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Conserved domains on  [gi|491429183|ref|WP_005286978|]
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cobalt-precorrin-4 methyltransferase [Edwardsiella tarda]

Protein Classification

cobalt-precorrin-4/precorrin-4 C(11)-methyltransferase( domain architecture ID 10794173)

cobalt-precorrin-4/precorrin-4 C(11)-methyltransferase catalyzes the methylation of C-11 in cobalt-precorrin-4 or precorrin-4 to form cobalt-precorrin-5 or precorrin-5 in the anaerobic pathway or aerobic pathway of adenosylcobalamin biosynthesis, respectively

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
1-257 0e+00

cobalt-precorrin-4 methyltransferase;


:

Pssm-ID: 185370  Cd Length: 257  Bit Score: 505.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   1 MSERFDPQCVWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAG 80
Cdd:PRK15473   1 MSETFDPRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQIIDLMEAGVKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  81 KTVVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEAL 160
Cdd:PRK15473  81 KTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLESF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183 161 ASHRSSMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLGDEY 240
Cdd:PRK15473 161 ASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFLGEEY 240
                        250
                 ....*....|....*..
gi 491429183 241 HYSRLYAADFSHEYRQA 257
Cdd:PRK15473 241 HYSKLYDADFSHEYRKA 257
 
Name Accession Description Interval E-value
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
1-257 0e+00

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 505.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   1 MSERFDPQCVWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAG 80
Cdd:PRK15473   1 MSETFDPRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQIIDLMEAGVKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  81 KTVVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEAL 160
Cdd:PRK15473  81 KTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLESF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183 161 ASHRSSMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLGDEY 240
Cdd:PRK15473 161 ASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFLGEEY 240
                        250
                 ....*....|....*..
gi 491429183 241 HYSRLYAADFSHEYRQA 257
Cdd:PRK15473 241 HYSKLYDADFSHEYRKA 257
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
10-257 3.26e-146

Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 442122 [Multi-domain]  Cd Length: 256  Bit Score: 409.06  E-value: 3.26e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAGKTVVRLQTG 89
Cdd:COG2875    5 VYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGAEIVDSASMTLEEIIALMKEAAAEGKDVVRLHSG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  90 DVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEALASHRSSMAI 169
Cdd:COG2875   85 DPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTPMPEGESLASLAAHGATLAI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183 170 YLSVQRIQRVVERLIAgGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLGDE-YHYSRLYAA 248
Cdd:COG2875  165 YLSAHRIDEVVEELLE-GYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEdFARSKLYDP 243

                 ....*....
gi 491429183 249 DFSHEYRQA 257
Cdd:COG2875  244 GFSHGFRPA 252
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
13-237 1.66e-135

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: 380.59  E-value: 1.66e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAGKTVVRLQTGDVS 92
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGAEIVDSAGMTLEEIIEVMREAAREGKDVVRLHTGDPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  93 LYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEALASHRSSMAIYLS 172
Cdd:cd11641   81 LYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPVPEGESLRELAKHGATLAIFLS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491429183 173 VQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLG 237
Cdd:cd11641  161 AALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
10-255 1.30e-115

precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 200107  Cd Length: 247  Bit Score: 331.21  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAGKTVVRLQTG 89
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLAHCRPGAEVVNSAGMSLEEIVDIMSDAHREGKDVARLHSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   90 DVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEALASHRSSMAI 169
Cdd:TIGR01465  81 DPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTPMPEGEKLADLAKHGATMAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  170 YLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLGDEYH-YSRLYAA 248
Cdd:TIGR01465 161 FLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRIGkRSKLYDP 240

                  ....*..
gi 491429183  249 DFSHEYR 255
Cdd:TIGR01465 241 DFSHSFR 247
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
10-216 9.50e-50

