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Conserved domains on  [gi|2279134399|ref|WP_255974483|]
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precorrin-6y C5,15-methyltransferase (decarboxylating) subunit CbiE [Streptomyces longispororuber]

Protein Classification

precorrin-6Y C5,15-methyltransferase (decarboxylating) subunit CbiT( domain architecture ID 11454932)

precorrin-6Y C5,15-methyltransferase (decarboxylating) subunit CbiT catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 8-375 2.10e-55

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: 187.68  E-value: 2.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399   8 IGWDGSPPTAAARSALQAATLVAGAGHHLALPEVSERAERIRLGSVSLAARRIAGHRGTAVVLADGDPGFFGVVRTLRAP 87
Cdd:COG2242    10 GGGGGLGAAAAAAAAAAAALVGGGRLLLLLLALLAAAALAWPPPLAALLLLLLARRGVVVVVLASGDPGFGGGGGTLLRL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  88 EYGLEVEVVPAVSSVAQAFARAGMPWDDAQVVVAHRRTLRRAVNVCRAHTKVAVLTSPGAGPAELGLLLEGVHR---TFV 164
Cdd:COG2242    90 LLAEEVRVIPAPSSFSLAAARLGWALAEVVVVSLLGRALLLLLLALLPGARLLLLLLDGAAPAAAAALLLLRGGggsLLL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 165 ICEELGTDREQVTVVTSDKAADHTWRDPNVVIVIggpvtgapgtggwLAGGDADSGPRGWALPAAEYTGPFGEGETEQLR 244
Cdd:COG2242   170 VLEGLGGGEERRRTGAAAAAAAADAAALNVVALL-------------VVAGPGARLPRTPGLPDEAFERDKGPITKREVR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 245 AAQLARLGPRTGDLVWDIGCGSGAFTAEAGRF--GAAVIAVDRDPDACARTLATARRFGIQ-AQIVHGTAPHVLEDLPEP 321
Cdd:COG2242   237 ALTLAKLALRPGDVLWDIGAGSGSVSIEAARLapGGRVYAIERDPERAALIRANARRFGVPnVEVVEGEAPEALADLPDP 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2279134399 322 DVVRVGGGG---AAVVSAVADRRPA--RIVTHAATRDAAELIGRDLTEHGYDVECALLQ 375
Cdd:COG2242   317 DAVFIGGSGgnlPEILEACWARLRPggRLVANAVTLETLALALEALAELGYGGELVQVQ 375
 
Name Accession Description Interval E-value
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 8-375 2.10e-55

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: 187.68  E-value: 2.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399   8 IGWDGSPPTAAARSALQAATLVAGAGHHLALPEVSERAERIRLGSVSLAARRIAGHRGTAVVLADGDPGFFGVVRTLRAP 87
Cdd:COG2242    10 GGGGGLGAAAAAAAAAAAALVGGGRLLLLLLALLAAAALAWPPPLAALLLLLLARRGVVVVVLASGDPGFGGGGGTLLRL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  88 EYGLEVEVVPAVSSVAQAFARAGMPWDDAQVVVAHRRTLRRAVNVCRAHTKVAVLTSPGAGPAELGLLLEGVHR---TFV 164
Cdd:COG2242    90 LLAEEVRVIPAPSSFSLAAARLGWALAEVVVVSLLGRALLLLLLALLPGARLLLLLLDGAAPAAAAALLLLRGGggsLLL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 165 ICEELGTDREQVTVVTSDKAADHTWRDPNVVIVIggpvtgapgtggwLAGGDADSGPRGWALPAAEYTGPFGEGETEQLR 244
Cdd:COG2242   170 VLEGLGGGEERRRTGAAAAAAAADAAALNVVALL-------------VVAGPGARLPRTPGLPDEAFERDKGPITKREVR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 245 AAQLARLGPRTGDLVWDIGCGSGAFTAEAGRF--GAAVIAVDRDPDACARTLATARRFGIQ-AQIVHGTAPHVLEDLPEP 321
Cdd:COG2242   237 ALTLAKLALRPGDVLWDIGAGSGSVSIEAARLapGGRVYAIERDPERAALIRANARRFGVPnVEVVEGEAPEALADLPDP 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2279134399 322 DVVRVGGGG---AAVVSAVADRRPA--RIVTHAATRDAAELIGRDLTEHGYDVECALLQ 375
Cdd:COG2242   317 DAVFIGGSGgnlPEILEACWARLRPggRLVANAVTLETLALALEALAELGYGGELVQVQ 375
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 28-197 2.35e-42

Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B.


