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Conserved domains on  [gi|1307901430|gb|AUE01688|]
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Cyclopropane-fatty-acyl-phospholipid synthase [Bifidobacterium breve]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CMAS super family cl47167
Mycolic acid cyclopropane synthetase; This family consist of ...
 142-410 4.36e-110

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


The actual alignment was detected with superfamily member pfam02353:

Pssm-ID: 481507 [Multi-domain]  Cd Length: 272  Bit Score: 325.05  E-value: 4.36e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 142 KADSETVSFHYDMSNEFYADFLGPSMTYTCAVFDNEHMSLEDAQANKLRLILDKLDLKPGERLLDIGCGWGSMVITAARR 221
Cdd:pfam02353   3 TRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 222 -GIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEhDFDGICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRL 300
Cdd:pfam02353  83 yDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDE-PFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 301 VNHQITISH-DKPHGKPGTDEFLDRYIFPDGDLGAPGFIESCIHDAGFNVVHQENLRQHYALTLHHWNQNLSEHWDDAVK 379
Cdd:pfam02353 162 LLHTITGLHpDETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIA 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1307901430 380 QVGFERAKVWGMYMAACALNFELDGIQIHQF 410
Cdd:pfam02353 242 LQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
 
Name Accession Description Interval E-value
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 142-410 4.36e-110

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 325.05  E-value: 4.36e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 142 KADSETVSFHYDMSNEFYADFLGPSMTYTCAVFDNEHMSLEDAQANKLRLILDKLDLKPGERLLDIGCGWGSMVITAARR 221
Cdd:pfam02353   3 TRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 222 -GIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEhDFDGICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRL 300
Cdd:pfam02353  83 yDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDE-PFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 301 VNHQITISH-DKPHGKPGTDEFLDRYIFPDGDLGAPGFIESCIHDAGFNVVHQENLRQHYALTLHHWNQNLSEHWDDAVK 379
Cdd:pfam02353 162 LLHTITGLHpDETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIA 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1307901430 380 QVGFERAKVWGMYMAACALNFELDGIQIHQF 410
Cdd:pfam02353 242 LQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 150-303 1.02e-73

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 227.89  E-value: 1.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 150 FHYDMSNEFYADFLGPSMTYTCAVFDNEHMSLEDAQANKLRLILDKLDLKPGERLLDIGCGWGSMVITAARR-GIKALGV 228
Cdd:COG2230     1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1307901430 229 TLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEHD-FDGICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRLVNH 303
Cdd:COG2230    81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGqFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLH 156
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
151-419 2.44e-69

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 224.34  E-value: 2.44e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 151 HYDMSNEFYADFLGPSMTYTCAVFDNEHmSLEDAQANKLRLILDKLDLKPGERLLDIGCGWGSMVITAARR-GIKALGVT 229
Cdd:PRK11705  119 HYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHyGVSVVGVT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 230 LSKEQAAYanewiAREGLQDLA-EVRVQDYREVPEHdFDGICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRLVNHqiTIS 308
Cdd:PRK11705  198 ISAEQQKL-----AQERCAGLPvEIRLQDYRDLNGQ-FDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLH--TIG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 309 HDKPhgKPGTDEFLDRYIFPDGDLGAPGFIESCIHDAgFNVVHQENLRQHYALTLHHWNQNLSEHWDDAVKQVG--FERa 386
Cdd:PRK11705  270 SNKT--DTNVDPWINKYIFPNGCLPSVRQIAQASEGL-FVMEDWHNFGADYDRTLMAWHENFEAAWPELADNYSerFYR- 345

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1307901430 387 kVWGMYMAACALNFELDGIQIHQFLAAKPDRVG 419
Cdd:PRK11705  346 -MWRYYLLSCAGAFRARDIQLWQVVFSPRGVEG 377
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 203-301 1.14e-10

