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Conserved domains on  [gi|1759490467|ref|NP_001361618|]
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protein O-mannosyl-transferase 1 isoform l [Homo sapiens]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 1001097)

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

EC:  2.4.1.109
Gene Ontology:  GO:0000030|GO:0016740|GO:0016757|GO:0005789
PubMed:  31285605|20378538|15809069

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 ...
 324-489 8.21e-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: 325.42  E-value: 8.21e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 324 VRYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVS 403
Cdd:cd23281    28 IKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDIIQLVHGKTGRFLNSHDVAAPLSPTHQEVS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 404 CYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRgyHGSTVWN 483
Cdd:cd23281   108 CYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSGKQLPDWGFGQLEVATDRAGN--QSSTVWN 185


                  ....*.
gi 1759490467 484 VEEHRY 489
Cdd:cd23281   186 VEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 1-181 1.92e-59

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: 200.61  E-value: 1.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467   1 MKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SNVPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAA 79
Cdd:pfam02366  36 AEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  80 MGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqkHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVL 159
Cdd:pfam02366 115 LLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLP 191

                         170       180
                  ....*....|....*....|..
gi 1759490467 160 VLGVAAVHAWHLLGDQTLSNVG 181
Cdd:pfam02366 192 VGLLTIWHLWQLLGDLSLLLKS 213
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 518-712 1.45e-57

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: 193.92  E-value: 1.45e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 518 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 596
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 597 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 673
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1759490467 674 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 712
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 ...
 324-489 8.21e-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: 325.42  E-value: 8.21e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 324 VRYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVS 403
Cdd:cd23281    28 IKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDIIQLVHGKTGRFLNSHDVAAPLSPTHQEVS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 404 CYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRgyHGSTVWN 483
Cdd:cd23281   108 CYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSGKQLPDWGFGQLEVATDRAGN--QSSTVWN 185


                  ....*.
gi 1759490467 484 VEEHRY 489
Cdd:cd23281   186 VEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 1-181 1.92e-59

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: 200.61  E-value: 1.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467   1 MKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SNVPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAA 79
Cdd:pfam02366  36 AEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  80 MGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqkHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVL 159
Cdd:pfam02366 115 LLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLP 191

                         170       180
                  ....*....|....*....|..
gi 1759490467 160 VLGVAAVHAWHLLGDQTLSNVG 181
Cdd:pfam02366 192 VGLLTIWHLWQLLGDLSLLLKS 213
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 518-712 1.45e-57

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: 193.92  E-value: 1.45e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 518 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 596
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 597 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 673
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1759490467 674 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 712
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 522-714 1.06e-11

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 67.61  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 522 ELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWVSGSLALaiyaLLSL 589
Cdd:COG1928   309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPAL----LWLL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 590 WYLLRRRRnvhdlpqdaWlrwvLAGALCAgGWAVNYLPFFL-MEKTLFLYHYLPALTFQILLLPVVLQHI---SDHLCRS 665
Cdd:COG1928   385 WRWIARRD---------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLIlgpARASERR 450

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1759490467 666 QLQRSI---FSALVVA----WYssachvsntlrPLTYGDkSLSPHELKALRWKDSW 714
Cdd:COG1928   451 RLGRLVvglYVGLVVAnfafFY-----------PILTGL-PIPYDEWQARMWFPSW 494
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 12-169 2.04e-09

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


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 59.64  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  12 PPFGHMVLALGGYLGGfdgnflwnrigaeyssnVPVWSLRLLPALAGALSVPMAYQIVLELhFSHCAAMGAALLMLIENA 91
Cdd:COG1807    65 PPLIYWLIALSYKLFG-----------------VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPL 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1759490467  92 LITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKhspfslswWFWLTLTGVACSCAVGIKYMGVFtyVLVLGVAAVHAW 169
Cdd:COG1807   127 LLLFGRLATPDALLLLFWTLALYALLRALERRR--------LRWLLLAGLALGLGFLTKGPVAL--LLPGLALLLYLL 194
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 333-466 5.99e-08