Pssm-ID: 381171 [Multi-domain]  Cd Length: 198  Bit Score: 147.26  E-value: 2.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  28 LVAGAGHHLALPEvSERAERIRLGSVSLAA--RRIAGHRGTAVVLADGDPGFFGVVRTLRAPEYGLEVEVVPAVSSVAQA 105
Cdd:cd11644    24 VVIGAKRLLELFP-DLGAEKIPLPSEDIAEllEEIAEAGKRVVVLASGDPGFYGIGKTLLRRLGGEEVEVIPGISSVQLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 106 FARAGMPWDDAQVVVAHRRTLRRAVNVCRAHTKVAVLTSPGAGPAELG-LLLE--GVHRTFVICEELGTDREQVTVVTSD 182
Cdd:cd11644   103 AARLGLPWEDARLVSLHGRDLENLRRALRRGRKVFVLTDGKNTPAEIArLLLErgLGDSRVTVGENLGYPDERITEGTAE 182

                         170
                  ....*....|....*
gi 2279134399 183 KAADHTWRDPNVVIV 197
Cdd:cd11644   183 ELAEEEFSDLNVVLI 197
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 27-196 3.43e-27

precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL.


Pssm-ID: 274146 [Multi-domain]  Cd Length: 204  Bit Score: 107.02  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  27 TLVAGAGHHLAL--PEVSERAERIRLGS-----VSLAARRIAGHRgtAVVLADGDPGFFGVVRTLRAPEYGLEVEVVPAV 99
Cdd:TIGR02467  24 DLVVGGERHLELlaELIGEKREIILTYKdldelLEFIAATRKEKR--VVVLASGDPLFYGIGRTLAERLGKERLEIIPGI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 100 SSVAQAFARAGMPWDDAQVVVAH-RRTLRRAVNVCRAHTKVAVLTSPGAGPAELG-LLLE---GVHRTFVICEELGTDRE 174
Cdd:TIGR02467 102 SSVQYAFARLGLPWQDAVVISLHgRELDELLLALLRGHRKVAVLTDPRNGPAEIArELIElgiGGSYELTVGENLGYEDE 181

                         170       180
                  ....*....|....*....|...
gi 2279134399 175 QVTVVT-SDKAADHTWRDPNVVI 196
Cdd:TIGR02467 182 RITEGTlEEIAAAQFDFSPLLVV 204
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
28-197 3.78e-22

cobalt-precorrin-7 (C(5))-methyltransferase;


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 93.39  E-value: 3.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  28 LVAGAGHHLALPEVSERAERIRLGSV--SLAARRIAGHRG-TAVVLADGDPGFFGVVRTLRAPEYGLE-VEVVPAVSSVA 103
Cdd:PRK05787   28 VVVGSKRVLELFPELIDGEAFVLTAGlrDLLEWLELAAKGkNVVVLSTGDPLFSGLGKLLKVRRAVAEdVEVIPGISSVQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 104 QAFARAGMPWDDAQVVVAHRRT--LRRAVNVCRAHTKVAVLTSPGAGPAELGLLLE---GVHRTFVICEELGTDREQVTV 178
Cdd:PRK05787  108 YAAARLGIDMNDVVFTTSHGRGpnFEELEDLLKNGRKVIMLPDPRFGPKEIAAELLergKLERRIVVGENLSYPDERIHK 187

                         170
                  ....*....|....*....
gi 2279134399 179 VTSDKAADHTWRDPNVVIV 197
Cdd:PRK05787  188 LTLSEIEPLEFSDMSVVVI 206
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 66-185 5.09e-11

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 61.59  E-value: 5.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  66 TAVVLADGDPGFFGVVRTL--RAPEYGLEVEVVPAVSSVAQAFARAGMPWDDAQVVVAH-------RRTLRRAVNVCRAH 136
Cdd:pfam00590  79 DVARLVSGDPLVYGTGSYLveALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVlflpglaRIELRLLEALLANG 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2279134399 137 TKVAVLTSPGAGPAELGLLLE--GVHRTFVICEELGTDREQVTVVTSDKAA 185
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLElyPDTTPVAVVERAGTPDEKVVRGTLGELA 209
rADc smart00650
Ribosomal RNA adenine dimethylases;
251-309 3.30e-06

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 46.73  E-value: 3.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279134399  251 LGPRTGDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACAR---TLATARRFgiqaQIVHG 309
Cdd:smart00650   9 ANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRlreKFAAADNL----TVIHG 66
 
Name Accession Description Interval E-value
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 8-375 2.10e-55