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: 58.21  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 203 RLLDIGCGWGSMVITAARR-GIKALGVTLSKEQAAYANEwIAREGLQDLAEVRVQDYREVPE---HDFDGICSIGMMEHV 278
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARK-AAAALLADNVEVLKGDAEELPPeadESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|...
gi 1307901430 279 gVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:cd02440    80 -VEDLARFLEEARRLLKPGGVLV 101
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
202-301 2.37e-09

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 57.43  E-value: 2.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430  202 ERLLDIGCGWGSMVITAARR--GIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEHDF-DGICSIGMMEHv 278
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERhpHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTyDLVFGFEVIHH- 79

                           90       100
                   ....*....|....*....|...
gi 1307901430  279 gVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:smart00828  80 -IKDKMDLFSNISRHLKDGGHLV 101
 
Name Accession Description Interval E-value
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 142-410 4.36e-110

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 325.05  E-value: 4.36e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 142 KADSETVSFHYDMSNEFYADFLGPSMTYTCAVFDNEHMSLEDAQANKLRLILDKLDLKPGERLLDIGCGWGSMVITAARR 221
Cdd:pfam02353   3 TRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 222 -GIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEhDFDGICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRL 300
Cdd:pfam02353  83 yDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDE-PFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 301 VNHQITISH-DKPHGKPGTDEFLDRYIFPDGDLGAPGFIESCIHDAGFNVVHQENLRQHYALTLHHWNQNLSEHWDDAVK 379
Cdd:pfam02353 162 LLHTITGLHpDETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIA 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1307901430 380 QVGFERAKVWGMYMAACALNFELDGIQIHQF 410
Cdd:pfam02353 242 LQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 150-303 1.02e-73

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 227.89  E-value: 1.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 150 FHYDMSNEFYADFLGPSMTYTCAVFDNEHMSLEDAQANKLRLILDKLDLKPGERLLDIGCGWGSMVITAARR-GIKALGV 228
Cdd:COG2230     1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1307901430 229 TLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEHD-FDGICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRLVNH 303
Cdd:COG2230    81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGqFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLH 156
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
151-419 2.44e-69

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 224.34  E-value: 2.44e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 151 HYDMSNEFYADFLGPSMTYTCAVFDNEHmSLEDAQANKLRLILDKLDLKPGERLLDIGCGWGSMVITAARR-GIKALGVT 229
Cdd:PRK11705  119 HYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHyGVSVVGVT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 230 LSKEQAAYanewiAREGLQDLA-EVRVQDYREVPEHdFDGICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRLVNHqiTIS 308
Cdd:PRK11705  198 ISAEQQKL-----AQERCAGLPvEIRLQDYRDLNGQ-FDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLH--TIG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 309 HDKPhgKPGTDEFLDRYIFPDGDLGAPGFIESCIHDAgFNVVHQENLRQHYALTLHHWNQNLSEHWDDAVKQVG--FERa 386
Cdd:PRK11705  270 SNKT--DTNVDPWINKYIFPNGCLPSVRQIAQASEGL-FVMEDWHNFGADYDRTLMAWHENFEAAWPELADNYSerFYR- 345

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1307901430 387 kVWGMYMAACALNFELDGIQIHQFLAAKPDRVG 419
Cdd:PRK11705  346 -MWRYYLLSCAGAFRARDIQLWQVVFSPRGVEG 377
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 205-296 5.04e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 84.54  E-value: 5.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 205 LDIGCGWGSMVITAARR-GIKALGVTLSKEQAAYANEWIAREGLQdlAEVRVQDYREVPEHD--FDGICSIGMMEHVGVK 281
Cdd:pfam13649   2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDgsFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*
gi 1307901430 282 NYQSYFEEMFRLLKP 296
Cdd:pfam13649  80 DLEAALREIARVLKP 94
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 190-301 2.23e-19

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: 84.28  E-value: 2.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 190 RLILDKLDLKPGERLLDIGCGWGSMVITAARRGIKALGVTLSKEQAAYANEWIAREGLQdlAEVRVQDYREVP--EHDFD 267
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPfpDGSFD 89

