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Conserved domains on  [gi|209870082|ref|NP_001129585|]
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protein O-mannosyl-transferase 1 isoform b [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 ...
 299-493 1.05e-126

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: 374.34  E-value: 1.05e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRNVFGkpVPCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 378
Cdd:cd23281    1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 379 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSG 458
Cdd:cd23281   79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 209870082 459 AHLPDWGYRQLEIVGEKLSRgyHGSTVWNVEEHRY 493
Cdd:cd23281  159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-267 9.35e-84

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


:

Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 265.33  E-value: 9.35e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   20 VALTGMGLLSRLWRLTYPRAVVFDEVYYGQYISFYMKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SN 98
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   99 VPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqk 178
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER--- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  179 HSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVCVFCHLLARAVALLVIPVVLYLLF 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 209870082  259 FYVHLILVF 267
Cdd:pfam02366 237 FYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 522-716 4.21e-55

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: 187.37  E-value: 4.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  522 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 600
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  601 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 677
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 209870082  678 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 716
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 ...
 299-493 1.05e-126

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: 374.34  E-value: 1.05e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRNVFGkpVPCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 378
Cdd:cd23281    1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 379 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSG 458
Cdd:cd23281   79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 209870082 459 AHLPDWGYRQLEIVGEKLSRgyHGSTVWNVEEHRY 493
Cdd:cd23281  159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-267 9.35e-84

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


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 265.33  E-value: 9.35e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   20 VALTGMGLLSRLWRLTYPRAVVFDEVYYGQYISFYMKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SN 98
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   99 VPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqk 178
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER--- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  179 HSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVCVFCHLLARAVALLVIPVVLYLLF 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 209870082  259 FYVHLILVF 267
Cdd:pfam02366 237 FYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 522-716 4.21e-55

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: 187.37  E-value: 4.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  522 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 600
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  601 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 677
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 209870082  678 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 716
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 20-257 1.78e-19

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 92.26  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  20 VALTGMGLLSRLWRLTYPRAVVFDEVYYG----QYISFYMKQIFFLDDSG----PPFGHMVLALGGYLGGFDGNFLWnri 91
Cdd:COG1928   26 LLVTLLAGVLRFWGLGRPNTLVFDETYYVkdawSLLTNGYERNWPDPGPFfvvhPPLGKWLIALGEWLFGYVNPFGW--- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  92 gaeyssnvpvwslRLLPALAGALSVPMAYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVL--- 168
Cdd:COG1928  103 -------------RFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGcll 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 169 -----------SYLKFFNCQKHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFtYVLVLGVAAV----HAWHLLGDQTLSN 233
Cdd:COG1928  170 ldrdqvrrrlaAAVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTVawdaGARRAAGVRRPWL 248

                        250       260
                 ....*....|....*....|....
gi 209870082 234 VCVFCHLLARAVALLVIPVVLYLL 257
Cdd:COG1928  249 GALLRDGIPAFFALVIVPLLTYLA 272
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 310-470 1.37e-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: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  310 VFGKPVPCWLHSHQDTYPMIYENGRGsSHQQQVTCYPFKDVNN----WWIVkdprrhqLVVSSPP---RPVRHGDMVQLV 382
Cdd:pfam02815   3 LKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  383 HGMTTRSLNTHDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWRLEIVNR----GSDTDVWKTILSEVRFVHVNTSAVL 454
Cdd:pfam02815  75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKksttGMGSDRIKPGDSYFRLQHVCTGCWL 151

                         170
                  ....*....|....*.
gi 209870082  455 KLSGAHLPDWGYRQLE 470
Cdd:pfam02815 152 FSHSVKLPKWGFGPEQ 167
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 526-718 4.02e-11

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 66.07  E-value: 4.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 526 ELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWVSGSLALaiyaLLSL 593
Cdd:COG1928  309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPAL----LWLL 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 594 WYLLRRRRnvhdlpqdaWlrwvLAGALCAgGWAVNYLPFFL-MEKTLFLYHYLPALTFQILLLPVVLQHI---SDHLCRS 669
Cdd:COG1928  385 WRWIARRD---------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLIlgpARASERR 450

