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Conserved domains on  [gi|442614658|ref|NP_001259102|]
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twisted, isoform B [Drosophila melanogaster]

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 ...
 321-503 3.46e-120

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: 358.54  E-value: 3.46e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKNHKTGGGYLHSHHHLYPKGSGARQQQVTTYTHKDENNKWLIRPHNKPGPPKGKVQILRHGDLVRLTHMAT 400
Cdd:cd23282    1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDLSDPVEYVRHGDLIRLEHVNT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 401 RRNLHSHNEPAPMTKKHLQVTGYGELGLGDANDVWRVLIVGGKVNETVHTVTSRLKFIHLLQNCALTSSGKQLPKWGFEQ 480
Cdd:cd23282   81 KRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWGWEQ 160

                        170       180
                 ....*....|....*....|...
gi 442614658 481 QEVSCNPNVRDKNSQWNVEDNEH 503
Cdd:cd23282  161 LEVTCNPNVRDKNSLWNVEDNRN 183
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 44-290 4.19e-64

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: 214.10  E-value: 4.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658   44 ATVFLVTFATRFYKVTEPDHICWDETHFGKMGSWYINRTFFFDVHPPLGKMLIGLSGYLTGYNGTFPFEKPGDKY--NET 121
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  122 RYQGMRYFCTTLGALIMPMGFDTVYDLTRSHEAALLAAAYLIFDVGLLTLNQYILLDPILLFFMMASVWGMVKVSKSTAs 201
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  202 ggsYGLRWWLWLFLTGTMLSCTISVKFVGLFVVLLVGLHTATELWLILGDLGQPILETVKQLACRAITLIVWPVLLYILF 281
Cdd:pfam02366 160 ---FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 442614658  282 FYIHLSVLN 290
Cdd:pfam02366 237 FYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 520-761 3.38e-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: 180.05  E-value: 3.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  520 ARFLESHAVMLQGNAGLKPkEGEVTSRPWQWPINYRGQFFSG---SSYRIYLLGNPLIWWSNLVFLALFVTVFLCNAVVQ 596
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTP-SHPYASRPWEWPLLLRGIRFWGwddRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  597 QRragfarsaaqnqaQVPDSetvaqdeesehsttdicscctpakeivpkavpsgsPEAPNPAQSLRAAAWLFLGWMLHYL 676
Cdd:pfam16192  80 QR-------------GYYDL-----------------------------------SDDWTRSRFYYSGGFLLLGWALHYL 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  677 PFWAMGRVLYFHHYFPALIFNSLLTGVMYNYILRV-------LPKWIHHVILGLVLSILVYSFAAFSPLAYGMSGplane 749
Cdd:pfam16192 112 PFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLfrrlprsLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPG----- 186

                         250
                  ....*....|..
gi 442614658  750 PNSTMYNLKWLS 761
Cdd:pfam16192 187 TSEECKKLKWLS 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 ...
 321-503 3.46e-120

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: 358.54  E-value: 3.46e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKNHKTGGGYLHSHHHLYPKGSGARQQQVTTYTHKDENNKWLIRPHNKPGPPKGKVQILRHGDLVRLTHMAT 400
Cdd:cd23282    1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDLSDPVEYVRHGDLIRLEHVNT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 401 RRNLHSHNEPAPMTKKHLQVTGYGELGLGDANDVWRVLIVGGKVNETVHTVTSRLKFIHLLQNCALTSSGKQLPKWGFEQ 480
Cdd:cd23282   81 KRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWGWEQ 160

                        170       180
                 ....*....|....*....|...
gi 442614658 481 QEVSCNPNVRDKNSQWNVEDNEH 503
Cdd:cd23282  161 LEVTCNPNVRDKNSLWNVEDNRN 183
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 44-290 4.19e-64

