPVRNG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 257 DIIRLEHKETSRNLHSHYHEAPMTRKHYQVTgygingTGDSNDF--------WRIEVVNRKFGNRIKVLRSRIRFIHLVT 328
Cdd:cd23285   75 DLIRLRHVSTDTYLLTHDVASPLTPTNMEFT------TVSDDDTderynetlFRVEIEDTDEGDVLKTKSSHFRLIHVDT 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767980357 329 GCVLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVED 367
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 ...
 186-365 4.06e-26

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: 105.07  E-value: 4.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 186 YGSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLH-KDYNNLWIIKKHNtNSDPLDPSFPVefvRHGDIIRLEHK 264
Cdd:cd23279    1 YGSAIKLKHVNSGY-RLHSHEVSY--GSGSGQQSVTAVPSaDDANSLWTVLPGL-GEPCQEQGKPV---KCGDIIRLQHV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 265 ETSRNLHSHYHEAPMTRkHYQVTGYGiNGTGDSNDFWRIEVVNRKFGNrIKVlRSRIRFIHLVTGCVLGSSGKVL----P 340
Cdd:cd23279   74 NTRKNLHSHNHSSPLSG-NQEVSAFG-GGDEDSGDNWIVECEGKKAKF-WKR-GEPVRLKHVDTGKYLSASKTHKftqqP 149

                        170       180
                 ....*....|....*....|....*
gi 767980357 341 KWGweQLEVTCTPYLKEtlNSIWNV 365
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 ...
 186-363 7.31e-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: 98.99  E-value: 7.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 186 YGSVITVKNLRMAIgYLHSHrhLYPEGIGARQQQVTTYLHK-DYNNLWIIKKHNTNSDPldpsfPVEFVRHGDIIRLEHK 264
Cdd:cd23294    3 CGSVIKLQHERTKF-RLHSH--EVPYGSGSGQQSVTGFPGVdDSNSYWIVKPANGERCK-----QGDVIKNGDVIRLQHV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 265 ETSRNLHSHYHEAPMTRKHyQVTGYGINGTGDSNDFWRIEVVNrkfGNRIKVLRSRIRFIHLVTGCVLGSSGKvlpKWGW 344
Cdd:cd23294   75 STRKWLHSHLHASPLSGNQ-EVSCFGGDGNSDTGDNWIVEIEG---GGKVWERDQKVRLKHVDTGGYLHSHDK---KYGR 147

                        170       180
                 ....*....|....*....|..
gi 767980357 345 E---QLEVTCTPylKETLNSIW 363
Cdd:cd23294  148 PipgQQEVCAVA--SKNSNTLW 167
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 187-367 1.23e-23

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: 98.22  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 187 GSVITVKNLRMAiGYLHSHRHLYPEGIGarQQQVTTYLHK---DYNNLWIIKKHNTNSDpldpsfpvEFVRHGDIIRLEH 263
Cdd:cd23263    1 GDVIWLKHSETG-KYLHSHRKNYPTGSG--QQEVTFESSSrkgDTNGLWIIESENGKQG--------GPVKWGDKIRLRH 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 264 KETSRNLHSHYHEAPMTRKHYQVTGYGINgtGDSNDFWRIEVVN-RKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKW 342
Cdd:cd23263   70 LSTGKYLSSEEGKKSPKSNHQEVLCLTDN--PDKSSLFKFEPIGsTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNIN 147

                        170       180
                 ....*....|....*....|....*
gi 767980357 343 GWEQLEVTCTPyLKETLNSIWNVED 367
Cdd:cd23263  148 NKTQQEVICHG-EREEVFKLWKAEL 171
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 203-353 4.11e-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: 91.27  E-value: 4.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  203 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHY 274
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRHLTTGRYLHSHE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  275 HEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG-- 343
Cdd:pfam02815  87 EQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGfg 164