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: 162.51  E-value: 9.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECH-----DSATLHLTQILDLMEAGVKAGKTVV 84
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPmtedkEPLEEAYEEIAEALAAALRAGKDVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   85 RLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRlagRTPVPEGEQLEALASHR 164
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLP---GLARIELRLLEALLANG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 491429183  165 SSMAIYLSVQRIQRVVERLIAgGYAPQTPAAVIYKATWPESRTVRGTLADIA 216
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLE-LYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
 
Name Accession Description Interval E-value
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
1-257 0e+00

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 505.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   1 MSERFDPQCVWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAG 80
Cdd:PRK15473   1 MSETFDPRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYAGSLINTELLDYCPAQAECHDSAELHLEQIIDLMEAGVKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  81 KTVVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEAL 160
Cdd:PRK15473  81 KTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLESF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183 161 ASHRSSMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLGDEY 240
Cdd:PRK15473 161 ASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGNFLGEEY 240
                        250
                 ....*....|....*..
gi 491429183 241 HYSRLYAADFSHEYRQA 257
Cdd:PRK15473 241 HYSKLYDADFSHEYRKA 257
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
10-257 3.26e-146

Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 442122 [Multi-domain]  Cd Length: 256  Bit Score: 409.06  E-value: 3.26e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAGKTVVRLQTG 89
Cdd:COG2875    5 VYFVGAGPGDPDLITVKGRRLLEEADVVLYAGSLVPPELLAYCKPGAEIVDSASMTLEEIIALMKEAAAEGKDVVRLHSG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  90 DVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEALASHRSSMAI 169
Cdd:COG2875   85 DPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTPMPEGESLASLAAHGATLAI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183 170 YLSVQRIQRVVERLIAgGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLGDE-YHYSRLYAA 248
Cdd:COG2875  165 YLSAHRIDEVVEELLE-GYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGAEdFARSKLYDP 243

                 ....*....
gi 491429183 249 DFSHEYRQA 257
Cdd:COG2875  244 GFSHGFRPA 252
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
13-237 1.66e-135

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: 380.59  E-value: 1.66e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAGKTVVRLQTGDVS 92
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVIYAGSLVPPELLAYAKPGAEIVDSAGMTLEEIIEVMREAAREGKDVVRLHTGDPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  93 LYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEALASHRSSMAIYLS 172
Cdd:cd11641   81 LYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPVPEGESLRELAKHGATLAIFLS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491429183 173 VQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLG 237
Cdd:cd11641  161 AALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
10-255 1.30e-115

precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 200107  Cd Length: 247  Bit Score: 331.21  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECHDSATLHLTQILDLMEAGVKAGKTVVRLQTG 89
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYAGSLVPPELLAHCRPGAEVVNSAGMSLEEIVDIMSDAHREGKDVARLHSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   90 DVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQLEALASHRSSMAI 169
Cdd:TIGR01465  81 DPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTPMPEGEKLADLAKHGATMAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  170 YLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGDFLGDEYH-YSRLYAA 248
Cdd:TIGR01465 161 FLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRIGkRSKLYDP 240

                  ....*..
gi 491429183  249 DFSHEYR 255
Cdd:TIGR01465 241 DFSHSFR 247
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
13-234 8.03e-66

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: 204.21  E-value: 8.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVIYaGSLINPALLDYCSPETECHD------SATLHLTQILDLMEAGVKAGKTVVRL 86
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLY-DRLVSPEILALAPPGAELIYvgkrpgRHSVPQEEINELLVELAREGKRVVRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  87 QTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIItrLAGRT-PVPEGEQLEALASHRS 165
Cdd:cd11642   80 KGGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTF--VTGHEaDGKLPDDDAALARPGG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491429183 166 SMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGD 234
Cdd:cd11642  158 TLVIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGE 226
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
10-234 1.19e-62

Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439778 [Multi-domain]  Cd Length: 245  Bit Score: 196.45  E-value: 1.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYaGSLINPALLDYCSPETECHD---SATLH-LTQ--ILDLMEAGVKAGKTV 83
Cdd:COG0007    4 VYLVGAGPGDPDLLTLKALRALQQADVVLY-DRLVSPEILALARPDAELIYvgkRGGRHsLPQeeINALLVELARAGKRV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  84 VRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIItrLAGRTPvPEGEQL--EALA 161
Cdd:COG0007   83 VRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTF--VTGHEK-DGKLDLdwAALA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491429183 162 SHRSSMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGD 234
Cdd:COG0007  160 RPGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGE 232
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
10-234 2.14e-54

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 175.79  E-value: 2.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYaGSLINPALLDYCSPETE---------CHDSATLHLTQILdlMEAGvKAG 80
Cdd:PRK06136   5 VYLVGAGPGDPDLITLKGVRLLEQADVVLY-DDLVSPEILAYAKPDAEliyvgkragRHSTKQEEINRLL--VDYA-RKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  81 KTVVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRLAGRTPVPEGEQ-LEA 159
Cdd:PRK06136  81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLEPEVnWSA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491429183 160 LASHRSSMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGD 234
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGE 235
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
10-234 3.84e-51

uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273643  Cd Length: 236  Bit Score: 167.02  E-value: 3.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYaGSLINPALLDYCSPETECHD---SATLHLT---QILDLMEAGVKAGKTV 83
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLY-DALVSPEILAYAPPQAELIDvgkRPGCHSKkqeEINRLLVELAREGKKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   84 VRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSL-IIT---RLAGRTPVPEgeqlEA 159
Cdd:TIGR01469  81 VRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVtFVTgheADDKALEVDW----EA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491429183  160 LASHRSSMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGD 234
Cdd:TIGR01469 157 LAKGAGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGE 231
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
10-216 9.50e-50

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: 162.51  E-value: 9.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLINPALLDYCSPETECH-----DSATLHLTQILDLMEAGVKAGKTVV 84
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPmtedkEPLEEAYEEIAEALAAALRAGKDVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   85 RLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITRlagRTPVPEGEQLEALASHR 164
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLP---GLARIELRLLEALLANG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 491429183  165 SSMAIYLSVQRIQRVVERLIAgGYAPQTPAAVIYKATWPESRTVRGTLADIA 216
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLE-LYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
10-234 2.94e-48

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 160.18  E-value: 2.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYaGSLINPALLDYCSPETE---------CHDSatlhlTQ--ILDLMEAGVK 78
Cdd:PLN02625  17 VFLVGTGPGDPDLLTLKALRLLQTADVVLY-DRLVSPDILDLVPPGAEllyvgkrggYHSR-----TQeeIHELLLSFAE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  79 AGKTVVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLIItrLAGRTP---VPEGE 155
Cdd:PLN02625  91 AGKTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRF--LTGHDReggTDPLD 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491429183 156 QLEALASHRSSMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGD 234
Cdd:PLN02625 169 VAEAAADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGE 247
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
12-233 1.37e-36

uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily use S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. 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. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and Ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381178 [Multi-domain]  Cd Length: 243  Bit Score: 129.60  E-value: 1.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  12 FVGAGPGDRELITLKGYRLLQQAQLVIyAGSLINPALLDY--------------------CSPETECHDSATLH---LTQ 68
Cdd:cd11724    4 LVGVGPGDPDLITLRALKAIKKADVVF-APPDLRKRFAEYlagkevlddphglftyygkkCSPLEEAEKECEELekqRAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  69 ILDLMEAGVKAGKTVVRLQTGDVSLYGSVREQGEELTKRGIawRVVPGVSAFLGAAAELGVEYTVPQLSQSLIITrlAGR 148
Cdd:cd11724   83 IVQKIREALAQGKNVALLDSGDPTIYGPWIWYLEEFADLNP--EVIPGVSSFNAANAALKRSLTGGGDSRSVILT--APF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183 149 TPVPEGEQLEALASHRSSMAIYLSVQRIQRVVERLiAGGYAPQTPAAVIYKATWPES-RTVRGTLADIAQPVQAAGIRKT 227
Cdd:cd11724  159 ALKENEDLLEDLAATGDTLVIFMMRLDLDELVEKL-KKHYPPDTPVAIVYHAGYSEKeKVIRGTLDDILEKLGGEKEPFL 237