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: 187.68  E-value: 2.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399   8 IGWDGSPPTAAARSALQAATLVAGAGHHLALPEVSERAERIRLGSVSLAARRIAGHRGTAVVLADGDPGFFGVVRTLRAP 87
Cdd:COG2242    10 GGGGGLGAAAAAAAAAAAALVGGGRLLLLLLALLAAAALAWPPPLAALLLLLLARRGVVVVVLASGDPGFGGGGGTLLRL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  88 EYGLEVEVVPAVSSVAQAFARAGMPWDDAQVVVAHRRTLRRAVNVCRAHTKVAVLTSPGAGPAELGLLLEGVHR---TFV 164
Cdd:COG2242    90 LLAEEVRVIPAPSSFSLAAARLGWALAEVVVVSLLGRALLLLLLALLPGARLLLLLLDGAAPAAAAALLLLRGGggsLLL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 165 ICEELGTDREQVTVVTSDKAADHTWRDPNVVIVIggpvtgapgtggwLAGGDADSGPRGWALPAAEYTGPFGEGETEQLR 244
Cdd:COG2242   170 VLEGLGGGEERRRTGAAAAAAAADAAALNVVALL-------------VVAGPGARLPRTPGLPDEAFERDKGPITKREVR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 245 AAQLARLGPRTGDLVWDIGCGSGAFTAEAGRF--GAAVIAVDRDPDACARTLATARRFGIQ-AQIVHGTAPHVLEDLPEP 321
Cdd:COG2242   237 ALTLAKLALRPGDVLWDIGAGSGSVSIEAARLapGGRVYAIERDPERAALIRANARRFGVPnVEVVEGEAPEALADLPDP 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2279134399 322 DVVRVGGGG---AAVVSAVADRRPA--RIVTHAATRDAAELIGRDLTEHGYDVECALLQ 375
Cdd:COG2242   317 DAVFIGGSGgnlPEILEACWARLRPggRLVANAVTLETLALALEALAELGYGGELVQVQ 375
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 28-197 2.35e-42

Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B.


Pssm-ID: 381171 [Multi-domain]  Cd Length: 198  Bit Score: 147.26  E-value: 2.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  28 LVAGAGHHLALPEvSERAERIRLGSVSLAA--RRIAGHRGTAVVLADGDPGFFGVVRTLRAPEYGLEVEVVPAVSSVAQA 105
Cdd:cd11644    24 VVIGAKRLLELFP-DLGAEKIPLPSEDIAEllEEIAEAGKRVVVLASGDPGFYGIGKTLLRRLGGEEVEVIPGISSVQLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 106 FARAGMPWDDAQVVVAHRRTLRRAVNVCRAHTKVAVLTSPGAGPAELG-LLLE--GVHRTFVICEELGTDREQVTVVTSD 182
Cdd:cd11644   103 AARLGLPWEDARLVSLHGRDLENLRRALRRGRKVFVLTDGKNTPAEIArLLLErgLGDSRVTVGENLGYPDERITEGTAE 182

                         170
                  ....*....|....*
gi 2279134399 183 KAADHTWRDPNVVIV 197
Cdd:cd11644   183 ELAEEEFSDLNVVLI 197
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 27-198 4.98e-36

Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441842 [Multi-domain]  Cd Length: 207  Bit Score: 131.04  E-value: 4.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  27 TLVAGAGHHLALPEvSERAERIRLGS-----VSLAARRIAGHRgtAVVLADGDPGFFGVVRTLRA---PEyglEVEVVPA 98
Cdd:COG2241    29 DVVVGGKRHLELFP-DLGAERIVWPSplselLEELLALLRGRR--VVVLASGDPLFYGIGATLARhlpAE---EVRVIPG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  99 VSSVAQAFARAGMPWDDAQVVVAHRRTLRRAVNVCRAHTKVAVLTSPGAGPAEL-GLLLE-GV-HRTFVICEELGTDREQ 175
Cdd:COG2241   103 ISSLQLAAARLGWPWQDAAVVSLHGRPLERLLPALAPGRRVLVLTDDGNTPAAIaRLLLErGFgDSRLTVLENLGGPDER 182

                         170       180
                  ....*....|....*....|...
gi 2279134399 176 VTVVTSDKAADHTWRDPNVVIVI 198
Cdd:COG2241   183 ITRGTAEELADADFSDLNVVAIE 205
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 27-196 3.43e-27

precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL.


