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Conserved domains on  [gi|6320109|ref|NP_010190|]
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putative dolichyl-phosphate-mannose-protein mannosyltransferase PMT5 [Saccharomyces cerevisiae S288C]

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_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 323-512 8.70e-121

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: 359.69  E-value: 8.70e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  323 VAVGSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLYPHIDQNNKWIIELAEHPNE-NVTSFQNLTDGTIIKLRQLKNG 401
Cdd:cd23283   1 VAYGSTIRIRHLNTRGGYLHSHPHNYPAGSKQQQITLYPHRDENNDWLVELANAPEEwSPTTFENLKDGDVVRLEHVATG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  402 CRLHSHDHKPPVSqNADWQKEVSCYGYEGFEGDINDDWIIEIDKKRSEPGPAQEHIRAIETKFRLKHYLTGCYLFSHPEK 481
Cdd:cd23283  81 RRLHSHDHRPPVS-DNDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGESKERVRAIDTKFRLVHVMTGCYLFSHGVK 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320109  482 LPEWGFGQQEVTCAYFAREDLTSWYIEENEN 512
Cdd:cd23283 160 LPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 51-293 6.51e-82

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


:

Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 260.71  E-value: 6.51e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109     51 CLLIFTAIVRLHNISLPNSVVFGENEVGTFVSQYVNNIFFTDVHPPLVAMLYATVSSVFGYKGLFNYGNIGTEY-TANVP 129
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYyPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    130 YVAMRFFSATLGIVSVLVLYLTLRVSGVKIAVAAICAVCFAIENSFVTLSRFTLIEGPFVFFMACAVYFFRRSELYLPNS 209
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPFS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    210 CKANKSLLAASIALGFAVSSKWAGLFTIAWAGIIVLWRVWFMIGDLSRPIGSSIKYMAFQFTCLLAIPAFIYFLIFSVHI 289
Cdd:pfam02366 162 RKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHF 241


                  ....
gi 6320109    290 KTLN 293
Cdd:pfam02366 242 WLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 531-720 6.17e-64

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: 211.25  E-value: 6.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    531 QKFVAIHKFMFYLNNYMDTSHAYSSEPKTWPLMLRGIDFW--NENGREVYFLGNAVLWWSVTAFICTFIIGVAVELLAWK 608
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWgwDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    609 LGVNILR-DKHIINFHYQVFQYLLGFAAHYFPYFFVGQKLFLYDYLPAYYFGILAFGHALDLISTY----ISNKRNNTGY 683
Cdd:pfam16192  81 RGYYDLSdDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLfrrlPRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 6320109    684 IVVAIFMVVCFYFFSEHSPLIYATGWSSNLCKRSKWL 720
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWL 197
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 323-512 8.70e-121

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: 359.69  E-value: 8.70e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  323 VAVGSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLYPHIDQNNKWIIELAEHPNE-NVTSFQNLTDGTIIKLRQLKNG 401
Cdd:cd23283   1 VAYGSTIRIRHLNTRGGYLHSHPHNYPAGSKQQQITLYPHRDENNDWLVELANAPEEwSPTTFENLKDGDVVRLEHVATG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  402 CRLHSHDHKPPVSqNADWQKEVSCYGYEGFEGDINDDWIIEIDKKRSEPGPAQEHIRAIETKFRLKHYLTGCYLFSHPEK 481
Cdd:cd23283  81 RRLHSHDHRPPVS-DNDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGESKERVRAIDTKFRLVHVMTGCYLFSHGVK 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320109  482 LPEWGFGQQEVTCAYFAREDLTSWYIEENEN 512
Cdd:cd23283 160 LPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 51-293 6.51e-82

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 260.71  E-value: 6.51e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109     51 CLLIFTAIVRLHNISLPNSVVFGENEVGTFVSQYVNNIFFTDVHPPLVAMLYATVSSVFGYKGLFNYGNIGTEY-TANVP 129
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYyPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    130 YVAMRFFSATLGIVSVLVLYLTLRVSGVKIAVAAICAVCFAIENSFVTLSRFTLIEGPFVFFMACAVYFFRRSELYLPNS 209
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPFS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    210 CKANKSLLAASIALGFAVSSKWAGLFTIAWAGIIVLWRVWFMIGDLSRPIGSSIKYMAFQFTCLLAIPAFIYFLIFSVHI 289
Cdd:pfam02366 162 RKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHF 241


