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Conserved domains on  [gi|847153854|ref|XP_012823681|]
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protein O-mannosyl-transferase 1 isoform X1 [Xenopus tropicalis]

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 4.06e-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: 372.80  E-value: 4.06e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLKNTLGkpVPCWLHSHKHTYPVRYEGGRGSSHQQQVTCYPYKDVNNWWIVKDPARQQMVVDSPPRPIRHGDT 378
Cdd:cd23281    1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 379 VQLLHGMSARFLNTHDVAAPFSPYSQEVSCYIDYNISMPAQSLWKVEIVNRESDMDTWKTIISEVKLIHVNTSAALKLSG 458
Cdd:cd23281   79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 847153854 459 TALPDWGFRQLEVVGDKASKsyHQSLVWNVEEHRY 493
Cdd:cd23281  159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-267 8.86e-61

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: 204.47  E-value: 8.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854   20 VALTILGLVSRLWRLSYPQAVVFDEVYYGQFISLYMKRIFYLDDSgPPLGHMLLALGGYVADFDGNFMWNRIGAEYS-SN 98
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854   99 VPVWSLRLLPALSGALCVPLAYQIVVELGFSARAGLAAGFLLLFENALITQSRLMLLESVLIFFILLALLSYLKFHgcqR 178
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---R 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  179 RSPFSVSWWFWLLLTGISCTFAIGVKYMGLFSYLLILGVAAVHYWQLIGDQTLGNVWLLFHLLARCLALLLMPVLLYLGI 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 847153854  259 FYLHLSILT 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 1.00e-47

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: 167.34  E-value: 1.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  522 SRFWELQWKMLTM-RTESSEHKYSSYPMDWITMDTSIAYWLHPKSTAQIQLLGNPVIWNSANLGALIYSALLIFYLLRQR 600
Cdd:pfam16192   1 KKFIELQKAMLTSnNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  601 RRIYDI-PQGSWEALQLTGVLFLGGWAVNYLPFFLMEKTLFLYHYLPALTCQILLLPPL--LEHLHQHLLRSEALQNTFA 677
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALldFLLSLFRRLPRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 847153854  678 ALLLVWGCSVYLTYRKICPLTYGDPPLSpAELRSLRWKD 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 4.06e-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: 372.80  E-value: 4.06e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLKNTLGkpVPCWLHSHKHTYPVRYEGGRGSSHQQQVTCYPYKDVNNWWIVKDPARQQMVVDSPPRPIRHGDT 378
Cdd:cd23281    1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 379 VQLLHGMSARFLNTHDVAAPFSPYSQEVSCYIDYNISMPAQSLWKVEIVNRESDMDTWKTIISEVKLIHVNTSAALKLSG 458
Cdd:cd23281   79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 847153854 459 TALPDWGFRQLEVVGDKASKsyHQSLVWNVEEHRY 493
Cdd:cd23281  159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-267 8.86e-61

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: 204.47  E-value: 8.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854   20 VALTILGLVSRLWRLSYPQAVVFDEVYYGQFISLYMKRIFYLDDSgPPLGHMLLALGGYVADFDGNFMWNRIGAEYS-SN 98
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854   99 VPVWSLRLLPALSGALCVPLAYQIVVELGFSARAGLAAGFLLLFENALITQSRLMLLESVLIFFILLALLSYLKFHgcqR 178
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---R 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  179 RSPFSVSWWFWLLLTGISCTFAIGVKYMGLFSYLLILGVAAVHYWQLIGDQTLGNVWLLFHLLARCLALLLMPVLLYLGI 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 847153854  259 FYLHLSILT 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 1.00e-47

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: 167.34  E-value: 1.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  522 SRFWELQWKMLTM-RTESSEHKYSSYPMDWITMDTSIAYWLHPKSTAQIQLLGNPVIWNSANLGALIYSALLIFYLLRQR 600
Cdd:pfam16192   1 KKFIELQKAMLTSnNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  601 RRIYDI-PQGSWEALQLTGVLFLGGWAVNYLPFFLMEKTLFLYHYLPALTCQILLLPPL--LEHLHQHLLRSEALQNTFA 677
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALldFLLSLFRRLPRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 847153854  678 ALLLVWGCSVYLTYRKICPLTYGDPPLSpAELRSLRWKD 716
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 20-220 5.38e-15

