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Conserved domains on  [gi|459371475|gb|EMG49268|]
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hypothetical protein G210_0030 [Candida maltosa Xu316]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 312-501 2.72e-94

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: 290.88  E-value: 2.72e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNE-LEKYLHSHDKSYPRGSNLQQVTLYEF-PDENNEWIIETKHKYYEHKLMDSKTPIKDGDIIRLYHKS 389
Cdd:cd23286    1 LLYGSTVTIRHLEsLGGYLHSHDLTYPSGSNEQQVTLYDFeDDANNEWIIETKTKEQMDKFPGQFREVRDGDVIRLRHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 390 TGHYLHANDIRPPISEHEYSYEINCNETRGLLGNVDYEFKVRTISKKSHSENDLPLIKLRTTETVFQLLSRGSSCSLMSH 469
Cdd:cd23286   81 TGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKLPNIKIKSTESVFQLYNRGTGCTLLSH 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 459371475 470 EQKLPEWGAFQNEVLCVQEPTIPNTLWYIESN 501
Cdd:cd23286  161 DTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 524-719 1.98e-54

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


:

Pssm-ID: 465056  Cd Length: 198  Bit Score: 185.44  E-value: 1.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  524 KLFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFFNNysskliDEDSSVIYYLGNIAIYYSVNLVVLISWVKYLFF 603
Cdd:pfam16192   2 KFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  604 AFINLNPYkQPSESSPAKSTFYENAWQFLLGWSLNYLPYFLVSRNLYLHHYLPALSFGILLLGQYLNY--------RVAK 675
Cdd:pfam16192  76 LLRWQRGY-YDLSDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFllslfrrlPRSL 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 459371475  676 NSFIGYSLVILVLVGSVYCYYELIPIIYGLPWTAAKCTAHKWIS 719
Cdd:pfam16192 155 RKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 43-284 7.80e-46

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: 163.64  E-value: 7.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475   43 LAIVIRLYKLYIPDRIVFDEIHIVKYIKHYYTGETFVDVHPPLGRLIYYYLTRLF-VPIDssvlqeFDADKIG-QLYPED 120
Cdd:pfam02366   6 LAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAgYDGN------FTFISIGgQYYPGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  121 FPYLWLRLFSGLCGIGHVLVTFFTSR-LTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLFAQSLVILNYKSFTQCQQ 199
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKrLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  200 FTKSWWFHLFATGVSLGLNISIKISGAFNYLWVGILTTVQLWEILGDLEISVTQWIKHIVSRVVALIIVPLTIYCSVFYI 279
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYV 239


                  ....*
gi 459371475  280 HFELL 284
Cdd:pfam02366 240 HFWLL 244
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 312-501 2.72e-94

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: 290.88  E-value: 2.72e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNE-LEKYLHSHDKSYPRGSNLQQVTLYEF-PDENNEWIIETKHKYYEHKLMDSKTPIKDGDIIRLYHKS 389
Cdd:cd23286    1 LLYGSTVTIRHLEsLGGYLHSHDLTYPSGSNEQQVTLYDFeDDANNEWIIETKTKEQMDKFPGQFREVRDGDVIRLRHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 390 TGHYLHANDIRPPISEHEYSYEINCNETRGLLGNVDYEFKVRTISKKSHSENDLPLIKLRTTETVFQLLSRGSSCSLMSH 469
Cdd:cd23286   81 TGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKLPNIKIKSTESVFQLYNRGTGCTLLSH 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 459371475 470 EQKLPEWGAFQNEVLCVQEPTIPNTLWYIESN 501
Cdd:cd23286  161 DTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 524-719 1.98e-54

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


Pssm-ID: 465056  Cd Length: 198  Bit Score: 185.44  E-value: 1.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  524 KLFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFFNNysskliDEDSSVIYYLGNIAIYYSVNLVVLISWVKYLFF 603
Cdd:pfam16192   2 KFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  604 AFINLNPYkQPSESSPAKSTFYENAWQFLLGWSLNYLPYFLVSRNLYLHHYLPALSFGILLLGQYLNY--------RVAK 675
Cdd:pfam16192  76 LLRWQRGY-YDLSDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFllslfrrlPRSL 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 459371475  676 NSFIGYSLVILVLVGSVYCYYELIPIIYGLPWTAAKCTAHKWIS 719
Cdd:pfam16192 155 RKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 43-284 7.80e-46