                  ....
gi 6320109    290 KTLN 293
Cdd:pfam02366 242 WLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 531-720 6.17e-64

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: 211.25  E-value: 6.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    531 QKFVAIHKFMFYLNNYMDTSHAYSSEPKTWPLMLRGIDFW--NENGREVYFLGNAVLWWSVTAFICTFIIGVAVELLAWK 608
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWgwDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    609 LGVNILR-DKHIINFHYQVFQYLLGFAAHYFPYFFVGQKLFLYDYLPAYYFGILAFGHALDLISTY----ISNKRNNTGY 683
Cdd:pfam16192  81 RGYYDLSdDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLfrrlPRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 6320109    684 IVVAIFMVVCFYFFSEHSPLIYATGWSSNLCKRSKWL 720
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWL 197
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 342-505 4.23e-59

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: 197.97  E-value: 4.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    342 HSHLHNYPAGSMQQQ------VTLYPHIDQNNK----WIIELAEHPNenvTSFQNLTDGTIIKLRQLKNGCRLHSHDH-K 410
Cdd:pfam02815  13 HSHQDEYLTGSEQQQkqpflrITLYPHGDANNSarslWRIEVVRHDA---WRGGLIKWGSPFRLRHLTTGRYLHSHEEqK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    411 PPVSQNADWQKEVSCYGYEGFEGDiNDdwIIEIDKKRSEPGPAQEHIRAIETKFRLKHYLTGCYLFSHPEKLPEWGFG-- 488
Cdd:pfam02815  90 PPLVEKEDWQKEVSAYGFRGFPGD-ND--IVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpe 166

                         170
                  ....*....|....*..
gi 6320109    489 QQEVTCAYFAREDLTSW 505
Cdd:pfam02815 167 QQKVTCAKEGHMDDALT 183
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 52-291 1.74e-15

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 79.94  E-value: 1.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109   52 LLIFTAIVRLHNISLPNSVVFGE-------NEVGTF--VSQYVNNIFFTDVHPPLVAMLYATVSSVFGYKGLFNYgnigt 122
Cdd:COG1928  28 VTLLAGVLRFWGLGRPNTLVFDEtyyvkdaWSLLTNgyERNWPDPGPFFVVHPPLGKWLIALGEWLFGYVNPFGW----- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  123 eytanvpyvamRFFSATLGIVSVLVLY-LTLRVSGvKIAVAAICAVCFAIENSFVTLSRFTLIEGPFVFFMACAVYFF-- 199
Cdd:COG1928 103 -----------RFAAALAGTLSVLLVArIARRLTR-STLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLll 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  200 ----RRSELYLPNSCKANKS-----------LLAASIALGFAVSSKWAGLFTIAWAGII-VLWRVWFM-IGDLSRPIGSS 262
Cdd:COG1928 171 drdqVRRRLAAAVAAGRAPSrwgprlgfrwwRLAAGVLLGLACGVKWSGLYFLAAFGLLtVAWDAGARrAAGVRRPWLGA 250

                       250       260       270
                ....*....|....*....|....*....|
gi 6320109  263 IKYMAFQ-FTCLLAIPAFIYFLIFSVHIKT 291
Cdd:COG1928 251 LLRDGIPaFFALVIVPLLTYLASWTGWFAS 280
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
455-510 3.49e-15

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 70.06  E-value: 3.49e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320109     455 EHIRAIETKFRLKHYLTGCYLFSHPEKLPEWGFGQQEVTCAYFARED-LTSWYIEEN 510
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDaNTLWLIEPV 57
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 528-723 1.56e-12

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 70.69  E-value: 1.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  528 SFWQkfvaIHKFMFYLNNYMDTSHAYSSEPKTWPLMLRGIDFWNENG-------------REVYFLGNAVLWWSVTAFIC 594
Cdd:COG1928 306 SLWH----YHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGqtgtlgcgagkcvRAVLAIGNPALWWLGLPALL 381

