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Conserved domains on  [gi|459371475|gb|EMG49268|]
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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, ...
32-727 5.77e-151

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


:

Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 455.80  E-value: 5.77e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  32 FENFLTFVILT-LAIVIRLYKLYIPDRIVFDEIHIVKYIKHYYTGETFVDVHPPLGRLIYYYLTRLFvpidsSVLQEFDA 110
Cdd:COG1928   21 LPYKLGPVLLTvLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFDVHPPLGKMLIALVGGLE-----GYDPPFDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 111 DKIG-QLYPEDFPYLWLRLFSGLCGIGHVLVTFFTSR-LTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLFAQSLVI 188
Cdd:COG1928   96 QLIGlTEYPFGYNYVGMRFFNALLGSLTVPLVYLIARrIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 189 LNYKSFTQCQQFTKSWWFHLFATGVSLGLNISIKISGAFNYLWVGILTTVQLWEILGDLEISVTQWIKHIVSRVVALIIV 268
Cdd:COG1928  176 YCFLRFHRQQPFSRRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIII 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 269 PLTIYCSVFYIHFELLPKEGPGSGFLSPHFRSTLVD---YESSPVEVLYGSTVTIKHNELEK-YLHSHDKSYPRGSNLQQ 344
Cdd:COG1928  256 PFDIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKGnpvYLNSRDPAYGSSTITIRHAGTGGgYLHSHNQLYPEGSEQQQ 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 345 VTLYEFPDENNEWIIETkhkYYEHKlmDSKTPIKDGDIIRLYHKSTGHYLHANDIRPPISEHEysYEINCNeTRGLLGNV 424
Cdd:COG1928  336 VTGYGHKDANNEWLIEL---SDENA--TQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQ--YEVSGY-GDSFEGDE 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 425 DYEFKVRtISKKSHSENDLPlikLRTTETVFQLLSRGSSCSLMSHEQKLPEWGAFQNEVLCVqEPTIPNTLWYIESNSHP 504
Cdd:COG1928  408 KDDWIIE-IVKDEANEDQER---IHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCA-KDRDPSTTWNIEENVND 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 505 LLDGQENVEkkFPKFTFWNKLFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFFNNysskliDEDSSVIYYLGNIA 584
Cdd:COG1928  483 RLPNPEKKV--YKKLSFWKKFIELNKAMFSSNNALVPDHDYSSEPYQWPTLLRGLRFWGW------GECIKKVYLMGNPA 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 585 IYYSVNLVVLISWVKYLFFAFINLNPYKqpSESSPAKSTFYENAWQFLLGWSLNYLPYFLVSRNLYLHHYLPALSFGILL 664
Cdd:COG1928  555 LWWFSVPALAFFTGIVIWRLIRWRRGYR--TLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILA 632
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 459371475 665 LG----QYLNYRVAKNSFIGYSLVILVLVGSVYCYYELIPIIYGLPWTAAKCTAHKWISNWDIDCLS 727
Cdd:COG1928  633 LAlvldFILRRPSRERRTLGLIVVAIFVALVIYFFFWFSPVTYGLPLSPQEFRRLMWLPSWDFHCNK 699
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
32-727 5.77e-151