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: 163.64  E-value: 7.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475   43 LAIVIRLYKLYIPDRIVFDEIHIVKYIKHYYTGETFVDVHPPLGRLIYYYLTRLF-VPIDssvlqeFDADKIG-QLYPED 120
Cdd:pfam02366   6 LAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAgYDGN------FTFISIGgQYYPGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  121 FPYLWLRLFSGLCGIGHVLVTFFTSR-LTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLFAQSLVILNYKSFTQCQQ 199
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKrLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  200 FTKSWWFHLFATGVSLGLNISIKISGAFNYLWVGILTTVQLWEILGDLEISVTQWIKHIVSRVVALIIVPLTIYCSVFYI 279
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYV 239


                  ....*
gi 459371475  280 HFELL 284
Cdd:pfam02366 240 HFWLL 244
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 315-496 1.52e-17

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: 81.26  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  315 GSTVTIKHNELEKYLHShdKSYPRGSNLQQVTLYEFPDENNE----WIIETKHkyyehklMDSKT--PIKDGDIIRLYHK 388
Cdd:pfam02815   6 GDVVRLFHSHQDEYLTG--SEQQQKQPFLRITLYPHGDANNSarslWRIEVVR-------HDAWRggLIKWGSPFRLRHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  389 STGHYLHANDI-RPPISEHE-YSYEINCNETRGLLGNVDYE--FKVRTISKKSHSEndlplikLRTTETVFQLLSRGSSC 464
Cdd:pfam02815  77 TTGRYLHSHEEqKPPLVEKEdWQKEVSAYGFRGFPGDNDIVeiFEKKSTTGMGSDR-------IKPGDSYFRLQHVCTGC 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 459371475  465 SLMSHEQKLPEWGA--FQNEVLCVQEPTIPNTLW 496
Cdd:pfam02815 150 WLFSHSVKLPKWGFgpEQQKVTCAKEGHMDDALT 183
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
312-361 6.79e-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: 6.79e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 459371475   312 VLYGSTVTIKHNELEKYLHSHDKSYPR-GSNLQQVTLYEFP--DENNEWIIET 361
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLPPwGDGQQEVTGYGNPaiDANTLWLIEP 56
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 525-721 6.86e-11

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 65.30  E-value: 6.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 525 LFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFF--NNYSSKLIDEDSSVIYY---LGNIAIYYS---VNLVVLIS 596
Cdd:COG1928  307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYyeTGQTGTLGCGAGKCVRAvlaIGNPALWWLglpALLWLLWR 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 597 WVKYLFFAfinlnpykqpsesspakstfyenAWQFLLGWSLNYLPYFLV-SRNLYLHHYLPALSFGIL----LLGQYL-- 669
Cdd:COG1928  387 WIARRDWR-----------------------AGAVLVGYAAGWLPWFLYlDRTMFFFYAIPFVPFLVLalalVLGLILgp 443

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 459371475 670 ---NYRVAKNSFIGYSLVILVLVGSVYCYyeliPIIYGLPWTAAKCTAHKWISNW 721
Cdd:COG1928  444 araSERRRLGRLVVGLYVGLVVANFAFFY----PILTGLPIPYDEWQARMWFPSW 494
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 37-305 1.28e-10