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1307901430 268 GICSIGMMEHvgVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:COG2226    90 LVISSFVLHH--LPDPERALAEIARVLKPGGRLV 121
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 179-301 2.89e-18

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: 80.45  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 179 MSLEDAQAN---KLRLILDKLdLKPGERLLDIGCGWGSMVITAARRGIKALGVTLSKEQAAYANEWIAREGLqdlaEVRV 255
Cdd:COG2227     1 MSDPDARDFwdrRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV----DFVQ 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1307901430 256 QDYREVPEHD--FDGICSIGMMEHvgVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:COG2227    76 GDLEDLPLEDgsFDLVICSEVLEH--LPDPAALLRELARLLKPGGLLL 121
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 205-301 7.20e-15

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 70.00  E-value: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 205 LDIGCGWGSMVITAARRGIKALGVTLSKEQAAYANEWIAREGLqdlaEVRVQDYREVPEHD--FDGICSIGMMEHvgVKN 282
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGL----TFVVGDAEDLPFPDnsFDLVLSSEVLHH--VED 74

                          90
                  ....*....|....*....
gi 1307901430 283 YQSYFEEMFRLLKPMGRLV 301
Cdd:pfam08241  75 PERALREIARVLKPGGILI 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 187-301 1.29e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 72.26  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 187 NKLRLILDKLDLKPGERLLDIGCGWG-SMVITAARRGIKALGVTLSKEQAAYANEWIAREGLQ--DLAEVRVQDYREVPE 263
Cdd:COG0500    13 GLAALLALLERLPKGGRVLDLGCGTGrNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGnvEFLVADLAELDPLPA 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1307901430 264 HDFDGICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:COG0500    93 ESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLL 130
PLN02244 PLN02244
tocopherol O-methyltransferase
 95-329 1.25e-12

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 68.62  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430  95 VKPPTPASIARVSAGILSHGFKKPPVPSTEGPSKFARIKRGLmphtekadsetvSFHYDMSNEFYADFLGPSMTYtcAVF 174
Cdd:PLN02244   20 GSRSTRLSRPSSSASGVRRTLARLEDAASPAPAATADLKEGI------------AEFYDESSGVWEDVWGEHMHH--GYY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 175 DNEhMSLEDAQANKLRLILDKL--------DLKPGERLLDIGCGWGSMVITAARR-GIKALGVTLSKEQAAYANEWIARE 245
Cdd:PLN02244   86 DPG-ASRGDHRQAQIRMIEESLawagvpddDEKRPKRIVDVGCGIGGSSRYLARKyGANVKGITLSPVQAARANALAAAQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 246 GLQDLAEVRVQDYREVPEHD--FDGICSIGMMEHVGVKnyQSYFEEMFRLLKPMGRLVnhQITISH-DKPHG----KPGT 318
Cdd:PLN02244  165 GLSDKVSFQVADALNQPFEDgqFDLVWSMESGEHMPDK--RKFVQELARVAAPGGRII--IVTWCHrDLEPGetslKPDE 240

                         250
                  ....*....|....*
gi 1307901430 319 DEFLDR----YIFPD 329
Cdd:PLN02244  241 QKLLDKicaaYYLPA 255
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
183-349 1.34e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 65.79  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 183 DAQANKLRLILDKLDLKPGERLLDIGCGWGSMVITAARRGIKALGVTLSKEQAAYAnewiAREGLQDlaEVRVQDYREVP 262
Cdd:COG4976    29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA----REKGVYD--RLLVADLADLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 263 EHD--FDGICSIGMMEHVGvkNYQSYFEEMFRLLKPMGRLVnhqITISHDKPHGkpgtdefldRYIFpdgdlgAPGFIES 340
Cdd:COG4976   103 EPDgrFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFI---FSVEDADGSG---------RYAH------SLDYVRD 162