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  595 tFIIGVAVELLAWKLGVnilrdkhiinfhyqvfqYLLGFAAHYFPYFFVGQK-LFLYDYLPAYYFGILAFGHALDLI-ST 672
Cdd:COG1928 382 -WLLWRWIARRDWRAGA-----------------VLVGYAAGWLPWFLYLDRtMFFFYAIPFVPFLVLALALVLGLIlGP 443

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6320109  673 YISNKRNNTGYIVVAIFM---VVCFYFFsehSPLIYAT-----GWSSNLckrskWLGSW 723
Cdd:COG1928 444 ARASERRRLGRLVVGLYVglvVANFAFF---YPILTGLpipydEWQARM-----WFPSW 494
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 323-512 8.70e-121

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: 359.69  E-value: 8.70e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  323 VAVGSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLYPHIDQNNKWIIELAEHPNE-NVTSFQNLTDGTIIKLRQLKNG 401
Cdd:cd23283   1 VAYGSTIRIRHLNTRGGYLHSHPHNYPAGSKQQQITLYPHRDENNDWLVELANAPEEwSPTTFENLKDGDVVRLEHVATG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  402 CRLHSHDHKPPVSqNADWQKEVSCYGYEGFEGDINDDWIIEIDKKRSEPGPAQEHIRAIETKFRLKHYLTGCYLFSHPEK 481
Cdd:cd23283  81 RRLHSHDHRPPVS-DNDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGESKERVRAIDTKFRLVHVMTGCYLFSHGVK 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320109  482 LPEWGFGQQEVTCAYFAREDLTSWYIEENEN 512
Cdd:cd23283 160 LPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 51-293 6.51e-82

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 260.71  E-value: 6.51e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109     51 CLLIFTAIVRLHNISLPNSVVFGENEVGTFVSQYVNNIFFTDVHPPLVAMLYATVSSVFGYKGLFNYGNIGTEY-TANVP 129
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYyPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    130 YVAMRFFSATLGIVSVLVLYLTLRVSGVKIAVAAICAVCFAIENSFVTLSRFTLIEGPFVFFMACAVYFFRRSELYLPNS 209
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPFS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    210 CKANKSLLAASIALGFAVSSKWAGLFTIAWAGIIVLWRVWFMIGDLSRPIGSSIKYMAFQFTCLLAIPAFIYFLIFSVHI 289
Cdd:pfam02366 162 RKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHF 241


                  ....
gi 6320109    290 KTLN 293
Cdd:pfam02366 242 WLLF 245
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 323-510 1.10e-66

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: 218.36  E-value: 1.10e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  323 VAVGSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLYPHIDQNNKWIIELAE-HPNENVTSFQNLTDGTIIKLRQLKNG 401
Cdd:cd23276   1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSKQQQVTGYGHKDENNWWQILKPRgDPSSNPPDPEYVRDGDEVRLLHKETN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  402 CRLHSHDHKPPVSqnaDWQKEVSCYGYEGFEGDINDDWIIEIDKKRSEPGPaqEHIRAIETKFRLKHYLTGCYLFSHPEK 481
Cdd:cd23276  81 RYLRTHDAAAPVT---SKHKEVSAYPDENEDGDDNDLWVVEIVKDEGKLED--KRIKPLTTRFRLRNKKTGCYLTSSGVK 155

                       170       180       190
                ....*....|....*....|....*....|
gi 6320109  482 LPEWGFGQQEVTC-AYFAREDLTSWYIEEN 510
Cdd:cd23276 156 LPEWGFRQGEVVCsKNKESDPSTLWNVEEN 185
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 531-720 6.17e-64

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: 211.25  E-value: 6.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    531 QKFVAIHKFMFYLNNYMDTSHAYSSEPKTWPLMLRGIDFW--NENGREVYFLGNAVLWWSVTAFICTFIIGVAVELLAWK 608
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWgwDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    609 LGVNILR-DKHIINFHYQVFQYLLGFAAHYFPYFFVGQKLFLYDYLPAYYFGILAFGHALDLISTY----ISNKRNNTGY 683
Cdd:pfam16192  81 RGYYDLSdDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLfrrlPRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 6320109    684 IVVAIFMVVCFYFFSEHSPLIYATGWSSNLCKRSKWL 720
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWL 197
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 322-512 1.01e-61