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 64.53  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  37 TFVILTLAIVIRLYKLYIPDRIVFDEIHIVK----YIKHYY------TGETFVdVHPPLGRLIyyyltrlfvpidssvlq 106
Cdd:COG1928   25 TLLVTLLAGVLRFWGLGRPNTLVFDETYYVKdawsLLTNGYernwpdPGPFFV-VHPPLGKWL----------------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 107 efdadkIG---QLYPEDFPYLWlRLFSGLCGIGHVLVTFF-TSRLTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLF 182
Cdd:COG1928   87 ------IAlgeWLFGYVNPFGW-RFAAALAGTLSVLLVARiARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 183 ----AQSLVIL-----------NYKSFTQCQQFTKSWWFH--LFATGVSLGLNISIKISGAFNYLWVGILTTvqLWEILG 245
Cdd:COG1928  160 fvlaAFGCLLLdrdqvrrrlaaAVAAGRAPSRWGPRLGFRwwRLAAGVLLGLACGVKWSGLYFLAAFGLLTV--AWDAGA 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 459371475 246 DLEISVTQWIKHIVSR-----VVALIIVPLTIYCSVF---------YIHFELLPKEGPGSGFLSPHFRStLVDY 305
Cdd:COG1928  238 RRAAGVRRPWLGALLRdgipaFFALVIVPLLTYLASWtgwfasdtgYDRHWAAQNPGSGLGWVPDALRS-LWHY 310
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 312-501 2.72e-94

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: 290.88  E-value: 2.72e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNE-LEKYLHSHDKSYPRGSNLQQVTLYEF-PDENNEWIIETKHKYYEHKLMDSKTPIKDGDIIRLYHKS 389
Cdd:cd23286    1 LLYGSTVTIRHLEsLGGYLHSHDLTYPSGSNEQQVTLYDFeDDANNEWIIETKTKEQMDKFPGQFREVRDGDVIRLRHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 390 TGHYLHANDIRPPISEHEYSYEINCNETRGLLGNVDYEFKVRTISKKSHSENDLPLIKLRTTETVFQLLSRGSSCSLMSH 469
Cdd:cd23286   81 TGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKLPNIKIKSTESVFQLYNRGTGCTLLSH 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 459371475 470 EQKLPEWGAFQNEVLCVQEPTIPNTLWYIESN 501
Cdd:cd23286  161 DTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 312-503 5.15e-56

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: 189.43  E-value: 5.15e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKH-NELEKYLHSHDKSYPRGSNLQQVTLYEFPDENNEWIIETKHKYYEHKLmDSKTPIKDGDIIRLYHKST 390
Cdd:cd23283    1 VAYGSTIRIRHlNTRGGYLHSHPHNYPAGSKQQQITLYPHRDENNDWLVELANAPEEWSP-TTFENLKDGDVVRLEHVAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 391 GHYLHANDIRPPISEHEYSYEINCNETRGLLGNVDYEFKVRTISKKSHSENDLPliKLRTTETVFQLLSRGSSCSLMSHE 470
Cdd:cd23283   80 GRRLHSHDHRPPVSDNDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGESKE--RVRAIDTKFRLVHVMTGCYLFSHG 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 459371475 471 QKLPEWGAFQNEVLCVQEPTIPNTLWYIESNSH 503
Cdd:cd23283  158 VKLPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 524-719 1.98e-54

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


Pssm-ID: 465056  Cd Length: 198  Bit Score: 185.44  E-value: 1.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  524 KLFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFFNNysskliDEDSSVIYYLGNIAIYYSVNLVVLISWVKYLFF 603
Cdd:pfam16192   2 KFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  604 AFINLNPYkQPSESSPAKSTFYENAWQFLLGWSLNYLPYFLVSRNLYLHHYLPALSFGILLLGQYLNY--------RVAK 675
Cdd:pfam16192  76 LLRWQRGY-YDLSDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFllslfrrlPRSL 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 459371475  676 NSFIGYSLVILVLVGSVYCYYELIPIIYGLPWTAAKCTAHKWIS 719
Cdd:pfam16192 155 RKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 312-501 6.69e-47

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: 164.43  E-value: 6.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNELEK-YLHSHDKSYPRGSNLQQVTLYEFPDENNEWIIETKHKYYEHKLMDSKtPIKDGDIIRLYHKST 390
Cdd:cd23276    1 VAYGSQITLRNANSGGgYLHSHNHTYPDGSKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDPE-YVRDGDEVRLLHKET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 391 GHYLHANDIRPPISEHEysYEINCNETRGLLGNVDYEFKVRTISKKSHSENDlpliKLRTTETVFQLLSRGSSCSLMSHE 470
Cdd:cd23276   80 NRYLRTHDAAAPVTSKH--KEVSAYPDENEDGDDNDLWVVEIVKDEGKLEDK----RIKPLTTRFRLRNKKTGCYLTSSG 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 459371475 471 QKLPEWGAFQNEVLCVQEPT-IPNTLWYIESN 501
Cdd:cd23276  154 VKLPEWGFRQGEVVCSKNKEsDPSTLWNVEEN 185
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 43-284 7.80e-46