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: 53.14  E-value: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 333 SHQQQVTCYPFKDVNN----WWIVkdprrhqLVVSSPP---RPVRHGDMVQLVHGMTTRSLNTHDV-AAPLSPHS---QE 401
Cdd:pfam02815  29 QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLRHLTTGRYLHSHEEqKPPLVEKEdwqKE 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1759490467 402 VSCYiDYNISmpAQNLWRLEIVNR----GSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLE 466
Cdd:pfam02815 102 VSAY-GFRGF--PGDNDIVEIFEKksttGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGPEQ 167
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
366-423 6.40e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.17  E-value: 6.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1759490467  366 PRPVRHGDMVQLVHGMTTRSLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWRLEIV 423
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 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 ...
 324-489 8.21e-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: 325.42  E-value: 8.21e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 324 VRYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVS 403
Cdd:cd23281    28 IKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHGDIIQLVHGKTGRFLNSHDVAAPLSPTHQEVS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 404 CYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRgyHGSTVWN 483
Cdd:cd23281   108 CYIDYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSGKQLPDWGFGQLEVATDRAGN--QSSTVWN 185


                  ....*.
gi 1759490467 484 VEEHRY 489
Cdd:cd23281   186 VEEHRY 191
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 1-181 1.92e-59

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: 200.61  E-value: 1.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467   1 MKQIFFLDDSgPPFGHMVLALGGYLGGFDGNFLWNRIGAEYS-SNVPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAA 79
Cdd:pfam02366  36 AEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  80 MGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqkHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVL 159
Cdd:pfam02366 115 LLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLP 191

                         170       180
                  ....*....|....*....|..
gi 1759490467 160 VLGVAAVHAWHLLGDQTLSNVG 181
Cdd:pfam02366 192 VGLLTIWHLWQLLGDLSLLLKS 213
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 518-712 1.45e-57

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: 193.92  E-value: 1.45e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 518 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 596
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 597 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 673
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRlpRSLRKRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1759490467 674 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 712
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 ...
 322-487 2.52e-56

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: 190.24  E-value: 2.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 322 HDVRYENGrgsSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQE 401
Cdd:cd23276    22 HNHTYPDG---SKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDPEYVRDGDEVRLLHKETNRYLRTHDAAAPVTSKHKE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 402 VSCYIDYNISMPAQNLWRLEIVN--RGSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRGyHGS 479
Cdd:cd23276    99 VSAYPDENEDGDDNDLWVVEIVKdeGKLEDKRIKPLTTRFRLRNKKTGCYLTSSGVKLPEWGFRQGEVVCSKNKES-DPS 177


                  ....*...
gi 1759490467 480 TVWNVEEH 487
Cdd:cd23276   178 TLWNVEEN 185
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 325-486 5.25e-41

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: 148.21  E-value: 5.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 325 RYENGRGSSHQQQVTCYPFKDVNNWWIVKdPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSC 404
Cdd:cd23285    28 RYEDGRISSQGQQVTGYPHKDANNQWQIL-PTDPIDEHEGTGRPVRNGDLIRLRHVSTDTYLLTHDVASPLTPTNMEFTT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 405 yIDYNISMPAQN--LWRLEIVNrGSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKlsRGYHGSTVW 482
Cdd:cd23285   107 -VSDDDTDERYNetLFRVEIED-TDEGDVLKTKSSHFRLIHVDTNVALWTHKKPLPDWGFGQQEVNGNK--NIKDKSNIW 182


                  ....
gi 1759490467 483 NVEE 486
Cdd:cd23285   183 VVDD 186
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 322-489 1.25e-37