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 455.80  E-value: 5.77e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  32 FENFLTFVILT-LAIVIRLYKLYIPDRIVFDEIHIVKYIKHYYTGETFVDVHPPLGRLIYYYLTRLFvpidsSVLQEFDA 110
Cdd:COG1928   21 LPYKLGPVLLTvLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFDVHPPLGKMLIALVGGLE-----GYDPPFDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 111 DKIG-QLYPEDFPYLWLRLFSGLCGIGHVLVTFFTSR-LTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLFAQSLVI 188
Cdd:COG1928   96 QLIGlTEYPFGYNYVGMRFFNALLGSLTVPLVYLIARrIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 189 LNYKSFTQCQQFTKSWWFHLFATGVSLGLNISIKISGAFNYLWVGILTTVQLWEILGDLEISVTQWIKHIVSRVVALIIV 268
Cdd:COG1928  176 YCFLRFHRQQPFSRRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIII 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 269 PLTIYCSVFYIHFELLPKEGPGSGFLSPHFRSTLVD---YESSPVEVLYGSTVTIKHNELEK-YLHSHDKSYPRGSNLQQ 344
Cdd:COG1928  256 PFDIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKGnpvYLNSRDPAYGSSTITIRHAGTGGgYLHSHNQLYPEGSEQQQ 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 345 VTLYEFPDENNEWIIETkhkYYEHKlmDSKTPIKDGDIIRLYHKSTGHYLHANDIRPPISEHEysYEINCNeTRGLLGNV 424
Cdd:COG1928  336 VTGYGHKDANNEWLIEL---SDENA--TQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQ--YEVSGY-GDSFEGDE 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 425 DYEFKVRtISKKSHSENDLPlikLRTTETVFQLLSRGSSCSLMSHEQKLPEWGAFQNEVLCVqEPTIPNTLWYIESNSHP 504
Cdd:COG1928  408 KDDWIIE-IVKDEANEDQER---IHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCA-KDRDPSTTWNIEENVND 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 505 LLDGQENVEkkFPKFTFWNKLFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFFNNysskliDEDSSVIYYLGNIA 584
Cdd:COG1928  483 RLPNPEKKV--YKKLSFWKKFIELNKAMFSSNNALVPDHDYSSEPYQWPTLLRGLRFWGW------GECIKKVYLMGNPA 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 585 IYYSVNLVVLISWVKYLFFAFINLNPYKqpSESSPAKSTFYENAWQFLLGWSLNYLPYFLVSRNLYLHHYLPALSFGILL 664
Cdd:COG1928  555 LWWFSVPALAFFTGIVIWRLIRWRRGYR--TLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILA 632
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 459371475 665 LG----QYLNYRVAKNSFIGYSLVILVLVGSVYCYYELIPIIYGLPWTAAKCTAHKWISNWDIDCLS 727
Cdd:COG1928  633 LAlvldFILRRPSRERRTLGLIVVAIFVALVIYFFFWFSPVTYGLPLSPQEFRRLMWLPSWDFHCNK 699
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
524-719 2.60e-54

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: 406576  Cd Length: 198  Bit Score: 185.06  E-value: 2.60e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  524 KLFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFFNNysskliDEDSSVIYYLGNIAIYYSVNLVVLISWVKYLFF 603
Cdd:pfam16192   2 KFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  604 AFINLNPYkQPSESSPAKSTFYENAWQFLLGWSLNYLPYFLVSRNLYLHHYLPALSFGILLLGQYLNY--------RVAK 675
Cdd:pfam16192  76 LLRWQRGY-YDLSDDDTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFllslfkrlPRSL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 459371475  676 NSFIGYSLVILVLVGSVYCYYELIPIIYGLPWTAAKCTAHKWIS 719
Cdd:pfam16192 155 RKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
312-361 6.43e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 58.12  E-value: 6.43e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 459371475   312 VLYGSTVTIKHNELEKYLHSHDKSYPR-GSNLQQVTLYEFP--DENNEWIIET 361
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLPPwGDGQQEVTGYGNPaiDANTLWLIEP 56
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
32-727 5.77e-151

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 455.80  E-value: 5.77e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  32 FENFLTFVILT-LAIVIRLYKLYIPDRIVFDEIHIVKYIKHYYTGETFVDVHPPLGRLIYYYLTRLFvpidsSVLQEFDA 110
Cdd:COG1928   21 LPYKLGPVLLTvLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFDVHPPLGKMLIALVGGLE-----GYDPPFDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 111 DKIG-QLYPEDFPYLWLRLFSGLCGIGHVLVTFFTSR-LTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLFAQSLVI 188
Cdd:COG1928   96 QLIGlTEYPFGYNYVGMRFFNALLGSLTVPLVYLIARrIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 189 LNYKSFTQCQQFTKSWWFHLFATGVSLGLNISIKISGAFNYLWVGILTTVQLWEILGDLEISVTQWIKHIVSRVVALIIV 268
Cdd:COG1928  176 YCFLRFHRQQPFSRRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIII 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 269 PLTIYCSVFYIHFELLPKEGPGSGFLSPHFRSTLVD---YESSPVEVLYGSTVTIKHNELEK-YLHSHDKSYPRGSNLQQ 344
Cdd:COG1928  256 PFDIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKGnpvYLNSRDPAYGSSTITIRHAGTGGgYLHSHNQLYPEGSEQQQ 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 345 VTLYEFPDENNEWIIETkhkYYEHKlmDSKTPIKDGDIIRLYHKSTGHYLHANDIRPPISEHEysYEINCNeTRGLLGNV 424
Cdd:COG1928  336 VTGYGHKDANNEWLIEL---SDENA--TQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQ--YEVSGY-GDSFEGDE 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 425 DYEFKVRtISKKSHSENDLPlikLRTTETVFQLLSRGSSCSLMSHEQKLPEWGAFQNEVLCVqEPTIPNTLWYIESNSHP 504
Cdd:COG1928  408 KDDWIIE-IVKDEANEDQER---IHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCA-KDRDPSTTWNIEENVND 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 505 LLDGQENVEkkFPKFTFWNKLFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFFNNysskliDEDSSVIYYLGNIA 584
Cdd:COG1928  483 RLPNPEKKV--YKKLSFWKKFIELNKAMFSSNNALVPDHDYSSEPYQWPTLLRGLRFWGW------GECIKKVYLMGNPA 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475 585 IYYSVNLVVLISWVKYLFFAFINLNPYKqpSESSPAKSTFYENAWQFLLGWSLNYLPYFLVSRNLYLHHYLPALSFGILL 664
Cdd:COG1928  555 LWWFSVPALAFFTGIVIWRLIRWRRGYR--TLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILA 632
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 459371475 665 LG----QYLNYRVAKNSFIGYSLVILVLVGSVYCYYELIPIIYGLPWTAAKCTAHKWISNWDIDCLS 727
Cdd:COG1928  633 LAlvldFILRRPSRERRTLGLIVVAIFVALVIYFFFWFSPVTYGLPLSPQEFRRLMWLPSWDFHCNK 699
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
524-719 2.60e-54