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: 214.10  E-value: 4.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658   44 ATVFLVTFATRFYKVTEPDHICWDETHFGKMGSWYINRTFFFDVHPPLGKMLIGLSGYLTGYNGTFPFEKPGDKY--NET 121
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  122 RYQGMRYFCTTLGALIMPMGFDTVYDLTRSHEAALLAAAYLIFDVGLLTLNQYILLDPILLFFMMASVWGMVKVSKSTAs 201
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  202 ggsYGLRWWLWLFLTGTMLSCTISVKFVGLFVVLLVGLHTATELWLILGDLGQPILETVKQLACRAITLIVWPVLLYILF 281
Cdd:pfam02366 160 ---FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 442614658  282 FYIHLSVLN 290
Cdd:pfam02366 237 FYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 520-761 3.38e-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: 180.05  E-value: 3.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  520 ARFLESHAVMLQGNAGLKPkEGEVTSRPWQWPINYRGQFFSG---SSYRIYLLGNPLIWWSNLVFLALFVTVFLCNAVVQ 596
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTP-SHPYASRPWEWPLLLRGIRFWGwddRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  597 QRragfarsaaqnqaQVPDSetvaqdeesehsttdicscctpakeivpkavpsgsPEAPNPAQSLRAAAWLFLGWMLHYL 676
Cdd:pfam16192  80 QR-------------GYYDL-----------------------------------SDDWTRSRFYYSGGFLLLGWALHYL 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  677 PFWAMGRVLYFHHYFPALIFNSLLTGVMYNYILRV-------LPKWIHHVILGLVLSILVYSFAAFSPLAYGMSGplane 749
Cdd:pfam16192 112 PFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLfrrlprsLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPG----- 186

                         250
                  ....*....|..
gi 442614658  750 PNSTMYNLKWLS 761
Cdd:pfam16192 187 TSEECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 340-496 1.29e-25

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: 104.37  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  340 HSHHHLYPKGSGARQQQ----VTTYTHKDENNK----WLIRPHNKPgppKGKVQILRHGDLVRLTHMATRRNLHSHNEP- 410
Cdd:pfam02815  13 HSHQDEYLTGSEQQQKQpflrITLYPHGDANNSarslWRIEVVRHD---AWRGGLIKWGSPFRLRHLTTGRYLHSHEEQk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  411 APMTKK---HLQVTGYGELGLGDANDVwrVLIV-----GGKVNETVHTVTSRLKFIHLLQNCALTSSGKQLPKWGFE--Q 480
Cdd:pfam02815  90 PPLVEKedwQKEVSAYGFRGFPGDNDI--VEIFekkstTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpeQ 167

                         170
                  ....*....|....*.
gi 442614658  481 QEVSCNPNVRDKNSQW 496
Cdd:pfam02815 168 QKVTCAKEGHMDDALT 183
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 24-239 1.82e-19

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 92.26  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  24 APRTAPTSSKEANWNWWLLLAtVFLVTFATRFYKVTEPDHICWDETHFGKMGSWYINR---------TFFFDVHPPLGKM 94
Cdd:COG1928    7 PARLVPPMPGDRLRGWLGTLL-VTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPLGKW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  95 LIGLSGYLTGYNGTFpfekpgdkynetryqGMRYFCTTLGALIMPMGFDTVYDLTRSHEAALLAAAYLIFDVGLLTLNQY 174
Cdd:COG1928   86 LIALGEWLFGYVNPF---------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 175 ILLDPILLFFMMASVWGMV---------------KVSKSTASGGSYGLRWwlWLFLTGTMLSCTISVKFVGLFVVLLVGL 239
Cdd:COG1928  151 ALLDIFLMFFVLAAFGCLLldrdqvrrrlaaavaAGRAPSRWGPRLGFRW--WRLAAGVLLGLACGVKWSGLYFLAAFGL 228
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
318-374 1.67e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 59.66  E-value: 1.67e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 442614658   318 PRDVAYGSLVTIKnHKTGGGYLHSHHHLYPKgSGARQQQVTTYTHK--DENNKWLIRPH 374
Cdd:smart00472   1 GGFVRWGDVVRLR-HVTTGRYLHSHDEKLPP-WGDGQQEVTGYGNPaiDANTLWLIEPV 57
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 545-601 9.51e-03

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 39.10  E-value: 9.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442614658 545 SRPWQWPINYR--------GQFFSGS------SYRIYLLGNPLIWWsnlvfLALFVTVFLCNAVVQQR--RAG 601
Cdd:COG1928  329 SKPWSWPLMLRpvsyyyetGQTGTLGcgagkcVRAVLAIGNPALWW-----LGLPALLWLLWRWIARRdwRAG 396
 
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 ...
 321-503 3.46e-120

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: 358.54  E-value: 3.46e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKNHKTGGGYLHSHHHLYPKGSGARQQQVTTYTHKDENNKWLIRPHNKPGPPKGKVQILRHGDLVRLTHMAT 400
Cdd:cd23282    1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGVGARQQQVTTYSHKDDNNLWLIKKHNQSSDLSDPVEYVRHGDLIRLEHVNT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 401 RRNLHSHNEPAPMTKKHLQVTGYGELGLGDANDVWRVLIVGGKVNETVHTVTSRLKFIHLLQNCALTSSGKQLPKWGFEQ 480
Cdd:cd23282   81 KRNLHSHKEKAPLTKKHYQVTGYGENGTGDANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWGWEQ 160

