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Conserved domains on  [gi|488979002|ref|WP_002889849|]
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MULTISPECIES: cyclopropane-fatty-acyl-phospholipid synthase family protein [Klebsiella]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 11454891)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.-.-
Gene Ontology:  GO:0032259|GO:0008757|GO:1904047|GO:0008168
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 12-142 2.79e-21

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


:

Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 86.91  E-value: 2.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  12 ESEHRIHNPFTPEKYATLGRALRMAPGTTILDLGSGSGEMLCSWARDHQIVGTGVDMSLLFSQQAAARAEELGVSDRVTF 91
Cdd:COG2230   26 EDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEV 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488979002  92 VHQDASGYVASQPCDVAACVGATW-IGGGVAGT-IELLKQSLTPGGMLLIGEP 142
Cdd:COG2230  106 RLADYRDLPADGQFDAIVSIGMFEhVGPENYPAyFAKVARLLKPGGRLLLHTP 158
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 12-142 2.79e-21

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 86.91  E-value: 2.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  12 ESEHRIHNPFTPEKYATLGRALRMAPGTTILDLGSGSGEMLCSWARDHQIVGTGVDMSLLFSQQAAARAEELGVSDRVTF 91
Cdd:COG2230   26 EDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEV 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488979002  92 VHQDASGYVASQPCDVAACVGATW-IGGGVAGT-IELLKQSLTPGGMLLIGEP 142
Cdd:COG2230  106 RLADYRDLPADGQFDAIVSIGMFEhVGPENYPAyFAKVARLLKPGGRLLLHTP 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-139 9.26e-09

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: 51.66  E-value: 9.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  40 TILDLGSGSGEMLCSWARDHQIVGTGVDMS---LLFSQQAAARAEElgvsDRVTFVHQDASGYV--ASQPCDVAACVGA- 113
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISpvaLELARKAAAALLA----DNVEVLKGDAEELPpeADESFDVIISDPPl 76

                         90       100
                 ....*....|....*....|....*.
gi 488979002 114 TWIGGGVAGTIELLKQSLTPGGMLLI 139
Cdd:cd02440   77 HHLVEDLARFLEEARRLLKPGGVLVL 102
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 37-168 1.85e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 49.34  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002   37 PGTTILDLGSGSGEMLCSWAR----DHQIVgtGVDMSLLFSQQAAARAEELGvSDRVTFVHQDA---SGYVASQPCDVAA 109
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEelgpNAEVV--GIDISEEAIEKARENAQKLG-FDNVEFEQGDIeelPELLEDDKFDVVI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488979002  110 CVGATWIGGGVAGTIELLKQSLTPGGMLLIGEP-WWRKRPATAEE------AIACGAQSPDDFLTL 168
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPdSLAELPAHVKEdstyyaGCVGGAILKKKLYEL 145
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 31-96 8.69e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 45.53  E-value: 8.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488979002  31 RALRMAPGTTILDLGSGSGEMLCSWARDHQIVG--TGVDmsllFSQQ----AAARAEELGVSDRVTFVHQDA 96
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGevVGLD----FSEGmlavGREKLRDLGLSGNVEFVQGDA 112
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
41-191 8.74e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 45.48  E-value: 8.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002    41 ILDLGSGSGEMLCSWARDH---QIVGTGVDmsllfSQQAAA---RAEELGVSDRVTFVHQDASGYVASQPCDVAacvgat 114
Cdd:smart00828   3 VLDFGCGYGSDLIDLAERHphlQLHGYTIS-----PEQAEVgreRIRALGLQGRIRIFYRDSAKDPFPDTYDLV------ 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002   115 wIGGGVAGTI----EL---LKQSLTPGGMLLIGEPWWRKRPATAEEAIACgaqspdDFLTLPALVAHFGELGYDVVEMVL 187
Cdd:smart00828  72 -FGFEVIHHIkdkmDLfsnISRHLKDGGHLVLADFIANLLSAIEHEETTS------YLVTREEWAELLARNNLRVVEGVD 144