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 209870082 670 QLQRSI---FSALVVA----WYssachvsntlrPLTYGDkSLSPHELKALRWKDSW 718
Cdd:COG1928  451 RLGRLVvglYVGLVVAnfafFY-----------PILTGL-PIPYDEWQARMWFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
299-356 1.21e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 1.21e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   299 VAFGSQVTLRNVFGkpvPCWLHSHQDTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 356
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 ...
 299-493 1.05e-126

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: 374.34  E-value: 1.05e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRNVFGkpVPCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 378
Cdd:cd23281    1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 379 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSG 458
Cdd:cd23281   79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 209870082 459 AHLPDWGYRQLEIVGEKLSRgyHGSTVWNVEEHRY 493
Cdd:cd23281  159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-267 9.35e-84

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


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 265.33  E-value: 9.35e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   20 VALTGMGLLSRLWRLTYPRAVVFDEVYYGQYISFYMKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SN 98
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   99 VPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqk 178
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER--- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  179 HSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVCVFCHLLARAVALLVIPVVLYLLF 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 209870082  259 FYVHLILVF 267
Cdd:pfam02366 237 FYVHFWLLF 245
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 299-491 4.00e-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: 224.52  E-value: 4.00e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRNVfgKPVPCWLHSHQDTYPMIyengrgsSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 378
Cdd:cd23276    1 VAYGSQITLRNA--NSGGGYLHSHNHTYPDG-------SKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDPEYVRDGDE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 379 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVN--RGSDTDVWKTILSEVRFVHVNTSAVLKL 456
Cdd:cd23276   72 VRLLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGDDNDLWVVEIVKdeGKLEDKRIKPLTTRFRLRNKKTGCYLTS 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 209870082 457 SGAHLPDWGYRQLEIVGEKLSRGyHGSTVWNVEEH 491
Cdd:cd23276  152 SGVKLPEWGFRQGEVVCSKNKES-DPSTLWNVEEN 185
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 522-716 4.21e-55