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: 163.64  E-value: 7.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475   43 LAIVIRLYKLYIPDRIVFDEIHIVKYIKHYYTGETFVDVHPPLGRLIYYYLTRLF-VPIDssvlqeFDADKIG-QLYPED 120
Cdd:pfam02366   6 LAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAgYDGN------FTFISIGgQYYPGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  121 FPYLWLRLFSGLCGIGHVLVTFFTSR-LTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLFAQSLVILNYKSFTQCQQ 199
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKrLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  200 FTKSWWFHLFATGVSLGLNISIKISGAFNYLWVGILTTVQLWEILGDLEISVTQWIKHIVSRVVALIIVPLTIYCSVFYI 279
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYV 239


                  ....*
gi 459371475  280 HFELL 284
Cdd:pfam02366 240 HFWLL 244
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 309-503 8.22e-41

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: 147.85  E-value: 8.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 309 PVEVLYGSTVTIKHNELE-KYLHSHDKSYPRGSNLQQVTLYEFPDENNEWIIETKH-KYYEHKLMDSKTPIKDGDIIRLY 386
Cdd:cd23284    1 PLDVAYGSKVTIKNQGLGgGLLHSHVQTYPEGSNQQQVTCYGHKDSNNEWIFERPRgLPSWDENDTDIEFIKDGDIVRLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 387 HKSTGHYLHANDIRPPISEHEysYEINC--NETrglLGNVDYEFKVRTISKKSHSENDlpliKLRTTETVFQLLSRGSSC 464
Cdd:cd23284   81 HKQTGRNLHSHPVPAPISKSD--YEVSGygDLT---VGDEKDNWVIEIVKQVGSEDPK----KLHTLTTSFRLRHEVLGC 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 459371475 465 SLMSHEQKLPEWGAFQNEVLCVQEPTI--PNTLWYIESNSH 503
Cdd:cd23284  152 YLAQTGVSLPEWGFKQGEVVCDKSNFKrdKRTWWNIETHTN 192
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 312-503 9.26e-31

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: 118.95  E-value: 9.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNELE-KYLHSHDKSYPRGSNL--QQVTLYEFPDENNEWIIetKHKYYEHKLMDSKTPIKDGDIIRLYHK 388
Cdd:cd23282    1 VAYGSVITLKNHRTGgGYLHSHWHLYPEGVGArqQQVTTYSHKDDNNLWLI--KKHNQSSDLSDPVEYVRHGDLIRLEHV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 389 STGHYLHANDIRPPISEHEYsyEINCNETRGLlGNVDYEFKVRTISKKshsENDlpliKLRTTETVFQLLSRGSSCSLMS 468
Cdd:cd23282   79 NTKRNLHSHKEKAPLTKKHY--QVTGYGENGT-GDANDVWRVEVVGGR---EGD----PVKTVRSKFRLVHYNTGCALHS 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 459371475 469 HEQKLPEWGAFQNEVLCvqEPTI--PNTLWYIESNSH 503
Cdd:cd23282  149 HGKQLPKWGWEQLEVTC--NPNVrdKNSLWNVEDNRN 183
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 312-499 2.17e-30

