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Conserved domains on  [gi|2462539961|ref|XP_054231897|]
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protein O-mannosyl-transferase 2 isoform X1 [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 ...
 337-536 8.37e-121

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar proteins; POMT2 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 2, is a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids. POMT2 transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins. POMT2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 467753 [Multi-domain]  Cd Length: 183  Bit Score: 361.62  E-value: 8.37e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 337 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 416
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 417 KEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGC 496
Cdd:cd23282    78 VN-------------TKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGC 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462539961 497 VLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVEDHIN 536
Cdd:cd23282   145 ALHSHGKQLPKWGWEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 62-306 5.27e-83

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: 265.33  E-value: 5.27e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961  62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNscADR 219
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 220 PFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFA 299
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFY 238


                  ....*..
gi 2462539961 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 ...
 555-822 2.78e-52

C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.


:

Pssm-ID: 465056  Cd Length: 198  Bit Score: 180.82  E-value: 2.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 555 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 634
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 635 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 714
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 715 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 794
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 2462539961 795 LFHPLAYGMVGPLAQdpqspMAGLRWLD 822
Cdd:pfam16192 176 YFSPLTYGMPGTSEE-----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 ...
 337-536 8.37e-121

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar proteins; POMT2 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 2, is a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids. POMT2 transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins. POMT2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467753 [Multi-domain]  Cd Length: 183  Bit Score: 361.62  E-value: 8.37e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 337 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 416
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 417 KEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGC 496
Cdd:cd23282    78 VN-------------TKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGC 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462539961 497 VLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVEDHIN 536
Cdd:cd23282   145 ALHSHGKQLPKWGWEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 62-306 5.27e-83

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: 265.33  E-value: 5.27e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961  62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNscADR 219
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 220 PFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFA 299
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFY 238


                  ....*..
gi 2462539961 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 ...
 555-822 2.78e-52

C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.


Pssm-ID: 465056  Cd Length: 198  Bit Score: 180.82  E-value: 2.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 555 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 634
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 635 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 714
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 715 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 794
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 2462539961 795 LFHPLAYGMVGPLAQdpqspMAGLRWLD 822
Cdd:pfam16192 176 YFSPLTYGMPGTSEE-----CKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 37-302 1.53e-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: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961  37 AVARSPKRPAWGSRRFEAVGWWALLaLVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINR---------TFFFDVHP 107
Cdd:COG1928     2 TAALPPARLVPPMPGDRLRGWLGTL-LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 108 PLGKMLIGLAGYLSGYDGTFlfqkpgdkyehhsymGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCL 187
Cdd:COG1928    81 PLGKWLIALGEWLFGYVNPF---------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 188 TLSQYILLDPILMFFIMAAMLSMV------------KYNSCADRPFSAP---WWFWLSLTGVSLAGALGVKFVGLFIILQ 252
Cdd:COG1928   146 VLSRTALLDIFLMFFVLAAFGCLLldrdqvrrrlaaAVAAGRAPSRWGPrlgFRWWRLAAGVLLGLACGVKWSGLYFLAA 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462539961 253 VGLNTIADLWY---LFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFAVHF 302
Cdd:COG1928   226 FGLLTVAWDAGarrAAGVRRPWLGALLRDGIPAFFALVIVPLLTYLASWTGWF 278
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 356-519 2.93e-18

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


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 83.57  E-value: 2.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 356 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHkecpLKkiwrw 427
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRH----LT----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 428 eqkeTSRNLHSHYHEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVL 498
Cdd:pfam02815  78 ----TGRYLHSHEEQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWL 151

                         170       180
                  ....*....|....*....|...
gi 2462539961 499 GSSGKVLPKWG--WEQLEVTCTP 519
Cdd:pfam02815 152 FSHSVKLPKWGfgPEQQKVTCAK 174
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
485-534 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 2462539961  485 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 534
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDANTLWLIEPV 57
 
Name Accession Description Interval E-value
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 337-536 8.37e-121

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar proteins; POMT2 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 2, is a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids. POMT2 transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins. POMT2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467753 [Multi-domain]  Cd Length: 183  Bit Score: 361.62  E-value: 8.37e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 337 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPldpSFPVEFVRHGDIIRLEH 416
Cdd:cd23282     1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDL---SDPVEYVRHGDLIRLEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 417 KEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGC 496
Cdd:cd23282    78 VN-------------TKRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGC 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462539961 497 VLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVEDHIN 536
Cdd:cd23282   145 ALHSHGKQLPKWGWEQLEVTCNPNVRDK-NSLWNVEDNRN 183
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 62-306 5.27e-83