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: 138.59  E-value: 1.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 322 HDVRYENGRGSsHQQQVTCYPFKDVNNWWIVKDPRRHQLVvSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQE 401
Cdd:cd23282    22 HWHLYPEGVGA-RQQQVTTYSHKDDNNLWLIKKHNQSSDL-SDPVEYVRHGDLIRLEHVNTKRNLHSHKEKAPLTKKHYQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 402 VSCYIDyNISMPAQNLWRLEIVNrGSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRgyHGSTV 481
Cdd:cd23282   100 VTGYGE-NGTGDANDVWRVEVVG-GREGDPVKTVRSKFRLVHYNTGCALHSHGKQLPKWGWEQLEVTCNPNVR--DKNSL 175


                  ....*...
gi 1759490467 482 WNVEEHRY 489
Cdd:cd23282   176 WNVEDNRN 183
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 333-487 2.00e-37

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: 138.22  E-value: 2.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 333 SHQQQVTCYPFKDVNNWWIVKDPRRHQL--VVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNI 410
Cdd:cd23284    33 SNQQQVTCYGHKDSNNEWIFERPRGLPSwdENDTDIEFIKDGDIVRLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTV 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1759490467 411 SMPAQNlWRLEIVNRGSDTDVWK--TILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRGYHGSTVWNVEEH 487
Cdd:cd23284   113 GDEKDN-WVIEIVKQVGSEDPKKlhTLTTSFRLRHEVLGCYLAQTGVSLPEWGFKQGEVVCDKSNFKRDKRTWWNIETH 190
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 326-486 3.63e-37

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: 137.43  E-value: 3.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 326 YENGrgsSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLS--PHSQEVS 403
Cdd:cd23283    26 YPAG---SKQQQITLYPHRDENNDWLVELANAPEEWSPTTFENLKDGDVVRLEHVATGRRLHSHDHRPPVSdnDWQNEVS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 404 CYIDYNISMPAQNLWRLEIVNRGSDTDV----WKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKlsRGYHGS 479
Cdd:cd23283   103 AYGYEGFEGDANDDWRVEILKDDSRPGEskerVRAIDTKFRLVHVMTGCYLFSHGVKLPEWGFEQQEVTCAK--SGLLEL 180


                  ....*..
gi 1759490467 480 TVWNVEE 486
Cdd:cd23283   181 SLWYIET 187
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 322-468 4.91e-19

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: 85.57  E-value: 4.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 322 HDVRYENGrgsSHQQQVTCYPFK-DVNNWWIVKDPRRHQLVVSSPP-RPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPH- 398
Cdd:cd23286    22 HDLTYPSG---SNEQQVTLYDFEdDANNEWIIETKTKEQMDKFPGQfREVRDGDVIRLRHVVTGKLLRASNARPPVSEQe 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1759490467 399 -SQEVSCYIDYNISMPAQNLWRLEIV-------NRGSDTDVwKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIV 468
Cdd:cd23286    99 yNNEVSCTGNANYSGDMDENWRIDVKgdeshaeLKLPNIKI-KSTESVFQLYNRGTGCTLLSHDTRLPDWAFHQQEVL 175
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 322-470 2.73e-18

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: 82.73  E-value: 2.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 322 HDVRYenGRGSShQQQVTCYP-FKDVNNWWIVK----DPRRHQlvvsspPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLS 396
Cdd:cd23279    19 HEVSY--GSGSG-QQSVTAVPsADDANSLWTVLpglgEPCQEQ------GKPVKCGDIIRLQHVNTRKNLHSHNHSSPLS 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1759490467 397 PHsQEVSCY--IDYNISmpaqNLWRLEIVnrGSDTDVWKtILSEVRFVHVNTSAVLKLSGAHLpdwgYRQLEIVGE 470
Cdd:cd23279    90 GN-QEVSAFggGDEDSG----DNWIVECE--GKKAKFWK-RGEPVRLKHVDTGKYLSASKTHK----FTQQPIAGQ 153
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 322-489 1.42e-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: 75.10  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 322 HDVRYenGRGSShQQQVTCYPFK-DVNNWWIVKDPRRHQLVVSSPprpVRHGDMVQLVHGMTTRSLNTHDVAAPLSpHSQ 400
Cdd:cd23294    21 HEVPY--GSGSG-QQSVTGFPGVdDSNSYWIVKPANGERCKQGDV---IKNGDVIRLQHVSTRKWLHSHLHASPLS-GNQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 401 EVSCYIDYNISMPAQNlWRLEIVNRGsdtDVWKTIlSEVRFVHVNTSAVLklsgaHLPDWGYR-----QLEIVGeklSRG 475
Cdd:cd23294    94 EVSCFGGDGNSDTGDN-WIVEIEGGG---KVWERD-QKVRLKHVDTGGYL-----HSHDKKYGrpipgQQEVCA---VAS 160