                        170       180
                 ....*....|....*....|...
gi 442614658 481 QEVSCNPNVRDKNSQWNVEDNEH 503
Cdd:cd23282  161 LEVTCNPNVRDKNSLWNVEDNRN 183
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 318-503 4.00e-76

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: 244.15  E-value: 4.00e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 318 PRDVAYGSLVTIKNHKTGGGYLHSHHHLYPKGSgaRQQQVTTYTHKDENNKWLI-RPHNKPGPPKGK--VQILRHGDLVR 394
Cdd:cd23284    1 PLDVAYGSKVTIKNQGLGGGLLHSHVQTYPEGS--NQQQVTCYGHKDSNNEWIFeRPRGLPSWDENDtdIEFIKDGDIVR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 395 LTHMATRRNLHSHNEPAPMTKKHLQVTGYGELGLGDANDVWRVLIV---GGKVNETVHTVTSRLKFIHLLQNCALTSSGK 471
Cdd:cd23284   79 LVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDNWVIEIVkqvGSEDPKKLHTLTTSFRLRHEVLGCYLAQTGV 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 442614658 472 QLPKWGFEQQEVSC--NPNVRDKNSQWNVEDNEH 503
Cdd:cd23284  159 SLPEWGFKQGEVVCdkSNFKRDKRTWWNIETHTN 192
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 321-501 1.09e-71

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: 231.84  E-value: 1.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKNHKTGGGYLHSHHHLYPKGSGarQQQVTTYTHKDENNKWLI-RPHNKPGPPKGKVQILRHGDLVRLTHMA 399
Cdd:cd23276    1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSK--QQQVTGYGHKDENNWWQIlKPRGDPSSNPPDPEYVRDGDEVRLLHKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 400 TRRNLHSHNEPAPMTKKHLQVTGYG-ELGLGDANDVWRVLIV---GGKVNETVHTVTSRLKFIHLLQNCALTSSGKQLPK 475
Cdd:cd23276   79 TNRYLRTHDAAAPVTSKHKEVSAYPdENEDGDDNDLWVVEIVkdeGKLEDKRIKPLTTRFRLRNKKTGCYLTSSGVKLPE 158

                        170       180
                 ....*....|....*....|....*..
gi 442614658 476 WGFEQQEVSCNPNVR-DKNSQWNVEDN 501
Cdd:cd23276  159 WGFRQGEVVCSKNKEsDPSTLWNVEEN 185
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 321-503 1.11e-67

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: 221.40  E-value: 1.11e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKNHKTGGGYLHSHHHLYPKGSGarQQQVTTYTHKDENNKWLIRPHNKPG-PPKGKVQILRHGDLVRLTHMA 399
Cdd:cd23283    1 VAYGSTIRIRHLNTRGGYLHSHPHNYPAGSK--QQQITLYPHRDENNDWLVELANAPEeWSPTTFENLKDGDVVRLEHVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 400 TRRNLHSHNEPAPMTKK--HLQVTGYG-ELGLGDANDVWRVLIVGGK-----VNETVHTVTSRLKFIHLLQNCALTSSGK 471
Cdd:cd23283   79 TGRRLHSHDHRPPVSDNdwQNEVSAYGyEGFEGDANDDWRVEILKDDsrpgeSKERVRAIDTKFRLVHVMTGCYLFSHGV 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 442614658 472 QLPKWGFEQQEVSCNPNVRDKNSQWNVEDNEH 503
Cdd:cd23283  159 KLPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 44-290 4.19e-64

