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Conserved domains on  [gi|50736564|ref|XP_419132|]
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mRNA cap guanine-N7 methyltransferase [Gallus gallus]

Protein Classification

mRNA cap guanine-N7 methyltransferase( domain architecture ID 10505544)

mRNA cap guanine-N7 methyltransferase is the catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
80-414 2.46e-140

mRNA capping enzyme; This family of enzymes are related to pfam03919.


:

Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 403.74  E-value: 2.46e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564    80 SEAGHGQAVAAHYNELQEVG--LEKRSQSRIFYLRNFNNWTKSVLIGEFIDRVRQKKSDITVLDLGCGKGGDLLKWRKGR 157
Cdd:pfam03291   6 TNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNSNKRKVLDLGCGKGGDLEKWFKGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   158 IKKLVCTDIADISVQQCKQRYEDMKARCRYNERIFDAEFIQADSTKDLLSSKYSDPDTRFDICSCQFVYHYSFETYEQAD 237
Cdd:pfam03291  86 ISQLIGTDIAEVSIEQCRERYNKLRSGNKSKYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFESEEKAR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   238 MMLKNACGNLSPGGYFIGTTPNSFEL----VKRLEASE--TNSFGNDVYNVKF-EKKGEYPLFGCKYDFHLEEVV-DVPE 309
Cdd:pfam03291 166 TMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFeEEPPQVPLFGIKYDYNLEDAVdDVPE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   310 FLVYFPLLEEMAKKHGMKLVYKMTFREFYEEKIKNeEHKMLLRRMQALEPYStfgdsrlasdkpddyehAKEFIKDGKAK 389
Cdd:pfam03291 246 YIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKK-EFKKLIKRMSAMESRP-----------------STRNFFGLQRS 307
                         330       340
                  ....*....|....*....|....*
gi 50736564   390 LPLGTLSKSEWEATSIYLVFAFEKQ 414
Cdd:pfam03291 308 AGKGTLGGDEWEAASFYLVFVFEKR 332
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
80-414 2.46e-140

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 403.74  E-value: 2.46e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564    80 SEAGHGQAVAAHYNELQEVG--LEKRSQSRIFYLRNFNNWTKSVLIGEFIDRVRQKKSDITVLDLGCGKGGDLLKWRKGR 157
Cdd:pfam03291   6 TNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNSNKRKVLDLGCGKGGDLEKWFKGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   158 IKKLVCTDIADISVQQCKQRYEDMKARCRYNERIFDAEFIQADSTKDLLSSKYSDPDTRFDICSCQFVYHYSFETYEQAD 237
Cdd:pfam03291  86 ISQLIGTDIAEVSIEQCRERYNKLRSGNKSKYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFESEEKAR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   238 MMLKNACGNLSPGGYFIGTTPNSFEL----VKRLEASE--TNSFGNDVYNVKF-EKKGEYPLFGCKYDFHLEEVV-DVPE 309
Cdd:pfam03291 166 TMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFeEEPPQVPLFGIKYDYNLEDAVdDVPE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   310 FLVYFPLLEEMAKKHGMKLVYKMTFREFYEEKIKNeEHKMLLRRMQALEPYStfgdsrlasdkpddyehAKEFIKDGKAK 389
Cdd:pfam03291 246 YIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKK-EFKKLIKRMSAMESRP-----------------STRNFFGLQRS 307
                         330       340
                  ....*....|....*....|....*
gi 50736564   390 LPLGTLSKSEWEATSIYLVFAFEKQ 414
Cdd:pfam03291 308 AGKGTLGGDEWEAASFYLVFVFEKR 332
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
138-254 6.77e-12

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 61.68  E-value: 6.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 138 TVLDLGCGKGGDLLKWRKGRIKKLVCTDIADISVQQCKQRyedmkarcRYNERIFDAEFIQADSTKDLLsskysDPDTRF 217
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKA--------AAALLADNVEVLKGDAEELPP-----EADESF 67
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 50736564 218 DICSCQFVYHYSFETYEQadmMLKNACGNLSPGGYFI 254
Cdd:cd02440  68 DVIISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
113-259 1.32e-11

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 61.57  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 113 NFNNWTKSvlIGEFIDRVRQKKSdiTVLDLGCGkGGDLLKWRKGRIKKLVCTDIADISVQQCKQRYEDMkarcrynerif 192
Cdd:COG2227   6 ARDFWDRR--LAALLARLLPAGG--RVLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAEL----------- 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50736564 193 DAEFIQADSTkDLlsskySDPDTRFDICSCQFVYHYsfetYEQADMMLKNACGNLSPGGYFIGTTPN 259
Cdd:COG2227  70 NVDFVQGDLE-DL-----PLEDGSFDLVICSEVLEH----LPDPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
80-414 2.46e-140