                         170
                  ....*....|....
gi 1759490467 476 YHGSTVWNVEEHRY 489
Cdd:cd23294   161 KNSNTLWLAAEGVY 174
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 322-486 1.16e-14

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


Pssm-ID: 467764 [Multi-domain]  Cd Length: 175  Bit Score: 72.69  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 322 HDVRYENGRGsshQQQVTCYPFK-DVNNWWIVKDPRRHQLvvsspPR--PVRHGDMVQLVHGMTTRSLNTHDVAAPLSpH 398
Cdd:cd23293    21 HDVKYGSGSG---QQSVTGVESSdDSNSYWQIRGPTGADC-----ERgtPIKCGQTIRLTHLNTGKNLHSHHFQSPLS-G 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 399 SQEVSCYIDYnismpaqnlwrleivNRGSDTDVWKTILS--------EVRFVHVNTSAVLKLSGAHL--PDWGyrQLEIV 468
Cdd:cd23293    92 NQEVSAFGED---------------GEGDTGDNWTVVCSgtywerdeAVRLKHVDTEVYLHVTGEQYgrPIHG--QREVS 154

                         170
                  ....*....|....*....
gi 1759490467 469 G-EKLSRGyhgsTVWNVEE 486
Cdd:cd23293   155 GmSSPSQA----NYWKAME 169
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 307-485 1.27e-12

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: 66.64  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 307 ETCALLASfppghlpHDVRYENGrgsSHQQQVTCY---PFKDVNNWWIVKDPRRHQLvvssppRPVRHGDMVQLVHGMTT 383
Cdd:cd23263    10 ETGKYLHS-------HRKNYPTG---SGQQEVTFEsssRKGDTNGLWIIESENGKQG------GPVKWGDKIRLRHLSTG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 384 RSLNTHDVAAPLSPHSQEVSCYIDYNISmpaQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYR 463
Cdd:cd23263    74 KYLSSEEGKKSPKSNHQEVLCLTDNPDK---SSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNINNKT 150

                         170       180
                  ....*....|....*....|..
gi 1759490467 464 QLEIVGEKlsRGYHGSTVWNVE 485
Cdd:cd23263   151 QQEVICHG--EREEVFKLWKAE 170
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 522-714 1.06e-11

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 67.61  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 522 ELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLH-----------PRTSAQIHLLGNIVIWVSGSLALaiyaLLSL 589
Cdd:COG1928   309 HYHQQILSFhTGLSSPHPYESKPWSWPLMLRPVSYYYEtgqtgtlgcgaGKCVRAVLAIGNPALWWLGLPAL----LWLL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 590 WYLLRRRRnvhdlpqdaWlrwvLAGALCAgGWAVNYLPFFL-MEKTLFLYHYLPALTFQILLLPVVLQHI---SDHLCRS 665
Cdd:COG1928   385 WRWIARRD---------W----RAGAVLV-GYAAGWLPWFLyLDRTMFFFYAIPFVPFLVLALALVLGLIlgpARASERR 450

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1759490467 666 QLQRSI---FSALVVA----WYssachvsntlrPLTYGDkSLSPHELKALRWKDSW 714
Cdd:COG1928   451 RLGRLVvglYVGLVVAnfafFY-----------PILTGL-PIPYDEWQARMWFPSW 494
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 12-169 2.04e-09