                  ....*....
gi 1307901430 341 CIHDAGFNV 349
Cdd:COG4976   163 LLAAAGFEV 171
PRK08317 PRK08317
hypothetical protein; Provisional
 192-301 2.21e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 63.42  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 192 ILDKLDLKPGERLLDIGCGWGSMVITAARR---GIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEHDFDG 268
Cdd:PRK08317   11 TFELLAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDA 90

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1307901430 269 ICSIGMMEHvgVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:PRK08317   91 VRSDRVLQH--LEDPARALAEIARVLRPGGRVV 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 203-301 1.14e-10

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: 58.21  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 203 RLLDIGCGWGSMVITAARR-GIKALGVTLSKEQAAYANEwIAREGLQDLAEVRVQDYREVPE---HDFDGICSIGMMEHV 278
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARK-AAAALLADNVEVLKGDAEELPPeadESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|...
gi 1307901430 279 gVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:cd02440    80 -VEDLARFLEEARRLLKPGGVLV 101
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 196-351 2.50e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 58.98  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 196 LDLKPGERLLDIGCGWGSMVITAARRGIKALGVTLSKEQaayanewIAREGLQDLAEVRVQDYREVPEHDFDGICSIGMM 275
Cdd:pfam13489  18 PKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIA-------IERALLNVRFDQFDEQEAAVPAGKFDVIVAREVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 276 EHvgVKNYQSYFEEMFRLLKPMGRLVNHQITISHDKPHgkpgtdEFLD-RYIFPDGDLGA---PGFIESCIHDAGFNVVH 351
Cdd:pfam13489  91 EH--VPDPPALLRQIAALLKPGGLLLLSTPLASDEADR------LLLEwPYLRPRNGHISlfsARSLKRLLEEAGFEVVS 162
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
200-301 5.48e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.99  E-value: 5.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 200 PGERLLDIGCGWGSMVITAARR--GIKALGVTLSKEQAAYANEWIAReglqdlAEVRVQDYREV-PEHDFDGICSIGMME 276
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPN------VRFVVADLRDLdPPEPFDLVVSNAALH 74

                          90       100
                  ....*....|....*....|....*
gi 1307901430 277 HvgVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:COG4106    75 W--LPDHAALLARLAAALAPGGVLA 97
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 190-301 6.72e-10

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 58.28  E-value: 6.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 190 RLILDKLDLKPGERLLDIGCGWGSMVITAARRGiKALGVTLSKEQA---AYANEWIAREGLQDlAEVRVQD-YREVPEHD 265
Cdd:COG2813    39 RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRN-PEARVTLVDVNAravELARANAAANGLEN-VEVLWSDgLSGVPDGS 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1307901430 266 FDGICS---IgmmeHVGVKNY----QSYFEEMFRLLKPMGRLV 301
Cdd:COG2813   117 FDLILSnppF----HAGRAVDkevaHALIADAARHLRPGGELW 155
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
202-301 2.37e-09

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 57.43  E-value: 2.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430  202 ERLLDIGCGWGSMVITAARR--GIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEHDF-DGICSIGMMEHv 278
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERhpHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTyDLVFGFEVIHH- 79

                           90       100
                   ....*....|....*....|...
gi 1307901430  279 gVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:smart00828  80 -IKDKMDLFSNISRHLKDGGHLV 101
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 205-300 1.11e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 52.37  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 205 LDIGCGWGSMVITAAR--RGIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQDYR--EVPEHDFDGICSIGMMEHVGV 280
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDlgELDPGSFDVVVASNVLHHLAD 80

                          90       100
                  ....*....|....*....|
gi 1307901430 281 KnyQSYFEEMFRLLKPMGRL 300
Cdd:pfam08242  81 P--RAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 198-301 4.61e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 52.03  E-value: 4.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 198 LKPGERLLDIGCGWGSMVITAARR---GIKALGVTLSKEQAAYANEWIAREGLQDLaEVRVQDYREVPEH----DFDGIC 270
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFDNV-EFEQGDIEELPELleddKFDVVI 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1307901430 271 SIGMMEHVGVKnyQSYFEEMFRLLKPMGRLV 301
Cdd:pfam13847  80 SNCVLNHIPDP--DKVLQEILRVLKPGGRLI 108
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 193-354 6.86e-08