Pssm-ID: 274146 [Multi-domain]  Cd Length: 204  Bit Score: 107.02  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  27 TLVAGAGHHLAL--PEVSERAERIRLGS-----VSLAARRIAGHRgtAVVLADGDPGFFGVVRTLRAPEYGLEVEVVPAV 99
Cdd:TIGR02467  24 DLVVGGERHLELlaELIGEKREIILTYKdldelLEFIAATRKEKR--VVVLASGDPLFYGIGRTLAERLGKERLEIIPGI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 100 SSVAQAFARAGMPWDDAQVVVAH-RRTLRRAVNVCRAHTKVAVLTSPGAGPAELG-LLLE---GVHRTFVICEELGTDRE 174
Cdd:TIGR02467 102 SSVQYAFARLGLPWQDAVVISLHgRELDELLLALLRGHRKVAVLTDPRNGPAEIArELIElgiGGSYELTVGENLGYEDE 181

                         170       180
                  ....*....|....*....|...
gi 2279134399 175 QVTVVT-SDKAADHTWRDPNVVI 196
Cdd:TIGR02467 182 RITEGTlEEIAAAQFDFSPLLVV 204
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
28-197 3.78e-22

cobalt-precorrin-7 (C(5))-methyltransferase;


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 93.39  E-value: 3.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  28 LVAGAGHHLALPEVSERAERIRLGSV--SLAARRIAGHRG-TAVVLADGDPGFFGVVRTLRAPEYGLE-VEVVPAVSSVA 103
Cdd:PRK05787   28 VVVGSKRVLELFPELIDGEAFVLTAGlrDLLEWLELAAKGkNVVVLSTGDPLFSGLGKLLKVRRAVAEdVEVIPGISSVQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 104 QAFARAGMPWDDAQVVVAHRRT--LRRAVNVCRAHTKVAVLTSPGAGPAELGLLLE---GVHRTFVICEELGTDREQVTV 178
Cdd:PRK05787  108 YAAARLGIDMNDVVFTTSHGRGpnFEELEDLLKNGRKVIMLPDPRFGPKEIAAELLergKLERRIVVGENLSYPDERIHK 187

                         170
                  ....*....|....*....
gi 2279134399 179 VTSDKAADHTWRDPNVVIV 197
Cdd:PRK05787  188 LTLSEIEPLEFSDMSVVVI 206
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 241-351 3.88e-16

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 74.29  E-value: 3.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 241 EQLRAAQLARLGPRTGDLVWDIGCGSGAFTAEAGRF--GAAVIAVDRDPDACARTLATARRFGIQA-QIVHGTAPHVLED 317
Cdd:TIGR02469   5 REVRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLvpNGRVYAIERNPEALDLIERNLRRFGVSNiVIVEGDAPEAPEA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2279134399 318 -LPEPDVVRVGGGGA---AVVSAVADRRP--ARIVTHAAT 351
Cdd:TIGR02469  85 lLPDPDAVFVGGSGGllqEILEAVERRLRpgGRIVLNAIT 124
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 241-370 3.30e-14

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 70.98  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 241 EQLRAAQLARLGPRTGDLVWDIGCGSGAFTAEAGRF---GAAVIAVDRDPDACARTLATARRFGI--QAQIVHGTAPHVL 315
Cdd:PRK00377   26 EEIRALALSKLRLRKGDMILDIGCGTGSVTVEASLLvgeTGKVYAVDKDEKAINLTRRNAEKFGVlnNIVLIKGEAPEIL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279134399 316 EDL-PEPDVVRVGGGG---AAVVSAVADR--RPARIVTHAATRDAAELIGRDLTEHGYDVE 370
Cdd:PRK00377  106 FTInEKFDRIFIGGGSeklKEIISASWEIikKGGRIVIDAILLETVNNALSALENIGFNLE 166
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 240-370 2.33e-12

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 67.89  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 240 TEQLRAAQLARLGPRTGDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACARTLATARRFGI-QAQIVHGTAPHVLEDL 318
Cdd:COG2265   218 AEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLkNVEFVAGDLEEVLPEL 297

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279134399 319 PE---PDVV-----RvGGGGAAVVSAVADRRPARIV---THAAT--RDAAELIgrdltEHGYDVE 370
Cdd:COG2265   298 LWggrPDVVvldppR-AGAGPEVLEALAALGPRRIVyvsCNPATlaRDLALLV-----EGGYRLE 356
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
234-351 6.62e-12

precorrin-6Y C5,15-methyltransferase subunit CbiT;


Pssm-ID: 180961  Cd Length: 196  Bit Score: 64.25  E-value: 6.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 234 PFGEGETEQLRAAQLaRLGPRTgdLVWDIGCGSGAFTAEAGRF--GAAVIAVDRDPDACARTLATARRFGIQ-AQIVHGT 310
Cdd:PRK07402   22 PLTKREVRLLLISQL-RLEPDS--VLWDIGAGTGTIPVEAGLLcpKGRVIAIERDEEVVNLIRRNCDRFGVKnVEVIEGS 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2279134399 311 APHVLEDL-PEPDVVRVGGGG--AAVVSAVADRRPA--RIVTHAAT 351
Cdd:PRK07402   99 APECLAQLaPAPDRVCIEGGRpiKEILQAVWQYLKPggRLVATASS 144
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 66-185 5.09e-11