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: 214.10  E-value: 4.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658   44 ATVFLVTFATRFYKVTEPDHICWDETHFGKMGSWYINRTFFFDVHPPLGKMLIGLSGYLTGYNGTFPFEKPGDKY--NET 121
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYypGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  122 RYQGMRYFCTTLGALIMPMGFDTVYDLTRSHEAALLAAAYLIFDVGLLTLNQYILLDPILLFFMMASVWGMVKVSKSTAs 201
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  202 ggsYGLRWWLWLFLTGTMLSCTISVKFVGLFVVLLVGLHTATELWLILGDLGQPILETVKQLACRAITLIVWPVLLYILF 281
Cdd:pfam02366 160 ---FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 442614658  282 FYIHLSVLN 290
Cdd:pfam02366 237 FYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 520-761 3.38e-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: 180.05  E-value: 3.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  520 ARFLESHAVMLQGNAGLKPkEGEVTSRPWQWPINYRGQFFSG---SSYRIYLLGNPLIWWSNLVFLALFVTVFLCNAVVQ 596
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTP-SHPYASRPWEWPLLLRGIRFWGwddRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  597 QRragfarsaaqnqaQVPDSetvaqdeesehsttdicscctpakeivpkavpsgsPEAPNPAQSLRAAAWLFLGWMLHYL 676
Cdd:pfam16192  80 QR-------------GYYDL-----------------------------------SDDWTRSRFYYSGGFLLLGWALHYL 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  677 PFWAMGRVLYFHHYFPALIFNSLLTGVMYNYILRV-------LPKWIHHVILGLVLSILVYSFAAFSPLAYGMSGplane 749
Cdd:pfam16192 112 PFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLfrrlprsLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPG----- 186

                         250
                  ....*....|..
gi 442614658  750 PNSTMYNLKWLS 761
Cdd:pfam16192 187 TSEECKKLKWLS 198
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 321-503 2.39e-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: 166.33  E-value: 2.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKNHKTGGGYLHSHHHLYPK------GSGArQQQVTTYTHKDENNKWLIRPHNKPG-PPKGKVQILRHGDLV 393
Cdd:cd23281    1 VAYGSQVTLRNTHGSPCWLHSHKHRYPIkypdgrGSSH-QQQVTCYPFKDVNNWWIIKDPGRQDlAVDDPPRPVRHGDII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 394 RLTHMATRRNLHSHNEPAPMTKKHLQVTGYGelglgDAN------DVWRVLIVGGKVN-ETVHTVTSRLKFIHLLQNCAL 466
Cdd:cd23281   80 QLVHGKTGRFLNSHDVAAPLSPTHQEVSCYI-----DYNismpaqNLWRIEIVNRDSEgDTWKAIKSQFRLIHVNTSAAL 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 442614658 467 TSSGKQLPKWGFEQQEVSCNPNVRDKNSQWNVEDNEH 503
Cdd:cd23281  155 KLSGKQLPDWGFGQLEVATDRAGNQSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 321-500 4.04e-44

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: 157.07  E-value: 4.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKnHKTGGGYLHSHHHLYPK-------GSGArqQQVTTYTHKDENNKWLIRPHNKPGPPKGKVQILRHGDLV 393
Cdd:cd23285    1 VHYGDVITIK-HRDTNAFLHSHPERYPLryedgriSSQG--QQVTGYPHKDANNQWQILPTDPIDEHEGTGRPVRNGDLI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 394 RLTHMATRRNLHSHNEPAPMTKKHLQVTG-YGELGLGDAND-VWRVLIVGGKVNETVHTVTSRLKFIHLLQNCALTSSGK 471
Cdd:cd23285   78 RLRHVSTDTYLLTHDVASPLTPTNMEFTTvSDDDTDERYNEtLFRVEIEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKK 157

                        170       180
                 ....*....|....*....|....*....
gi 442614658 472 QLPKWGFEQQEVSCNPNVRDKNSQWNVED 500
Cdd:cd23285  158 PLPDWGFGQQEVNGNKNIKDKSNIWVVDD 186
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 321-501 5.37e-37

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: 137.18  E-value: 5.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKNHKTGGGYLHSHHHLYPKGSGarQQQVTTYTHK-DENNKWLIRPHNKPGPPK--GKVQILRHGDLVRLTH 397
Cdd:cd23286    1 LLYGSTVTIRHLESLGGYLHSHDLTYPSGSN--EQQVTLYDFEdDANNEWIIETKTKEQMDKfpGQFREVRDGDVIRLRH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 398 MATRRNLHSHNEPAPMTKK--HLQVTGYGELGL-GDANDVWRVLIVGGKVNET-------VHTVTSRLKFIHLLQNCALT 467
Cdd:cd23286   79 VVTGKLLRASNARPPVSEQeyNNEVSCTGNANYsGDMDENWRIDVKGDESHAElklpnikIKSTESVFQLYNRGTGCTLL 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 442614658 468 SSGKQLPKWGFEQQEVSCNPNVRDKNSQWNVEDN 501
Cdd:cd23286  159 SHDTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 323-498 1.44e-28