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 54.37  E-value: 6.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 193 LDKLDLKPGERLLDIGCGWGS----MvitAARRGIKALGVTLSKEQAAYANEwiaRE-GLQDLAEVRVQD--YREVPEHD 265
Cdd:PLN02336  259 VDKLDLKPGQKVLDVGCGIGGgdfyM---AENFDVHVVGIDLSVNMISFALE---RAiGRKCSVEFEVADctKKTYPDNS 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 266 FDGICSIGMMEHVGVKnyQSYFEEMFRLLKPMGRLVnhqitIS-HDKPHGKPgTDEFLDrYIFPDG----DLGAPGfieS 340
Cdd:PLN02336  333 FDVIYSRDTILHIQDK--PALFRSFFKWLKPGGKVL-----ISdYCRSPGTP-SPEFAE-YIKQRGydlhDVQAYG---Q 400

                         170
                  ....*....|....
gi 1307901430 341 CIHDAGFNVVHQEN 354
Cdd:PLN02336  401 MLKDAGFDDVIAED 414
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 190-300 6.24e-07

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 49.13  E-value: 6.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 190 RLILDKLDLKPGERLLDIGCGWGSMVITAARRGIKAlGVTLSkEQAAYANEwIAREGLQ----DLAEVRVQD-YREVPEH 264
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDA-ELTMV-DINARALE-SARENLAanglENGEVVASDvYSGVEDG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1307901430 265 DFDGICS---IgmmeHVGVKNYQSYFEEMF----RLLKPMGRL 300
Cdd:pfam05175  98 KFDLIISnppF----HAGLATTYNVAQRFIadakRHLRPGGEL 136
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 194-301 1.35e-06

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 49.38  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 194 DKLDLKPGERLLDIGCGWGSMVITAARRG---IKALGVTLSKEQAAyanewIAREGLQDLAEVRVQDYRE-------VPE 263
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLA-----VGREKLRDLGLSGNVEFVQgdaealpFPD 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1307901430 264 HDFDGIcSIGMmehvG---VKNYQSYFEEMFRLLKPMGRLV 301
Cdd:PRK00216  120 NSFDAV-TIAF----GlrnVPDIDKALREMYRVLKPGGRLV 155
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 191-307 1.63e-06

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 50.17  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 191 LILDKLDLKPGERLLDIGCGWGSMVITAAR--RGIKALGVTLSKEQAAYANEWIAREGLQDLaEVRVQDYREVPEH--DF 266
Cdd:COG2242   238 LTLAKLALRPGDVLWDIGAGSGSVSIEAARlaPGGRVYAIERDPERAALIRANARRFGVPNV-EVVEGEAPEALADlpDP 316

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1307901430 267 DGICsIGmmehVGVKNYQSYFEEMFRLLKPMGRLVNHQITI 307
Cdd:COG2242   317 DAVF-IG----GSGGNLPEILEACWARLRPGGRLVANAVTL 352
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 193-257 3.62e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 47.91  E-value: 3.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1307901430 193 LDKLDLKPGERLLDIGCGWGSMVITAARRGIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQD 257
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD 120
arsM PRK11873
arsenite methyltransferase;
198-301 4.06e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 48.02  E-value: 4.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 198 LKPGERLLDIGCGWGSMVITAARR----GiKALGVTLSKE--QAAYANewiAREGLQDLAEVRVQDYRE--VPEHDFDGI 269
Cdd:PRK11873   75 LKPGETVLDLGSGGGFDCFLAARRvgptG-KVIGVDMTPEmlAKARAN---ARKAGYTNVEFRLGEIEAlpVADNSVDVI 150