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: 205.25  E-value: 1.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  322 EVAVGSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLYPHIDQNNKWIIEL---AEHPNENVTSFQNLTDGTIIKLRQL 398
Cdd:cd23284   3 DVAYGSKVTIKNQGLGGGLLHSHVQTYPEGSNQQQVTCYGHKDSNNEWIFERprgLPSWDENDTDIEFIKDGDIVRLVHK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  399 KNGCRLHSHDHKPPVSQNadwQKEVSCYGYEGFeGDINDDWIIEIDKKRSEPGPaqEHIRAIETKFRLKHYLTGCYLFSH 478
Cdd:cd23284  83 QTGRNLHSHPVPAPISKS---DYEVSGYGDLTV-GDEKDNWVIEIVKQVGSEDP--KKLHTLTTSFRLRHEVLGCYLAQT 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6320109  479 PEKLPEWGFGQQEVTCAY--FAREDLTSWYIEENEN 512
Cdd:cd23284 157 GVSLPEWGFKQGEVVCDKsnFKRDKRTWWNIETHTN 192
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 342-505 4.23e-59

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: 197.97  E-value: 4.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    342 HSHLHNYPAGSMQQQ------VTLYPHIDQNNK----WIIELAEHPNenvTSFQNLTDGTIIKLRQLKNGCRLHSHDH-K 410
Cdd:pfam02815  13 HSHQDEYLTGSEQQQkqpflrITLYPHGDANNSarslWRIEVVRHDA---WRGGLIKWGSPFRLRHLTTGRYLHSHEEqK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    411 PPVSQNADWQKEVSCYGYEGFEGDiNDdwIIEIDKKRSEPGPAQEHIRAIETKFRLKHYLTGCYLFSHPEKLPEWGFG-- 488
Cdd:pfam02815  90 PPLVEKEDWQKEVSAYGFRGFPGD-ND--IVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpe 166

                         170
                  ....*....|....*..
gi 6320109    489 QQEVTCAYFAREDLTSW 505
Cdd:pfam02815 167 QQKVTCAKEGHMDDALT 183
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 323-512 5.27e-58

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: 194.83  E-value: 5.27e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  323 VAVGSAVSL-NHVgTAGGYLHSHLHNYPAG--SMQQQVTLYPHIDQNNKWIIELAEHPNENVTSFQNLTDGTIIKLRQLK 399
Cdd:cd23282   1 VAYGSVITLkNHR-TGGGYLHSHWHLYPEGvgARQQQVTTYSHKDDNNLWLIKKHNQSSDLSDPVEYVRHGDLIRLEHVN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  400 NGCRLHSHDHKPPVSQNadwQKEVSCYGYEGfEGDINDDWIIEIdkkrsEPGPAQEHIRAIETKFRLKHYLTGCYLFSHP 479
Cdd:cd23282  80 TKRNLHSHKEKAPLTKK---HYQVTGYGENG-TGDANDVWRVEV-----VGGREGDPVKTVRSKFRLVHYNTGCALHSHG 150

                       170       180       190
                ....*....|....*....|....*....|...
gi 6320109  480 EKLPEWGFGQQEVTCAYFAREDLTSWYIEENEN 512
Cdd:cd23282 151 KQLPKWGWEQLEVTCNPNVRDKNSLWNVEDNRN 183
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 326-510 5.60e-50

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: 173.39  E-value: 5.60e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  326 GSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLYPHI-DQNNKWIIE--LAEHPNENVTSFQNLTDGTIIKLRQLKNGC 402
Cdd:cd23286   4 GSTVTIRHLESLGGYLHSHDLTYPSGSNEQQVTLYDFEdDANNEWIIEtkTKEQMDKFPGQFREVRDGDVIRLRHVVTGK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  403 RLHSHDHKPPVSQNaDWQKEVSCYGYEGFEGDINDDWIIEIDKKRS--EPGPAQEHIRAIETKFRLKHYLTGCYLFSHPE 480
Cdd:cd23286  84 LLRASNARPPVSEQ-EYNNEVSCTGNANYSGDMDENWRIDVKGDEShaELKLPNIKIKSTESVFQLYNRGTGCTLLSHDT 162

