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Conserved domains on  [gi|2331583102|ref|WP_265736909|]
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MULTISPECIES: cephalosporin hydroxylase family protein [Bacillus]

Protein Classification

cephalosporin hydroxylase family protein( domain architecture ID 10007503)

cephalosporin hydroxylase family protein similar to mycobacterial rhamnosyl O-methyltransferase that catalyzes the O-methylation of the hydroxyl group on C-2 of the first rhamnosyl residue linked to the phenolic group of glycosylated phenolphthiocerol dimycocerosates (PGL) and p-hydroxybenzoic acid derivatives (p-HBAD)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CmcI COG3510
Cephalosporin hydroxylase [Defense mechanisms];
1-206 8.92e-97

Cephalosporin hydroxylase [Defense mechanisms];


:

Pssm-ID: 442733  Cd Length: 239  Bit Score: 281.01  E-value: 8.92e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102   1 MDNISNEFLNQYYNSLVWLNdTHWFGVPICKLPSDLFLYQEIIYELKPDLIIECGTFHGGSALYLASMLDLIG-KGHVLT 79
Cdd:COG3510    20 LDDLSEEWLRASYKNKYSYN-FSWLGRPIIQYPQDMVAYQEIIWELKPDLIIETGIAHGGSLIFSASMLALLGmKGKVLG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  80 IDITPQP-NR------PSHNRITYLTASSVSVQAVQTIVSMRKPDDVVLVILDSDHSKEHVSKELLLYKSIVTTGSYMIV 152
Cdd:COG3510    99 IDIDIRPhNRaaieahPLAPRIELIEGSSTAPEIVEQVKALAKPGERVMVILDSNHTHEHVLAELEAYAPLVTPGSYLVV 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2331583102 153 EDTSINGNPL------LPDWGPGPMEAVDEFLTKNNNFIIDESK-HKFFISFNPKGFLKKI 206
Cdd:COG3510   179 FDTIIEDLPVdmfpdrPWGPGNNPKTAVEEYLKEHPEFEIDKSIeHKLLITVAPDGYLKRI 239
 
Name Accession Description Interval E-value
CmcI COG3510
Cephalosporin hydroxylase [Defense mechanisms];
1-206 8.92e-97

Cephalosporin hydroxylase [Defense mechanisms];


Pssm-ID: 442733  Cd Length: 239  Bit Score: 281.01  E-value: 8.92e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102   1 MDNISNEFLNQYYNSLVWLNdTHWFGVPICKLPSDLFLYQEIIYELKPDLIIECGTFHGGSALYLASMLDLIG-KGHVLT 79
Cdd:COG3510    20 LDDLSEEWLRASYKNKYSYN-FSWLGRPIIQYPQDMVAYQEIIWELKPDLIIETGIAHGGSLIFSASMLALLGmKGKVLG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  80 IDITPQP-NR------PSHNRITYLTASSVSVQAVQTIVSMRKPDDVVLVILDSDHSKEHVSKELLLYKSIVTTGSYMIV 152
Cdd:COG3510    99 IDIDIRPhNRaaieahPLAPRIELIEGSSTAPEIVEQVKALAKPGERVMVILDSNHTHEHVLAELEAYAPLVTPGSYLVV 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2331583102 153 EDTSINGNPL------LPDWGPGPMEAVDEFLTKNNNFIIDESK-HKFFISFNPKGFLKKI 206
Cdd:COG3510   179 FDTIIEDLPVdmfpdrPWGPGNNPKTAVEEYLKEHPEFEIDKSIeHKLLITVAPDGYLKRI 239
CmcI pfam04989
Cephalosporin hydroxylase; Members of this family are about 220 amino acids long. The CmcI ...
 18-206 7.99e-93

Cephalosporin hydroxylase; Members of this family are about 220 amino acids long. The CmcI protein is presumed to represent the cephalosporin-7--hydroxylase. However this has not been experimentally verified.


Pssm-ID: 428241  Cd Length: 206  Bit Score: 270.04  E-value: 7.99e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  18 WLNDTHWFGVPICKLPSDLFLYQEIIYELKPDLIIECGTFHGGSALYLASMLDLI-GKGHVLTIDIT-PQPNR------P 89
Cdd:pfam04989   3 YSYNFSWLGRPIIQYPQDMWAYQEIIFELKPDLIIETGIAHGGSAIFSASILALLgSPRKVLGVDIDiRAHNRaaieahP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  90 SHNRITYLTASSVSVQAVQTIVSMRKPDDVVLVILDSDHSKEHVSKELLLYKSIVTTGSYMIVEDTSINGNPLL----PD 165
Cdd:pfam04989  83 MAPRIEMIEGSSTDPEIIEQVRSLANEPGKILVILDSDHTHDHVLAELEAYAPLVSAGSYCVVFDTNIEDLPVLffpdPP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2331583102 166 WGPG--PMEAVDEFLTKNNNFIIDES-KHKFFISFNPKGFLKKI 206
Cdd:pfam04989 163 WGPGnnPKTAVEEYLATFPEFEIDKEiENKLLITVAPDGFLKRI 206
 
