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Conserved domains on  [gi|1677531299|ref|NP_001340127|]
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protein O-mannosyl-transferase 1 isoform f [Homo sapiens]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 11449133)

dolichyl-phosphate-mannose--protein mannosyltransferase is a glycosyltransferase family 39 protein that transfers mannosyl residues to the hydroxyl group of serine or threonine residues, initiating the assembly of O-mannosyl glycans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 267-461 3.13e-127

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: 374.72  E-value: 3.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRNVFGkpVPCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 346
Cdd:cd23281     1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 347 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSG 426
Cdd:cd23281    79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1677531299 427 AHLPDWGYRQLEIVGEKLSRgyHGSTVWNVEEHRY 461
Cdd:cd23281   159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 1-235 1.26e-66

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: 219.49  E-value: 1.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299   1 MKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SNVPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAA 79
Cdd:pfam02366  36 AEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  80 MGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqkHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVL 159
Cdd:pfam02366 115 LLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLP 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677531299 160 VLGVAAVHAWHLLGDQTLSNVGadvqccmrpacmgqmqmsqgvcVFCHLLARAVALLVIPVVLYLLFFYVHLILVF 235
Cdd:pfam02366 192 VGLLTIWHLWQLLGDLSLLLKS----------------------IWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 490-684 2.73e-56

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: 190.06  E-value: 2.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 490 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 568
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 569 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 645
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1677531299 646 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 684
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
 
Name Accession Description Interval E-value
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 267-461 3.13e-127

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: 374.72  E-value: 3.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRNVFGkpVPCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 346
Cdd:cd23281     1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 347 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSG 426
Cdd:cd23281    79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1677531299 427 AHLPDWGYRQLEIVGEKLSRgyHGSTVWNVEEHRY 461
Cdd:cd23281   159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 1-235 1.26e-66

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: 219.49  E-value: 1.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299   1 MKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SNVPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAA 79
Cdd:pfam02366  36 AEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  80 MGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqkHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVL 159
Cdd:pfam02366 115 LLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLP 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677531299 160 VLGVAAVHAWHLLGDQTLSNVGadvqccmrpacmgqmqmsqgvcVFCHLLARAVALLVIPVVLYLLFFYVHLILVF 235
Cdd:pfam02366 192 VGLLTIWHLWQLLGDLSLLLKS----------------------IWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 490-684 2.73e-56

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: 190.06  E-value: 2.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 490 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 568
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 569 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 645
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1677531299 646 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 684
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 278-438 1.18e-14

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: 72.78  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 278 VFGKPVPCWLHSHQDTYPMIYENGRGsSHQQQVTCYPFKDVNN----WWIVkdprrhqLVVSSPP---RPVRHGDMVQLV 350
Cdd:pfam02815   3 LKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 351 HGMTTRSLNTHDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWRLEIVNR----GSDTDVWKTILSEVRFVHVNTSAVL 422
Cdd:pfam02815  75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKksttGMGSDRIKPGDSYFRLQHVCTGCWL 151

                         170
                  ....*....|....*.
gi 1677531299 423 KLSGAHLPDWGYRQLE 438
Cdd:pfam02815 152 FSHSVKLPKWGFGPEQ 167
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 494-686 1.13e-11

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 67.61  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 494 ELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWVSGSLALaiyaLLSL 561
Cdd:COG1928   309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPAL----LWLL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 562 WYLLRRRRnvhdlpqdaWlrwvLAGALCAgGWAVNYLPFFL-MEKTLFLYHYLPALTFQILLLPVVLQHI---SDHLCRS 637
Cdd:COG1928   385 WRWIARRD---------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLIlgpARASERR 450

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1677531299 638 QLQRSI---FSALVVA----WYssachvsntlrPLTYGDkSLSPHELKALRWKDSW 686
Cdd:COG1928   451 RLGRLVvglYVGLVVAnfafFY-----------PILTGL-PIPYDEWQARMWFPSW 494
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 12-169 6.42e-09