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 403.74  E-value: 2.46e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564    80 SEAGHGQAVAAHYNELQEVG--LEKRSQSRIFYLRNFNNWTKSVLIGEFIDRVRQKKSDITVLDLGCGKGGDLLKWRKGR 157
Cdd:pfam03291   6 TNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNSNKRKVLDLGCGKGGDLEKWFKGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   158 IKKLVCTDIADISVQQCKQRYEDMKARCRYNERIFDAEFIQADSTKDLLSSKYSDPDTRFDICSCQFVYHYSFETYEQAD 237
Cdd:pfam03291  86 ISQLIGTDIAEVSIEQCRERYNKLRSGNKSKYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFESEEKAR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   238 MMLKNACGNLSPGGYFIGTTPNSFEL----VKRLEASE--TNSFGNDVYNVKF-EKKGEYPLFGCKYDFHLEEVV-DVPE 309
Cdd:pfam03291 166 TMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFeEEPPQVPLFGIKYDYNLEDAVdDVPE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   310 FLVYFPLLEEMAKKHGMKLVYKMTFREFYEEKIKNeEHKMLLRRMQALEPYStfgdsrlasdkpddyehAKEFIKDGKAK 389
Cdd:pfam03291 246 YIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKK-EFKKLIKRMSAMESRP-----------------STRNFFGLQRS 307
                         330       340
                  ....*....|....*....|....*
gi 50736564   390 LPLGTLSKSEWEATSIYLVFAFEKQ 414
Cdd:pfam03291 308 AGKGTLGGDEWEAASFYLVFVFEKR 332
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
139-251 4.46e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.81  E-value: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   139 VLDLGCGKGGDLLKWRKGRIKKLVCTDIADISVQQCKQRYEDMKARCrynerifdaEFIQADSTkdllssKYSDPDTRFD 218
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNV---------EFVQGDAE------DLPFPDGSFD 65
                          90       100       110
                  ....*....|....*....|....*....|...
gi 50736564   219 ICSCQFVYHYSfeTYEQADMMLKNACGNLSPGG 251
Cdd:pfam13649  66 LVVSSGVLHHL--PDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
138-254 6.77e-12

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 61.68  E-value: 6.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 138 TVLDLGCGKGGDLLKWRKGRIKKLVCTDIADISVQQCKQRyedmkarcRYNERIFDAEFIQADSTKDLLsskysDPDTRF 217
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKA--------AAALLADNVEVLKGDAEELPP-----EADESF 67
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 50736564 218 DICSCQFVYHYSFETYEQadmMLKNACGNLSPGGYFI 254
Cdd:cd02440  68 DVIISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
113-259 1.32e-11

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 61.57  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 113 NFNNWTKSvlIGEFIDRVRQKKSdiTVLDLGCGkGGDLLKWRKGRIKKLVCTDIADISVQQCKQRYEDMkarcrynerif 192
Cdd:COG2227   6 ARDFWDRR--LAALLARLLPAGG--RVLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAEL----------- 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50736564 193 DAEFIQADSTkDLlsskySDPDTRFDICSCQFVYHYsfetYEQADMMLKNACGNLSPGGYFIGTTPN 259
Cdd:COG2227  70 NVDFVQGDLE-DL-----PLEDGSFDLVICSEVLEH----LPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
125-270 3.22e-11

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 60.78  E-value: 3.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 125 EFIDRVRQKKSDiTVLDLGCGKGGDLLKWRKgRIKKLVCTDIADISVQQCKQRYEDMKARcrynerifdAEFIQADSTKD 204
Cdd:COG2226  13 ALLAALGLRPGA-RVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAGLN---------VEFVVGDAEDL 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50736564 205 LLsskysdPDTRFDICSCQFVYHYsFETYEQAdmmLKNACGNLSPGGYFI---GTTPNSFELVKRLEAS 270
Cdd:COG2226  82 PF------PDGSFDLVISSFVLHH-LPDPERA---LAEIARVLKPGGRLVvvdFSPPDLAELEELLAEA 140
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
126-254 2.68e-08