                   ....
gi 488979002   188 ADQE 191
Cdd:smart00828 145 ASLE 148
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 34-107 5.80e-04

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 40.14  E-value: 5.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488979002   34 RMAPGTTILDLGSGSGEMLCSWARDH-QIVGTGVDMS---LlfsQQAAARAEELGVsDRVTFVHQDASGYVASQPCDV 107
Cdd:TIGR03534  83 RLKKGPRVLDLGTGSGAIALALAKERpDARVTAVDISpeaL---AVARKNARRLGL-ENVEFLQGDWFEPLPSGKFDL 156
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 12-142 2.79e-21

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 86.91  E-value: 2.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  12 ESEHRIHNPFTPEKYATLGRALRMAPGTTILDLGSGSGEMLCSWARDHQIVGTGVDMSLLFSQQAAARAEELGVSDRVTF 91
Cdd:COG2230   26 EDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEV 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488979002  92 VHQDASGYVASQPCDVAACVGATW-IGGGVAGT-IELLKQSLTPGGMLLIGEP 142
Cdd:COG2230  106 RLADYRDLPADGQFDAIVSIGMFEhVGPENYPAyFAKVARLLKPGGRLLLHTP 158
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 24-158 2.91e-10

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: 56.93  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  24 EKYATLGRALRMAPGTTILDLGSGSGEMLCSWARDHQIVgTGVDMSLLFSQQAAARAEELGVsdRVTFVHQDASGY-VAS 102
Cdd:COG2226    9 DGREALLAALGLRPGARVLDLGCGTGRLALALAERGARV-TGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpFPD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488979002 103 QPCDVAACVGATWIGGGVAGTIELLKQSLTPGGMLLIGEPWWRKRPATAEEAIACG 158
Cdd:COG2226   86 GSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAG 141
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
37-139 5.84e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 52.13  E-value: 5.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  37 PGTTILDLGSGSGEMLCSWAR---DHQIvgTGVDMSLLFSQQAAARAeelgvsDRVTFVHQDASGYVASQPCDVAACVGA 113
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAErfpGARV--TGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEPFDLVVSNAA 72

                         90       100
                 ....*....|....*....|....*..
gi 488979002 114 -TWIgGGVAGTIELLKQSLTPGGMLLI 139
Cdd:COG4106   73 lHWL-PDHAALLARLAAALAPGGVLAV 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-139 9.26e-09

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: 51.66  E-value: 9.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  40 TILDLGSGSGEMLCSWARDHQIVGTGVDMS---LLFSQQAAARAEElgvsDRVTFVHQDASGYV--ASQPCDVAACVGA- 113
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISpvaLELARKAAAALLA----DNVEVLKGDAEELPpeADESFDVIISDPPl 76

                         90       100
                 ....*....|....*....|....*.
gi 488979002 114 TWIGGGVAGTIELLKQSLTPGGMLLI 139
Cdd:cd02440   77 HHLVEDLARFLEEARRLLKPGGVLVL 102
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 34-142 3.11e-08

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: 50.79  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  34 RMAPGTTILDLGSGSGEMLCSWAR-DHQIvgTGVDMSLLFSQQAAARAEELgvsdRVTFVHQDASGY-VASQPCDVAACV 111
Cdd:COG2227   21 LLPAGGRVLDVGCGTGRLALALARrGADV--TGVDISPEALEIARERAAEL----NVDFVQGDLEDLpLEDGSFDLVICS 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488979002 112 GA-TWIgGGVAGTIELLKQSLTPGGMLLIGEP 142
Cdd:COG2227   95 EVlEHL-PDPAALLRELARLLKPGGLLLLSTP 125
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
31-139 8.96e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 50.77  E-value: 8.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  31 RALRMAPGTTILDLGSGSGEMLCSWARDHQIVgTGVDmsllFSQQAAARAEELGVSDRvtFVHQDASG-YVASQPCDVAA 109
Cdd:COG4976   40 ARLPPGPFGRVLDLGCGTGLLGEALRPRGYRL-TGVD----LSEEMLAKAREKGVYDR--LLVADLADlAEPDGRFDLIV 112

