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Conserved domains on  [gi|32455271|ref|NP_037514|]
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protein O-mannosyl-transferase 2 [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

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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 ...
 337-523 2.34e-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: 371.25  E-value: 2.34e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 337 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 416
Cdd:cd23282   1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 417 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 496
Cdd:cd23282  78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                       170       180
                ....*....|....*....|....*..
gi 32455271 497 WEQLEVTCTPYLKETlNSIWNVEDHIN 523
Cdd:cd23282 158 WEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 62-306 2.32e-82

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: 262.25  E-value: 2.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271    62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNscADR 219
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   220 PFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFA 299
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFY 238


                  ....*..
gi 32455271   300 VHFMVLS 306
Cdd:pfam02366 239 VHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 542-746 2.12e-60

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: 202.00  E-value: 2.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   542 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 621
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   622 GARLPAEVAGLSQvLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGI 701
Cdd:pfam16192  82 GYYDLSDDWTRSR-FYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 32455271   702 HVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQdpqspMAGLRWLD 746
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 ...
 337-523 2.34e-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: 371.25  E-value: 2.34e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 337 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 416
Cdd:cd23282   1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 417 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 496
Cdd:cd23282  78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                       170       180
                ....*....|....*....|....*..
gi 32455271 497 WEQLEVTCTPYLKETlNSIWNVEDHIN 523
Cdd:cd23282 158 WEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 62-306 2.32e-82

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: 262.25  E-value: 2.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271    62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNscADR 219
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   220 PFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFA 299
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFY 238


                  ....*..
gi 32455271   300 VHFMVLS 306
Cdd:pfam02366 239 VHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 542-746 2.12e-60

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: 202.00  E-value: 2.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   542 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 621
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   622 GARLPAEVAGLSQvLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGI 701
Cdd:pfam16192  82 GYYDLSDDWTRSR-FYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 32455271   702 HVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQdpqspMAGLRWLD 746
Cdd:pfam16192 159 GYAIVVVLLALVIYVFIYFSPLTYGMPGTSEE-----CKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 356-506 1.56e-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: 92.81  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   356 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHY 427
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRHLTTGRYLHSHE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   428 HEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG-- 496
Cdd:pfam02815  87 EQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGfg 164

                         170
                  ....*....|
gi 32455271   497 WEQLEVTCTP 506
Cdd:pfam02815 165 PEQQKVTCAK 174
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 37-302 1.54e-20

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 95.73  E-value: 1.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271  37 AVARSPKRPAWGSRRFEAVGWWALLaLVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINR---------TFFFDVHP 107
Cdd:COG1928   2 TAALPPARLVPPMPGDRLRGWLGTL-LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 108 PLGKMLIGLAGYLSGYDGTFlfqkpgdkyehhsymGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCL 187
Cdd:COG1928  81 PLGKWLIALGEWLFGYVNPF---------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHL 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 188 TLSQYILLDPILMFFIMAAMLSMV------------KYNSCADRPFSAP---WWFWLSLTGVSLAGALGVKFVGLFIILQ 252
Cdd:COG1928 146 VLSRTALLDIFLMFFVLAAFGCLLldrdqvrrrlaaAVAAGRAPSRWGPrlgFRWWRLAAGVLLGLACGVKWSGLYFLAA 225

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 32455271 253 VGLNTIADLWY---LFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFAVHF 302
Cdd:COG1928 226 FGLLTVAWDAGarrAAGVRRPWLGALLRDGIPAFFALVIVPLLTYLASWTGWF 278
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
404-459 1.71e-10

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 56.97  E-value: 1.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 32455271    404 EFVRHGDIIRLEHKETSRNLHSHYH-EAPMTRKHYQVTGYGiNGTGDSNDFWRIEVV 459
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEkLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 565-748 8.33e-04

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 42.57  E-value: 8.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 565 SKPWHWPIN-------YQGLRF----SGVNDTDFRVYLLGNPVVWWLNLLSIALyllsgSIIAVAMQRGARLPAevagls 633
Cdd:COG1928 329 SKPWSWPLMlrpvsyyYETGQTgtlgCGAGKCVRAVLAIGNPALWWLGLPALLW-----LLWRWIARRDWRAGA------ 397