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: 187.37  E-value: 4.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  522 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 600
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  601 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 677
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 209870082  678 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 716
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 296-491 3.95e-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: 3.95e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 296 PLEVAFGSQVTLRNVfgKPVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKDPRRHQL--VVSSPPRPV 373
Cdd:cd23284    1 PLDVAYGSKVTIKNQ--GLGGGLLHSHVQTYP-------EGSNQQQVTCYGHKDSNNEWIFERPRGLPSwdENDTDIEFI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 374 RHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNlWRLEIVNRGSDTDVWK--TILSEVRFVHVNTS 451
Cdd:cd23284   72 KDGDIVRLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDN-WVIEIVKQVGSEDPKKlhTLTTSFRLRHEVLG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 209870082 452 AVLKLSGAHLPDWGYRQLEIVGEKLSRGYHGSTVWNVEEH 491
Cdd:cd23284  151 CYLAQTGVSLPEWGFKQGEVVCDKSNFKRDKRTWWNIETH 190
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 299-490 2.77e-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: 168.24  E-value: 2.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRNVFGKpvpCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKdPRRHQLVVSSPPRPVRHGDM 378
Cdd:cd23285    1 VHYGDVITIKHRDTN---AFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQIL-PTDPIDEHEGTGRPVRNGDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 379 VQLVHGMTTRSLNTHDVAAPLSPHSQEVSCyIDYNISMPAQN--LWRLEIVNrGSDTDVWKTILSEVRFVHVNTSAVLKL 456
Cdd:cd23285   77 IRLRHVSTDTYLLTHDVASPLTPTNMEFTT-VSDDDTDERYNetLFRVEIED-TDEGDVLKTKSSHFRLIHVDTNVALWT 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 209870082 457 SGAHLPDWGYRQLEIVGEKlsRGYHGSTVWNVEE 490
Cdd:cd23285  155 HKKPLPDWGFGQQEVNGNK--NIKDKSNIWVVDD 186
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 299-490 7.01e-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: 159.00  E-value: 7.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRNVfgKPVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDM 378
Cdd:cd23283    1 VAYGSTIRIRHL--NTRGGYLHSHPHNYP-------AGSKQQQITLYPHRDENNDWLVELANAPEEWSPTTFENLKDGDV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 379 VQLVHGMTTRSLNTHDVAAPLS--PHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDV----WKTILSEVRFVHVNTSA 452
Cdd:cd23283   72 VRLEHVATGRRLHSHDHRPPVSdnDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGEskerVRAIDTKFRLVHVMTGC 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 209870082 453 VLKLSGAHLPDWGYRQLEIVGEKlsRGYHGSTVWNVEE 490
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 ...
 299-493 3.34e-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: 3.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRN--VFGKpvpcWLHSHQDTYPmiyeNGRGSsHQQQVTCYPFKDVNNWWIVKDPRRHQLVvSSPPRPVRHG 376
Cdd:cd23282    1 VAYGSVITLKNhrTGGG----YLHSHWHLYP----EGVGA-RQQQVTTYSHKDDNNLWLIKKHNQSSDL-SDPVEYVRHG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 377 DMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDyNISMPAQNLWRLEIVNrGSDTDVWKTILSEVRFVHVNTSAVLKL 456
Cdd:cd23282   71 DLIRLEHVNTKRNLHSHKEKAPLTKKHYQVTGYGE-NGTGDANDVWRVEVVG-GREGDPVKTVRSKFRLVHYNTGCALHS 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 209870082 457 SGAHLPDWGYRQLEIVGEKLSRgyHGSTVWNVEEHRY 493
Cdd:cd23282  149 HGKQLPKWGWEQLEVTCNPNVR--DKNSLWNVEDNRN 183
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 299-472 2.92e-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: 97.89  E-value: 2.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRNVFGkpVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFK-DVNNWWIVKDPRRHQLVVSSPP-RPVRHG 376
Cdd:cd23286    1 LLYGSTVTIRHLES--LGGYLHSHDLTYP-------SGSNEQQVTLYDFEdDANNEWIIETKTKEQMDKFPGQfREVRDG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 377 DMVQLVHGMTTRSLNTHDVAAPLSPH--SQEVSCYIDYNISMPAQNLWRLEIV-------NRGSDTDVwKTILSEVRFVH 447
Cdd:cd23286   72 DVIRLRHVVTGKLLRASNARPPVSEQeyNNEVSCTGNANYSGDMDENWRIDVKgdeshaeLKLPNIKI-KSTESVFQLYN 150

                        170       180
                 ....*....|....*....|....*
gi 209870082 448 VNTSAVLKLSGAHLPDWGYRQLEIV 472
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 ...
 301-474 1.87e-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: 91.98  E-value: 1.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 301 FGSQVTLRNVFGKpvpCWLHSHQDTYpmiyenGRGSShQQQVTCYP-FKDVNNWWIVK----DPRRHQlvvsspPRPVRH 375
Cdd:cd23279    1 YGSAIKLKHVNSG---YRLHSHEVSY------GSGSG-QQSVTAVPsADDANSLWTVLpglgEPCQEQ------GKPVKC 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 376 GDMVQLVHGMTTRSLNTHDVAAPLSPHsQEVSCY--IDYNISmpaqNLWRLEIVnrGSDTDVWKtILSEVRFVHVNTSAV 453
Cdd:cd23279   65 GDIIRLQHVNTRKNLHSHNHSSPLSGN-QEVSAFggGDEDSG----DNWIVECE--GKKAKFWK-RGEPVRLKHVDTGKY 136

                        170       180
                 ....*....|....*....|.
gi 209870082 454 LKLSGAHLpdwgYRQLEIVGE 474
Cdd:cd23279  137 LSASKTHK----FTQQPIAGQ 153
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 20-257 1.78e-19

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 92.26  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  20 VALTGMGLLSRLWRLTYPRAVVFDEVYYG----QYISFYMKQIFFLDDSG----PPFGHMVLALGGYLGGFDGNFLWnri 91
Cdd:COG1928   26 LLVTLLAGVLRFWGLGRPNTLVFDETYYVkdawSLLTNGYERNWPDPGPFfvvhPPLGKWLIALGEWLFGYVNPFGW--- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  92 gaeyssnvpvwslRLLPALAGALSVPMAYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVL--- 168
Cdd:COG1928  103 -------------RFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGcll 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 169 -----------SYLKFFNCQKHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFtYVLVLGVAAV----HAWHLLGDQTLSN 233
Cdd:COG1928  170 ldrdqvrrrlaAAVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTVawdaGARRAAGVRRPWL 248

                        250       260
                 ....*....|....*....|....
gi 209870082 234 VCVFCHLLARAVALLVIPVVLYLL 257
Cdd:COG1928  249 GALLRDGIPAFFALVIVPLLTYLA 272
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 299-493 3.68e-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: 85.51  E-value: 3.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 299 VAFGSQVTLRNVfgkPVPCWLHSHQDTYpmiyenGRGSShQQQVTCYPFK-DVNNWWIVKDPRRHQLVVSSPprpVRHGD 377
Cdd:cd23294    1 VTCGSVIKLQHE---RTKFRLHSHEVPY------GSGSG-QQSVTGFPGVdDSNSYWIVKPANGERCKQGDV---IKNGD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 378 MVQLVHGMTTRSLNTHDVAAPLSpHSQEVSCYIDYNISMPAQNlWRLEIVNRGsdtDVWKtiLSE-VRFVHVNTSAVLkl 456
Cdd:cd23294   68 VIRLQHVSTRKWLHSHLHASPLS-GNQEVSCFGGDGNSDTGDN-WIVEIEGGG---KVWE--RDQkVRLKHVDTGGYL-- 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 209870082 457 sgaHLPDWGYR-----QLEIVGeklSRGYHGSTVWNVEEHRY 493
Cdd:cd23294  139 ---HSHDKKYGrpipgQQEVCA---VASKNSNTLWLAAEGVY 174
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 319-490 1.26e-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: 72.30  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 319 LHSHQDTYpmiyenGRGSShQQQVTCYPFK-DVNNWWIVKDPRRHQLvvsspPR--PVRHGDMVQLVHGMTTRSLNTHDV 395
Cdd:cd23293   18 LHSHDVKY------GSGSG-QQSVTGVESSdDSNSYWQIRGPTGADC-----ERgtPIKCGQTIRLTHLNTGKNLHSHHF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 396 AAPLSpHSQEVSCYIDYnismpaqnlwrleivNRGSDTDVWKTILS--------EVRFVHVNTSAVLKLSGAHL--PDWG 465
Cdd:cd23293   86 QSPLS-GNQEVSAFGED---------------GEGDTGDNWTVVCSgtywerdeAVRLKHVDTEVYLHVTGEQYgrPIHG 149

                        170       180
                 ....*....|....*....|....*.
gi 209870082 466 yrQLEIVG-EKLSRGyhgsTVWNVEE 490
Cdd:cd23293  150 --QREVSGmSSPSQA----NYWKAME 169
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 310-470 1.37e-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: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  310 VFGKPVPCWLHSHQDTYPMIYENGRGsSHQQQVTCYPFKDVNN----WWIVkdprrhqLVVSSPP---RPVRHGDMVQLV 382
Cdd:pfam02815   3 LKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  383 HGMTTRSLNTHDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWRLEIVNR----GSDTDVWKTILSEVRFVHVNTSAVL 454
Cdd:pfam02815  75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKksttGMGSDRIKPGDSYFRLQHVCTGCWL 151

                         170
                  ....*....|....*.
gi 209870082  455 KLSGAHLPDWGYRQLE 470
Cdd:pfam02815 152 FSHSVKLPKWGFGPEQ 167
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 302-489 3.23e-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: 3.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 302 GSQVTLRNVF-GKpvpcWLHSHQDTYPMiyengrgSSHQQQVTCY---PFKDVNNWWIVKDPRRHQLvvssppRPVRHGD 377
Cdd:cd23263    1 GDVIWLKHSEtGK----YLHSHRKNYPT-------GSGQQEVTFEsssRKGDTNGLWIIESENGKQG------GPVKWGD 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 378 MVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISmpaQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLS 457
Cdd:cd23263   64 KIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDK---SSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSH 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 209870082 458 GAHLPDWGYRQLEIVGEKlsRGYHGSTVWNVE 489
Cdd:cd23263  141 EKKFNINNKTQQEVICHG--EREEVFKLWKAE 170
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 526-718 4.02e-11