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 78.40  E-value: 5.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  20 VALTILGLVSRLWRLSYPQAVVFDEVYYGQFISLYMKRIFYLDDSG--------PPLGHMLLALGgyvadfdgnfMWnri 91
Cdd:COG1928   26 LLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNGYERNWPDpgpffvvhPPLGKWLIALG----------EW--- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  92 gaeYSSNVPVWSLRLLPALSGALCVPLAYQIVVELGFSARAGLAAGFLLLFENALITQSRLMLLES-------------- 157
Cdd:COG1928   93 ---LFGYVNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIflmffvlaafgcll 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 847153854 158 VLIFFILLALLSYLKFHGCQRRSPFSVSWWFWLLLTGISCTFAIGVKYMGLFsYLLILGVAAV 220
Cdd:COG1928  170 LDRDQVRRRLAAAVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTV 231
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 312-472 5.22e-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: 70.86  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  312 GKPVPCWLHSHKHTYPVRYEGGRGSsHQQQVTCYPYKDVNN----WWIVKdparqqmVVDSPP---RPIRHGDTVQLLHG 384
Cdd:pfam02815   5 GGDVVRLFHSHQDEYLTGSEQQQKQ-PFLRITLYPHGDANNsarsLWRIE-------VVRHDAwrgGLIKWGSPFRLRHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  385 MSARFLNTHDVAAPF----SPYSQEVSCYiDYNISmpAQSLWKVEIVNRES----DMDTWKTIISEVKLIHVNTSAALKL 456
Cdd:pfam02815  77 TTGRYLHSHEEQKPPlvekEDWQKEVSAY-GFRGF--PGDNDIVEIFEKKSttgmGSDRIKPGDSYFRLQHVCTGCWLFS 153

                         170
                  ....*....|....*...
gi 847153854  457 SGTALPDWGFR--QLEVV 472
Cdd:pfam02815 154 HSVKLPKWGFGpeQQKVT 171
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 524-648 6.19e-09

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 59.14  E-value: 6.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 524 FWELQWKMLTMRTE-SSEHKYSSYPMDWITMDTSIAYWLHPKSTAQ-----------IQLLGNPVIWnsanLGALIYSAL 591
Cdd:COG1928  307 LWHYHQQILSFHTGlSSPHPYESKPWSWPLMLRPVSYYYETGQTGTlgcgagkcvraVLAIGNPALW----WLGLPALLW 382

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 847153854 592 LIFYLLRQRrriydipqgSWEALQLtgvlfLGGWAVNYLPFFL-MEKTLFLYHYLPAL 648
Cdd:COG1928  383 LLWRWIARR---------DWRAGAV-----LVGYAAGWLPWFLyLDRTMFFFYAIPFV 426
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
299-356 1.35e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 1.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 847153854   299 VVYGSQITLKN-TLGkpvpCWLHSHKHTYPvryeggRGSSHQQQVTCYPYK--DVNNWWIV 356
Cdd:smart00472   4 VRWGDVVRLRHvTTG----RYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLI 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 4.06e-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: 372.80  E-value: 4.06e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLKNTLGkpVPCWLHSHKHTYPVRYEGGRGSSHQQQVTCYPYKDVNNWWIVKDPARQQMVVDSPPRPIRHGDT 378
Cdd:cd23281    1 VAYGSQVTLRNTHG--SPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 379 VQLLHGMSARFLNTHDVAAPFSPYSQEVSCYIDYNISMPAQSLWKVEIVNRESDMDTWKTIISEVKLIHVNTSAALKLSG 458
Cdd:cd23281   79 IQLVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSG 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 847153854 459 TALPDWGFRQLEVVGDKASKsyHQSLVWNVEEHRY 493
Cdd:cd23281  159 KQLPDWGFGQLEVATDRAGN--QSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 299-491 1.63e-67

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: 220.28  E-value: 1.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLKNTlgKPVPCWLHSHKHTYPvryeggrGSSHQQQVTCYPYKDVNNWWIVKDPARQQMVVDSPPRPIRHGDT 378
Cdd:cd23276    1 VAYGSQITLRNA--NSGGGYLHSHNHTYP-------DGSKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDPEYVRDGDE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 379 VQLLHGMSARFLNTHDVAAPFSPYSQEVSCYIDYNISMPAQSLWKVEIVNRESDM--DTWKTIISEVKLIHVNTSAALKL 456
Cdd:cd23276   72 VRLLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGDDNDLWVVEIVKDEGKLedKRIKPLTTRFRLRNKKTGCYLTS 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 847153854 457 SGTALPDWGFRQLEVVGDKASKSyHQSLVWNVEEH 491
Cdd:cd23276  152 SGVKLPEWGFRQGEVVCSKNKES-DPSTLWNVEEN 185
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 20-267 8.86e-61