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 634 qvllrgggqVLLGWTLHYFPFFL-MGRVLYFHHYFPAMLFssMLTGILWdTLLRLCAWGLASWPLARGIHVAGILSLLLG 712
Cdd:COG1928 398 ---------VLVGYAAGWLPWFLyLDRTMFFFYAIPFVPF--LVLALAL-VLGLILGPARASERRRLGRLVVGLYVGLVV 465

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 32455271 713 TAYSFylFHPLAYGMVGPLAQdPQSPMaglrWLDSW 748
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 ...
 337-523 2.34e-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: 371.25  E-value: 2.34e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 337 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 416
Cdd:cd23282   1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 417 KETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG 496
Cdd:cd23282  78 VNTKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWG 157

                       170       180
                ....*....|....*....|....*..
gi 32455271 497 WEQLEVTCTPYLKETlNSIWNVEDHIN 523
Cdd:cd23282 158 WEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 62-306 2.32e-82

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: 262.25  E-value: 2.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271    62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNscADR 219
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   220 PFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFA 299
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFY 238


                  ....*..
gi 32455271   300 VHFMVLS 306
Cdd:pfam02366 239 VHFWLLF 245
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 337-521 7.34e-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: 250.71  E-value: 7.34e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 337 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGarQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPsfPVEFVRHGDIIRLEH 416
Cdd:cd23276   1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSK--QQQVTGYGHKDENNWWQILKPRGDPSSNPP--DPEYVRDGDEVRLLH 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 417 KETSRNLHSHYHEAPMTRKHYQVTGYGINGT-GDSNDFWRIEVVNRKFGN---RIKVLRSRIRFIHLVTGCVLGSSGKVL 492
Cdd:cd23276  77 KETNRYLRTHDAAAPVTSKHKEVSAYPDENEdGDDNDLWVVEIVKDEGKLedkRIKPLTTRFRLRNKKTGCYLTSSGVKL 156

                       170       180
                ....*....|....*....|....*....
gi 32455271 493 PKWGWEQLEVTCTPYLKETLNSIWNVEDH 521
Cdd:cd23276 157 PEWGFRQGEVVCSKNKESDPSTLWNVEEN 185
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 334-523 8.59e-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: 232.21  E-value: 8.59e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 334 PEHLAYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIKK-HNTNSDPLDPSfPVEFVRHGDII 412
Cdd:cd23284   1 PLDVAYGSKVTIKNQGLGGGLLHSHVQTYPEG--SNQQQVTCYGHKDSNNEWIFERpRGLPSWDENDT-DIEFIKDGDIV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 413 RLEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVV---NRKFGNRIKVLRSRIRFIHLVTGCVLGSSG 489
Cdd:cd23284  78 RLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDNWVIEIVkqvGSEDPKKLHTLTTSFRLRHEVLGCYLAQTG 157

                       170       180       190
                ....*....|....*....|....*....|....*
gi 32455271 490 KVLPKWGWEQLEVTCTP-YLKETLNSIWNVEDHIN 523
Cdd:cd23284 158 VSLPEWGFKQGEVVCDKsNFKRDKRTWWNIETHTN 192
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 338-520 4.18e-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: 211.77  E-value: 4.18e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 338 AYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIkkHNTNSDPLDPSFPVEFVRHGDIIRLEHK 417
Cdd:cd23283   2 AYGSTIRIRHLNTRGGYLHSHPHNYPAG--SKQQQITLYPHRDENNDWLV--ELANAPEEWSPTTFENLKDGDVVRLEHV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 418 ETSRNLHSHYHEAPMTRKHYQ--VTGYGING-TGDSNDFWRIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSG 489
Cdd:cd23283  78 ATGRRLHSHDHRPPVSDNDWQneVSAYGYEGfEGDANDDWRVEILKDDSrpgesKERVRAIDTKFRLVHVMTGCYLFSHG 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 32455271 490 KVLPKWGWEQLEVTCTPYLKETlNSIWNVED 520
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 ...
 542-746 2.12e-60