                         90       100       110
                 ....*....|....*....|....*....|
gi 488979002 110 CVGATWIGGGVAGTIELLKQSLTPGGMLLI 139
Cdd:COG4976  113 AADVLTYLGDLAAVFAGVARALKPGGLFIF 142
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 37-168 1.85e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 49.34  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002   37 PGTTILDLGSGSGEMLCSWAR----DHQIVgtGVDMSLLFSQQAAARAEELGvSDRVTFVHQDA---SGYVASQPCDVAA 109
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEelgpNAEVV--GIDISEEAIEKARENAQKLG-FDNVEFEQGDIeelPELLEDDKFDVVI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488979002  110 CVGATWIGGGVAGTIELLKQSLTPGGMLLIGEP-WWRKRPATAEE------AIACGAQSPDDFLTL 168
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPdSLAELPAHVKEdstyyaGCVGGAILKKKLYEL 145
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 41-135 5.61e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.40  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002   41 ILDLGSGSGEMLCSWARDHQIVGTGVDMSLLFSQQAAARAEELGVsdRVTFVHQDASGY-VASQPCDVAACVGA-TWIG- 117
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpFPDGSFDLVVSSGVlHHLPd 78

                          90
                  ....*....|....*...
gi 488979002  118 GGVAGTIELLKQSLTPGG 135
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 14-139 7.96e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 48.37  E-value: 7.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  14 EHRIHNPFTPEKYATLGRALRMAPGTTILDLGSGSGEMLCSWARDHQIVGTGVDMSLLFSQQAAARAEELGVSdRVTFVH 93
Cdd:COG0500    3 DSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLG-NVEFLV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488979002  94 QDASGYVA--SQPCDVAACVGA-TWIGGGV-AGTIELLKQSLTPGGMLLI 139
Cdd:COG0500   82 ADLAELDPlpAESFDLVVAFGVlHHLPPEErEALLRELARALKPGGVLLL 131
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 29-95 8.37e-06

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: 45.52  E-value: 8.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488979002  29 LGRALRMAPGTTILDLGSGSGE-MLCSWARDHQIVGTGVDMSLLFSQQAAARAEELGVSDRVTFVHQD 95
Cdd:COG4123   29 LAAFAPVKKGGRVLDLGTGTGViALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGD 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 31-96 8.69e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 45.53  E-value: 8.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488979002  31 RALRMAPGTTILDLGSGSGEMLCSWARDHQIVG--TGVDmsllFSQQ----AAARAEELGVSDRVTFVHQDA 96
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGevVGLD----FSEGmlavGREKLRDLGLSGNVEFVQGDA 112
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
41-191 8.74e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 45.48  E-value: 8.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002    41 ILDLGSGSGEMLCSWARDH---QIVGTGVDmsllfSQQAAA---RAEELGVSDRVTFVHQDASGYVASQPCDVAacvgat 114
Cdd:smart00828   3 VLDFGCGYGSDLIDLAERHphlQLHGYTIS-----PEQAEVgreRIRALGLQGRIRIFYRDSAKDPFPDTYDLV------ 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002   115 wIGGGVAGTI----EL---LKQSLTPGGMLLIGEPWWRKRPATAEEAIACgaqspdDFLTLPALVAHFGELGYDVVEMVL 187
Cdd:smart00828  72 -FGFEVIHHIkdkmDLfsnISRHLKDGGHLVLADFIANLLSAIEHEETTS------YLVTREEWAELLARNNLRVVEGVD 144


                   ....
gi 488979002   188 ADQE 191
Cdd:smart00828 145 ASLE 148
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 37-139 4.42e-05