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 61.59  E-value: 5.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  66 TAVVLADGDPGFFGVVRTL--RAPEYGLEVEVVPAVSSVAQAFARAGMPWDDAQVVVAH-------RRTLRRAVNVCRAH 136
Cdd:pfam00590  79 DVARLVSGDPLVYGTGSYLveALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVlflpglaRIELRLLEALLANG 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2279134399 137 TKVAVLTSPGAGPAELGLLLE--GVHRTFVICEELGTDREQVTVVTSDKAA 185
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLElyPDTTPVAVVERAGTPDEKVVRGTLGELA 209
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 243-322 5.65e-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: 60.01  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 243 LRAAQLARLGPRTGDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACARTLATARRFGIQAQIVHGTAphvlEDLPEPD 322
Cdd:COG2226    10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDA----EDLPFPD 85
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 56-177 4.50e-09

Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme.


Pssm-ID: 381172 [Multi-domain]  Cd Length: 223  Bit Score: 56.36  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  56 AARRIAGHR---GTAVVLADGDPGFFG----VVRTLRAPEYglEVEVVPAVSSVAQAFARAGMP---WDDAQVVV---AH 122
Cdd:cd11645    73 AAEEIAEELkegKDVAFLTLGDPSLYStfsyLLERLRAPGV--EVEIIPGITSFSAAAARLGIPlaeGDESLAILpatYD 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2279134399 123 RRTLRRAVNVCRAhtkvAVLTSPGAGPAELGLLLE--GVHRTFVICEELGTDREQVT 177
Cdd:cd11645   151 EEELEKALENFDT----VVLMKVGRNLEEIKELLEelGLLDKAVYVERCGMEGERIY 203
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 261-322 2.46e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.41  E-value: 2.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2279134399 261 DIGCGSGAFTAE-AGRFGAAVIAVDRDPDACARTLATARRFGIQAQIVHGTAphvlEDLPEPD 322
Cdd:pfam13649   3 DLGCGTGRLTLAlARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDA----EDLPFPD 61
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 231-306 7.43e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 51.47  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 231 YTGPFGEGETEQLRAAQ-------LARLGPRTGDLVWDIGCGSGAFTAE-AGRFGAAVIAVDRDPDACARTLATARRFGI 302
Cdd:COG2230    20 YSCAYFEDPDDTLEEAQeakldliLRKLGLKPGMRVLDIGCGWGGLALYlARRYGVRVTGVTLSPEQLEYARERAAEAGL 99


                  ....
gi 2279134399 303 QAQI 306
Cdd:COG2230   100 ADRV 103
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 56-177 7.45e-07

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


Pssm-ID: 441844 [Multi-domain]  Cd Length: 229  Bit Score: 49.71  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  56 AARRIAGH---RGTAVVLADGDPGFFG----VVRTLRapEYGLEVEVVPAVSSVAQAFARAGMP--WDDAQVVV----AH 122
Cdd:COG2243    79 AAARIAEEleaGRDVAFLTEGDPSLYStfmyLLERLR--ERGFEVEVIPGITSFSAAAAALGIPlaEGDEPLTVlpgtLL 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2279134399 123 RRTLRRAVNVCRAhtkVAVLTSPGAGPAELGLLLE-GVHRTFVICEELGTDREQVT 177
Cdd:COG2243   157 EEELERALDDFDT---VVIMKVGRNFPKVREALEEaGLLDRAWYVERAGMPDERIV 209
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
241-331 1.04e-06

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 48.84  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 241 EQLRAAQLARLGPRTGDLVWDIGCGSGAFTAEAG-RFGA-AVIAVDRDPDACARTLATARRFGIQ-AQIVHGTAPHVLED 317
Cdd:PRK08287   17 EEVRALALSKLELHRAKHLIDVGAGTGSVSIEAAlQFPSlQVTAIERNPDALRLIKENRQRFGCGnIDIIPGEAPIELPG 96

                          90
                  ....*....|....
gi 2279134399 318 lpEPDVVRVGGGGA 331
Cdd:PRK08287   97 --KADAIFIGGSGG 108
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 248-324 1.59e-06

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: 46.93  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 248 LARLGPRTGDlVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACARTLATARRFGIQaqIVHG---------------TAP 312
Cdd:COG2227    18 LARLLPAGGR-VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVD--FVQGdledlpledgsfdlvICS 94

                          90
                  ....*....|..
gi 2279134399 313 HVLEDLPEPDVV 324
Cdd:COG2227    95 EVLEHLPDPAAL 106
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 247-322 3.27e-06