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: 202.00  E-value: 2.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   542 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 621
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   622 GARLPAEVAGLSQvLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGI 701
Cdd:pfam16192  82 GYYDLSDDWTRSR-FYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 32455271   702 HVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQdpqspMAGLRWLD 746
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 ...
 337-523 4.52e-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: 176.34  E-value: 4.52e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 337 LAYGSVITVKNLRMAIGYLHSHRHLYP----EGIG-ARQQQVTTYLHKDYNNLWIIKKHNTNSDPldPSFPVEFVRHGDI 411
Cdd:cd23281   1 VAYGSQVTLRNTHGSPCWLHSHKHRYPikypDGRGsSHQQQVTCYPFKDVNNWWIIKDPGRQDLA--VDDPPRPVRHGDI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 412 IRLEHKETSRNLHSHYHEAPMTRKHYQVTGY-GINGTGDSNDFWRIEVVNRKF-GNRIKVLRSRIRFIHLVTGCVLGSSG 489
Cdd:cd23281  79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYiDYNISMPAQNLWRIEIVNRDSeGDTWKAIKSQFRLIHVNTSAALKLSG 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 32455271 490 KVLPKWGWEQLEVTcTPYLKETLNSIWNVEDHIN 523
Cdd:cd23281 159 KQLPDWGFGQLEVA-TDRAGNQSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 337-519 3.28e-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: 3.28e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 337 LAYGSVITVKNLRMAIGYLHSHRHLYPegIGARQQQVTTY-LHKDYNNLWII-KKHNTNSDPLDPSFpvEFVRHGDIIRL 414
Cdd:cd23286   1 LLYGSTVTIRHLESLGGYLHSHDLTYP--SGSNEQQVTLYdFEDDANNEWIIeTKTKEQMDKFPGQF--REVRDGDVIRL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 415 EHKETSRNLHSHYHEAPMTRK--HYQVTGYG-INGTGDSNDFWRIEVVNRK-------FGNRIKVLRSRIRFIHLVTGCV 484
Cdd:cd23286  77 RHVVTGKLLRASNARPPVSEQeyNNEVSCTGnANYSGDMDENWRIDVKGDEshaelklPNIKIKSTESVFQLYNRGTGCT 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 32455271 485 LGSSGKVLPKWGWEQLEVTC--TPYLKETLnsiWNVE 519
Cdd:cd23286 157 LLSHDTRLPDWAFHQQEVLCvnSPTIPNTL---FYVE 190
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 339-520 1.22e-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: 121.63  E-value: 1.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 339 YGSVITVKNlRMAIGYLHSHRHLYP----EG-IGARQQQVTTYLHKDYNNLWIIKkhntnsdPLDPSFPVE----FVRHG 409
Cdd:cd23285   3 YGDVITIKH-RDTNAFLHSHPERYPlryeDGrISSQGQQVTGYPHKDANNQWQIL-------PTDPIDEHEgtgrPVRNG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 410 DIIRLEHKETSRNLHSHYHEAPMTRKHYQVTgygingTGDSNDF--------WRIEVVNRKFGNRIKVLRSRIRFIHLVT 481
Cdd:cd23285  75 DLIRLRHVSTDTYLLTHDVASPLTPTNMEFT------TVSDDDTderynetlFRVEIEDTDEGDVLKTKSSHFRLIHVDT 148

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 32455271 482 GCVLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVED 520
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 ...
 339-518 3.33e-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: 105.84  E-value: 3.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 339 YGSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLH-KDYNNLWIIKKHNtNSDPLDPSFPVefvRHGDIIRLEHK 417
Cdd:cd23279   1 YGSAIKLKHVNSGY-RLHSHEVSY--GSGSGQQSVTAVPSaDDANSLWTVLPGL-GEPCQEQGKPV---KCGDIIRLQHV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 418 ETSRNLHSHYHEAPMTRkHYQVTGYGiNGTGDSNDFWRIEVVNRKFGNrIKVlRSRIRFIHLVTGCVLGSSGKVL----P 493
Cdd:cd23279  74 NTRKNLHSHNHSSPLSG-NQEVSAFG-GGDEDSGDNWIVECEGKKAKF-WKR-GEPVRLKHVDTGKYLSASKTHKftqqP 149