                       170       180       190
                ....*....|....*....|....*....|
gi 6320109  481 KLPEWGFGQQEVTCAYFAREDLTSWYIEEN 510
Cdd:cd23286 163 RLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 326-510 4.45e-33

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: 125.19  E-value: 4.45e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  326 GSAVSLNHVGTaGGYLHSHLHNYPAGSMQQQVTLYPHI---DQNNKWIIElaehpNENVTSFQNLTDGTIIKLRQLKNGC 402
Cdd:cd23263   1 GDVIWLKHSET-GKYLHSHRKNYPTGSGQQEVTFESSSrkgDTNGLWIIE-----SENGKQGGPVKWGDKIRLRHLSTGK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  403 RLHSHDHKPpvsQNADWQKEVSCYGYEGfegDINDDWIIEIDKKRsepGPAQEHIRaIETKFRLKHYLTGCYLFSHPEKL 482
Cdd:cd23263  75 YLSSEEGKK---SPKSNHQEVLCLTDNP---DKSSLFKFEPIGST---KYKQKYVK-KDSYFRLKHVNTNFWLHSHEKKF 144

                       170       180
                ....*....|....*....|....*...
gi 6320109  483 PEWGFGQQEVTCAYFAREDLTSWYIEEN 510
Cdd:cd23263 145 NINNKTQQEVICHGEREEVFKLWKAELI 172
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 323-510 3.67e-31

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: 120.49  E-value: 3.67e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  323 VAVGSAVSLNHVGTAGGYLHSHLHNYP-------AGSMQQQVTLYPHIDQNNKWIIELAEHPNENVTS-FQNLTDGTIIK 394
Cdd:cd23281   1 VAYGSQVTLRNTHGSPCWLHSHKHRYPikypdgrGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDpPRPVRHGDIIQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  395 LRQLKNGCRLHSHDHKPPVSQNadwQKEVSCYgyegFEGDIN----DDWIIEIDKKRSEPGPAQehirAIETKFRLKHYL 470
Cdd:cd23281  81 LVHGKTGRFLNSHDVAAPLSPT---HQEVSCY----IDYNISmpaqNLWRIEIVNRDSEGDTWK----AIKSQFRLIHVN 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6320109  471 TGCYLFSHPEKLPEWGFGQQEVTCAYFAREDLTSWYIEEN 510
Cdd:cd23281 150 TSAALKLSGKQLPDWGFGQLEVATDRAGNQSSTVWNVEEH 189
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 323-509 7.08e-31

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: 119.02  E-value: 7.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  323 VAVGSAVSLNHVGTaGGYLHSHLHNYPAGSMQQQVTLYPHI-DQNNKWIIELAehPNENVTSFQNLTDGTIIKLRQLKNG 401
Cdd:cd23294   1 VTCGSVIKLQHERT-KFRLHSHEVPYGSGSGQQSVTGFPGVdDSNSYWIVKPA--NGERCKQGDVIKNGDVIRLQHVSTR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  402 CRLHSHDHKPPVSQNadwqKEVSCYGYEGfEGDINDDWIIEIDkkrsepGPAQEHIRaiETKFRLKHYLTGCYLFSHPEK 481
Cdd:cd23294  78 KWLHSHLHASPLSGN----QEVSCFGGDG-NSDTGDNWIVEIE------GGGKVWER--DQKVRLKHVDTGGYLHSHDKK 144