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 46.87  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 247 QLARL-----GPRTGDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACARTLATARRFGIQ-AQIVHGTAphvlEDLPE 320
Cdd:COG1041    13 RLARAlvnlaGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEdADVIRGDA----RDLPL 88


                  ..
gi 2279134399 321 PD 322
Cdd:COG1041    89 AD 90
rADc smart00650
Ribosomal RNA adenine dimethylases;
251-309 3.30e-06

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 46.73  E-value: 3.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279134399  251 LGPRTGDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACAR---TLATARRFgiqaQIVHG 309
Cdd:smart00650   9 ANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRlreKFAAADNL----TVIHG 66
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
254-324 4.50e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 47.34  E-value: 4.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279134399 254 RTGDLVWDIGCGSGAFTAEAGRFGAA-VIAVDRDPDACARTLATARRFGIQAQI--VHGTAPHVleDLPEP-DVV 324
Cdd:COG4076    34 KPGDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARRIIAANGLSDRItvINADATDL--DLPEKaDVI 106
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
245-324 5.82e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 46.82  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 245 AAQL----ARLGPRTGDLVWDIGCGSGAFTAEAGRFGAA-VIAVDRDPDACARTLATARRFGIQAQIVHGTAPHVlEDLP 319
Cdd:COG2263    31 AAELlhlaYLRGDIEGKTVLDLGCGTGMLAIGAALLGAKkVVGVDIDPEALEIARENAERLGVRVDFIRADVTRI-PLGG 109


                  ....*
gi 2279134399 320 EPDVV 324
Cdd:COG2263   110 SVDTV 114
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 259-324 6.71e-06

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: 44.73  E-value: 6.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2279134399 259 VWDIGCGSGAFTAEAGRFGAA-VIAVDRDPDACARTL-ATARRFGIQAQIVHGTAPHVLEDLPEP-DVV 324
Cdd:cd02440     2 VLDLGCGTGALALALASGPGArVTGVDISPVALELARkAAAALLADNVEVLKGDAEELPPEADESfDVI 70
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 261-322 8.14e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.19  E-value: 8.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279134399 261 DIGCGSGAFTAEAGRFGAAVIAVDRDPDACARtlATARRFGIQAQIVHGTAphvlEDLPEPD 322
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTGVDISPEMLEL--AREKAPREGLTFVVGDA----EDLPFPD 57
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
241-322 8.93e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 45.76  E-value: 8.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 241 EQLRAAQLARLGPRTGDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDAcartLATARRFGIQAQIVHGTaphvLEDLPE 320
Cdd:COG4976    32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEM----LAKAREKGVYDRLLVAD----LADLAE 103


                  ..
gi 2279134399 321 PD 322
Cdd:COG4976   104 PD 105
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 239-299 2.77e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 45.53  E-value: 2.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2279134399 239 ETEQLRAAQLARLGPRTGDLVWDIGCGSG--AFTAEAGRFGAAVIAVDRDPDAcartLATARR 299
Cdd:COG2890    96 ETEELVELALALLPAGAPPRVLDLGTGSGaiALALAKERPDARVTAVDISPDA----LAVARR 154
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 245-324 7.72e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.37  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 245 AAQLARLgPRTGDLVwDIGCGSGAFTAE-AGRFGAAVIAVDRDPDACARTLATARRFGI-QAQIVHGTApHVLEDLPEP- 321
Cdd:COG0500    18 LALLERL-PKGGRVL-DLGCGTGRNLLAlAARFGGRVIGIDLSPEAIALARARAAKAGLgNVEFLVADL-AELDPLPAEs 94


                  ....
gi 2279134399 322 -DVV 324
Cdd:COG0500    95 fDLV 98
PRK08317 PRK08317
hypothetical protein; Provisional
 241-395 9.32e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 43.39  E-value: 9.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 241 EQLRAAQLARLGPRTGDLVWDIGCGSGAFTAE-AGRFGAA--VIAVDRDPDACArtLATARRF--GIQAQIVHGTAPH-- 313
Cdd:PRK08317    5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARElARRVGPEgrVVGIDRSEAMLA--LAKERAAglGPNVEFVRGDADGlp 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 314 -------------VLEDLPEPD--------VVRVGGGGAA--------VVSAVADRRPARIVTHAATRDAAELIGRDLte 364
Cdd:PRK08317   83 fpdgsfdavrsdrVLQHLEDPAralaeiarVLRPGGRVVVldtdwdtlVWHSGDRALMRKILNFWSDHFADPWLGRRL-- 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2279134399 365 HGYDVECAlLQSVELDTRVWTEKERTVGFLL 395
Cdd:PRK08317  161 PGLFREAG-LTDIEVEPYTLIETDLKEADKG 190
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
235-306 2.40e-04