                       170       180
                ....*....|....*....|....*
gi 32455271 494 KWGweQLEVTCTPYLKEtlNSIWNV 518
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 ...
 339-516 2.85e-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: 100.14  E-value: 2.85e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 339 YGSVITVKNLRMAIgYLHSHrhLYPEGIGARQQQVTTYLHK-DYNNLWIIKKHNTNSDPldpsfPVEFVRHGDIIRLEHK 417
Cdd:cd23294   3 CGSVIKLQHERTKF-RLHSH--EVPYGSGSGQQSVTGFPGVdDSNSYWIVKPANGERCK-----QGDVIKNGDVIRLQHV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 418 ETSRNLHSHYHEAPMTRKHyQVTGYGINGTGDSNDFWRIEVVNrkfGNRIKVLRSRIRFIHLVTGCVLGSSGKvlpKWGW 497
Cdd:cd23294  75 STRKWLHSHLHASPLSGNQ-EVSCFGGDGNSDTGDNWIVEIEG---GGKVWERDQKVRLKHVDTGGYLHSHDK---KYGR 147

                       170       180
                ....*....|....*....|..
gi 32455271 498 E---QLEVTCTPylKETLNSIW 516
Cdd:cd23294 148 PipgQQEVCAVA--SKNSNTLW 167
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 340-520 1.60e-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: 97.84  E-value: 1.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 340 GSVITVKNLRMAiGYLHSHRHLYPEGIGarQQQVTTYLHK---DYNNLWIIKKHNTNSDpldpsfpvEFVRHGDIIRLEH 416
Cdd:cd23263   1 GDVIWLKHSETG-KYLHSHRKNYPTGSG--QQEVTFESSSrkgDTNGLWIIESENGKQG--------GPVKWGDKIRLRH 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 417 KETSRNLHSHYHEAPMTRKHYQVTGYGINgtGDSNDFWRIEVVN-RKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKW 495
Cdd:cd23263  70 LSTGKYLSSEEGKKSPKSNHQEVLCLTDN--PDKSSLFKFEPIGsTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNIN 147

                       170       180
                ....*....|....*....|....*
gi 32455271 496 GWEQLEVTCTPyLKETLNSIWNVED 520
Cdd:cd23263 148 NKTQQEVICHG-EREEVFKLWKAEL 171
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 356-506 1.56e-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: 92.81  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   356 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHY 427
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRHLTTGRYLHSHE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271   428 HEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWG-- 496
Cdd:pfam02815  87 EQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGfg 164

                         170
                  ....*....|
gi 32455271   497 WEQLEVTCTP 506
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 ...
 340-522 8.60e-21

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: 90.41  E-value: 8.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 340 GSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLHK-DYNNLWIIK-KHNTNSDPLDPsfpvefVRHGDIIRLEHK 417
Cdd:cd23293   4 GSVVKLLNTRHNV-RLHSHDVKY--GSGSGQQSVTGVESSdDSNSYWQIRgPTGADCERGTP------IKCGQTIRLTHL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 418 ETSRNLHSHYHEAPMTRkHYQVTGYGINGTGDSNDFWRIeVVNRKFGNRikvlRSRIRFIHLVTGCVLGSSGKVL--PKW 495
Cdd:cd23293  75 NTGKNLHSHHFQSPLSG-NQEVSAFGEDGEGDTGDNWTV-VCSGTYWER----DEAVRLKHVDTEVYLHVTGEQYgrPIH 148

                       170       180
                ....*....|....*....|....*..
gi 32455271 496 GweQLEVTCTPYLkeTLNSIWNVEDHI 522
Cdd:cd23293 149 G--QREVSGMSSP--SQANYWKAMEGI 171
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 37-302 1.54e-20

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 95.73  E-value: 1.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271  37 AVARSPKRPAWGSRRFEAVGWWALLaLVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINR---------TFFFDVHP 107
Cdd:COG1928   2 TAALPPARLVPPMPGDRLRGWLGTL-LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 108 PLGKMLIGLAGYLSGYDGTFlfqkpgdkyehhsymGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCL 187
Cdd:COG1928  81 PLGKWLIALGEWLFGYVNPF---------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHL 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 188 TLSQYILLDPILMFFIMAAMLSMV------------KYNSCADRPFSAP---WWFWLSLTGVSLAGALGVKFVGLFIILQ 252
Cdd:COG1928 146 VLSRTALLDIFLMFFVLAAFGCLLldrdqvrrrlaaAVAAGRAPSRWGPrlgFRWWRLAAGVLLGLACGVKWSGLYFLAA 225