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: 58.10  E-value: 6.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  12 PPFGHMVLALGGYLGGfdgnflwnrigaeyssnVPVWSLRLLPALAGALSVPMAYQIVLELhFSHCAAMGAALLMLIENA 91
Cdd:COG1807    65 PPLIYWLIALSYKLFG-----------------VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPL 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677531299  92 LITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKhspfslswWFWLTLTGVACSCAVGIKYMGVFtyVLVLGVAAVHAW 169
Cdd:COG1807   127 LLLFGRLATPDALLLLFWTLALYALLRALERRR--------LRWLLLAGLALGLGFLTKGPVAL--LLPGLALLLYLL 194
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
267-324 9.75e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 9.75e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  267 VAFGSQVTLRNVFGkpvPCWLHSHQDTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 324
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
 
Name Accession Description Interval E-value
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 267-461 3.13e-127

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: 374.72  E-value: 3.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRNVFGkpVPCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 346
Cdd:cd23281     1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 347 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSG 426
Cdd:cd23281    79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1677531299 427 AHLPDWGYRQLEIVGEKLSRgyHGSTVWNVEEHRY 461
Cdd:cd23281   159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 267-459 1.14e-69

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: 225.29  E-value: 1.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRNVfgKPVPCWLHSHQDTYPMIyengrgsSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 346
Cdd:cd23276     1 VAYGSQITLRNA--NSGGGYLHSHNHTYPDG-------SKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDPEYVRDGDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 347 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVN--RGSDTDVWKTILSEVRFVHVNTSAVLKL 424
Cdd:cd23276    72 VRLLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGDDNDLWVVEIVKdeGKLEDKRIKPLTTRFRLRNKKTGCYLTS 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1677531299 425 SGAHLPDWGYRQLEIVGEKLSRGyHGSTVWNVEEH 459
Cdd:cd23276   152 SGVKLPEWGFRQGEVVCSKNKES-DPSTLWNVEEN 185
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 1-235 1.26e-66

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: 219.49  E-value: 1.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299   1 MKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SNVPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAA 79
Cdd:pfam02366  36 AEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  80 MGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqkHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVL 159
Cdd:pfam02366 115 LLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLP 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677531299 160 VLGVAAVHAWHLLGDQTLSNVGadvqccmrpacmgqmqmsqgvcVFCHLLARAVALLVIPVVLYLLFFYVHLILVF 235
Cdd:pfam02366 192 VGLLTIWHLWQLLGDLSLLLKS----------------------IWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 490-684 2.73e-56

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: 190.06  E-value: 2.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 490 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 568
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 569 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 645
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1677531299 646 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 684
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 264-459 2.54e-50

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: 173.66  E-value: 2.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 264 PLEVAFGSQVTLRNVfgKPVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKDPRRHQL--VVSSPPRPV 341
Cdd:cd23284     1 PLDVAYGSKVTIKNQ--GLGGGLLHSHVQTYP-------EGSNQQQVTCYGHKDSNNEWIFERPRGLPSwdENDTDIEFI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 342 RHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNlWRLEIVNRGSDTDVWK--TILSEVRFVHVNTS 419
Cdd:cd23284    72 KDGDIVRLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDN-WVIEIVKQVGSEDPKKlhTLTTSFRLRHEVLG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1677531299 420 AVLKLSGAHLPDWGYRQLEIVGEKLSRGYHGSTVWNVEEH 459
Cdd:cd23284   151 CYLAQTGVSLPEWGFKQGEVVCDKSNFKRDKRTWWNIETH 190
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 267-458 1.10e-48