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: 204.47  E-value: 8.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854   20 VALTILGLVSRLWRLSYPQAVVFDEVYYGQFISLYMKRIFYLDDSgPPLGHMLLALGGYVADFDGNFMWNRIGAEYS-SN 98
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854   99 VPVWSLRLLPALSGALCVPLAYQIVVELGFSARAGLAAGFLLLFENALITQSRLMLLESVLIFFILLALLSYLKFHgcqR 178
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---R 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  179 RSPFSVSWWFWLLLTGISCTFAIGVKYMGLFSYLLILGVAAVHYWQLIGDQTLGNVWLLFHLLARCLALLLMPVLLYLGI 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236


                  ....*....
gi 847153854  259 FYLHLSILT 267
Cdd:pfam02366 237 FYVHFWLLF 245
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 299-490 4.89e-55

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: 186.73  E-value: 4.89e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLKNTLGKpvpCWLHSHKHTYPVRYEGGRGSSHQQQVTCYPYKDVNNWWIVKdPARQQMVVDSPPRPIRHGDT 378
Cdd:cd23285    1 VHYGDVITIKHRDTN---AFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQIL-PTDPIDEHEGTGRPVRNGDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 379 VQLLHGMSARFLNTHDVAAPFSPYSQEVSC------YIDYNismpaQSLWKVEIVNRESDmDTWKTIISEVKLIHVNTSA 452
Cdd:cd23285   77 IRLRHVSTDTYLLTHDVASPLTPTNMEFTTvsdddtDERYN-----ETLFRVEIEDTDEG-DVLKTKSSHFRLIHVDTNV 150

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 847153854 453 ALKLSGTALPDWGFRQLEVVGDKASKsyHQSLVWNVEE 490
Cdd:cd23285  151 ALWTHKKPLPDWGFGQQEVNGNKNIK--DKSNIWVVDD 186
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 296-491 1.75e-49

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: 171.73  E-value: 1.75e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 296 PLEVVYGSQITLKNTlgKPVPCWLHSHKHTYPvryEGgrgsSHQQQVTCYPYKDVNNWWIVKDPARQQM--VVDSPPRPI 373
Cdd:cd23284    1 PLDVAYGSKVTIKNQ--GLGGGLLHSHVQTYP---EG----SNQQQVTCYGHKDSNNEWIFERPRGLPSwdENDTDIEFI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 374 RHGDTVQLLHGMSARFLNTHDVAAPFSPYSQEVSCYIDYNISMPAQSlWKVEIVNRESDMDTWK--TIISEVKLIHVNTS 451
Cdd:cd23284   72 KDGDIVRLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDN-WVIEIVKQVGSEDPKKlhTLTTSFRLRHEVLG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 847153854 452 AALKLSGTALPDWGFRQLEVVGDKASKSYHQSLVWNVEEH 491
Cdd:cd23284  151 CYLAQTGVSLPEWGFKQGEVVCDKSNFKRDKRTWWNIETH 190
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 522-716 1.00e-47

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: 167.34  E-value: 1.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  522 SRFWELQWKMLTM-RTESSEHKYSSYPMDWITMDTSIAYWLHPKSTAQIQLLGNPVIWNSANLGALIYSALLIFYLLRQR 600
Cdd:pfam16192   1 KKFIELQKAMLTSnNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  601 RRIYDI-PQGSWEALQLTGVLFLGGWAVNYLPFFLMEKTLFLYHYLPALTCQILLLPPL--LEHLHQHLLRSEALQNTFA 677
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALldFLLSLFRRLPRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 847153854  678 ALLLVWGCSVYLTYRKICPLTYGDPPLSpAELRSLRWKD 716
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 299-490 1.42e-47

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: 166.70  E-value: 1.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLK--NTLGKpvpcWLHSHKHTYPvryeggrGSSHQQQVTCYPYKDVNNWWIVKDPARQQMVVDSPPRPIRHG 376
Cdd:cd23283    1 VAYGSTIRIRhlNTRGG----YLHSHPHNYP-------AGSKQQQITLYPHRDENNDWLVELANAPEEWSPTTFENLKDG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 377 DTVQLLHGMSARFLNTHDVAAPFS--PYSQEVSCYIDYNISMPAQSLWKVEIVNRESDMD----TWKTIISEVKLIHVNT 450
Cdd:cd23283   70 DVVRLEHVATGRRLHSHDHRPPVSdnDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGeskeRVRAIDTKFRLVHVMT 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 847153854 451 SAALKLSGTALPDWGFRQLEVVGDKASKsYHQSLvWNVEE 490
Cdd:cd23283  150 GCYLFSHGVKLPEWGFEQQEVTCAKSGL-LELSL-WYIET 187
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 299-493 3.18e-42