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1307901430 270 CSIGMMEHVGVKnyQSYFEEMFRLLKPMGRLV 301
Cdd:PRK11873  151 ISNCVINLSPDK--ERVFKEAFRVLKPGGRFA 180
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 192-301 6.59e-05

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 44.19  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 192 ILDKLDLKPGERLLDIGCGWGS--MVITAaRRGIKALGVTLSKEQAAYANEwiaREGLQDLAEVRVQDY--REVPEHDFD 267
Cdd:PTZ00098   44 ILSDIELNENSKVLDIGSGLGGgcKYINE-KYGAHVHGVDICEKMVNIAKL---RNSDKNKIEFEANDIlkKDFPENTFD 119

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1307901430 268 GICSIGMMEHVGVKNYQSYFEEMFRLLKPMGRLV 301
Cdd:PTZ00098  120 MIYSRDAILHLSYADKKKLFEKCYKWLKPNGILL 153
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 189-301 5.20e-04

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 41.67  E-value: 5.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 189 LRLILDKLDLKPGERLLDIGC--GWGSMVIT-AARRGIKALGVTLSKEQAAY-----ANEWIAREGlQDLAEvRVQDYre 260
Cdd:COG0604   128 WQALFDRGRLKPGETVLVHGAagGVGSAAVQlAKALGARVIATASSPEKAELlralgADHVIDYRE-EDFAE-RVRAL-- 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1307901430 261 VPEHDFDGIcsigmMEHVGvknyQSYFEEMFRLLKPMGRLV 301
Cdd:COG0604   204 TGGRGVDVV-----LDTVG----GDTLARSLRALAPGGRLV 235
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 177-312 6.93e-04

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 41.15  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 177 EHMSLEDAQANK------LRLILDKLDLKPGERLLDIGCG-WGSMVITAAR-RGIKALGVTLSKEQAAYANEWIAREGLQ 248
Cdd:cd05188   105 DGLSLEEAALLPeplataYHALRRAGVLKPGDTVLVLGAGgVGLLAAQLAKaAGARVIVTDRSDEKLELAKELGADHVID 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307901430 249 DLAEVRVQDYREVPEHDFDGICsigmmEHVGVknyQSYFEEMFRLLKPMGRLVNHQITISHDKP 312
Cdd:cd05188   185 YKEEDLEEELRLTGGGGADVVI-----DAVGG---PETLAQALRLLRPGGRIVVVGGTSGGPPL 240
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 191-301 6.98e-04

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 40.91  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 191 LILDKLDLKPGERLLDIGCGWGSMVITAARrgikALG----VT---LSKEQAAYANEWIAREGLQDLAEVRVQDYREV-P 262
Cdd:COG2519    82 YIIARLDIFPGARVLEAGTGSGALTLALAR----AVGpegkVYsyeRREDFAEIARKNLERFGLPDNVELKLGDIREGiD 157

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1307901430 263 EHDFDGIcSIGMMEHVgvknyqSYFEEMFRLLKPMGRLV 301
Cdd:COG2519   158 EGDVDAV-FLDMPDPW------EALEAVAKALKPGGVLV 189
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 197-269 1.31e-03

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 40.13  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 197 DLKPGERLLDIGCGWGsmVIT---AAR-RGIKALGVTLSKEQAAYANEWIAREGLQDLAEVRVQDYREVPEHD----FDG 268
Cdd:COG4123    34 PVKKGGRVLDLGTGTG--VIAlmlAQRsPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELppgsFDL 111