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: 118.17  E-value: 2.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNELEKYLHSHDKSYPR-------GSNLQQVTLYEFPDENNEWIIE-TKHKYYEHKlmdSKTPIKDGDII 383
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLryedgriSSQGQQVTGYPHKDANNQWQILpTDPIDEHEG---TGRPVRNGDLI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 384 RLYHKSTGHYLHANDIRPPI-SEHEysyEINC---NETrgllgNVDYE---FKVRTiskkshsENDLPLIKLRTTETVFQ 456
Cdd:cd23285   78 RLRHVSTDTYLLTHDVASPLtPTNM---EFTTvsdDDT-----DERYNetlFRVEI-------EDTDEGDVLKTKSSHFR 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 459371475 457 LLSRGSSCSLMSHEQKLPEWGAFQNEVLCVQEPTIPNTLWYIE 499
Cdd:cd23285  143 LIHVDTNVALWTHKKPLPDWGFGQQEVNGNKNIKDKSNIWVVD 185
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 315-501 2.96e-26

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: 105.93  E-value: 2.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 315 GSTVTIKHNELEKYLHSHDKSYPRGSNLQQVTLY---EFPDENNEWIIETKHkyyehklMDSKTPIKDGDIIRLYHKSTG 391
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTFEsssRKGDTNGLWIIESEN-------GKQGGPVKWGDKIRLRHLSTG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 392 HYLHA-NDIRPPISEHeysYEINCNETRgllGNVDYEFKVRTISKKSHSENDLPLiklrttETVFQLLSRGSSCSLMSHE 470
Cdd:cd23263   74 KYLSSeEGKKSPKSNH---QEVLCLTDN---PDKSSLFKFEPIGSTKYKQKYVKK------DSYFRLKHVNTNFWLHSHE 141

                        170       180       190
                 ....*....|....*....|....*....|.
gi 459371475 471 QKLPEWGAFQNEVLCVQEPTIPNTLWYIESN 501
Cdd:cd23263  142 KKFNINNKTQQEVICHGEREEVFKLWKAELI 172
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 312-503 2.67e-24

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: 100.85  E-value: 2.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNELEK-YLHSHDKSYP------RG-SNLQQVTLYEFPDENNEWIIetKHKYYEHKLMDSKT-PIKDGDI 382
Cdd:cd23281    1 VAYGSQVTLRNTHGSPcWLHSHKHRYPikypdgRGsSHQQQVTCYPFKDVNNWWII--KDPGRQDLAVDDPPrPVRHGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 383 IRLYHKSTGHYLHANDIRPPISEHeySYEINCnetrgllgNVDYEFKV------RTISKKSHSENDLPLiklrTTETVFQ 456
Cdd:cd23281   79 IQLVHGKTGRFLNSHDVAAPLSPT--HQEVSC--------YIDYNISMpaqnlwRIEIVNRDSEGDTWK----AIKSQFR 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 459371475 457 LLSRGSSCSLMSHEQKLPEWGAFQNEVLCVQEPTIPNTLWYIESNSH 503
Cdd:cd23281  145 LIHVNTSAALKLSGKQLPDWGFGQLEVATDRAGNQSSTVWNVEEHRY 191
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 314-496 7.78e-19

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: 84.66  E-value: 7.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 314 YGSTVTIKHNELEKYLHSHDKSYPRGSNLQQVTLY-EFPDENNEWIIETKHKYYEHKLMDsktPIKDGDIIRLYHKSTGH 392
Cdd:cd23279    1 YGSAIKLKHVNSGYRLHSHEVSYGSGSGQQSVTAVpSADDANSLWTVLPGLGEPCQEQGK---PVKCGDIIRLQHVNTRK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 393 YLHANDIRPPISEHeysYEINC-NETRGLLGNVdyeFKVRTISKKShsendlpliKLRTTETVFQLLSRGSS---CSLMS 468
Cdd:cd23279   78 NLHSHNHSSPLSGN---QEVSAfGGGDEDSGDN---WIVECEGKKA---------KFWKRGEPVRLKHVDTGkylSASKT 142

                        170       180
                 ....*....|....*....|....*....
gi 459371475 469 HEQ-KLPEWGafQNEVLCVQEPTiPNTLW 496
Cdd:cd23279  143 HKFtQQPIAG--QLEVSAASSKD-SDSQW 168
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 315-496 1.52e-17