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 32455271 253 VGLNTIADLWY---LFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFAVHF 302
Cdd:COG1928 226 FGLLTVAWDAGarrAAGVRRPWLGALLRDGIPAFFALVIVPLLTYLASWTGWF 278
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 409-532 6.46e-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: 6.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 409 GDIIRLEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKvLRSRIRFIHLVTGCVLGSS 488
Cdd:cd23263   1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQGGPVK-WGDKIRLRHLSTGKYLSSE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32455271 489 GKVLPKWGWEQlEVTCTPYLKETlNSIWNVE--DHINPKLPNISLD 532
Cdd:cd23263  80 EGKKSPKSNHQ-EVLCLTDNPDK-SSLFKFEpiGSTKYKQKYVKKD 123
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
404-459 1.71e-10

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 56.97  E-value: 1.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 32455271    404 EFVRHGDIIRLEHKETSRNLHSHYH-EAPMTRKHYQVTGYGiNGTGDSNDFWRIEVV 459
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEkLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
472-521 3.29e-08

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 50.42  E-value: 3.29e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 32455271    472 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 521
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
334-390 1.07e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 1.07e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 32455271    334 PEHLAYGSVITVKNLRMAiGYLHSHRHLYPEgIGARQQQVTTYLHK--DYNNLWIIKKH 390
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTG-RYLHSHDEKLPP-WGDGQQEVTGYGNPaiDANTLWLIEPV 57
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 406-504 1.18e-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: 43.52  E-value: 1.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 406 VRHGDIIRLEHKETSRNLHShyHEAPMTRKHYQ--VTGYgiNGTGDSNDFWRIEVVNR---KFGNRIKVlRSRIRFIHLV 480
Cdd:cd23294   1 VTCGSVIKLQHERTKFRLHS--HEVPYGSGSGQqsVTGF--PGVDDSNSYWIVKPANGercKQGDVIKN-GDVIRLQHVS 75

                        90       100
                ....*....|....*....|....
gi 32455271 481 TGCVLGSSGKVLPKWGweQLEVTC 504
Cdd:cd23294  76 TRKWLHSHLHASPLSG--NQEVSC 97
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 565-748 8.33e-04

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 42.57  E-value: 8.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 565 SKPWHWPIN-------YQGLRF----SGVNDTDFRVYLLGNPVVWWLNLLSIALyllsgSIIAVAMQRGARLPAevagls 633
Cdd:COG1928 329 SKPWSWPLMlrpvsyyYETGQTgtlgCGAGKCVRAVLAIGNPALWWLGLPALLW-----LLWRWIARRDWRAGA------ 397

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 634 qvllrgggqVLLGWTLHYFPFFL-MGRVLYFHHYFPAMLFssMLTGILWdTLLRLCAWGLASWPLARGIHVAGILSLLLG 712
Cdd:COG1928 398 ---------VLVGYAAGWLPWFLyLDRTMFFFYAIPFVPF--LVLALAL-VLGLILGPARASERRRLGRLVVGLYVGLVV 465

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 32455271 713 TAYSFylFHPLAYGMVGPLAQdPQSPMaglrWLDSW 748
Cdd:COG1928 466 ANFAF--FYPILTGLPIPYDE-WQARM----WFPSW 494
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 405-485 2.72e-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: 2.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32455271 405 FVRHGDIIRLEHKETSRNLH---SHYHEAPMTRKHYQV------TGYGINGTGDSNDFWRIEVVNRKF-GNRIKvLRSRI 474
Cdd:cd23280   6 FLKGGDVVRLFHKELEAYLSaegSFVDEVLTEDVHLRVrpvddrKPRTLFPPTSGDTFWQIEKEDTPLkGGVIK-WGDQC 84

                        90
                ....*....|.
gi 32455271 475 RFIHLVTGCVL 485
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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