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Conserved domains on  [gi|1212974529|ref|NP_001340124|]
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protein O-mannosyl-transferase 1 isoform d [Homo sapiens]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 11449133)

dolichyl-phosphate-mannose--protein mannosyltransferase is a glycosyltransferase family 39 protein that transfers mannosyl residues to the hydroxyl group of serine or threonine residues, initiating the assembly of O-mannosyl glycans

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
2-603 3.02e-110

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


:

Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 346.01  E-value: 3.02e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529   2 AYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNCQkhsPFSLSWWFWLTLTGVACS 81
Cdd:COG1928   127 VYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ---PFSRRWLKWLLLTGISLG 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529  82 CAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVCVFCHLLARAVALLVIPVVLYLLFFYVHLILVFRSGPHDQIMSS 161
Cdd:COG1928   204 CAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSGPGDSFMPS 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 162 AFQASLEGglARITQGQPLEVAFGSQVTLRNVfgKPVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKd 241
Cdd:COG1928   284 LFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDANNEWLIE- 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 242 prrHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWRLEIVNRGSDTD--VW 319
Cdd:COG1928   352 ---LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDEANEDqeRI 427
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 320 KTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSrgyHGSTVWNVEEHrygasqeqrerERELHSPAQVDVSR 399
Cdd:COG1928   428 HPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLPNPEKKVYK 493
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 400 NLSFMARFSELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWY 478
Cdd:COG1928   494 KLSFWKKFIELNKAMFSSnNALVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAFFTGIVIWR 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 479 LLRRRRNVHDLPQDAWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLcrSQLQRSI 558
Cdd:COG1928   574 LIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRP--SRERRTL 651
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1212974529 559 FSALVVAWYSSACHVSNTLRPLTYGdKSLSPHELKALRWKDSWDI 603
Cdd:COG1928   652 GLIVVAIFVALVIYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
2-603 3.02e-110

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 346.01  E-value: 3.02e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529   2 AYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNCQkhsPFSLSWWFWLTLTGVACS 81
Cdd:COG1928   127 VYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ---PFSRRWLKWLLLTGISLG 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529  82 CAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVCVFCHLLARAVALLVIPVVLYLLFFYVHLILVFRSGPHDQIMSS 161
Cdd:COG1928   204 CAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSGPGDSFMPS 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 162 AFQASLEGglARITQGQPLEVAFGSQVTLRNVfgKPVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKd 241
Cdd:COG1928   284 LFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDANNEWLIE- 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 242 prrHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWRLEIVNRGSDTD--VW 319
Cdd:COG1928   352 ---LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDEANEDqeRI 427
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 320 KTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSrgyHGSTVWNVEEHrygasqeqrerERELHSPAQVDVSR 399
Cdd:COG1928   428 HPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLPNPEKKVYK 493
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 400 NLSFMARFSELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWY 478
Cdd:COG1928   494 KLSFWKKFIELNKAMFSSnNALVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAFFTGIVIWR 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 479 LLRRRRNVHDLPQDAWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLcrSQLQRSI 558
Cdd:COG1928   574 LIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRP--SRERRTL 651
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1212974529 559 FSALVVAWYSSACHVSNTLRPLTYGdKSLSPHELKALRWKDSWDI 603
Cdd:COG1928   652 GLIVVAIFVALVIYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
405-599 5.63e-58

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: 193.14  E-value: 5.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 405 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 483
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 484 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 560
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFKRlpRSLRKRVGY 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1212974529 561 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 599
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
182-239 1.56e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.41  E-value: 1.56e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529  182 VAFGSQVTLRNVFGkpvPCWLHSHQDTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 239
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
2-603 3.02e-110

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 346.01  E-value: 3.02e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529   2 AYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNCQkhsPFSLSWWFWLTLTGVACS 81
Cdd:COG1928   127 VYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ---PFSRRWLKWLLLTGISLG 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529  82 CAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVCVFCHLLARAVALLVIPVVLYLLFFYVHLILVFRSGPHDQIMSS 161
Cdd:COG1928   204 CAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSGPGDSFMPS 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 162 AFQASLEGglARITQGQPLEVAFGSQVTLRNVfgKPVPCWLHSHQDTYPmiyengrGSSHQQQVTCYPFKDVNNWWIVKd 241
Cdd:COG1928   284 LFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDANNEWLIE- 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 242 prrHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWRLEIVNRGSDTD--VW 319
Cdd:COG1928   352 ---LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDEANEDqeRI 427
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 320 KTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSrgyHGSTVWNVEEHrygasqeqrerERELHSPAQVDVSR 399
Cdd:COG1928   428 HPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLPNPEKKVYK 493
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 400 NLSFMARFSELQWRMLAL-RSDDSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWY 478
Cdd:COG1928   494 KLSFWKKFIELNKAMFSSnNALVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAFFTGIVIWR 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 479 LLRRRRNVHDLPQDAWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLcrSQLQRSI 558
Cdd:COG1928   574 LIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRP--SRERRTL 651
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1212974529 559 FSALVVAWYSSACHVSNTLRPLTYGdKSLSPHELKALRWKDSWDI 603
Cdd:COG1928   652 GLIVVAIFVALVIYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
405-599 5.63e-58

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: 193.14  E-value: 5.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 405 ARFSELQWRMLALRSD-DSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRR 483
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 484 RNVHDLPQD-AWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCR--SQLQRSIFS 560
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFKRlpRSLRKRVGY 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1212974529 561 ALVVAWYSSACHVSNTLRPLTYGDKSLSpHELKALRWKD 599
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
1-150 7.63e-47

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: 164.79  E-value: 7.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529   1 MAYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNcqkHSPFSLSWWFWLTLTGVAC 80
Cdd:pfam02366  99 LVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KAPFSRKWWLWLLLTGIAL 175
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529  81 SCAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVCVFCHLLARAVALLVIPVVLYLLFFYVHLILVF 150
Cdd:pfam02366 176 GLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
193-353 2.55e-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: 71.63  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 193 VFGKPVPCWLHSHQDTYPMIYENGRGsSHQQQVTCYPFKDVNN----WWIVkdprrhqLVVSSPP---RPVRHGDMVQLV 265
Cdd:pfam02815   3 LKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529 266 HGMTTRSLNTHDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWRLEIVNR----GSDTDVWKTILSEVRFVHVNTSAVL 337
Cdd:pfam02815  75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKksttGMGSDRIKPGDSYFRLQHVCTGCWL 151
                         170
                  ....*....|....*.
gi 1212974529 338 KLSGAHLPDWGYRQLE 353
Cdd:pfam02815 152 FSHSVKLPKWGFGPEQ 167
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
182-239 1.56e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.41  E-value: 1.56e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212974529  182 VAFGSQVTLRNVFGkpvPCWLHSHQDTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 239
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
253-310 8.10e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.40  E-value: 8.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1212974529  253 PRPVRHGDMVQLVHGMTTRSLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWRLEIV 310
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
324-374 1.55e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 36.94  E-value: 1.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1212974529  324 SEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRGyHGSTVWNVEEH 374
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAI-DANTLWLIEPV 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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