                       170       180
                ....*....|....*....|....*...
gi 6320109  482 LPEWGFGQQEVTCAYFAREDlTSWYIEE 509
Cdd:cd23294 145 YGRPIPGQQEVCAVASKNSN-TLWLAAE 171
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 326-509 5.37e-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: 111.23  E-value: 5.37e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  326 GSAVSLNHVGTaGGYLHSHLHNYP-------AGSMQQQVTLYPHIDQNNKWIIELAEHPNENVTSFQNLTDGTIIKLRQL 398
Cdd:cd23285   4 GDVITIKHRDT-NAFLHSHPERYPlryedgrISSQGQQVTGYPHKDANNQWQILPTDPIDEHEGTGRPVRNGDLIRLRHV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  399 KNGCRLHSHD-HKPPVSQNadwqKEVSCYGYEGFEGDINDD-WIIEIDKKRSEPgpaqeHIRAIETKFRLKHYLTGCYLF 476
Cdd:cd23285  83 STDTYLLTHDvASPLTPTN----MEFTTVSDDDTDERYNETlFRVEIEDTDEGD-----VLKTKSSHFRLIHVDTNVALW 153

                       170       180       190
                ....*....|....*....|....*....|...
gi 6320109  477 SHPEKLPEWGFGQQEVTCAYFAREDLTSWYIEE 509
Cdd:cd23285 154 THKKPLPDWGFGQQEVNGNKNIKDKSNIWVVDD 186
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 326-509 9.82e-24

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: 98.52  E-value: 9.82e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  326 GSAVSLNHVGTaGGYLHSHLHNYPAGSMQQQVTLYPHI-DQNNKWIIElaEHPNEnvtSFQNLTD----GTIIKLRQLKN 400
Cdd:cd23279   2 GSAIKLKHVNS-GYRLHSHEVSYGSGSGQQSVTAVPSAdDANSLWTVL--PGLGE---PCQEQGKpvkcGDIIRLQHVNT 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  401 GCRLHSHDHKPPVSQNadwqKEVSCYGYEGfeGDINDDWIIEIDKKRSepgpaqEHIRaIETKFRLKHYLTGCYLFSHPE 480
Cdd:cd23279  76 RKNLHSHNHSSPLSGN----QEVSAFGGGD--EDSGDNWIVECEGKKA------KFWK-RGEPVRLKHVDTGKYLSASKT 142

                       170       180       190
                ....*....|....*....|....*....|...
gi 6320109  481 KL----PEwgFGQQEVTCAYFAREDlTSWYIEE 509
Cdd:cd23279 143 HKftqqPI--AGQLEVSAASSKDSD-SQWKAVE 172
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 323-509 2.48e-19

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: 86.17  E-value: 2.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  323 VAVGSAVSLNHVGTaGGYLHSHLHNYPAGSMQQQVTLYPHI-DQNNKWIIElaEHPNENVTSFQNLTDGTIIKLRQLKNG 401
Cdd:cd23293   1 VTCGSVVKLLNTRH-NVRLHSHDVKYGSGSGQQSVTGVESSdDSNSYWQIR--GPTGADCERGTPIKCGQTIRLTHLNTG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  402 CRLHSHDHKPPVSQNadwqKEVSCYGYEGfEGDINDDWIIEIDKK---RSEPgpaqehiraietkFRLKHYLTGCYL--- 475
Cdd:cd23293  78 KNLHSHHFQSPLSGN----QEVSAFGEDG-EGDTGDNWTVVCSGTyweRDEA-------------VRLKHVDTEVYLhvt 139

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 6320109  476 ---FSHPEKlpewgfGQQEVtCAYFAREDLTSWYIEE 509
Cdd:cd23293 140 geqYGRPIH------GQREV-SGMSSPSQANYWKAME 169
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 52-291 1.74e-15

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 79.94  E-value: 1.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109   52 LLIFTAIVRLHNISLPNSVVFGE-------NEVGTF--VSQYVNNIFFTDVHPPLVAMLYATVSSVFGYKGLFNYgnigt 122
Cdd:COG1928  28 VTLLAGVLRFWGLGRPNTLVFDEtyyvkdaWSLLTNgyERNWPDPGPFFVVHPPLGKWLIALGEWLFGYVNPFGW----- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  123 eytanvpyvamRFFSATLGIVSVLVLY-LTLRVSGvKIAVAAICAVCFAIENSFVTLSRFTLIEGPFVFFMACAVYFF-- 199
Cdd:COG1928 103 -----------RFAAALAGTLSVLLVArIARRLTR-STLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLll 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  200 ----RRSELYLPNSCKANKS-----------LLAASIALGFAVSSKWAGLFTIAWAGII-VLWRVWFM-IGDLSRPIGSS 262
Cdd:COG1928 171 drdqVRRRLAAAVAAGRAPSrwgprlgfrwwRLAAGVLLGLACGVKWSGLYFLAAFGLLtVAWDAGARrAAGVRRPWLGA 250