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: 112.39  E-value: 1.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 323 YGSLVTIKnHKTGGGYLHSHHHLYpkGSGARQQQVTTYTH-KDENNKWLIRP-HNKPGPPKGKVqiLRHGDLVRLTHMAT 400
Cdd:cd23279    1 YGSAIKLK-HVNSGYRLHSHEVSY--GSGSGQQSVTAVPSaDDANSLWTVLPgLGEPCQEQGKP--VKCGDIIRLQHVNT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 401 RRNLHSHNEPAPMTKKHlQVTGYGeLGLGDANDVWRVlIVGGKVNETVHtVTSRLKFIHLLQNCALTSSGK----QLPKW 476
Cdd:cd23279   76 RKNLHSHNHSSPLSGNQ-EVSAFG-GGDEDSGDNWIV-ECEGKKAKFWK-RGEPVRLKHVDTGKYLSASKThkftQQPIA 151

                        170       180
                 ....*....|....*....|..
gi 442614658 477 GfeQQEVSCNpNVRDKNSQWNV 498
Cdd:cd23279  152 G--QLEVSAA-SSKDSDSQWKA 170
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 340-496 1.29e-25

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: 104.37  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  340 HSHHHLYPKGSGARQQQ----VTTYTHKDENNK----WLIRPHNKPgppKGKVQILRHGDLVRLTHMATRRNLHSHNEP- 410
Cdd:pfam02815  13 HSHQDEYLTGSEQQQKQpflrITLYPHGDANNSarslWRIEVVRHD---AWRGGLIKWGSPFRLRHLTTGRYLHSHEEQk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  411 APMTKK---HLQVTGYGELGLGDANDVwrVLIV-----GGKVNETVHTVTSRLKFIHLLQNCALTSSGKQLPKWGFE--Q 480
Cdd:pfam02815  90 PPLVEKedwQKEVSAYGFRGFPGDNDI--VEIFekkstTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpeQ 167

                         170
                  ....*....|....*.
gi 442614658  481 QEVSCNPNVRDKNSQW 496
Cdd:pfam02815 168 QKVTCAKEGHMDDALT 183
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 321-496 3.70e-25

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: 102.84  E-value: 3.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSlvTIK-NHKTGGGYLHSHHHLYPKGSGarQQQVTTYTHK-DENNKWLIRPHNKPGPPKGKVqiLRHGDLVRLTHM 398
Cdd:cd23294    1 VTCGS--VIKlQHERTKFRLHSHEVPYGSGSG--QQSVTGFPGVdDSNSYWIVKPANGERCKQGDV--IKNGDVIRLQHV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 399 ATRRNLHSHNEPAPMTKKhLQVTGYGELGLGDANDVWRVLIVGGKvNETVHTVTSRLKfiHLLQNCALTSSGKQLPKWGF 478
Cdd:cd23294   75 STRKWLHSHLHASPLSGN-QEVSCFGGDGNSDTGDNWIVEIEGGG-KVWERDQKVRLK--HVDTGGYLHSHDKKYGRPIP 150

                        170
                 ....*....|....*...
gi 442614658 479 EQQEVSCNPNvRDKNSQW 496
Cdd:cd23294  151 GQQEVCAVAS-KNSNTLW 167
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 321-498 1.31e-24

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: 101.19  E-value: 1.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 321 VAYGSLVTIKNHKTGGgYLHSHHHLYpkGSGARQQQVTTYTHKDENNK-WLIRPHNKPGPPKGKVqiLRHGDLVRLTHMA 399
Cdd:cd23293    1 VTCGSVVKLLNTRHNV-RLHSHDVKY--GSGSGQQSVTGVESSDDSNSyWQIRGPTGADCERGTP--IKCGQTIRLTHLN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 400 TRRNLHSHNEPAPMTkKHLQVTGYGELGLGDANDVWRVLIVGG--KVNETVhtvtsRLKfiHLLQNCALTSSGKQL--PK 475
Cdd:cd23293   76 TGKNLHSHHFQSPLS-GNQEVSAFGEDGEGDTGDNWTVVCSGTywERDEAV-----RLK--HVDTEVYLHVTGEQYgrPI 147

                        170       180
                 ....*....|....*....|...
gi 442614658 476 WGfeQQEVSCNPNVRDkNSQWNV 498
Cdd:cd23293  148 HG--QREVSGMSSPSQ-ANYWKA 167
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 324-501 8.89e-21