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 42.47  E-value: 2.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279134399 235 FGEG--ETEQLRAAQLARLgPRTGDLVWDIGCGSG--AFTAEagRFGAA-VIAVDRDPDACARTLATARRFGIQAQI 306
Cdd:COG2264   127 FGTGthPTTRLCLEALEKL-LKPGKTVLDVGCGSGilAIAAA--KLGAKrVLAVDIDPVAVEAARENAELNGVEDRI 200
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 239-323 2.74e-04

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.46  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 239 ETEQLRAAQLARLGPRTGDLVWDIGCGSGA--FTAEAGRFGAAVIAVDRDPDAcartLATARR-----FGIQAQIVHGta 311
Cdd:PRK09328   92 ETEELVEWALEALLLKEPLRVLDLGTGSGAiaLALAKERPDAEVTAVDISPEA----LAVARRnakhgLGARVEFLQG-- 165

                          90
                  ....*....|..
gi 2279134399 312 pHVLEDLPEPDV 323
Cdd:PRK09328  166 -DWFEPLPGGRF 176
PRK14968 PRK14968
putative methyltransferase; Provisional
 256-308 3.03e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 3.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2279134399 256 GDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACARTLATARRFGIQAQIVH 308
Cdd:PRK14968   24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVE 76
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 43-112 4.77e-04

Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone.


Pssm-ID: 381173 [Multi-domain]  Cd Length: 238  Bit Score: 41.25  E-value: 4.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2279134399  43 ERAERirlgSVSLAArriAGHRgTAVVlADGDPGFFG----VVRTLRAPEYGLEVEVVPAVSSVAQAFARAGMP 112
Cdd:cd11646    57 ERARE----ALELAL---EGKR-VALV-SSGDPGIYGmaglVLELLDERWDDIEVEVVPGITAALAAAALLGAP 121
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
261-324 4.90e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 39.04  E-value: 4.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279134399 261 DIGCGSGAFTAE-AGRF-GAAVIAVDRDPDAcartLATARRFGIQAQIVHGTAPHVleDLPEP-DVV 324
Cdd:COG4106     7 DLGCGTGRLTALlAERFpGARVTGVDLSPEM----LARARARLPNVRFVVADLRDL--DPPEPfDLV 67
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 245-398 5.41e-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: 41.30  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 245 AAQ-LARLGPRTGDLVWDIGCGSGAFTA-------EAGRfgaaVIAVDRDPDACARTLATARRFG-----------IQAQ 305
Cdd:COG2519    80 AGYiIARLDIFPGARVLEAGTGSGALTLalaravgPEGK----VYSYERREDFAEIARKNLERFGlpdnvelklgdIREG 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 306 IVHGTAPHVLEDLPEPDvvrvggggaAVVSAVADR-RP-ARIVTHAATRDAAELIGRDLTEHGYdvecALLQSVELDTRV 383
Cdd:COG2519   156 IDEGDVDAVFLDMPDPW---------EALEAVAKAlKPgGVLVAYVPTVNQVSKLVEALRESGF----TDIEAVETLLRE 222

                         170       180
                  ....*....|....*....|....*
gi 2279134399 384 WT-EKERT---------VGFLLSGR 398
Cdd:COG2519   223 WKvEGLAVrpehrmvghTGFLVFAR 247
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 251-309 6.88e-04

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 41.26  E-value: 6.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279134399 251 LGPRTGDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACAR---TLATARRFgiqaQIVHG 309
Cdd:COG0030    33 AGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAIlreTFAAYPNL----TVIEG 90
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 254-324 7.32e-04

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: 41.10  E-value: 7.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2279134399 254 RTGDLVWDIGCGSGAFTAEAGRFGAA-VIAVDRDPDACARTLATARRFGIQAQIVhgtaPHVLEDLPEP--DVV 324
Cdd:pfam06325 160 KPGESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVEARLE----VYLPGDLPKEkaDVV 229
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 253-320 2.06e-03

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 38.97  E-value: 2.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279134399 253 PRTGDLVWDIGCGSGAFTAE-AGRF-GAAVIAVDRDPDACARTLATARRFGIQ-AQIVHGTAPHVLEDLPE 320
Cdd:COG0220    30 GNDAPLVLEIGFGKGEFLVElAAANpDINFIGIEVHEPGVAKALKKAEEEGLTnVRLLRGDAVELLELFPD 100
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
 65-111 2.49e-03

Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.