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: 265.33  E-value: 5.27e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961  62 ALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKY--EHH 139
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 140 SYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNscADR 219
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 220 PFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFA 299
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFY 238


                  ....*..
gi 2462539961 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 ...
 337-534 7.24e-75

MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein mannosyltransferase (PMT); The PMT (EC 2.4.1.109) family includes mammalian protein O-mannosyl-transferases (POMT1 and POMT2) and yeast PMT1-7. PMTs are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467747 [Multi-domain]  Cd Length: 185  Bit Score: 241.47  E-value: 7.24e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 337 LAYGSVITVKNLRMAIGYLHSHRHLYPEGIGarQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPsfPVEFVRHGDIIRLEH 416
Cdd:cd23276     1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSK--QQQVTGYGHKDENNWWQILKPRGDPSSNPP--DPEYVRDGDEVRLLH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 417 KEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGT-GDSNDFWRIEVVNRKFGN---RIKVLRSRIRFIHL 492
Cdd:cd23276    77 KE-------------TNRYLRTHDAAAPVTSKHKEVSAYPDENEdGDDNDLWVVEIVKDEGKLedkRIKPLTTRFRLRNK 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462539961 493 VTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 534
Cdd:cd23276   144 KTGCYLTSSGVKLPEWGFRQGEVVCSKNKESDPSTLWNVEEN 185
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 334-536 1.06e-67

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: 222.58  E-value: 1.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 334 PEHLAYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIKK-HNTNSDPLDPSfPVEFVRHGDII 412
Cdd:cd23284     1 PLDVAYGSKVTIKNQGLGGGLLHSHVQTYPEG--SNQQQVTCYGHKDSNNEWIFERpRGLPSWDENDT-DIEFIKDGDIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 413 RLEHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVV---NRKFGNRIKVLRSRIRF 489
Cdd:cd23284    78 RLVHKQ-------------TGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDNWVIEIVkqvGSEDPKKLHTLTTSFRL 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462539961 490 IHLVTGCVLGSSGKVLPKWGWEQLEVTCTP-YLKETLNSIWNVEDHIN 536
Cdd:cd23284   145 RHEVLGCYLAQTGVSLPEWGFKQGEVVCDKsNFKRDKRTWWNIETHTN 192
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 338-533 2.45e-60

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: 202.53  E-value: 2.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 338 AYGSVITVKNLRMAIGYLHSHRHLYPEGigARQQQVTTYLHKDYNNLWIIkkHNTNSDPLDPSFPVEFVRHGDIIRLEHK 417
Cdd:cd23283     2 AYGSTIRIRHLNTRGGYLHSHPHNYPAG--SKQQQITLYPHRDENNDWLV--ELANAPEEWSPTTFENLKDGDVVRLEHV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 418 EcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQ--VTGYGING-TGDSNDFWRIEVVNRKF-----GNRIKVLRSRIRF 489
Cdd:cd23283    78 A-------------TGRRLHSHDHRPPVSDNDWQneVSAYGYEGfEGDANDDWRVEILKDDSrpgesKERVRAIDTKFRL 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462539961 490 IHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVED 533
Cdd:cd23283   145 VHVMTGCYLFSHGVKLPEWGFEQQEVTCAKSGLLE-LSLWYIET 187
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 555-822 2.78e-52

C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.


Pssm-ID: 465056  Cd Length: 198  Bit Score: 180.82  E-value: 2.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 555 LLESHMVMIRGNSGLKPKDnEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQR 634
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPSH-PYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 635 GARLpaevagqvlwaLPPLTWRQQgtctpgegrlpadgpsfafttphlplsfaferkprnheikklapghtarlsqvLLR 714
Cdd:pfam16192  82 GYYD-----------LSDDWTRSR-----------------------------------------------------FYY 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 715 GGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPlaRGIHVAGILSLLLGTAYSFY 794
Cdd:pfam16192  98 SGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR--KRVGYAIVVVLLALVIYVFI 175