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


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 59.64  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  12 PPFGHMVLALGGYLGGfdgnflwnrigaeyssnVPVWSLRLLPALAGALSVPMAYQIVLELhFSHCAAMGAALLMLIENA 91
Cdd:COG1807    65 PPLIYWLIALSYKLFG-----------------VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPL 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1759490467  92 LITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKhspfslswWFWLTLTGVACSCAVGIKYMGVFtyVLVLGVAAVHAW 169
Cdd:COG1807   127 LLLFGRLATPDALLLLFWTLALYALLRALERRR--------LRWLLLAGLALGLGFLTKGPVAL--LLPGLALLLYLL 194
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 333-466 5.99e-08

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: 53.14  E-value: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467 333 SHQQQVTCYPFKDVNN----WWIVkdprrhqLVVSSPP---RPVRHGDMVQLVHGMTTRSLNTHDV-AAPLSPHS---QE 401
Cdd:pfam02815  29 QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLRHLTTGRYLHSHEEqKPPLVEKEdwqKE 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1759490467 402 VSCYiDYNISmpAQNLWRLEIVNR----GSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLE 466
Cdd:pfam02815 102 VSAY-GFRGF--PGDNDIVEIFEKksttGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGPEQ 167
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 49-172 6.11e-06

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


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 49.66  E-value: 6.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  49 SLRLLPALAGALSVPMAYqiVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKhspf 128
Cdd:COG4745    87 TARLPVALVGGLLPLLAL--LLRERLGDAEVLALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVRAIDTRR---- 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1759490467 129 slswWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLL 172
Cdd:COG4745   161 ----RRYLYLAAVALALAFATKENAVLYLLCWLGALLLLLDHRL 200
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 10-169 2.14e-05

Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are not captured by pfam02366.


Pssm-ID: 433048 [Multi-domain]  Cd Length: 160  Bit Score: 45.33  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  10 SGPPFGHMVLALGGYLGGFDGnflwnrigaeyssnvpvWSLRLLPALAGALSVPMAYQIVLELhFSHCAAMGAALLMLIE 89
Cdd:pfam13231   1 DHPPLAAWLIALFTALFGDSE-----------------WAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVV 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  90 NALITQSRLMLLESVLIFFNLLAVLSYLKFfnCQKHspfSLSWWFWLtltGVACSCAVGIKYMGVFTYVLVLGVAAVHAW 169
Cdd:pfam13231  63 PLFVALSRLFTPDAPLLLFWALALYFLLRA--LEKG---RLKWWLLA---GAAAGLGFLSKYTAALLVLAALLYLLISPG 134
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
366-423 6.40e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.17  E-value: 6.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1759490467  366 PRPVRHGDMVQLVHGMTTRSLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWRLEIV 423
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
437-487 1.32e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.32  E-value: 1.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1759490467  437 SEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRGyHGSTVWNVEEH 487
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAI-DANTLWLIEPV 57
COG5305 COG5305
Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT ...
 47-172 6.69e-03

Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT family [General function prediction only];


Pssm-ID: 444104 [Multi-domain]  Cd Length: 402  Bit Score: 39.63  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490467  47 VWSLRLLPALAGALSVPMAYQIVLELHFSHCAAMGAALLMLIENALITQSRlmllE----SVLIFFNLLAVLSYLKFFNC 122
Cdd:COG5305   107 EWALRSLSALFGLLAIPLIYWLGRELFRSRRVALLAAALMAVSPFHIYYAQ----EarmySLLTLLVLLSLLALLRALRR 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1759490467 123 QkhspfSLSWWFWLTLTGVAcscavgikymGVFTYVLVLGVAAVHAWHLL 172
Cdd:COG5305   183 P-----TRRLWLLYALANAL----------GLYTHYFFALVLIAHGLYLL 217
 
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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