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: 81.26  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  315 GSTVTIKHNELEKYLHShdKSYPRGSNLQQVTLYEFPDENNE----WIIETKHkyyehklMDSKT--PIKDGDIIRLYHK 388
Cdd:pfam02815   6 GDVVRLFHSHQDEYLTG--SEQQQKQPFLRITLYPHGDANNSarslWRIEVVR-------HDAWRggLIKWGSPFRLRHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  389 STGHYLHANDI-RPPISEHE-YSYEINCNETRGLLGNVDYE--FKVRTISKKSHSEndlplikLRTTETVFQLLSRGSSC 464
Cdd:pfam02815  77 TTGRYLHSHEEqKPPLVEKEdWQKEVSAYGFRGFPGDNDIVeiFEKKSTTGMGSDR-------IKPGDSYFRLQHVCTGC 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 459371475  465 SLMSHEQKLPEWGA--FQNEVLCVQEPTIPNTLW 496
Cdd:pfam02815 150 WLFSHSVKLPKWGFgpEQQKVTCAKEGHMDDALT 183
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 312-496 2.09e-17

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: 80.50  E-value: 2.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNELEKYLHSHDKSYPRGSNLQQVTLY-EFPDENNEWIIETKHKyYEHKlmdSKTPIKDGDIIRLYHKST 390
Cdd:cd23294    1 VTCGSVIKLQHERTKFRLHSHEVPYGSGSGQQSVTGFpGVDDSNSYWIVKPANG-ERCK---QGDVIKNGDVIRLQHVST 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 391 GHYLHANDIRPPISEHEysyEINCNETRGlLGNVDYEFKVRTISKKSHSENDLPlIKLRTTETvfqllsrgsSCSLMSHE 470
Cdd:cd23294   77 RKWLHSHLHASPLSGNQ---EVSCFGGDG-NSDTGDNWIVEIEGGGKVWERDQK-VRLKHVDT---------GGYLHSHD 142

                        170       180
                 ....*....|....*....|....*.
gi 459371475 471 QKLPEWGAFQNEVLCVQEPTiPNTLW 496
Cdd:cd23294  143 KKYGRPIPGQQEVCAVASKN-SNTLW 167
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
312-361 6.79e-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: 6.79e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 459371475   312 VLYGSTVTIKHNELEKYLHSHDKSYPR-GSNLQQVTLYEFP--DENNEWIIET 361
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLPPwGDGQQEVTGYGNPaiDANTLWLIEP 56
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 525-721 6.86e-11

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 65.30  E-value: 6.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 525 LFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFF--NNYSSKLIDEDSSVIYY---LGNIAIYYS---VNLVVLIS 596
Cdd:COG1928  307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYyeTGQTGTLGCGAGKCVRAvlaIGNPALWWLglpALLWLLWR 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 597 WVKYLFFAfinlnpykqpsesspakstfyenAWQFLLGWSLNYLPYFLV-SRNLYLHHYLPALSFGIL----LLGQYL-- 669
Cdd:COG1928  387 WIARRDWR-----------------------AGAVLVGYAAGWLPWFLYlDRTMFFFYAIPFVPFLVLalalVLGLILgp 443

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 459371475 670 ---NYRVAKNSFIGYSLVILVLVGSVYCYyeliPIIYGLPWTAAKCTAHKWISNW 721
Cdd:COG1928  444 araSERRRLGRLVVGLYVGLVVANFAFFY----PILTGLPIPYDEWQARMWFPSW 494
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 37-305 1.28e-10

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 64.53  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  37 TFVILTLAIVIRLYKLYIPDRIVFDEIHIVK----YIKHYY------TGETFVdVHPPLGRLIyyyltrlfvpidssvlq 106
Cdd:COG1928   25 TLLVTLLAGVLRFWGLGRPNTLVFDETYYVKdawsLLTNGYernwpdPGPFFV-VHPPLGKWL----------------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 107 efdadkIG---QLYPEDFPYLWlRLFSGLCGIGHVLVTFF-TSRLTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLF 182
Cdd:COG1928   87 ------IAlgeWLFGYVNPFGW-RFAAALAGTLSVLLVARiARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 183 ----AQSLVIL-----------NYKSFTQCQQFTKSWWFH--LFATGVSLGLNISIKISGAFNYLWVGILTTvqLWEILG 245
Cdd:COG1928  160 fvlaAFGCLLLdrdqvrrrlaaAVAAGRAPSRWGPRLGFRwwRLAAGVLLGLACGVKWSGLYFLAAFGLLTV--AWDAGA 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 459371475 246 DLEISVTQWIKHIVSR-----VVALIIVPLTIYCSVF---------YIHFELLPKEGPGSGFLSPHFRStLVDY 305
Cdd:COG1928  238 RRAAGVRRPWLGALLRdgipaFFALVIVPLLTYLASWtgwfasdtgYDRHWAAQNPGSGLGWVPDALRS-LWHY 310
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 315-406 1.68e-10