                         170
                  ....*....|
gi 767980357  344 WEQLEVTCTP 353
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 ...
 187-369 1.49e-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: 89.25  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 187 GSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLHK-DYNNLWIIK-KHNTNSDPLDPsfpvefVRHGDIIRLEHK 264
Cdd:cd23293    4 GSVVKLLNTRHNV-RLHSHDVKY--GSGSGQQSVTGVESSdDSNSYWQIRgPTGADCERGTP------IKCGQTIRLTHL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 265 ETSRNLHSHYHEAPMTRkHYQVTGYGINGTGDSNDFWRIeVVNRKFGNRikvlRSRIRFIHLVTGCVLGSSGKVL--PKW 342
Cdd:cd23293   75 NTGKNLHSHHFQSPLSG-NQEVSAFGEDGEGDTGDNWTV-VCSGTYWER----DEAVRLKHVDTEVYLHVTGEQYgrPIH 148

                        170       180
                 ....*....|....*....|....*..
gi 767980357 343 GweQLEVTCTPYLkeTLNSIWNVEDHI 369
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) ...
 256-379 5.34e-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: 84.74  E-value: 5.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 256 GDIIRLEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKvLRSRIRFIHLVTGCVLGSS 335
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQGGPVK-WGDKIRLRHLSTGKYLSSE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767980357 336 GKVLPKWGWEQlEVTCTPYLKETlNSIWNVE--DHINPKLPNISLD 379
Cdd:cd23263   80 EGKKSPKSNHQ-EVLCLTDNPDK-SSLFKFEpiGSTKYKQKYVKKD 123
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 37-127 1.60e-12

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 70.31  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357  37 AVARSPKRPAWGSRRFEAVGWWALLaLVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINR---------TFFFDVHP 107
Cdd:COG1928    2 TAALPPARLVPPMPGDRLRGWLGTL-LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHP 80

                         90       100
                 ....*....|....*....|
gi 767980357 108 PLGKMLIGLAGYLSGYDGTF 127
Cdd:COG1928   81 PLGKWLIALGEWLFGYVNPF 100
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
251-306 1.96e-10

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 56.58  E-value: 1.96e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767980357   251 EFVRHGDIIRLEHKETSRNLHSHYH-EAPMTRKHYQVTGYGiNGTGDSNDFWRIEVV 306
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEkLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
319-368 3.65e-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: 3.65e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767980357   319 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 368
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
183-237 7.88e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.48  E-value: 7.88e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767980357   183 DLAYGSVITVKNLRMAiGYLHSHRHLYPEgIGARQQQVTTYLHK--DYNNLWIIKKH 237
Cdd:smart00472   3 FVRWGDVVRLRHVTTG-RYLHSHDEKLPP-WGDGQQEVTGYGNPaiDANTLWLIEPV 57
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 253-351 1.76e-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: 42.75  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 253 VRHGDIIRLEHKETSRNLHShyHEAPMTRKHYQ--VTGYgiNGTGDSNDFWRIEVVNR---KFGNRIKVlRSRIRFIHLV 327
Cdd:cd23294    1 VTCGSVIKLQHERTKFRLHS--HEVPYGSGSGQqsVTGF--PGVDDSNSYWIVKPANGercKQGDVIKN-GDVIRLQHVS 75

                         90       100
                 ....*....|....*....|....
gi 767980357 328 TGCVLGSSGKVLPKWGweQLEVTC 351
Cdd:cd23294   76 TRKWLHSHLHASPLSG--NQEVSC 97
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 252-332 2.34e-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: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980357 252 FVRHGDIIRLEHKETSRNLH---SHYHEAPMTRKHYQV------TGYGINGTGDSNDFWRIEVVNRKF-GNRIKvLRSRI 321
Cdd:cd23280    6 FLKGGDVVRLFHKELEAYLSaegSFVDEVLTEDVHLRVrpvddrKPRTLFPPTSGDTFWQIEKEDTPLkGGVIK-WGDQC 84

                         90
                 ....*....|.
gi 767980357 322 RFIHLVTGCVL 332
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH