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Conserved domains on  [gi|1720401381|ref|XP_030108128|]
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protein O-mannosyl-transferase 1 isoform X4 [Mus musculus]

Protein Classification

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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 ...
 6-178 1.24e-108

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: 317.33  E-value: 1.24e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381   6 PVPSRPAW----------RYENGRGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDIVQLVHGMTTRLL 75
Cdd:cd23281    11 NTHGSPCWlhshkhrypiKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDIIQLVHGKTGRFL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  76 NTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLE 155
Cdd:cd23281    91 NSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSGKQLPDWGFGQLE 170

                         170       180
                  ....*....|....*....|...
gi 1720401381 156 VVGEKlsPGYHESMVWNVEEHRY 178
Cdd:cd23281   171 VATDR--AGNQSSTVWNVEEHRY 191
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 207-401 6.80e-62

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: 198.15  E-value: 6.80e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 207 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 285
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 286 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 362
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720401381 363 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 401
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 ...
 6-178 1.24e-108

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: 317.33  E-value: 1.24e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381   6 PVPSRPAW----------RYENGRGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDIVQLVHGMTTRLL 75
Cdd:cd23281    11 NTHGSPCWlhshkhrypiKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDIIQLVHGKTGRFL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  76 NTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLE 155
Cdd:cd23281    91 NSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSGKQLPDWGFGQLE 170

                         170       180
                  ....*....|....*....|...
gi 1720401381 156 VVGEKlsPGYHESMVWNVEEHRY 178
Cdd:cd23281   171 VATDR--AGNQSSTVWNVEEHRY 191
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 207-401 6.80e-62

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: 198.15  E-value: 6.80e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 207 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 285
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 286 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 362
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720401381 363 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 401
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 211-403 1.81e-10

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 62.60  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 211 ELQWKMLTL-KNEDLEHQYSSTPLEWLTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWTSASLATVVytlLFF 278
Cdd:COG1928   309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPALLW---LLW 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 279 WYLLRRRrsicdlpedaWsrwvLAGALCTgGWALNYLPFFL-MERVLFLYHYLPALTFQILLLPIVLQH---ASDHLCRS 354
Cdd:COG1928   386 RWIARRD----------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLilgPARASERR 450

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401381 355 QLQRNV---FSALVVA----WYssachvsnmlrPLTYGDTsLSPGELRALRWKDSW 403
Cdd:COG1928   451 RLGRLVvglYVGLVVAnfafFY-----------PILTGLP-IPYDEWQARMWFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
126-176 3.62e-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: 3.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720401381  126 SEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 176
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
 
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 ...
 6-178 1.24e-108

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: 317.33  E-value: 1.24e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381   6 PVPSRPAW----------RYENGRGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDIVQLVHGMTTRLL 75
Cdd:cd23281    11 NTHGSPCWlhshkhrypiKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDIIQLVHGKTGRFL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  76 NTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLE 155
Cdd:cd23281    91 NSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSGKQLPDWGFGQLE 170

                         170       180
                  ....*....|....*....|...
gi 1720401381 156 VVGEKlsPGYHESMVWNVEEHRY 178
Cdd:cd23281   171 VATDR--AGNQSSTVWNVEEHRY 191
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 207-401 6.80e-62

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: 198.15  E-value: 6.80e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 207 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 285
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 286 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 362
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720401381 363 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 401
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 20-176 1.14e-53

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: 176.37  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  20 GSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNI 99
Cdd:cd23276    28 DGSKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDPEYVRDGDEVRLLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENE 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401381 100 SMPAQNLWKLDIVNRESN--RDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 176
Cdd:cd23276   108 DGDDNDLWVVEIVKDEGKleDKRIKPLTTRFRLRNKKTGCYLTSSGVKLPEWGFRQGEVVCSK-NKESDPSTLWNVEEN 185
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 14-175 3.73e-39

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: 138.58  E-value: 3.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  14 RYENGRGSSHQQQVTCYPFKDINNWWIVKdPGRHQLVVNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSC 93
Cdd:cd23285    28 RYEDGRISSQGQQVTGYPHKDANNQWQIL-PTDPIDEHEGTGRPVRNGDLIRLRHVSTDTYLLTHDVASPLTPTNMEFTT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  94 yIDYNISMPAQN--LWKLDIVNRESNrDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSPGyhESMVW 171
Cdd:cd23285   107 -VSDDDTDERYNetLFRVEIEDTDEG-DVLKTKSSHFRLIHVDTNVALWTHKKPLPDWGFGQQEVNGNKNIKD--KSNIW 182


                  ....
gi 1720401381 172 NVEE 175
Cdd:cd23285   183 VVDD 186
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 22-176 8.08e-38

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: 135.14  E-value: 8.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  22 SHQQQVTCYPFKDINNWWIVKDPGRHQLVVNN--PPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNI 99
Cdd:cd23284    33 SNQQQVTCYGHKDSNNEWIFERPRGLPSWDENdtDIEFIKDGDIVRLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTV 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401381 100 SMPAQNlWKLDIVNRESNRDTWK--TILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSPGYHESMVWNVEEH 176
Cdd:cd23284   113 GDEKDN-WVIEIVKQVGSEDPKKlhTLTTSFRLRHEVLGCYLAQTGVSLPEWGFKQGEVVCDKSNFKRDKRTWWNIETH 190
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 22-178 2.41e-35

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: 128.58  E-value: 2.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  22 SHQQQVTCYPFKDINNWWIVKDPGRHQLVvNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDyNISM 101
Cdd:cd23282    32 ARQQQVTTYSHKDDNNLWLIKKHNQSSDL-SDPVEYVRHGDLIRLEHVNTKRNLHSHKEKAPLTKKHYQVTGYGE-NGTG 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401381 102 PAQNLWKLDIVNRESNrDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVgekLSPGYHE-SMVWNVEEHRY 178
Cdd:cd23282   110 DANDVWRVEVVGGREG-DPVKTVRSKFRLVHYNTGCALHSHGKQLPKWGWEQLEVT---CNPNVRDkNSLWNVEDNRN 183
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 19-175 2.77e-35

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: 128.57  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  19 RGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLS--PHSQEVSCYID 96
Cdd:cd23283    27 PAGSKQQQITLYPHRDENNDWLVELANAPEEWSPTTFENLKDGDVVRLEHVATGRRLHSHDHRPPVSdnDWQNEVSAYGY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  97 YNISMPAQNLWKLDIVNRESNRD----TWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKlSPGYHESmVWN 172
Cdd:cd23283   107 EGFEGDANDDWRVEILKDDSRPGeskeRVRAIDTKFRLVHVMTGCYLFSHGVKLPEWGFEQQEVTCAK-SGLLELS-LWY 184


                  ...
gi 1720401381 173 VEE 175
Cdd:cd23283   185 IET 187
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 20-157 2.18e-21

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: 90.96  E-value: 2.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  20 GSSHQQQVTCYPFK-DINNWWIVKDPGRHQLV-VNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPH--SQEVSCYI 95
Cdd:cd23286    28 SGSNEQQVTLYDFEdDANNEWIIETKTKEQMDkFPGQFREVRDGDVIRLRHVVTGKLLRASNARPPVSEQeyNNEVSCTG 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401381  96 DYNISMPAQNLWKLDIVNRESNRDTW------KTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVV 157
Cdd:cd23286   108 NANYSGDMDENWRIDVKGDESHAELKlpnikiKSTESVFQLYNRGTGCTLLSHDTRLPDWAFHQQEVL 175
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 18-159 2.79e-16

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: 76.18  E-value: 2.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  18 GRGSShQQQVTCYP-FKDINNWWIVK----DPGRHQlvvnnpPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHsQEVS 92
Cdd:cd23279    24 GSGSG-QQSVTAVPsADDANSLWTVLpglgEPCQEQ------GKPVKCGDIIRLQHVNTRKNLHSHNHSSPLSGN-QEVS 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401381  93 CY--IDYNISmpaqNLWKLDIVNreSNRDTWKtILSEVRFVHVNTSAILKLSGAHLpdwgFRQLEVVGE 159
Cdd:cd23279    96 AFggGDEDSG----DNWIVECEG--KKAKFWK-RGEPVRLKHVDTGKYLSASKTHK----FTQQPIAGQ 153
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 18-139 2.32e-12

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: 65.09  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  18 GRGSShQQQVTCYPFK-DINNWWIVKDPGRHQLVvnnPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSpHSQEVSCYID 96
Cdd:cd23294    26 GSGSG-QQSVTGFPGVdDSNSYWIVKPANGERCK---QGDVIKNGDVIRLQHVSTRKWLHSHLHASPLS-GNQEVSCFGG 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720401381  97 YNISMPAQNlWKLDIvnrESNRDTWKTIlSEVRFVHVNTSAIL 139
Cdd:cd23294   101 DGNSDTGDN-WIVEI---EGGGKVWERD-QKVRLKHVDTGGYL 138
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 20-158 1.73e-10

MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 (SDF-2); The metazoan SDF-2 family includes SDF-2 and SDF2-like protein 1 (SDF2L1). SDF-2 is a secretory protein involved in multiple endoplasmic reticulum (ER) functions, including the misfolded protein catabolic process, protein glycosylation, and ER protein quality control. SDF2L1, also called PWP1-interacting protein 8, is an endoplasmic reticulum (ER)-localized protein that plays a role in ER-associated degradation (ERAD) of misfolded proinsulin in pancreatic beta-cells. It is a component of the endoplasmic reticulum (ER) chaperone complex and interacts with alpha- and beta-defensins. SDF2L1 may also act as a tumor suppressor that play an important role in a variety of cancers, such as breast cancer and ovarian cancer. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467764 [Multi-domain]  Cd Length: 175  Bit Score: 59.59  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  20 GS-SHQQQVTCYPFK-DINNWWIVKdpGRHQLVVNNPpRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSpHSQEVSCYIDY 97
Cdd:cd23293    26 GSgSGQQSVTGVESSdDSNSYWQIR--GPTGADCERG-TPIKCGQTIRLTHLNTGKNLHSHHFQSPLS-GNQEVSAFGED 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720401381  98 NISMPAQNlWKLDIVNRESNRDtwktilSEVRFVHVNTSAILKLSGAHL--PDWGfrQLEVVG 158
Cdd:cd23293   102 GEGDTGDN-WTVVCSGTYWERD------EAVRLKHVDTEVYLHVTGEQYgrPIHG--QREVSG 155
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 21-160 1.73e-10

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 59.32  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381  21 SSHQQQVTCY---PFKDINNWWIVkdpgrhQLVVNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDY 97
Cdd:cd23263    25 GSGQQEVTFEsssRKGDTNGLWII------ESENGKQGGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDN 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720401381  98 NISmpaQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEK 160
Cdd:cd23263    99 PDK---SSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNINNKTQQEVICHG 158
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 211-403 1.81e-10

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 62.60  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 211 ELQWKMLTL-KNEDLEHQYSSTPLEWLTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWTSASLATVVytlLFF 278
Cdd:COG1928   309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPALLW---LLW 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401381 279 WYLLRRRrsicdlpedaWsrwvLAGALCTgGWALNYLPFFL-MERVLFLYHYLPALTFQILLLPIVLQH---ASDHLCRS 354
Cdd:COG1928   386 RWIARRD----------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLilgPARASERR 450

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401381 355 QLQRNV---FSALVVA----WYssachvsnmlrPLTYGDTsLSPGELRALRWKDSW 403
Cdd:COG1928   451 RLGRLVvglYVGLVVAnfafFY-----------PILTGLP-IPYDEWQARMWFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
126-176 3.62e-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: 3.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720401381  126 SEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 176
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
55-112 2.61e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 38.86  E-value: 2.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720401381   55 PRPVRHGDIVQLVHGMTTRLLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWKLDIV 112
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 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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