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: 151.30  E-value: 3.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLKN--TLGKpvpcWLHSHKHTYPVRYEggrgsSHQQQVTCYPYKDVNNWWIVKdPARQQMVVDSPPRPIRHG 376
Cdd:cd23282    1 VAYGSVITLKNhrTGGG----YLHSHWHLYPEGVG-----ARQQQVTTYSHKDDNNLWLIK-KHNQSSDLSDPVEYVRHG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 377 DTVQLLHGMSARFLNTHDVAAPFSPYSQEVSCYIDyNISMPAQSLWKVEIVNRESDmDTWKTIISEVKLIHVNTSAALKL 456
Cdd:cd23282   71 DLIRLEHVNTKRNLHSHKEKAPLTKKHYQVTGYGE-NGTGDANDVWRVEVVGGREG-DPVKTVRSKFRLVHYNTGCALHS 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 847153854 457 SGTALPDWGFRQLEVVGDKasKSYHQSLVWNVEEHRY 493
Cdd:cd23282  149 HGKQLPKWGWEQLEVTCNP--NVRDKNSLWNVEDNRN 183
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 299-472 1.05e-26

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: 107.91  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLKN--TLGKpvpcWLHSHKHTYPvryeggrGSSHQQQVTCYPYK-DVNNWWIVKDPARQQMV-VDSPPRPIR 374
Cdd:cd23286    1 LLYGSTVTIRHleSLGG----YLHSHDLTYP-------SGSNEQQVTLYDFEdDANNEWIIETKTKEQMDkFPGQFREVR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 375 HGDTVQLLHGMSARFLNTHDVAAPFSP--YSQEVSCYIDYNISMPAQSLWKVEIVNRESDMDTW------KTIISEVKLI 446
Cdd:cd23286   70 DGDVIRLRHVVTGKLLRASNARPPVSEqeYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKlpnikiKSTESVFQLY 149

                        170       180
                 ....*....|....*....|....*.
gi 847153854 447 HVNTSAALKLSGTALPDWGFRQLEVV 472
Cdd:cd23286  150 NRGTGCTLLSHDTRLPDWAFHQQEVL 175
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 301-490 8.72e-22

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: 93.13  E-value: 8.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 301 YGSQITLKNTLGKpvpCWLHSHKHTYpvryegGRGSShQQQVTCYP-YKDVNNWWIVK--DPARQQMVVDspprPIRHGD 377
Cdd:cd23279    1 YGSAIKLKHVNSG---YRLHSHEVSY------GSGSG-QQSVTAVPsADDANSLWTVLpgLGEPCQEQGK----PVKCGD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 378 TVQLLHGMSARFLNTHDVAAPFSPySQEVSCY--IDYNISmpaqSLWKVEIVNreSDMDTWKtIISEVKLIHVNTSAALk 455
Cdd:cd23279   67 IIRLQHVNTRKNLHSHNHSSPLSG-NQEVSAFggGDEDSG----DNWIVECEG--KKAKFWK-RGEPVRLKHVDTGKYL- 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 847153854 456 lsgTALPDWGFR------QLEVVGDKASKSYHQslvWNVEE 490
Cdd:cd23279  138 ---SASKTHKFTqqpiagQLEVSAASSKDSDSQ---WKAVE 172
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 299-454 1.04e-15

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: 75.49  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 299 VVYGSQITLKNtlgKPVPCWLHSHKHTYpvryegGRGSShQQQVTCYPYK-DVNNWWIVKDPARQQMVvdsPPRPIRHGD 377
Cdd:cd23294    1 VTCGSVIKLQH---ERTKFRLHSHEVPY------GSGSG-QQSVTGFPGVdDSNSYWIVKPANGERCK---QGDVIKNGD 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 847153854 378 TVQLLHGMSARFLNTHDVAAPFSPySQEVSCYIDYNISmPAQSLWKVEIvnrESDMDTWKTiISEVKLIHVNTSAAL 454
Cdd:cd23294   68 VIRLQHVSTRKWLHSHLHASPLSG-NQEVSCFGGDGNS-DTGDNWIVEI---EGGGKVWER-DQKVRLKHVDTGGYL 138
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 20-220 5.38e-15

