|
Name |
Accession |
Description |
Interval |
E-value |
| PMT1 |
COG1928 |
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ... |
14-720 |
3.04e-130 |
|
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 224839 [Multi-domain] Cd Length: 699 Bit Score: 401.87 E-value: 3.04e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 14 DINLNVVALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDgSGPPFGHMLLALGGYLGGFDGNFLWNRIG- 92
Cdd:COG1928 22 PYKLGPVLLTVLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFD-VHPPLGKMLIALVGGLEGYDPPFDFQLIGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 93 AEYSSNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLK 172
Cdd:COG1928 101 TEYPFGYNYVGMRFFNALLGSLTVPLVYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 173 FSNSQkhrPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPT 252
Cdd:COG1928 181 FHRQQ---PFSRRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 253 LMYLLFFYVHLILVYRSGPHDQIMSSAFQASLEGglARITQGQPLEVAYGSQVTLKNVfgKPVPCWLHSHQSTYPmiyen 332
Cdd:COG1928 258 DIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP----- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 333 grGSSHQQQVTCYPFKDVNNWWIVKdpgrHQLVVNNPPRPVRHGDVVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYvDY 412
Cdd:COG1928 329 --EGSEQQQVTGYGHKDANNEWLIE----LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 413 NISMPSQNLWRLDIVNRES--DTEVWKTILSEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSrgyHESMVWNVEE 490
Cdd:COG1928 402 SFEGDEKDDWIIEIVKDEAneDQERIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 491 HrygksqeqkerELELHSPAQMDVSRNLSFMARFLELQWRML-TAKSDDSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQI 569
Cdd:COG1928 479 N-----------VNDRLPNPEKKVYKKLSFWKKFIELNKAMFsSNNALVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKV 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 570 HLLGNIVIWASASLAMVVYVLLFFWYLLRRRRSICDIPEDSWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALT 649
Cdd:COG1928 548 YLMGNPALWWFSVPALAFFTGIVIWRLIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALY 627
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953099264 650 FQILLLPVVLQHVSDHLCRSQllRSLFSALVVAWYSCACHVFNTLRPLTYGdKSLSPSELKALRWKDSWDI 720
Cdd:COG1928 628 FAILALALVLDFILRRPSRER--RTLGLIVVAIFVALVIYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
|
|
| PMT |
pfam02366 |
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ... |
20-267 |
1.66e-69 |
|
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 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 undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 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: 227.58 E-value: 1.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 20 VALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDGSgPPFGHMLLALGGYLGGFDGNFLWNRIGAEYS-SN 98
Cdd:pfam02366 1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 99 VPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFsnsQK 178
Cdd:pfam02366 80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKF---ER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 179 HRPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPTLMYLLF 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236
|
....*....
gi 1953099264 259 FYVHLILVY 267
Cdd:pfam02366 237 FYVHFWLLF 245
|
|
| MIR |
smart00472 |
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
299-356 |
9.41e-07 |
|
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 46.18 E-value: 9.41e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 299 VAYGSQVTLKNVFGkpvPCWLHSHQSTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 356
Cdd:smart00472 4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PMT1 |
COG1928 |
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ... |
14-720 |
3.04e-130 |
|
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 224839 [Multi-domain] Cd Length: 699 Bit Score: 401.87 E-value: 3.04e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 14 DINLNVVALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDgSGPPFGHMLLALGGYLGGFDGNFLWNRIG- 92
Cdd:COG1928 22 PYKLGPVLLTVLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFD-VHPPLGKMLIALVGGLEGYDPPFDFQLIGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 93 AEYSSNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLK 172
Cdd:COG1928 101 TEYPFGYNYVGMRFFNALLGSLTVPLVYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 173 FSNSQkhrPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPT 252
Cdd:COG1928 181 FHRQQ---PFSRRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 253 LMYLLFFYVHLILVYRSGPHDQIMSSAFQASLEGglARITQGQPLEVAYGSQVTLKNVfgKPVPCWLHSHQSTYPmiyen 332
Cdd:COG1928 258 DIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP----- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 333 grGSSHQQQVTCYPFKDVNNWWIVKdpgrHQLVVNNPPRPVRHGDVVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYvDY 412
Cdd:COG1928 329 --EGSEQQQVTGYGHKDANNEWLIE----LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 413 NISMPSQNLWRLDIVNRES--DTEVWKTILSEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSrgyHESMVWNVEE 490
Cdd:COG1928 402 SFEGDEKDDWIIEIVKDEAneDQERIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 491 HrygksqeqkerELELHSPAQMDVSRNLSFMARFLELQWRML-TAKSDDSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQI 569
Cdd:COG1928 479 N-----------VNDRLPNPEKKVYKKLSFWKKFIELNKAMFsSNNALVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKV 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 570 HLLGNIVIWASASLAMVVYVLLFFWYLLRRRRSICDIPEDSWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALT 649
Cdd:COG1928 548 YLMGNPALWWFSVPALAFFTGIVIWRLIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALY 627
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953099264 650 FQILLLPVVLQHVSDHLCRSQllRSLFSALVVAWYSCACHVFNTLRPLTYGdKSLSPSELKALRWKDSWDI 720
Cdd:COG1928 628 FAILALALVLDFILRRPSRER--RTLGLIVVAIFVALVIYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
|
|
| PMT |
pfam02366 |
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ... |
20-267 |
1.66e-69 |
|
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 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 undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 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: 227.58 E-value: 1.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 20 VALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDGSgPPFGHMLLALGGYLGGFDGNFLWNRIGAEYS-SN 98
Cdd:pfam02366 1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 99 VPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFsnsQK 178
Cdd:pfam02366 80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKF---ER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 179 HRPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPTLMYLLF 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236
|
....*....