                         250       260
                  ....*....|....*....|....*...
gi 2462539961 795 LFHPLAYGMVGPLAQdpqspMAGLRWLD 822
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 ...
 337-536 2.35e-47

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar proteins; POMT1 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 1, belongs to the glycosyltransferase 39 family. It transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins, but not of cadherins and protocaherins. POMT1 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467752 [Multi-domain]  Cd Length: 191  Bit Score: 166.71  E-value: 2.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 337 LAYGSVITVKNLRMAIGYLHSHRHLYP----EGIG-ARQQQVTTYLHKDYNNLWIIKKHNTNSDPldPSFPVEFVRHGDI 411
Cdd:cd23281     1 VAYGSQVTLRNTHGSPCWLHSHKHRYPikypDGRGsSHQQQVTCYPFKDVNNWWIIKDPGRQDLA--VDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 412 IRLEHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGY-GINGTGDSNDFWRIEVVNRKF-GNRIKVLRSRIRF 489
Cdd:cd23281    79 IQLVHGK-------------TGRFLNSHDVAAPLSPTHQEVSCYiDYNISMPAQNLWRIEIVNRDSeGDTWKAIKSQFRL 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462539961 490 IHLVTGCVLGSSGKVLPKWGWEQLEVTcTPYLKETLNSIWNVEDHIN 536
Cdd:cd23281   146 IHVNTSAALKLSGKQLPDWGFGQLEVA-TDRAGNQSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 337-532 6.42e-31

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 7 (PMT7) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called PMTs, are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT7. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467757 [Multi-domain]  Cd Length: 192  Bit Score: 120.23  E-value: 6.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 337 LAYGSVITVKNLRMAIGYLHSHRHLYPegIGARQQQVTTY-LHKDYNNLWII-KKHNTNSDPLDPSFpvEFVRHGDIIRL 414
Cdd:cd23286     1 LLYGSTVTIRHLESLGGYLHSHDLTYP--SGSNEQQVTLYdFEDDANNEWIIeTKTKEQMDKFPGQF--REVRDGDVIRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 415 EHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRK--HYQVTGYG-INGTGDSNDFWRIEVVNRK-------FGNRIKVLR 484
Cdd:cd23286    77 RHVV-------------TGKLLRASNARPPVSEQeyNNEVSCTGnANYSGDMDENWRIDVKGDEshaelklPNIKIKSTE 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462539961 485 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTC--TPYLKETLnsiWNVE 532
Cdd:cd23286   144 SVFQLYNRGTGCTLLSHDTRLPDWAFHQQEVLCvnSPTIPNTL---FYVE 190
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 339-533 2.52e-28

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 4 (PMT4) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called PMTs, are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT4. It forms a functional homodimer and may form a heterodimer with PMT6. PMT4 specifically acts on secretory proteins with an ER-luminally oriented Ser/Thr-rich region flanked by a membrane anchor such as FUS1, AXL2, GAS1, KEX2, MID2, WSC1, WSC2, OPY2, PRM5, RAX2, or YNL176. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467756 [Multi-domain]  Cd Length: 187  Bit Score: 112.39  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 339 YGSVITVKNlRMAIGYLHSHRHLYP----EG-IGARQQQVTTYLHKDYNNLWIIKkhntnsdPLDPSFPVE----FVRHG 409
Cdd:cd23285     3 YGDVITIKH-RDTNAFLHSHPERYPlryeDGrISSQGQQVTGYPHKDANNQWQIL-------PTDPIDEHEgtgrPVRNG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 410 DIIRLEHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTgygingTGDSNDF--------WRIEVVNRKFGNRIK 481
Cdd:cd23285    75 DLIRLRHVS-------------TDTYLLTHDVASPLTPTNMEFT------TVSDDDTderynetlFRVEIEDTDEGDVLK 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462539961 482 VLRSRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETlNSIWNVED 533
Cdd:cd23285   136 TKSSHFRLIHVDTNVALWTHKKPLPDWGFGQQEVNGNKNIKDK-SNIWVVDD 186
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 339-531 5.01e-23