                 ....*.
gi 491429183 228 ALILVG 233
Cdd:cd11724  238 GLIYVG 243
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
10-234 5.53e-35

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 130.50  E-value: 5.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYaGSLINPALLDYCSPETE---CHDSATLHLT--QILD--LMEAGvKAGKT 82
Cdd:PRK07168   5 VYLVGAGPGDEGLITKKAIECLKRADIVLY-DRLLNPFFLSYTKQTCElmyCGKMPKNHIMrqEMINahLLQFA-KEGKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  83 VVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSliITRLAGRTPVPEGEQLEALAS 162
Cdd:PRK07168  83 VVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNS--VTLLTGHAKGPLTDHGKYNSS 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491429183 163 HRS-SMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALILVGD 234
Cdd:PRK07168 161 HNSdTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGD 233
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
13-233 1.42e-28

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. 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. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381167 [Multi-domain]  Cd Length: 219  Bit Score: 107.86  E-value: 1.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVIYAGS---LINPALLDYCSPETECHD-SATLHLTQILDLMEAGVKAGKTVVRLQT 88
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKdskLLSLVLRAILKDGKRIYDlHDPNVEEEMAELLLEEARQGKDVAFLSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  89 GDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEytvpqLSQSLIITRLAGRTPVPEGEQLEALASHRSSMA 168
Cdd:cd09815   81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGID-----LGESFLFVTASDLLENPRLLVLKALAKERRHLV 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491429183 169 IYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIaQPVQAAGIRKTALILVG 233
Cdd:cd09815  156 LFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKEL-RAERTERGKPLTTILVG 219
cysG PRK10637
siroheme synthase CysG;
10-237 8.09e-25

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 102.14  E-value: 8.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYaGSLINPALLD-----------------YCSPETEchdsatlhLTQILdL 72
Cdd:PRK10637 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVVY-DRLVSDDIMNlvrrdadrvfvgkragyHCVPQEE--------INQIL-L 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  73 MEAgvKAGKTVVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQLSQSLiitRLAGRTPVP 152
Cdd:PRK10637 288 REA--QKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSV---RLVTGHLKT 362
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183 153 EGE-QLEALASHRSSMAIYLSVQRIQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQpvQAAGIRKTALIL 231
Cdd:PRK10637 363 GGElDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPADMPVALVENGTSVTQRVVSGTLTQLGE--LAQQVNSPSLII 440

                 ....*.
gi 491429183 232 VGDFLG 237
Cdd:PRK10637 441 VGRVVG 446
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
13-219 3.18e-19

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: 83.33  E-value: 3.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVIYAGS----------------LINPALLDYCSPETECHDSATLHLTQILDLMEAG 76
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVIFVPVSkggegsaaliiaaallIPDKEIIPLEFPMTKDREELEEAWDEAAEEIAEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  77 VKAGKTVVRLQTGDVSLYGS---VReqgEELTKRGIAWRVVPGVSAFLGAAAELGVEYTvpQLSQSL-IITRLAGRtpvp 152
Cdd:cd11645   81 LKEGKDVAFLTLGDPSLYSTfsyLL---ERLRAPGVEVEIIPGITSFSAAAARLGIPLA--EGDESLaILPATYDE---- 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491429183 153 egEQLEALASHRSSMAIYLSVQRIQRVVERLIAGGYAPQtpAAVIYKATWPESRTVRGTLADIAQPV 219
Cdd:cd11645  152 --EELEKALENFDTVVLMKVGRNLEEIKELLEELGLLDK--AVYVERCGMEGERIYTDLEELKEEKL 214
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
10-216 6.93e-19