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 53.77  E-value: 2.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 126 FIDRVRQKKSDITVLDLGCGKGGDLLKWRKGRIKKLVCTDIADISVQQCKQRYEDMKarcrynerIFDAEFIQADSTKDL 205
Cdd:COG0500  17 LLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAG--------LGNVEFLVADLAELD 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 50736564 206 lsskySDPDTRFDICSCQFVYHY-SFETYEQAdmmLKNACGNLSPGGYFI 254
Cdd:COG0500  89 -----PLPAESFDLVVAFGVLHHlPPEEREAL---LRELARALKPGGVLL 130
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
133-293 8.78e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 51.26  E-value: 8.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   133 KKSDITVLDLGCGKGGDLLKWRK--GRIKKLVCTDIADISVQQCKQRyedmkARCRYNERIfdaEFIQADSTKdlLSSKY 210
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEKAREN-----AQKLGFDNV---EFEQGDIEE--LPELL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   211 SdpDTRFDICSCQFVYHYSFETyeqaDMMLKNACGNLSPGGYFIGTTPNSFELVKRLEASETNSFGNDVYNVKFEKKgEY 290
Cdd:pfam13847  71 E--DDKFDVVISNCVLNHIPDP----DKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKK-LY 143

                  ...
gi 50736564   291 PLF 293
Cdd:pfam13847 144 ELL 146
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
122-260 1.95e-06

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 47.69  E-value: 1.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 122 LIGEFIDRVRQKKsDITVLDLGCGKG--GDLLKWRKGRIkklVCTDIAdisvqqckqryEDMKARCRynERIFDAEFIQA 199
Cdd:COG4976  34 LAEELLARLPPGP-FGRVLDLGCGTGllGEALRPRGYRL---TGVDLS-----------EEMLAKAR--EKGVYDRLLVA 96
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50736564 200 DSTkDLlsskySDPDTRFDICSCQFVYHYsfetyeQADM--MLKNACGNLSPGGYFIGTTPNS 260
Cdd:COG4976  97 DLA-DL-----AEPDGRFDLIVAADVLTY------LGDLaaVFAGVARALKPGGLFIFSVEDA 147
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
140-254 5.36e-06

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.58  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   140 LDLGCGKGGDLLKWRKgRIKKLVCTDIAdisvqqckqryEDMKARCRYNERIFDAEFIQADSTKDLLsskysdPDTRFDI 219
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDIS-----------PEMLELAREKAPREGLTFVVGDAEDLPF------PDNSFDL 62
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 50736564   220 CSCQFVYHYsFETYEQAdmmLKNACGNLSPGGYFI 254
Cdd:pfam08241  63 VLSSEVLHH-VEDPERA---LREIARVLKPGGILI 93
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
140-253 1.35e-04

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 40.81  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564   140 LDLGCGKGGDLLKWRK-GRIKKLVCTDIADISVQQCKQRyedMKARCRYNerIFDAEFIQADSTKDLLSSkysdpdtrFD 218
Cdd:pfam08242   1 LEIGCGTGTLLRALLEaLPGLEYTGLDISPAALEAARER---LAALGLLN--AVRVELFQLDLGELDPGS--------FD 67
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 50736564   219 ICSCQFVYHYSFETyEQAdmmLKNACGNLSPGGYF 253
Cdd:pfam08242  68 VVVASNVLHHLADP-RAV---LRNIRRLLKPGGVL 98
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
138-254 2.58e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 138 TVLDLGCGkGGDLLKW--RKGRIKKLVCTDIADISVQQCKQRYEdmkarcrynerifDAEFIQADSTkDLlsskysDPDT 215
Cdd:COG4106   4 RVLDLGCG-TGRLTALlaERFPGARVTGVDLSPEMLARARARLP-------------NVRFVVADLR-DL------DPPE 62
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 50736564 216 RFDICSCQFVYHYSfetyEQADMMLKNACGNLSPGGYFI 254
Cdd:COG4106  63 PFDLVVSNAALHWL----PDHAALLARLAAALAPGGVLA 97
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
138-258 3.27e-04

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.07  E-value: 3.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50736564 138 TVLDLGCGKGGDLLKWRKGRIKKLVCTDIADISVQQCKQRYEDMKARCRynerifdAEFIQADSTkDLlsskysDPDTRF 217
Cdd:COG2230  54 RVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADR-------VEVRLADYR-DL------PADGQF 119
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 50736564 218 D-ICSCQFVYHYSFETYEQadmMLKNACGNLSPGGYFIGTTP 258
Cdd:COG2230 120 DaIVSIGMFEHVGPENYPA---YFAKVARLLKPGGRLLLHTP 158
 
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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