                  .
gi 1307901430 269 I 269
Cdd:COG4123   112 V 112
PRK14968 PRK14968
putative methyltransferase; Provisional
 191-228 1.73e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.50  E-value: 1.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1307901430 191 LILDKLDLKPGERLLDIGCGWGSMVITAARRGIKALGV 228
Cdd:PRK14968   14 LLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGV 51
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 177-301 2.84e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 39.49  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 177 EHMSLEDAQA---NKLR---LILDKLDLKPGERLL--DIGCGWGSMVITAARrgiKALGVTLSKEQAAYANEWIAREGLQ 248
Cdd:cd08275   109 DGMSFEEAAAfpvNYLTayyALFELGNLRPGQSVLvhSAAGGVGLAAGQLCK---TVPNVTVVGTASASKHEALKENGVT 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1307901430 249 DLAEVRVQDY----REVPEHDFDGIcsigmMEHVGVknyqSYFEEMFRLLKPMGRLV 301
Cdd:cd08275   186 HVIDYRTQDYveevKKISPEGVDIV-----LDALGG----EDTRKSYDLLKPMGRLV 233
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 193-269 3.23e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 39.17  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 193 LDKLDlKPGERLLDIGCGWGSMVITAARRG-IKALGVTLSKE--QAAYANewIAREGLQDLAEVRVQDyrEVPEHDFDGI 269
Cdd:pfam06325 155 LERLV-KPGESVLDVGCGSGILAIAALKLGaKKVVGVDIDPVavRAAKEN--AELNGVEARLEVYLPG--DLPKEKADVV 229
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
190-301 5.11e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 38.19  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 190 RLILDKLDLKPGERLLDIGCGWGSMVIT---AARRGIKALGVTLSKEQAAYANEWIAREGLQDLaEVRVQDYREVPEHD- 265
Cdd:pfam01209  32 DFTMKCMGVKRGNKFLDVAGGTGDWTFGlsdSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNI-EFLQGNAEELPFEDd 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1307901430 266 -FDgICSIGMmehvGVKN---YQSYFEEMFRLLKPMGRLV 301
Cdd:pfam01209 111 sFD-IVTISF----GLRNfpdYLKVLKEAFRVLKPGGRVV 145
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 168-302 6.01e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 38.43  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 168 TYTCAVFDNEHMsledaqanklrliLDKLDLKPGERLLDIGC--GWGSMVIT-AARRGIKALGVTL-SKEQAAYA--NEW 241
Cdd:cd08274   158 TFPCSYSTAENM-------------LERAGVGAGETVLVTGAsgGVGSALVQlAKRRGAIVIAVAGaAKEEAVRAlgADT 224

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307901430 242 IAREGLQDLAevrvqDYREVPEHDFDGIcsigmMEHVGvknyQSYFEEMFRLLKPMGRLVN 302
Cdd:cd08274   225 VILRDAPLLA-----DAKALGGEPVDVV-----ADVVG----GPLFPDLLRLLRPGGRYVT 271
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 191-301 6.75e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 37.76  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307901430 191 LILDKLDLKPGERLLDIGCGWGSMviTA--ARRGIKALGVTLSKEQAAYANEWIAREGLQDlAEVRVQD-YREVPEHD-F 266
Cdd:COG2518    57 RMLEALDLKPGDRVLEIGTGSGYQ--AAvlARLAGRVYSVERDPELAERARERLAALGYDN-VTVRVGDgALGWPEHApF 133

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1307901430 267 DGICSIGMMEHVGvknyqsyfEEMFRLLKPMGRLV 301
Cdd:COG2518   134 DRIIVTAAAPEVP--------EALLEQLAPGGRLV 160
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
190-240 7.33e-03

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 37.86  E-value: 7.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1307901430 190 RLILDKLDLKPGERLLDIGCGWGSMVITAARRgIKALGVTLSKEQAAYANE 240
Cdd:COG0286    33 RLMVELLDPKPGETVYDPACGSGGFLVEAAEY-LKEHGGDERKKLSLYGQE 82
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 190-231 8.73e-03

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 37.56  E-value: 8.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1307901430 190 RLILDKLDLKpGERLLDIGCGWGsMV-ITAARRGikALGVTLS 231
Cdd:COG3897    61 RYLLDHPEVA-GKRVLELGCGLG-LVgIAAAKAG--AADVTAT 99
 
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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