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: 82.45  E-value: 6.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIY----------AGSLINPAL-------LDYcsPETECHDSATLHLTQILDL 72
Cdd:COG2243    5 LYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkaslAREIVAPYLppariveLVF--PMTTDYEALVAAWDEAAAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  73 MEAGVKAGKTVVRLQTGDVSLYGS---VReqgEELTKRGIAWRVVPGVSAFLGAAAELGveytVP--QLSQSLIItrLAG 147
Cdd:COG2243   83 IAEELEAGRDVAFLTEGDPSLYSTfmyLL---ERLRERGFEVEVIPGITSFSAAAAALG----IPlaEGDEPLTV--LPG 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491429183 148 RTPVpegEQLEALASHRSSMAIYLSVQRIQRVVERLIAGGYAPQtpAAVIYKATWPESRTVRGtLADIA 216
Cdd:COG2243  154 TLLE---EELERALDDFDTVVIMKVGRNFPKVREALEEAGLLDR--AWYVERAGMPDERIVPG-LAEVD 216
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
13-217 4.34e-15

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: 71.37  E-value: 4.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVIYAGSLInpALLDYCSPETechdsATLHLTQILDLMEAGVKAGKTVVRLQTGDVS 92
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLL--ELFPDLGAEK-----IPLPSEDIAELLEEIAEAGKRVVVLASGDPG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  93 LYGSvreqGEELTKR--GIAWRVVPGVSAFLGAAAELGVEYtvpqlsQSLIITRLAGRtpvpEGEQLEALASHRSSMAIY 170
Cdd:cd11644   74 FYGI----GKTLLRRlgGEEVEVIPGISSVQLAAARLGLPW------EDARLVSLHGR----DLENLRRALRRGRKVFVL 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491429183 171 LS-VQRIQRVVERLIAGGYaPQTPAAVIYKATWPESRTVRGTLADIAQ 217
Cdd:cd11644  140 TDgKNTPAEIARLLLERGL-GDSRVTVGENLGYPDERITEGTAEELAE 186
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
13-142 1.16e-13

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 68.02  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQlVIYA-------GSLINPALLDYCSPETE---CH-------DSATLHLTQILDLMEA 75
Cdd:PRK05576   7 IGLGPGDPELLTVKAARILEEAD-VVYApasrkggGSLALNIVRPYLKEETEiveLHfpmskdeEEKEAVWKENAEEIAA 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491429183  76 GVKAGKTVVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELGVEYTVPQlsQSLII 142
Cdd:PRK05576  86 EAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGD--ESLAI 150
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
10-216 4.55e-12

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 63.35  E-value: 4.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIyaGSlinPALLDYCSPETEC-HDSATLHLTQILDLMEAgVKAGKTVVRLQT 88
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVVV--GS---KRVLELFPELIDGeAFVLTAGLRDLLEWLEL-AAKGKNVVVLST 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  89 GDVSLYG---------SVREQGEeltkrgiawrVVPGVSAFLGAAAELGVeytvpQLSQSLIITrLAGRTPVPEgEQLEA 159
Cdd:PRK05787  76 GDPLFSGlgkllkvrrAVAEDVE----------VIPGISSVQYAAARLGI-----DMNDVVFTT-SHGRGPNFE-ELEDL 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491429183 160 LASHRSsmAIYLSVQRI--QRVVERLIAGGyAPQTPAAVIYKATWPESRTVRGTLADIA 216
Cdd:PRK05787 139 LKNGRK--VIMLPDPRFgpKEIAAELLERG-KLERRIVVGENLSYPDERIHKLTLSEIE 194
PRK05948 PRK05948
precorrin-2 C(20)-methyltransferase;
11-217 1.85e-11

precorrin-2 C(20)-methyltransferase;