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: 169.01  E-value: 1.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRNVFGKpvpCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKdPRRHQLVVSSPPRPVRHGDM 346
Cdd:cd23285     1 VHYGDVITIKHRDTN---AFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQIL-PTDPIDEHEGTGRPVRNGDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 347 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCyIDYNISMPAQN--LWRLEIVNrGSDTDVWKTILSEVRFVHVNTSAVLKL 424
Cdd:cd23285    77 IRLRHVSTDTYLLTHDVASPLTPTNMEFTT-VSDDDTDERYNetLFRVEIED-TDEGDVLKTKSSHFRLIHVDTNVALWT 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1677531299 425 SGAHLPDWGYRQLEIVGEKlsRGYHGSTVWNVEE 458
Cdd:cd23285   155 HKKPLPDWGFGQQEVNGNK--NIKDKSNIWVVDD 186
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 267-458 4.10e-45

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: 159.38  E-value: 4.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRNVfgKPVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 346
Cdd:cd23283     1 VAYGSTIRIRHL--NTRGGYLHSHPHNYP-------AGSKQQQITLYPHRDENNDWLVELANAPEEWSPTTFENLKDGDV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 347 VQLVHGMTTRSLNTHDVAAPLS--PHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDV----WKTILSEVRFVHVNTSA 420
Cdd:cd23283    72 VRLEHVATGRRLHSHDHRPPVSdnDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGEskerVRAIDTKFRLVHVMTGC 151

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1677531299 421 VLKLSGAHLPDWGYRQLEIVGEKlsRGYHGSTVWNVEE 458
Cdd:cd23283   152 YLFSHGVKLPEWGFEQQEVTCAK--SGLLELSLWYIET 187
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 267-461 2.62e-44

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: 157.08  E-value: 2.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRN--VFGKpvpcWLHSHQDTYPmiyeNGRGSsHQQQVTCYPFKDVNNWWIVKDPRRHQLVvSSPPRPVRHG 344
Cdd:cd23282     1 VAYGSVITLKNhrTGGG----YLHSHWHLYP----EGVGA-RQQQVTTYSHKDDNNLWLIKKHNQSSDL-SDPVEYVRHG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 345 DMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDyNISMPAQNLWRLEIVNrGSDTDVWKTILSEVRFVHVNTSAVLKL 424
Cdd:cd23282    71 DLIRLEHVNTKRNLHSHKEKAPLTKKHYQVTGYGE-NGTGDANDVWRVEVVG-GREGDPVKTVRSKFRLVHYNTGCALHS 148

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1677531299 425 SGAHLPDWGYRQLEIVGEKLSRgyHGSTVWNVEEHRY 461
Cdd:cd23282   149 HGKQLPKWGWEQLEVTCNPNVR--DKNSLWNVEDNRN 183
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 267-440 1.81e-23

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: 98.28  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRNVFGkpVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFK-DVNNWWIVKDPRRHQLVVSSPP-RPVRHG 344
Cdd:cd23286     1 LLYGSTVTIRHLES--LGGYLHSHDLTYP-------SGSNEQQVTLYDFEdDANNEWIIETKTKEQMDKFPGQfREVRDG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 345 DMVQLVHGMTTRSLNTHDVAAPLSPH--SQEVSCYIDYNISMPAQNLWRLEIV-------NRGSDTDVwKTILSEVRFVH 415
Cdd:cd23286    72 DVIRLRHVVTGKLLRASNARPPVSEQeyNNEVSCTGNANYSGDMDENWRIDVKgdeshaeLKLPNIKI-KSTESVFQLYN 150

                         170       180
                  ....*....|....*....|....*
gi 1677531299 416 VNTSAVLKLSGAHLPDWGYRQLEIV 440
Cdd:cd23286   151 RGTGCTLLSHDTRLPDWAFHQQEVL 175
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 269-442 2.51e-21