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 78.40  E-value: 5.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  20 VALTILGLVSRLWRLSYPQAVVFDEVYYGQFISLYMKRIFYLDDSG--------PPLGHMLLALGgyvadfdgnfMWnri 91
Cdd:COG1928   26 LLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNGYERNWPDpgpffvvhPPLGKWLIALG----------EW--- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  92 gaeYSSNVPVWSLRLLPALSGALCVPLAYQIVVELGFSARAGLAAGFLLLFENALITQSRLMLLES-------------- 157
Cdd:COG1928   93 ---LFGYVNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIflmffvlaafgcll 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 847153854 158 VLIFFILLALLSYLKFHGCQRRSPFSVSWWFWLLLTGISCTFAIGVKYMGLFsYLLILGVAAV 220
Cdd:COG1928  170 LDRDQVRRRLAAAVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLY-FLAAFGLLTV 231
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 312-472 5.22e-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: 70.86  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  312 GKPVPCWLHSHKHTYPVRYEGGRGSsHQQQVTCYPYKDVNN----WWIVKdparqqmVVDSPP---RPIRHGDTVQLLHG 384
Cdd:pfam02815   5 GGDVVRLFHSHQDEYLTGSEQQQKQ-PFLRITLYPHGDANNsarsLWRIE-------VVRHDAwrgGLIKWGSPFRLRHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  385 MSARFLNTHDVAAPF----SPYSQEVSCYiDYNISmpAQSLWKVEIVNRES----DMDTWKTIISEVKLIHVNTSAALKL 456
Cdd:pfam02815  77 TTGRYLHSHEEQKPPlvekEDWQKEVSAY-GFRGF--PGDNDIVEIFEKKSttgmGSDRIKPGDSYFRLQHVCTGCWLFS 153

                         170
                  ....*....|....*...
gi 847153854  457 SGTALPDWGFR--QLEVV 472
Cdd:pfam02815 154 HSVKLPKWGFGpeQQKVT 171
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 319-490 1.29e-13

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: 69.61  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 319 LHSHKhtypVRYegGRGSShQQQVTCYPYK-DVNNWWIVKDPARQQMvvdspPR--PIRHGDTVQLLHGMSARFLNTHDV 395
Cdd:cd23293   18 LHSHD----VKY--GSGSG-QQSVTGVESSdDSNSYWQIRGPTGADC-----ERgtPIKCGQTIRLTHLNTGKNLHSHHF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 396 AAPFSPySQEVSCYIDynismpaqslwkveivNRESD-MDTWKTIIS--------EVKLIHVNTSAALKLSGTAL--PDW 464
Cdd:cd23293   86 QSPLSG-NQEVSAFGE----------------DGEGDtGDNWTVVCSgtywerdeAVRLKHVDTEVYLHVTGEQYgrPIH 148

                        170       180
                 ....*....|....*....|....*.
gi 847153854 465 GfrQLEVVGDKASKsyhQSLVWNVEE 490
Cdd:cd23293  149 G--QREVSGMSSPS---QANYWKAME 169
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 302-475 5.69e-13

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: 67.41  E-value: 5.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 302 GSQITLKNTlgkPVPCWLHSHKHTYPvryeggrGSSHQQQVTCYPYK---DVNNWWIVKdpaRQQMVVDSPprpIRHGDT 378
Cdd:cd23263    1 GDVIWLKHS---ETGKYLHSHRKNYP-------TGSGQQEVTFESSSrkgDTNGLWIIE---SENGKQGGP---VKWGDK 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 379 VQLLHGMSARFLNTHDVAAPFSPYSQEVSCYIDYNISmpaQSLWKVEIVNreSDMDTWKTIISE--VKLIHVNTSAALKL 456
Cdd:cd23263   65 IRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDK---SSLFKFEPIG--STKYKQKYVKKDsyFRLKHVNTNFWLHS 139

                        170
                 ....*....|....*....
gi 847153854 457 SGTALPDWGFRQLEVVGDK 475
Cdd:cd23263  140 HEKKFNINNKTQQEVICHG 158
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 524-648 6.19e-09

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 59.14  E-value: 6.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 524 FWELQWKMLTMRTE-SSEHKYSSYPMDWITMDTSIAYWLHPKSTAQ-----------IQLLGNPVIWnsanLGALIYSAL 591
Cdd:COG1928  307 LWHYHQQILSFHTGlSSPHPYESKPWSWPLMLRPVSYYYETGQTGTlgcgagkcvraVLAIGNPALW----WLGLPALLW 382