                       250       260       270
                ....*....|....*....|....*....|
gi 6320109  263 IKYMAFQ-FTCLLAIPAFIYFLIFSVHIKT 291
Cdd:COG1928 251 LLRDGIPaFFALVIVPLLTYLASWTGWFAS 280
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
455-510 3.49e-15

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 70.06  E-value: 3.49e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320109     455 EHIRAIETKFRLKHYLTGCYLFSHPEKLPEWGFGQQEVTCAYFARED-LTSWYIEEN 510
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDaNTLWLIEPV 57
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 528-723 1.56e-12

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 70.69  E-value: 1.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  528 SFWQkfvaIHKFMFYLNNYMDTSHAYSSEPKTWPLMLRGIDFWNENG-------------REVYFLGNAVLWWSVTAFIC 594
Cdd:COG1928 306 SLWH----YHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGqtgtlgcgagkcvRAVLAIGNPALWWLGLPALL 381

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  595 tFIIGVAVELLAWKLGVnilrdkhiinfhyqvfqYLLGFAAHYFPYFFVGQK-LFLYDYLPAYYFGILAFGHALDLI-ST 672
Cdd:COG1928 382 -WLLWRWIARRDWRAGA-----------------VLVGYAAGWLPWFLYLDRtMFFFYAIPFVPFLVLALALVLGLIlGP 443

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6320109  673 YISNKRNNTGYIVVAIFM---VVCFYFFsehSPLIYAT-----GWSSNLckrskWLGSW 723
Cdd:COG1928 444 ARASERRRLGRLVVGLYVglvVANFAFF---YPILTGLpipydEWQARM-----WFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
387-443 6.14e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 58.12  E-value: 6.14e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320109     387 LTDGTIIKLRQLKNGCRLHSHDHKPPVSQnaDWQKEVSCYGYegFEGDINDDWIIEI 443
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLPPWG--DGQQEVTGYGN--PAIDANTLWLIEP 56
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
323-374 9.26e-11

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: 9.26e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6320109     323 VAVGSAVSLNHVGTaGGYLHSHLHNYPA-GSMQQQVTLYPH--IDQNNKWIIELA 374
Cdd:smart00472   4 VRWGDVVRLRHVTT-GRYLHSHDEKLPPwGDGQQEVTGYGNpaIDANTLWLIEPV 57
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 47-246 1.10e-10

PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 63.49  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109   47 LLVGCLLIFTAIVRLHNISLPNSVVFGE-----NEVGTFVSQYVNNIFFTDvHPPLVAMLYATVSSVFGykglfnygnig 121
Cdd:COG1807  13 LLLLALLLRLLGLGSLPLWDPDEARYAEiaremLESGDWLTPTLAGEPYFD-KPPLIYWLIALSYKLFG----------- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  122 teytanVPYVAMRFFSATLGIVSVLVLYLTLR-VSGVKIAV--AAICAVCFAiensFVTLSRFTLIEGPFVFFMACAVYF 198
Cdd:COG1807  81 ------VSEFAARLPSALLGLLTVLLVYLLARrLFGRRAALlaALLLLTSPL----LLLFGRLATPDALLLLFWTLALYA 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6320109  199 FRRSELYlpnscKANKSLLAASIALGFAVSSKWAGLFTIAWAGIIVLW 246
Cdd:COG1807 151 LLRALER-----RRLRWLLLAGLALGLGFLTKGPVALLLPGLALLLYL 193
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 93-289 2.87e-09

Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are not captured by pfam02366.