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: 91.59  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 269 FGSQVTLRNVFGKpvpCWLHSHQDTYpmiyenGRGSShQQQVTCYP-FKDVNNWWIVK----DPRRHQlvvsspPRPVRH 343
Cdd:cd23279     1 YGSAIKLKHVNSG---YRLHSHEVSY------GSGSG-QQSVTAVPsADDANSLWTVLpglgEPCQEQ------GKPVKC 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 344 GDMVQLVHGMTTRSLNTHDVAAPLSPHsQEVSCY--IDYNISmpaqNLWRLEIVnrGSDTDVWKtILSEVRFVHVNTSAV 421
Cdd:cd23279    65 GDIIRLQHVNTRKNLHSHNHSSPLSGN-QEVSAFggGDEDSG----DNWIVECE--GKKAKFWK-RGEPVRLKHVDTGKY 136

                         170       180
                  ....*....|....*....|.
gi 1677531299 422 LKLSGAHLpdwgYRQLEIVGE 442
Cdd:cd23279   137 LSASKTHK----FTQQPIAGQ 153
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 267-461 4.66e-19

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: 85.12  E-value: 4.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 267 VAFGSQVTLRNVfgkPVPCWLHSHQDTYpmiyenGRGSShQQQVTCYPFK-DVNNWWIVKDPRRHQLVVSSPprpVRHGD 345
Cdd:cd23294     1 VTCGSVIKLQHE---RTKFRLHSHEVPY------GSGSG-QQSVTGFPGVdDSNSYWIVKPANGERCKQGDV---IKNGD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 346 MVQLVHGMTTRSLNTHDVAAPLSpHSQEVSCYIDYNISMPAQNlWRLEIVNRGsdtDVWKtiLSE-VRFVHVNTSAVLkl 424
Cdd:cd23294    68 VIRLQHVSTRKWLHSHLHASPLS-GNQEVSCFGGDGNSDTGDN-WIVEIEGGG---KVWE--RDQkVRLKHVDTGGYL-- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1677531299 425 sgaHLPDWGYR-----QLEIVGeklSRGYHGSTVWNVEEHRY 461
Cdd:cd23294   139 ---HSHDKKYGrpipgQQEVCA---VASKNSNTLWLAAEGVY 174
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 278-438 1.18e-14

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: 72.78  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 278 VFGKPVPCWLHSHQDTYPMIYENGRGsSHQQQVTCYPFKDVNN----WWIVkdprrhqLVVSSPP---RPVRHGDMVQLV 350
Cdd:pfam02815   3 LKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 351 HGMTTRSLNTHDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWRLEIVNR----GSDTDVWKTILSEVRFVHVNTSAVL 422
Cdd:pfam02815  75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKksttGMGSDRIKPGDSYFRLQHVCTGCWL 151

                         170
                  ....*....|....*.
gi 1677531299 423 KLSGAHLPDWGYRQLE 438
Cdd:pfam02815 152 FSHSVKLPKWGFGPEQ 167
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 287-458 1.58e-14

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: 71.92  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 287 LHSHQDTYpmiyenGRGSShQQQVTCYPFK-DVNNWWIVKDPRRHQLvvsspPR--PVRHGDMVQLVHGMTTRSLNTHDV 363
Cdd:cd23293    18 LHSHDVKY------GSGSG-QQSVTGVESSdDSNSYWQIRGPTGADC-----ERgtPIKCGQTIRLTHLNTGKNLHSHHF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 364 AAPLSpHSQEVSCYIDYnismpaqnlwrleivNRGSDTDVWKTILS--------EVRFVHVNTSAVLKLSGAHL--PDWG 433
Cdd:cd23293    86 QSPLS-GNQEVSAFGED---------------GEGDTGDNWTVVCSgtywerdeAVRLKHVDTEVYLHVTGEQYgrPIHG 149

                         170       180
                  ....*....|....*....|....*.
gi 1677531299 434 yrQLEIVG-EKLSRGyhgsTVWNVEE 458
Cdd:cd23293   150 --QREVSGmSSPSQA----NYWKAME 169
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 270-457 2.43e-14