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: 90.13  E-value: 8.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 324 GSLVTIKNHKTGGgYLHSHHHLYPKGSGarQQQVTTYTHK---DENNKWLI-RPHNKPGppkgkvQILRHGDLVRLTHMA 399
Cdd:cd23263    1 GDVIWLKHSETGK-YLHSHRKNYPTGSG--QQEVTFESSSrkgDTNGLWIIeSENGKQG------GPVKWGDKIRLRHLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 400 TRRNLHSHNEPAPMTKKHLQVTGYGElgLGDANDVWRVLIVGGKvNETVHTVT--SRLKFIHLLQNCALTSSGKQLPKWG 477
Cdd:cd23263   72 TGKYLSSEEGKKSPKSNHQEVLCLTD--NPDKSSLFKFEPIGST-KYKQKYVKkdSYFRLKHVNTNFWLHSHEKKFNINN 148

                        170       180
                 ....*....|....*....|....
gi 442614658 478 FEQQEVSCNPNVRDKNSQWNVEDN 501
Cdd:cd23263  149 KTQQEVICHGEREEVFKLWKAELI 172
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 24-239 1.82e-19

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 92.26  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  24 APRTAPTSSKEANWNWWLLLAtVFLVTFATRFYKVTEPDHICWDETHFGKMGSWYINR---------TFFFDVHPPLGKM 94
Cdd:COG1928    7 PARLVPPMPGDRLRGWLGTLL-VTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPLGKW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  95 LIGLSGYLTGYNGTFpfekpgdkynetryqGMRYFCTTLGALIMPMGFDTVYDLTRSHEAALLAAAYLIFDVGLLTLNQY 174
Cdd:COG1928   86 LIALGEWLFGYVNPF---------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 175 ILLDPILLFFMMASVWGMV---------------KVSKSTASGGSYGLRWwlWLFLTGTMLSCTISVKFVGLFVVLLVGL 239
Cdd:COG1928  151 ALLDIFLMFFVLAAFGCLLldrdqvrrrlaaavaAGRAPSRWGPRLGFRW--WRLAAGVLLGLACGVKWSGLYFLAAFGL 228
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
318-374 1.67e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 59.66  E-value: 1.67e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 442614658   318 PRDVAYGSLVTIKnHKTGGGYLHSHHHLYPKgSGARQQQVTTYTHK--DENNKWLIRPH 374
Cdd:smart00472   1 GGFVRWGDVVRLR-HVTTGRYLHSHDEKLPP-WGDGQQEVTGYGNPaiDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
385-440 3.22e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 58.89  E-value: 3.22e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 442614658   385 QILRHGDLVRLTHMATRRNLHSHNEPAPMT-KKHLQVTGYGElGLGDANDVWRVLIV 440
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLPPWgDGQQEVTGYGN-PAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
446-501 1.06e-10

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 57.74  E-value: 1.06e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 442614658   446 ETVHTVTSRLKFIHLLQNCALTSSGKQLPKWGFEQQEVSCNPN-VRDKNSQWNVEDN 501
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNpAIDANTLWLIEPV 57
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
 88-282 3.22e-03

Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 40.75  E-value: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658  88 HPPLGKMLIGLSGYLTGyngtfpfekpgDKYNETRYQGMryfctTLGALIMPMGFDTVYDLTRSHEAALLAAAYLIFDVG 167
Cdd:COG4346   79 HPPLGKYIIALSMLLLG-----------DKPLYWRLPSI-----ILGALIVILVFLTARRLSGNIVAGLIASLLLALDPL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614658 168 LLTLNQYILLDPILLFFMMASVWGMVKvSKSTASGGSYGLRWwlwlfltgtmlsctiSVKFVGLFVVLlvglhtatELWL 247
Cdd:COG4346  143 LRVMSSIAMLDIYVAFFTALALYFAVS-GRLLLSSIALGLAA---------------ASKYSGLFLLI--------PLLL 198

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442614658 248 ILGDLGqpiletvKQLACRAITLIVWPVLLYILFF 282
Cdd:COG4346  199 YLREIE-------KSPIKRFLYGILIPLAVFLIVS 226
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 545-601 9.51e-03

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 39.10  E-value: 9.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442614658 545 SRPWQWPINYR--------GQFFSGS------SYRIYLLGNPLIWWsnlvfLALFVTVFLCNAVVQQR--RAG 601
Cdd:COG1928  329 SKPWSWPLMLRpvsyyyetGQTGTLGcgagkcVRAVLAIGNPALWW-----LGLPALLWLLWRWIARRdwRAG 396
 
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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