Name Accession Description Interval E-value
CmcI COG3510
Cephalosporin hydroxylase [Defense mechanisms];
1-206 8.92e-97

Cephalosporin hydroxylase [Defense mechanisms];


Pssm-ID: 442733  Cd Length: 239  Bit Score: 281.01  E-value: 8.92e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102   1 MDNISNEFLNQYYNSLVWLNdTHWFGVPICKLPSDLFLYQEIIYELKPDLIIECGTFHGGSALYLASMLDLIG-KGHVLT 79
Cdd:COG3510    20 LDDLSEEWLRASYKNKYSYN-FSWLGRPIIQYPQDMVAYQEIIWELKPDLIIETGIAHGGSLIFSASMLALLGmKGKVLG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  80 IDITPQP-NR------PSHNRITYLTASSVSVQAVQTIVSMRKPDDVVLVILDSDHSKEHVSKELLLYKSIVTTGSYMIV 152
Cdd:COG3510    99 IDIDIRPhNRaaieahPLAPRIELIEGSSTAPEIVEQVKALAKPGERVMVILDSNHTHEHVLAELEAYAPLVTPGSYLVV 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2331583102 153 EDTSINGNPL------LPDWGPGPMEAVDEFLTKNNNFIIDESK-HKFFISFNPKGFLKKI 206
Cdd:COG3510   179 FDTIIEDLPVdmfpdrPWGPGNNPKTAVEEYLKEHPEFEIDKSIeHKLLITVAPDGYLKRI 239
CmcI pfam04989
Cephalosporin hydroxylase; Members of this family are about 220 amino acids long. The CmcI ...
 18-206 7.99e-93

Cephalosporin hydroxylase; Members of this family are about 220 amino acids long. The CmcI protein is presumed to represent the cephalosporin-7--hydroxylase. However this has not been experimentally verified.


Pssm-ID: 428241  Cd Length: 206  Bit Score: 270.04  E-value: 7.99e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  18 WLNDTHWFGVPICKLPSDLFLYQEIIYELKPDLIIECGTFHGGSALYLASMLDLI-GKGHVLTIDIT-PQPNR------P 89
Cdd:pfam04989   3 YSYNFSWLGRPIIQYPQDMWAYQEIIFELKPDLIIETGIAHGGSAIFSASILALLgSPRKVLGVDIDiRAHNRaaieahP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  90 SHNRITYLTASSVSVQAVQTIVSMRKPDDVVLVILDSDHSKEHVSKELLLYKSIVTTGSYMIVEDTSINGNPLL----PD 165
Cdd:pfam04989  83 MAPRIEMIEGSSTDPEIIEQVRSLANEPGKILVILDSDHTHDHVLAELEAYAPLVSAGSYCVVFDTNIEDLPVLffpdPP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2331583102 166 WGPG--PMEAVDEFLTKNNNFIIDES-KHKFFISFNPKGFLKKI 206
Cdd:pfam04989 163 WGPGnnPKTAVEEYLATFPEFEIDKEiENKLLITVAPDGFLKRI 206
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-155 1.58e-07

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 47.69  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  52 IECGTFHGGSALYLASMLDLIGKGHVLTIDITPQPNRPSHN-RITYLTA-SSVSVQAVQTIVSMRKPDDVVLVILDSDHS 129
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAALRDNGLGRLTAVDPDPGAEEAGALlRKAGLDDrVRLIVGDSREALPSLADGPIDLLFIDGDHT 80

                          90       100
                  ....*....|....*....|....*.
gi 2331583102 130 KEHVSKELLLYKSIVTTGSYMIVEDT 155
Cdd:pfam13578  81 YEAVLNDLELWLPRLAPGGVILFHDI 106
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 37-178 1.15e-05

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 44.02  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331583102  37 FLYQeIIYELKPDLIIECGTFHGGSALYLASMLDliGKGHVLTIDItpqpnRPSHNRIT--YLTASSVSVQ-------AV 107
Cdd:COG4122     7 LLYL-LARLLGAKRILEIGTGTGYSTLWLARALP--DDGRLTTIEI-----DPERAAIAreNFARAGLADRirlilgdAL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2331583102 108 QTIVSMRKPD-DVVLVildsDHSKEHVSKELLLYKSIVTTGSYMIVEDTSINGNPLLPDWGPGPMEAVDEFL 178
Cdd:COG4122    79 EVLPRLADGPfDLVFI----DADKSNYPDYLELALPLLRPGGLIVADNVLWHGRVADPARRDPSTRAIREFN 146
 
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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