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 847153854 592 LIFYLLRQRrriydipqgSWEALQLtgvlfLGGWAVNYLPFFL-MEKTLFLYHYLPAL 648
Cdd:COG1928  383 LLWRWIARR---------DWRAGAV-----LVGYAAGWLPWFLyLDRTMFFFYAIPFV 426
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 19-220 1.11e-07

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: 54.24  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  19 FVALTILGLVSRLWRLSYPQAVVFDEVYY----------GQFISLYMKRIFYLDDsgPPLGHMLLALGGYVadfdgnfmw 88
Cdd:COG1807   10 LLLLLLLALLLRLLGLGSLPLWDPDEARYaeiaremlesGDWLTPTLAGEPYFDK--PPLIYWLIALSYKL--------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  89 nrigaeysSNVPVWSLRLLPALSGALCVPLAYQIVVELgFSARAGLAAGFLLLFENALITQSRLMLLESVLIFFILLALL 168
Cdd:COG1807   79 --------FGVSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALY 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 847153854 169 SYLKFHGCQRrspfsvswWFWLLLTGISCTFAIGVKY-MGLFSYLLILGVAAV 220
Cdd:COG1807  150 ALLRALERRR--------LRWLLLAGLALGLGFLTKGpVALLLPGLALLLYLL 194
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
299-356 1.35e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 1.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 847153854   299 VVYGSQITLKN-TLGkpvpCWLHSHKHTYPvryeggRGSSHQQQVTCYPYK--DVNNWWIV 356
Cdd:smart00472   4 VRWGDVVRLRHvTTG----RYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLI 54
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
441-491 2.02e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 2.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 847153854   441 SEVKLIHVNTSAALKLSGTALPDWGFRQLEVVGDKASKSYHQSLvWNVEEH 491
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDANTL-WLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
370-427 2.05e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 39.63  E-value: 2.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 847153854   370 PRPIRHGDTVQLLHGMSARFLNTHDVA-APFSPYSQEVSCYIDYNISmpAQSLWKVEIV 427
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 318-396 1.07e-03

MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2) and similar proteins; AtSDF2, also called SDF2-like protein, acts as a crucial component of the unfolded protein response (UPR) in Arabidopsis thaliana. It is involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. It may be involved in the quality control of glycoproteins. AtSDF2 forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity. AtSDF2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467765 [Multi-domain]  Cd Length: 176  Bit Score: 40.44  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854 318 WLHSHKHTYPVryeggrgsSHQQQVTCY---PYKDVNNWWIVkdparqqmVVDSPPRPIRHGDTVQLLHGMSARFLNTHD 394
Cdd:cd23294   79 WLHSHLHASPL--------SGNQEVSCFggdGNSDTGDNWIV--------EIEGGGKVWERDQKVRLKHVDTGGYLHSHD 142


                 ..
gi 847153854 395 VA 396
Cdd:cd23294  143 KK 144
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 102-222 3.74e-03

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: 38.78  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  102 WSLRLLPALSGALCVPLAYQIVVELgFSARAGLAAGFLLLFENALITQSRLMLLESVLIFFILLALlsYLKFHGCQRRSp 181
Cdd:pfam13231  22 WAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVVPLFVALSRLFTPDAPLLLFWALAL--YFLLRALEKGR- 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 847153854  182 fsvswWFWLLLTGISCTFAIGVKYmglfsYLLILGVAAVHY 222
Cdd:pfam13231  98 -----LKWWLLAGAAAGLGFLSKY-----TAALLVLAALLY 128
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 1-153 4.59e-03

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


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 40.42  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854   1 MAVSLKSPLVVTVAIDLHFVALTILGLVSRLWRLSypqAVVF--DEVYYGQFISLYMKRIFYLDDS---GPPLGHMLLAL 75
Cdd:COG4745    1 MSSSPLSSRTRRDRTLLAVLAITALALLLRLVGLG---ARPFhwDEARVAYWSLRLLETGAYEYRPiyhGPFLYHVTAAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153854  76 GGYVADFDgnfmwnrigaeyssnvpvWSLRLLPALSGALCVPLAYqivvelGFSARAG----LAAGFLLLFENALITQSR 151
Cdd:COG4745   78 FGLFGASD------------------FTARLPVALVGGLLPLLAL------LLRERLGdaevLALALLLAFSPVLVYYSR 133


                 ..
gi 847153854 152 LM 153
Cdd:COG4745  134 FM 135
 
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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