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: 96.60  E-value: 5.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 339 YGSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLH-KDYNNLWIIKKHNtNSDPLDPSFPVefvRHGDIIRLEHK 417
Cdd:cd23279     1 YGSAIKLKHVNSGY-RLHSHEVSY--GSGSGQQSVTAVPSaDDANSLWTVLPGL-GEPCQEQGKPV---KCGDIIRLQHV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 418 EcplkkiwrweqkeTSRNLHSHYHEAPMTRkHYQVTGYGiNGTGDSNDFWRIEVVNRKFGNrIKVlRSRIRFIHLVTGCV 497
Cdd:cd23279    74 N-------------TRKNLHSHNHSSPLSG-NQEVSAFG-GGDEDSGDNWIVECEGKKAKF-WKR-GEPVRLKHVDTGKY 136

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462539961 498 LGSSGKVL----PKWGweQLEVTCTPYLKEtlNSIWNV 531
Cdd:cd23279   137 LSASKTHKftqqPIAG--QLEVSAASSKDS--DSQWKA 170
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 339-529 5.84e-21

MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2) and similar proteins; AtSDF2, also called SDF2-like protein, acts as a crucial component of the unfolded protein response (UPR) in Arabidopsis thaliana. It is involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. It may be involved in the quality control of glycoproteins. AtSDF2 forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity. AtSDF2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467765 [Multi-domain]  Cd Length: 176  Bit Score: 90.90  E-value: 5.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 339 YGSVITVKNLRMAIgYLHSHrhLYPEGIGARQQQVTTYLHK-DYNNLWIIKKHNTNSDPldpsfPVEFVRHGDIIRLEHK 417
Cdd:cd23294     3 CGSVIKLQHERTKF-RLHSH--EVPYGSGSGQQSVTGFPGVdDSNSYWIVKPANGERCK-----QGDVIKNGDVIRLQHV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 418 EcplkkiwrweqkeTSRNLHSHYHEAPMTRKHyQVTGYGINGTGDSNDFWRIEVVNrkfGNRIKVLRSRIRFIHLVTGCV 497
Cdd:cd23294    75 S-------------TRKWLHSHLHASPLSGNQ-EVSCFGGDGNSDTGDNWIVEIEG---GGKVWERDQKVRLKHVDTGGY 137

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462539961 498 LGSSGKvlpKWGWE---QLEVTCTPylKETLNSIW 529
Cdd:cd23294   138 LHSHDK---KYGRPipgQQEVCAVA--SKNSNTLW 167
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 37-302 1.53e-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: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961  37 AVARSPKRPAWGSRRFEAVGWWALLaLVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINR---------TFFFDVHP 107
Cdd:COG1928     2 TAALPPARLVPPMPGDRLRGWLGTL-LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 108 PLGKMLIGLAGYLSGYDGTFlfqkpgdkyehhsymGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCL 187
Cdd:COG1928    81 PLGKWLIALGEWLFGYVNPF---------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 188 TLSQYILLDPILMFFIMAAMLSMV------------KYNSCADRPFSAP---WWFWLSLTGVSLAGALGVKFVGLFIILQ 252
Cdd:COG1928   146 VLSRTALLDIFLMFFVLAAFGCLLldrdqvrrrlaaAVAAGRAPSRWGPrlgFRWWRLAAGVLLGLACGVKWSGLYFLAA 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462539961 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) ...
 340-533 2.65e-20

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: 88.98  E-value: 2.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 340 GSVITVKNLRMAiGYLHSHRHLYPEGIGarQQQVTTYLHK---DYNNLWIIKKHNTNSDpldpsfpvEFVRHGDIIRLEH 416
Cdd:cd23263     1 GDVIWLKHSETG-KYLHSHRKNYPTGSG--QQEVTFESSSrkgDTNGLWIIESENGKQG--------GPVKWGDKIRLRH 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 417 kecplkkiwrweqKETSRNLHSHYHEAPMTRKHYQVTGYGINgtGDSNDFWRIEVVN-RKFGNRIKVLRSRIRFIHLVTG 495
Cdd:cd23263    70 -------------LSTGKYLSSEEGKKSPKSNHQEVLCLTDN--PDKSSLFKFEPIGsTKYKQKYVKKDSYFRLKHVNTN 134

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462539961 496 CVLGSSGKVLPKWGWEQLEVTCTPyLKETLNSIWNVED 533
Cdd:cd23263   135 FWLHSHEKKFNINNKTQQEVICHG-EREEVFKLWKAEL 171
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 356-519 2.93e-18