Pssm-ID: 433048 [Multi-domain]  Cd Length: 160  Bit Score: 56.50  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109     93 VHPPLVAMLYATVSSVFGYKGLfnygnigteytanvpyvAMRFFSATLGIVSVLVLYLTLRVSGVKIAvAAICAVCFAIE 172
Cdd:pfam13231   1 DHPPLAAWLIALFTALFGDSEW-----------------AVRLPSALAGVLTILLLYLLARRLFGKRA-ALLAALLLAVV 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109    173 NSFVTLSRFTLIEGPFVFFMACAVYFFRRselylpnSCKAN--KSLLAASIALGFAVSSK-WAGLFTIAwAGIIVLWRVW 249
Cdd:pfam13231  63 PLFVALSRLFTPDAPLLLFWALALYFLLR-------ALEKGrlKWWLLAGAAAGLGFLSKyTAALLVLA-ALLYLLISPG 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 6320109    250 fmigdlSRPIGSSIKYMAfqftcllaipAFIYFLIFSVHI 289
Cdd:pfam13231 135 ------RRRLKSPKPYLG----------LLLALLLFSPVL 158
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
 95-302 8.76e-06

Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 49.41  E-value: 8.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109   95 PPLVAMLYATVSSVFGykglfnygniGTEYTANVPYVAMRFFSATLGIVSVLVLYLTLR-VSGVKIAVAAicAVCFAIen 173
Cdd:COG1287  87 GPLFDQLIALLALILG----------LGSPSQSSVYTVAAWFPPIFGALTVIPVYLLGRrLGGRKAGLLA--ALLLAL-- 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  174 SFVTLSRFTLI----EGPFVFFMACAVYFF----RRSELYLPNSCKANKSLL---AASIALGFAVSSkWAGLFTIawAGI 242
Cdd:COG1287 153 SPGQLSRSLLGfadhHVAELFFSTLAVLFLvlalKRAKREKRDLEALKRPLLyavLAGVALGLYLLT-WGGYVLF--VGI 229

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  243 IVLWRVWFMIGDLSRpiGSSIKYMAFQFTCLLAIpAFIYFLIFSvhiktlNVNGISSSFF 302
Cdd:COG1287 230 LALFALLQLLLDLLR--GRSPEYLAIVGAVSFAV-AALLVLPFI------PRLGFSGTGL 280
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
 94-285 1.85e-05

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


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 47.68  E-value: 1.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109   94 HPPLVAMLYATVSSVFGYKglfnygnigteytanvpYVAMRFFSATLGIVSVLVLYLTLRVSGVKIAVAAICAVCFAIEN 173
Cdd:COG4346  79 HPPLGKYIIALSMLLLGDK-----------------PLYWRLPSIILGALIVILVFLTARRLSGNIVAGLIASLLLALDP 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  174 SFVTLSRFTLIEGPFVFFMACAVYFFrrselylpnsckANKSLLAASIALGFAVSSKWAGLFtiawaGIIVLWRVwfmig 253
Cdd:COG4346 142 LLRVMSSIAMLDIYVAFFTALALYFA------------VSGRLLLSSIALGLAAASKYSGLF-----LLIPLLLY----- 199

                       170       180       190
                ....*....|....*....|....*....|..
gi 6320109  254 dlsrpIGSSIKYMAFQFTCLLAIPAFIYFLIF 285
Cdd:COG4346 200 -----LREIEKSPIKRFLYGILIPLAVFLIVS 226
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 133-247 3.99e-04

Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General function prediction only];


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 43.89  E-value: 3.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320109  133 MRFFSATLGIVSVLVLYLtLRVSGVKIAVAAIcAVCFAIENSFVTLSRFTLIEGPFVFFM----ACAVYFF-RRSELYLP 207
Cdd:COG4745  88 ARLPVALVGGLLPLLALL-LRERLGDAEVLAL-ALLLAFSPVLVYYSRFMRNDVLLAAFTllalGAAVRAIdTRRRRYLY 165

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6320109  208 nsckanksllAASIALGFAVSSK-WAGLFTIAW--AGIIVLWR 247
Cdd:COG4745 166 ----------LAAVALALAFATKeNAVLYLLCWlgALLLLLDH 198
 
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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