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: 60.36  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 315 GSTVTIKHNELEKYLHSHDKSYPRGSNLQQVTLYEFPDENNE-WIIETKHKyyehKLMDSKTPIKDGDIIRLYHKSTGHY 393
Cdd:cd23293    4 GSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSyWQIRGPTG----ADCERGTPIKCGQTIRLTHLNTGKN 79

                         90
                 ....*....|...
gi 459371475 394 LHANDIRPPISEH 406
Cdd:cd23293   80 LHSHHFQSPLSGN 92
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 312-399 8.28e-10

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: 58.55  E-value: 8.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 312 VLYGSTVTIKHNELEKYLHSHDKSYPRGSNLQQVTLYEF-PDENNEWIIEtkhkyYEHKLMDSKTPIKDGDIIRLYHKST 390
Cdd:cd23263   59 VKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDnPDKSSLFKFE-----PIGSTKYKQKYVKKDSYFRLKHVNT 133


                 ....*....
gi 459371475 391 GHYLHANDI 399
Cdd:cd23263  134 NFWLHSHEK 142
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
375-417 4.94e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.25  E-value: 4.94e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 459371475   375 TPIKDGDIIRLYHKSTGHYLHANDIRPPISEHEYsYEINCNET 417
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQ-QEVTGYGN 43
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 315-396 6.59e-05

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: 44.18  E-value: 6.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 315 GSTVTIKHNELEKYLHSHDKSYPRgSNLQQVTLYefpDENNE------WIIETKHKYYEhklmdsktpiKDGDIiRLYHK 388
Cdd:cd23293   66 GQTIRLTHLNTGKNLHSHHFQSPL-SGNQEVSAF---GEDGEgdtgdnWTVVCSGTYWE----------RDEAV-RLKHV 130


                 ....*...
gi 459371475 389 STGHYLHA 396
Cdd:cd23293  131 DTEVYLHV 138
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 303-360 1.36e-03

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: 40.44  E-value: 1.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 459371475 303 VDYESSPVEVLYGSTVTIKHNELEKYLHSHDKSYPRG-SNLQQVTLYEFPDENNEWIIE 360
Cdd:cd23294  112 VEIEGGGKVWERDQKVRLKHVDTGGYLHSHDKKYGRPiPGQQEVCAVASKNSNTLWLAA 170
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 38-217 3.99e-03

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: 39.99  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  38 FVILTLAIVIRLYKLYIPDRIVFDE----------IHIVKYIKHYYTGETFVDvHPPLgrliYYYLTRLFVPIdssvlqe 107
Cdd:COG1807   11 LLLLLLALLLRLLGLGSLPLWDPDEaryaeiaremLESGDWLTPTLAGEPYFD-KPPL----IYWLIALSYKL------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 108 fdadkIGqlypedFPYLWLRLFSGLCGIGHVLVTFFTSRLTCTPIIsAIVSSLVCLenSS---ITDSRLILLDGPLLFAQ 184
Cdd:COG1807   79 -----FG------VSEFAARLPSALLGLLTVLLVYLLARRLFGRRA-ALLAALLLL--TSpllLLFGRLATPDALLLLFW 144

                        170       180       190
                 ....*....|....*....|....*....|...
gi 459371475 185 SLVILnykSFTQCQQFTKSWWFHLFATGVSLGL 217
Cdd:COG1807  145 TLALY---ALLRALERRRLRWLLLAGLALGLGF 174
 
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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