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


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 83.57  E-value: 2.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 356 HSHRHLYPEG----IGARQQQVTTYLHKDYNN----LWIIKKhntnsdPLDPSFPVEFVRHGDIIRLEHkecpLKkiwrw 427
Cdd:pfam02815  13 HSHQDEYLTGseqqQKQPFLRITLYPHGDANNsarsLWRIEV------VRHDAWRGGLIKWGSPFRLRH----LT----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 428 eqkeTSRNLHSHYHEAPMTRK----HYQVTGYGINGTGDSNDFwrIEVVNRKF-----GNRIKVLRSRIRFIHLVTGCVL 498
Cdd:pfam02815  78 ----TGRYLHSHEEQKPPLVEkedwQKEVSAYGFRGFPGDNDI--VEIFEKKSttgmgSDRIKPGDSYFRLQHVCTGCWL 151

                         170       180
                  ....*....|....*....|...
gi 2462539961 499 GSSGKVLPKWG--WEQLEVTCTP 519
Cdd:pfam02815 152 FSHSVKLPKWGfgPEQQKVTCAK 174
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 340-535 1.40e-17

MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 (SDF-2); The metazoan SDF-2 family includes SDF-2 and SDF2-like protein 1 (SDF2L1). SDF-2 is a secretory protein involved in multiple endoplasmic reticulum (ER) functions, including the misfolded protein catabolic process, protein glycosylation, and ER protein quality control. SDF2L1, also called PWP1-interacting protein 8, is an endoplasmic reticulum (ER)-localized protein that plays a role in ER-associated degradation (ERAD) of misfolded proinsulin in pancreatic beta-cells. It is a component of the endoplasmic reticulum (ER) chaperone complex and interacts with alpha- and beta-defensins. SDF2L1 may also act as a tumor suppressor that play an important role in a variety of cancers, such as breast cancer and ovarian cancer. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467764 [Multi-domain]  Cd Length: 175  Bit Score: 81.16  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 340 GSVITVKNLRMAIgYLHSHRHLYpeGIGARQQQVTTYLHK-DYNNLWIIK-KHNTNSDPLDPsfpvefVRHGDIIRLEHK 417
Cdd:cd23293     4 GSVVKLLNTRHNV-RLHSHDVKY--GSGSGQQSVTGVESSdDSNSYWQIRgPTGADCERGTP------IKCGQTIRLTHL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 418 EcplkkiwrweqkeTSRNLHSHYHEAPMTRkHYQVTGYGINGTGDSNDFWRIeVVNRKFGNRikvlRSRIRFIHLVTGCV 497
Cdd:cd23293    75 N-------------TGKNLHSHHFQSPLSG-NQEVSAFGEDGEGDTGDNWTV-VCSGTYWER----DEAVRLKHVDTEVY 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462539961 498 LGSSGKVL--PKWGweQLEVTCTPYLkeTLNSIWNVEDHI 535
Cdd:cd23293   136 LHVTGEQYgrPIHG--QREVSGMSSP--SQANYWKAMEGI 171
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 409-545 1.13e-15

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 75.50  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961 409 GDIIRLEHKEcplkkiwrweqkeTSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKvLRSRIR 488
Cdd:cd23263     1 GDVIWLKHSE-------------TGKYLHSHRKNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQGGPVK-WGDKIR 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462539961 489 FIHLVTGCVLGSSGKVLPKWGWEQlEVTCTPYLKETlNSIWNVE--DHINPKLPNISLD 545
Cdd:cd23263    67 LRHLSTGKYLSSEEGKKSPKSNHQ-EVLCLTDNPDK-SSLFKFEpiGSTKYKQKYVKKD 123
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
485-534 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 2462539961  485 SRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDH 534
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
404-472 3.04e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 47.72  E-value: 3.04e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539961  404 EFVRHGDIIRLEHKEcplkkiwrweqkeTSRNLHSHYH-EAPMTRKHYQVTGYGiNGTGDSNDFWRIEVV 472
Cdd:smart00472   2 GFVRWGDVVRLRHVT-------------TGRYLHSHDEkLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 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 2462539961  334 PEHLAYGSVITVKNLRMAiGYLHSHRHLYPEgIGARQQQVTTYLHK--DYNNLWIIKKH 390
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTG-RYLHSHDEKLPP-WGDGQQEVTGYGNPaiDANTLWLIEPV 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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