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 66.07  E-value: 4.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 526 ELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWVSGSLALaiyaLLSL 593
Cdd:COG1928  309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPAL----LWLL 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 594 WYLLRRRRnvhdlpqdaWlrwvLAGALCAgGWAVNYLPFFL-MEKTLFLYHYLPALTFQILLLPVVLQHI---SDHLCRS 669
Cdd:COG1928  385 WRWIARRD---------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLIlgpARASERR 450

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 209870082 670 QLQRSI---FSALVVA----WYssachvsntlrPLTYGDkSLSPHELKALRWKDSW 718
Cdd:COG1928  451 RLGRLVvglYVGLVVAnfafFY-----------PILTGL-PIPYDEWQARMWFPSW 494
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 16-250 2.04e-10

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


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 62.72  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  16 NLSLVALTGMGLLSRLWRLTYPRAVVFDEVYY----------GQYISFYMKQIFFLDDsgPPFGHMVLALGGYLGGfdgn 85
Cdd:COG1807    7 ARPLLLLLLLALLLRLLGLGSLPLWDPDEARYaeiaremlesGDWLTPTLAGEPYFDK--PPLIYWLIALSYKLFG---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  86 flwnrigaeyssnVPVWSLRLLPALAGALSVPMAYQIVLELhFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLL 165
Cdd:COG1807   81 -------------VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082 166 AVLSYLKFFNCQKhspfslswWFWLTLTGVACSCAVGIKYMGVFtyvlvLGVAAVHAWHLLGDQTLSNVCVFCHLLARAV 245
Cdd:COG1807  147 ALYALLRALERRR--------LRWLLLAGLALGLGFLTKGPVAL-----LLPGLALLLYLLLTRRWRRLRRLRLLLGLLL 213


                 ....*
gi 209870082 246 ALLVI 250
Cdd:COG1807  214 ALLLA 218
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
299-356 1.21e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 1.21e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   299 VAFGSQVTLRNVFGkpvPCWLHSHQDTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 356
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 17-226 3.64e-06

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


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 50.05  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  17 LSLVALTGMGLLSRLWRLTYpRAVVFDEVYYGQYISFYMKQIFFLDDS---GPPFGHMVLALGGYLGGFDgnflwnriga 93
Cdd:COG4745   17 LAVLAITALALLLRLVGLGA-RPFHWDEARVAYWSLRLLETGAYEYRPiyhGPFLYHVTAALFGLFGASD---------- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  94 eyssnvpvWSLRLLPALAGALSVPMAYqiVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKF 173
Cdd:COG4745   86 --------FTARLPVALVGGLLPLLAL--LLRERLGDAEVLALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVRA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 209870082 174 FNCQKhspfslswWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLL 226
Cdd:COG4745  156 IDTRR--------RRYLYLAAVALALAFATKENAVLYLLCWLGALLLLLDHRL 200
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 64-255 4.84e-06

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: 47.26  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082   64 SGPPFGHMVLALGGYLGGFDGnflwnrigaeyssnvpvWSLRLLPALAGALSVPMAYQIVLELhFSHCAAMGAALLMLIE 143
Cdd:pfam13231   1 DHPPLAAWLIALFTALFGDSE-----------------WAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVV 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209870082  144 NALITQSRLMLLESVLIFFNLLAVLSYLKFfnCQKHSpfslswWFWLTLTGVACSCAVGIKYMGVftyvlVLGVAAVHAw 223
Cdd:pfam13231  63 PLFVALSRLFTPDAPLLLFWALALYFLLRA--LEKGR------LKWWLLAGAAAGLGFLSKYTAA-----LLVLAALLY- 128

                         170       180       190
                  ....*....|....*....|....*....|..
gi 209870082  224 hLLGDQTLSNVCVFCHLLARAVALLVIPVVLY 255
Cdd:pfam13231 129 -LLISPGRRRLKSPKPYLGLLLALLLFSPVLI 159
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
370-427 7.03e-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: 7.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 209870082   370 PRPVRHGDMVQLVHGMTTRSLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWRLEIV 427
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
441-491 1.43e-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: 1.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 209870082   441 SEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRGyHGSTVWNVEEH 491
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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