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: 406576  Cd Length: 198  Bit Score: 185.06  E-value: 2.60e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  524 KLFEIHQVMFRLNKSFTNNHPYASNPMLWLFLTKGISFFNNysskliDEDSSVIYYLGNIAIYYSVNLVVLISWVKYLFF 603
Cdd:pfam16192   2 KFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  604 AFINLNPYkQPSESSPAKSTFYENAWQFLLGWSLNYLPYFLVSRNLYLHHYLPALSFGILLLGQYLNY--------RVAK 675
Cdd:pfam16192  76 LLRWQRGY-YDLSDDDTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFllslfkrlPRSL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 459371475  676 NSFIGYSLVILVLVGSVYCYYELIPIIYGLPWTAAKCTAHKWIS 719
Cdd:pfam16192 155 RKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
43-284 7.38e-46

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: 163.64  E-value: 7.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475   43 LAIVIRLYKLYIPDRIVFDEIHIVKYIKHYYTGETFVDVHPPLGRLIYYYLTRLF-VPIDssvlqeFDADKIG-QLYPED 120
Cdd:pfam02366   6 LAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAgYDGN------FTFISIGgQYYPGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  121 FPYLWLRLFSGLCGIGHVLVTFFTSR-LTCTPIISAIVSSLVCLENSSITDSRLILLDGPLLFAQSLVILNYKSFTQCQQ 199
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKrLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  200 FTKSWWFHLFATGVSLGLNISIKISGAFNYLWVGILTTVQLWEILGDLEISVTQWIKHIVSRVVALIIVPLTIYCSVFYI 279
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYV 239

                  ....*
gi 459371475  280 HFELL 284
Cdd:pfam02366 240 HFWLL 244
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
315-496 1.44e-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: 81.26  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  315 GSTVTIKHNELEKYLHShdKSYPRGSNLQQVTLYEFPDENNE----WIIETKHkyyehklMDSKT--PIKDGDIIRLYHK 388
Cdd:pfam02815   6 GDVVRLFHSHQDEYLTG--SEQQQKQPFLRITLYPHGDANNSarslWRIEVVR-------HDAWRggLIKWGSPFRLRHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371475  389 STGHYLHANDI-RPPISEHE-YSYEINCNETRGLLGNVDYE--FKVRTISKKSHSEndlplikLRTTETVFQLLSRGSSC 464
Cdd:pfam02815  77 TTGRYLHSHEEqKPPLVEKEdWQKEVSAYGFRGFPGDNDIVeiFEKKSTTGMGSDR-------IKPGDSYFRLQHVCTGC 149
                         170       180       190
                  ....*....|....*....|....*....|....
gi 459371475  465 SLMSHEQKLPEWGA--FQNEVLCVQEPTIPNTLW 496
Cdd:pfam02815 150 WLFSHSVKLPKWGFgpEQQKVTCAKEGHMDDALT 183
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
312-361 6.43e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 58.12  E-value: 6.43e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 459371475   312 VLYGSTVTIKHNELEKYLHSHDKSYPR-GSNLQQVTLYEFP--DENNEWIIET 361
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLPPwGDGQQEVTGYGNPaiDANTLWLIEP 56
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
375-417 4.68e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.25  E-value: 4.68e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 459371475   375 TPIKDGDIIRLYHKSTGHYLHANDIRPPISEHEYsYEINCNET 417
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQ-QEVTGYGN 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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