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: 71.26  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 270 GSQVTLRNVF-GKpvpcWLHSHQDTYPMiyengrgSSHQQQVTCY---PFKDVNNWWIVKDPRRHQLvvssppRPVRHGD 345
Cdd:cd23263     1 GDVIWLKHSEtGK----YLHSHRKNYPT-------GSGQQEVTFEsssRKGDTNGLWIIESENGKQG------GPVKWGD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 346 MVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISmpaQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLS 425
Cdd:cd23263    64 KIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDK---SSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSH 140

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1677531299 426 GAHLPDWGYRQLEIVGEKlsRGYHGSTVWNVE 457
Cdd:cd23263   141 EKKFNINNKTQQEVICHG--EREEVFKLWKAE 170
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 494-686 1.13e-11

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 67.61  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 494 ELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWVSGSLALaiyaLLSL 561
Cdd:COG1928   309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPAL----LWLL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 562 WYLLRRRRnvhdlpqdaWlrwvLAGALCAgGWAVNYLPFFL-MEKTLFLYHYLPALTFQILLLPVVLQHI---SDHLCRS 637
Cdd:COG1928   385 WRWIARRD---------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLIlgpARASERR 450

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1677531299 638 QLQRSI---FSALVVA----WYssachvsntlrPLTYGDkSLSPHELKALRWKDSW 686
Cdd:COG1928   451 RLGRLVvglYVGLVVAnfafFY-----------PILTGL-PIPYDEWQARMWFPSW 494
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 12-169 6.42e-09

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: 58.10  E-value: 6.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  12 PPFGHMVLALGGYLGGfdgnflwnrigaeyssnVPVWSLRLLPALAGALSVPMAYQIVLELhFSHCAAMGAALLMLIENA 91
Cdd:COG1807    65 PPLIYWLIALSYKLFG-----------------VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPL 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677531299  92 LITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKhspfslswWFWLTLTGVACSCAVGIKYMGVFtyVLVLGVAAVHAW 169
Cdd:COG1807   127 LLLFGRLATPDALLLLFWTLALYALLRALERRR--------LRWLLLAGLALGLGFLTKGPVAL--LLPGLALLLYLL 194
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 49-231 3.54e-07

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


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 53.52  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  49 SLRLLPALAGALSVPMAYqiVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKhspf 128
Cdd:COG4745    87 TARLPVALVGGLLPLLAL--LLRERLGDAEVLALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVRAIDTRR---- 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299 129 slswWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLLgdQTLSNVGADVQCCMRPACMGQMQMSQGVCVFCHL 208
Cdd:COG4745   161 ----RRYLYLAAVALALAFATKENAVLYLLCWLGALLLLLDHRL--FRARRRGTSVLLVLRRLRRLVRRLRLLLRWWRHL 234

                         170       180
                  ....*....|....*....|...
gi 1677531299 209 LARAVALLVIPVVLYLLFFYVHL 231
Cdd:COG4745   235 VGALAVFLAVAVFFYAPRGGPGL 257
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
267-324 9.75e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 9.75e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  267 VAFGSQVTLRNVFGkpvPCWLHSHQDTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 324
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 10-169 5.87e-05

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: 43.79  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  10 SGPPFGHMVLALGGYLGGFDGnflwnrigaeyssnvpvWSLRLLPALAGALSVPMAYQIVLELhFSHCAAMGAALLMLIE 89
Cdd:pfam13231   1 DHPPLAAWLIALFTALFGDSE-----------------WAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVV 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677531299  90 NALITQSRLMLLESVLIFFNLLAVLSYLKFfnCQKHSpfslswWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAW 169
Cdd:pfam13231  63 PLFVALSRLFTPDAPLLLFWALALYFLLRA--LEKGR------LKWWLLAGAAAGLGFLSKYTAALLVLAALLYLLISPG 134
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
338-395 6.03e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.17  E-value: 6.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1677531299  338 PRPVRHGDMVQLVHGMTTRSLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWRLEIV 395
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
409-459 1.26e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.32  E-value: 1.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1677531299  409 SEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRGyHGSTVWNVEEH 459
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAI-DANTLWLIEPV 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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