Pssm-ID: 381168 [Multi-domain]  Cd Length: 225  Bit Score: 38.91  E-value: 2.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2279134399  65 GTAVVLADGDPGFFG----VVRTLRapEYGLEVEVVPAVSSVAQAFARAGM 111
Cdd:cd11641    69 KDVVRLHTGDPSLYGaireQIDALD--KLGIPYEVVPGVSSFFAAAAALGT 117
PRK14967 PRK14967
putative methyltransferase; Provisional
 239-344 2.96e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 38.88  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 239 ETEQLRAAQLARLGPRTGDLVWDIGCGSGAFTAEAGRFGAA-VIAVDRDPDACARTLATARRFGIQAQIVHGTAPHVLED 317
Cdd:PRK14967   20 EDTQLLADALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGsVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEF 99

                          90       100
                  ....*....|....*....|....*..
gi 2279134399 318 LPEPDVVRVGGGGAAVVSAVADRRPAR 344
Cdd:PRK14967  100 RPFDVVVSNPPYVPAPPDAPPSRGPAR 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 248-301 4.41e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 37.79  E-value: 4.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2279134399 248 LARLGPRTGDL--VWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACARTLATARRFG 301
Cdd:pfam13489  13 LLRLLPKLPSPgrVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQ 68
NodS pfam05401
Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The ...
 224-293 4.47e-03

Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involved in N methylation of LCOs. NodS uses N-deacetylated chitooligosaccharides, the products of the NodBC proteins, as its methyl acceptors.


Pssm-ID: 428457  Cd Length: 201  Bit Score: 38.06  E-value: 4.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279134399 224 WALPAAEYtgpfgegetEQLRAAQLARLGPRTGDL--VWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACART 293
Cdd:pfam05401  19 WNIDSCAF---------EQKRLAAILELCLGDGDAadALEIGCAAGAFTEMLAILCERLTVVDLMPEAIAKA 81
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
235-324 4.64e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 38.59  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 235 FGEG--ETEQLRAAQLARLgPRTGDLVWDIGCGSG--AFTAEagRFGAA-VIAVDRDPDACARTLATARRFGIQAQIvhg 309
Cdd:PRK00517   98 FGTGthPTTRLCLEALEKL-VLPGKTVLDVGCGSGilAIAAA--KLGAKkVLAVDIDPQAVEAARENAELNGVELNV--- 171

                          90
                  ....*....|....*
gi 2279134399 310 tapHVLEDLPEPDVV 324
Cdd:PRK00517  172 ---YLPQGDLKADVI 183
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
 56-112 5.51e-03

precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273642 [Multi-domain]  Cd Length: 230  Bit Score: 38.06  E-value: 5.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2279134399  56 AARRIAGH--RGTAVVLA-DGDPGFFG----VVRTLRAPeyGLEVEVVPAVSSVAQAFARAGMP 112
Cdd:TIGR01467  79 AAEAVAAEleEGRDVAFLtLGDPSLYStfsyLLQRLQGM--GIEVEVVPGITSFAACASAAGLP 140
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 245-309 6.14e-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: 6.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2279134399 245 AAQLARLGPRTGDLVWDIGCGSGAFTAEAGRFGAAVIAVDRDPDACARTLATARRFGI-QAQIVHG 309
Cdd:COG2518    56 ARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAALGYdNVTVRVG 121
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 38-202 6.76e-03

Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme.


Pssm-ID: 381169  Cd Length: 228  Bit Score: 37.80  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399  38 LPEVSERAERI----RLGSVSLAARRI------AGHRGTAVV-LADGDPGFFG----VVRTLRapEYGLEVEVVPAVSSV 102
Cdd:cd11642    36 LALAPPGAELIyvgkRPGRHSVPQEEInellveLAREGKRVVrLKGGDPFVFGrggeEIEALR--EAGIPFEVVPGITSA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279134399 103 AQAFARAGMPwddaqvvVAHRRtLRRAVNVCRAHTKVAVLTSPGAGPAELGL---LLEGVHRTFVICEEL---------- 169
Cdd:cd11642   114 IAAAAYAGIP-------LTHRG-VASSVTFVTGHEADGKLPDDDAALARPGGtlvIYMGVSNLEEIAERLiaaglppdtp 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2279134399 170 ------GTDREQVTVVTS-----DKAADHTWRDPnVVIVIGGPV 202
Cdd:cd11642   186 vaivenATTPDQRVVVGTlaelaEKAAEAGIRSP-ALIVVGEVV 228
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
 56-112 9.85e-03

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 37.27  E-value: 9.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2279134399  56 AARRIAGH--RG-TAVVLADGDPGFFGVVRTLR---APEYglEVEVVPAVSSVAQAFARAGMP 112
Cdd:PRK05990   87 SAEAVAAHldAGrDVAVICEGDPFFYGSYMYLHdrlAPRY--ETEVIPGVCSMLGCWSVLGAP 147
 
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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