gi 1953099264 259 FYVHLILVY 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 |
3.60e-59 |
|
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: 435204 [Multi-domain] Cd Length: 198 Bit Score: 198.15 E-value: 3.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 522 ARFLELQWRMLTAKSD-DSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQIHLLGNIVIWASASLAMVVYVLLFFWYLLRRR 600
Cdd:pfam16192 1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 601 RSICDIPED-SWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALTFQILLLPVVLQHVSDHLCR--SQLLRSLFS 677
Cdd:pfam16192 81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFKRlpRSLRKRVGY 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1953099264 678 ALVVAWYSCACHVFNTLRPLTYGDKSLSpSELKALRWKD 716
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
|
|
| MIR |
pfam02815 |
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ... |
310-472 |
6.17e-17 |
|
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: 79.33 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 310 VFGKPVPCWLHSHQSTYPMIYENGRGSsHQQQVTCYPFKDVNN----WWIVkdpgrhqLVVNNPP---RPVRHGDVVQLV 382
Cdd:pfam02815 3 LKGGDVVRLFHSHQDEYLTGSEQQQKQ-PFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 383 HGMTTRFLNTHDV-AAPLSPHS---QEVSCYvDYNISM----PSQNLWRLDIVNRESDTEvwKTILSEVRLVHVNTSAVL 454
Cdd:pfam02815 75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGFPgdndIVEIFEKKSTTGMGSDRI--KPGDSYFRLQHVCTGCWL 151
|
170 180
....*....|....*....|
gi 1953099264 455 KLSGAHLPDWGF--QQLEVV 472
Cdd:pfam02815 152 FSHSVKLPKWGFgpEQQKVT 171
|
|
| MIR |
smart00472 |
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
299-356 |
9.41e-07 |
|
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 46.18 E-value: 9.41e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 299 VAYGSQVTLKNVFGkpvPCWLHSHQSTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 356
Cdd:smart00472 4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
|
|
| ArnT |
COG1807 |
4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell ... |
102-218 |
5.43e-06 |
|
4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224720 [Multi-domain] Cd Length: 535 Bit Score: 49.78 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 102 WSLRLLPALTGAFSIPMAYQILLELgFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKfsnsQKHRP 181
Cdd:COG1807 84 WSARLPSALAGALTALLVYWLAKRL-FGRLAALLAALILLLTPLFFLIGRLALLDAALAFFLTLALALLYL----ALRAR 158
|
90 100 110
....*....|....*....|....*....|....*..
gi 1953099264 182 FSLSWWFwlmLTGVACSCAVGVKYMGIFtYLLVLAVA 218
Cdd:COG1807 159 GKLKWLL---LLGLALGLGFLTKGPGAL-LLPLILLL 191
|
|
| MIR |
smart00472 |
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
370-427 |
2.35e-05 |
|
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 42.33 E-value: 2.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953099264 370 PRPVRHGDVVQLVHGMTTRFLNTHDVA-APLSPHSQEVSCYVDYNISmpSQNLWRLDIV 427
Cdd:smart00472 1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
|
|
| MIR |
smart00472 |
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
441-491 |
2.98e-05 |
|
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 41.94 E-value: 2.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1953099264 441 SEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSRGyHESMVWNVEEH 491
Cdd:smart00472 8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAI-DANTLWLIEPV 57
|
|
| COG4745 |
COG4745 |
Predicted membrane-bound mannosyltransferase [General function prediction only]; |
17-216 |
9.09e-03 |
|
Predicted membrane-bound mannosyltransferase [General function prediction only];
Pssm-ID: 227088 Cd Length: 556 Bit Score: 39.08 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 17 LNVVALTAVGLLSRLWHLAYpRAVVFDEVYYGQYISFYMkriFFLDGSGPPFGHmllalggylggfdGNFLWnrigaeYS 96
Cdd:COG4745 16 LAVIAVVAIALLARLYNLGL-RPFHFDESRHATWILKYL---EQGAWSYRPIYH-------------GPFLY------HV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 97 SNVPV-------WSLRLLPALTGAFSIPMAYQILLELGfsHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVls 169
Cdd:COG4745 73 NYAVFgllgasdATARLVVAVTGVLLPLTAWLYRTRLG--DKEVLALATLLAFSPVLVYYSRFMRNDLLLAAFTLLAV-- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953099264 170 YLKFSNSQKHRPfslswwFWLMLTGVACSCAVGVK-----YMGIFTYLLVLA 216
Cdd:COG4745 149 GFAVRYLDTERF------RYLYASAVSLALAFTAKenallYVAAFLGASALV 194
|
|
| PMT_2 |
pfam13231 |
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ... |
102-223 |
9.98e-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: 37.24 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 102 WSLRLLPALTGAFSIPMAYQILLELgFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFSNSQKhrp 181
Cdd:pfam13231 22 WAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVVPLFVALSRLFTPDAPLLLFWALALYFLLRALEKGR--- 97
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90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1953099264 182 fslswWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAW 223
Cdd:pfam13231 98 -----LKWWLLAGAAAGLGFLSKYTAALLVLAALLYLLISPG 134
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