Pssm-ID: 180320  Cd Length: 238  Bit Score: 61.97  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  11 WFVGAGPGDRELITLKGYRLLQQAQLVIY----------AGSLINPalldYCSPETEchdSATLHLTQILD---LMEAGV 77
Cdd:PRK05948   7 YGISVGPGDPELITLKGLRLLQSAPVVAFpaglagqpglAEQIIAP----WLSPQQI---KLPLYFPYVQDeeqLEQAWQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  78 KA----------GKTVVRLQTGDVSLYGSVREQGEELTKR--GIAWRVVPGVSAFLGAAAELGVEYTVPqlSQSLIItrL 145
Cdd:PRK05948  80 AAadqvwhyleqGEDVAFACEGDVSFYSTFTYLAQTLQELypQVAIQTIPGVCSPLAAAAALGIPLTLG--SQRLAI--L 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491429183 146 AGRTPVPEGEQLEALAshrsSMAIYLSVQRI-QRVVERLIAGGYAPQtpAAVIYKATWPESRTVRgTLADIAQ 217
Cdd:PRK05948 156 PALYHLEELEQALTWA----DVVVLMKVSSVyPQVWQWLKARNLLEQ--ASLVERATTPEQVIYR-NLEDYPD 221
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
13-214 3.91e-11

precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273641 [Multi-domain]  Cd Length: 239  Bit Score: 61.16  E-value: 3.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   13 VGAGPGDRELITLKGYRLLQQAQLVI-YAG--SLINPALldycsPETECHDSAtlhLTQILDLMEAGV---KAGKTVVRL 86
Cdd:TIGR01466   4 VGIGPGAEELMTPEAKEALAEADVIVgYKTylDLIEDLI-----PGKEVVTSG---MREEIARAELAIelaAEGRTVALV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   87 QTGDVSLYGSVREQGEELTKRGIAW--RVVPGVSAFLGAAAELGV----EYTVPQLSQSLiitrlagrTPVPEGEQ-LEA 159
Cdd:TIGR01466  76 SSGDPGIYGMAALVFEALEKKGAEVdiEVIPGITAASAAASLLGAplghDFCVISLSDLL--------TPWPEIEKrLRA 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491429183  160 LASHRSSMAIY--LSVQR---IQRVVERLIAggYA-PQTPAAVIYKATWPESRTVRGTLAD 214
Cdd:TIGR01466 148 AAEADFVIAIYnpRSKRRpeqFRRAMEILLE--HRkPDTPVGIVRNAGREGEEVEITTLAE 206
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
13-128 5.71e-11

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: 60.79  E-value: 5.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183   13 VGAGPGDRELITLKGYRLLQQAQLVIY------AGSLINPALLDYCSPETECHDSATLHLTQILDLME-----------A 75
Cdd:TIGR01467   6 VGVGPGDPELITVKALEALRSADVIAVpaskkgRESLARKIVEDYLKPNDTRILELVFPMTKDRDELEkawdeaaeavaA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491429183   76 GVKAGKTVVRLQTGDVSLYGSVREQGEELTKRGIAWRVVPGVSAFLGAAAELG 128
Cdd:TIGR01467  86 ELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAG 138
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
13-129 1.08e-10

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 60.00  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVIY---------AGSLINPALLD-------YCSPETECHDSATLHLTQILDLMEAG 76
Cdd:PRK05990   8 LGVGPGDPELLTLKALRLLQAAPVVAYfvakgkkgnAFGIVEAHLSPgqtllplVYPVTTEILPPPLCYETVIADFYDTS 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  77 VK-------AGKTVVRLQTGDVSLYGSVREQGEELTKRGIAwRVVPGVSAFLGAAAELGV 129
Cdd:PRK05990  88 AEavaahldAGRDVAVICEGDPFFYGSYMYLHDRLAPRYET-EVIPGVCSMLGCWSVLGA 146
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
13-128 4.85e-10

Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440634  Cd Length: 250  Bit Score: 58.16  E-value: 4.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVI-YAG--SLINPALldycsPETECHDSAtlhLTQILDLMEAGV---KAGKTVVRL 86
Cdd:COG1010    9 VGLGPGSAELMTPRARAALAEADVVVgYGTylDLIPPLL-----PGKEVHASG---MREEVERAREALelaAEGKTVAVV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491429183  87 QTGDVSLYG---SVREQGEEL-TKRGIAWRVVPGVSAFLGAAAELG 128
Cdd:COG1010   81 SSGDPGVYGmagLVLEVLEEGgAWRDVEVEVVPGITAAQAAAARLG 126
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
13-215 5.42e-10

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: 57.81  E-value: 5.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVI-YAG--SLINPALldycsPETECHDSAtlhLTQILDLMEAGV---KAGKTVVRL 86
Cdd:cd11646    4 VGIGPGSADLMTPRAREALEEADVIVgYKTylDLIEDLL-----PGKEVISSG---MGEEVERAREALelaLEGKRVALV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  87 QTGDVSLYG---SVREQGEElTKRGIAWRVVPGVSAFLGAAAELGV----EYTVPQLSQSLiitrlagrTPVPEGEQ-LE 158
Cdd:cd11646   76 SSGDPGIYGmagLVLELLDE-RWDDIEVEVVPGITAALAAAALLGAplghDFAVISLSDLL--------TPWEVIEKrLR 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491429183 159 ALASHRSSMAIY--LSVQR---IQRVVErLIAGGYAPQTPAAVIYKATWPESRTVRGTLADI 215
Cdd:cd11646  147 AAAEADFVIALYnpRSKKRpwqLEKALE-ILLEHRPPDTPVGIVRNAGREGEEVTITTLGEL 207
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
13-217 1.63e-09

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: 55.92  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  13 VGAGPGDRELITLKGYRLLQQAQLVIyaGSlinPALLDYCSPET-ECHDsATLHLTQILDLMEAGVkAGKTVVRLQTGDV 91
Cdd:COG2241    7 VGIGPGGPDGLTPAAREAIAEADVVV--GG---KRHLELFPDLGaERIV-WPSPLSELLEELLALL-RGRRVVVLASGDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  92 SLYGSVREQGEELTKRgiAWRVVPGVSAFLGAAAELGVEYtvpqlsQSLIITRLAGRtpvPEGEQLEALASHRsSMAIYL 171
Cdd:COG2241   80 LFYGIGATLARHLPAE--EVRVIPGISSLQLAAARLGWPW------QDAAVVSLHGR---PLERLLPALAPGR-RVLVLT 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491429183 172 S-VQRIQRVVERLIAGGYaPQTPAAVIYKATWPESRTVRGTLADIAQ 217
Cdd:COG2241  148 DdGNTPAAIARLLLERGF-GDSRLTVLENLGGPDERITRGTAEELAD 193
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
10-230 2.74e-05

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 44.39  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  10 VWFVGAGPGDRELITLKGYRLLQQAQLVIYAGSLInpallDYCSPETECHDSATLHLTQILDLMEAGVKA---GKTVVRL 86
Cdd:PRK05765   4 LYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYL-----RLISDLLDGKEVIGARMKEEIFRANTAIEKaleGNIVALV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491429183  87 QTGDVSLYGSVREQGEELTKRGIA--WRVVPGVSAFLGAAAELG----VEYTVPQLSQSLiitrlagrtpVPEGEQL--- 157
Cdd:PRK05765  79 SSGDPQVYGMAGLVFELISRRKLDvdVEVIPGVTAALAAAARLGsplsLDFVVISLSDLL----------IPREEILhrv 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491429183 158 EALASHRSSMAIYLSVQR-IQRVVERLIAGGYAPQTPAAVIYKATWPESRTVRGTLADIAQPVQAAGIRKTALI 230
Cdd:PRK05765 149 TKAAEADFVIVFYNPINEnLLIEVMDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWKEHMDEIGMTTTMII 222
 
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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