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: 43.61  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  37 PGTTILDLGSGSGEMLCSWARdhqIVG-----TGVDMSLLFSQQAAARAEELGVSDRVTFVHQDASGYVASQPCDVAAC- 110
Cdd:COG2519   91 PGARVLEAGTGSGALTLALAR---AVGpegkvYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIDEGDVDAVFLd 167

                         90       100
                 ....*....|....*....|....*....
gi 488979002 111 VGATWIgggvagTIELLKQSLTPGGMLLI 139
Cdd:COG2519  168 MPDPWE------ALEAVAKALKPGGVLVA 190
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
40-137 4.49e-05

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 43.41  E-value: 4.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  40 TILDLGSGSGEMLCSWA-RDHQIvgTGVDMSLLFSQQAAARAEELGVSDRVTFVH---QDASGYVAsQPCDVA---ACVg 112
Cdd:PRK11036  47 RVLDAGGGEGQTAIKLAeLGHQV--ILCDLSAEMIQRAKQAAEAKGVSDNMQFIHcaaQDIAQHLE-TPVDLIlfhAVL- 122

                         90       100
                 ....*....|....*....|....*
gi 488979002 113 aTWIGGGVAgTIELLKQSLTPGGML 137
Cdd:PRK11036 123 -EWVADPKS-VLQTLWSVLRPGGAL 145
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 42-96 2.47e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 39.19  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488979002   42 LDLGSGSGEMLCSWARDHQIVgTGVDmsllFSQQAAARAEELGVSDRVTFVHQDA 96
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARV-TGVD----ISPEMLELAREKAPREGLTFVVGDA 50
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 5-96 4.04e-04

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 40.55  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002    5 PRIFTISESeHRIHNPFTPEkYATLGRALRMAPGTTILDLGSGSGEMLCSWARdhQIVGTGVDMSLLFSQQAAARA---- 80
Cdd:pfam08704  10 PELWTLNLP-HRTQILYTPD-ISLITMMLELRPGSVVCESGTGSGSLSHAIIR--TVAPTGHLFTFEFHEQRADKAreef 85

                          90
                  ....*....|....*.
gi 488979002   81 EELGVSDRVTFVHQDA 96
Cdd:pfam08704  86 REHGIDQLVTVTHRDV 101
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
31-110 5.05e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.40  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  31 RALRMA--PGTTILDLGSGSG--EMLCswARDHQIVGTGVDMSLLFSQQAAARAEELGVSDRVTFVHQDASGYVASQPCD 106
Cdd:COG4076   27 AAIERVvkPGDVVLDIGTGSGllSMLA--ARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKAD 104


                 ....
gi 488979002 107 VAAC 110
Cdd:COG4076  105 VIIS 108
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 34-107 5.80e-04

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 40.14  E-value: 5.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488979002   34 RMAPGTTILDLGSGSGEMLCSWARDH-QIVGTGVDMS---LlfsQQAAARAEELGVsDRVTFVHQDASGYVASQPCDV 107
Cdd:TIGR03534  83 RLKKGPRVLDLGTGSGAIALALAKERpDARVTAVDISpeaL---AVARKNARRLGL-ENVEFLQGDWFEPLPSGKFDL 156
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 32-95 1.33e-03

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 38.98  E-value: 1.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979002  32 ALRMAPGTTILDLGSGSGEMLCSWARDH-QIVGTGVDMSllfsqQAA---AR--AEELGVSDRVTFVHQD 95
Cdd:COG2890  107 LLPAGAPPRVLDLGTGSGAIALALAKERpDARVTAVDIS-----PDAlavARrnAERLGLEDRVRFLQGD 171
PRK08317 PRK08317
hypothetical protein; Provisional
 31-98 9.16e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 36.45  E-value: 9.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488979002  31 RALRMAPGTTILDLGSGSGEMLCSWARDhqiVG-----TGVDMSLLFSQQAAARAEELGvsDRVTFVHQDASG 98
Cdd:PRK08317  13 ELLAVQPGDRVLDVGCGPGNDARELARR---VGpegrvVGIDRSEAMLALAKERAAGLG--PNVEFVRGDADG 80
 
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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