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Conserved domains on  [gi|517057395|ref|WP_018246213|]
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bifunctional cobalt-precorrin-7 (C(5))-methyltransferase/cobalt-precorrin-6B (C(15))-methyltransferase [Rhizobium leguminosarum]

Protein Classification

bifunctional cobalt-precorrin-7 (C(5))-methyltransferase/cobalt-precorrin-6B (C(15))-methyltransferase( domain architecture ID 11454932)

bifunctional cobalt-precorrin-7 (C(5))-methyltransferase/cobalt-precorrin-6B (C(15))-methyltransferase such as the cobalamin biosynthesis bifunctional protein CbiET, which catalyzes two methylations (at C-5 and C-15) in precorrin-6Y and its decarboxylation, to produce precorrin-8X as part of the biosynthesis of cobalamin

CATH:  3.40.50.150
EC:  2.1.1.196|2.1.1.289|2.1.1.132
Gene Ontology:  GO:0009236|GO:0008276|GO:0008168
PubMed:  23688113|12429089|23922391|16042605|12869542|11153269|11215515
SCOP:  4003082|3000118

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 ...
 12-410 2.68e-126

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: 370.65  E-value: 2.68e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  12 WLTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERLSWQSPFERSVEAILERRGTPVVVLASGDPFLY 91
Cdd:COG2242    1 ALVLVGGGGGGGGGLGAAAAAAAAAAAALVGGGRLLLLLLALLAAAALAWPPPLAALLLLLLARRGVVVVVLASGDPGFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  92 GVGATLSRYVAADEMRAIPAPSAFSLAASRLGWPLQDVASLSLHGRPINLIRPHLHPGRRIIALTSDEKGPGDLAALLTA 171
Cdd:COG2242   81 GGGGTLLRLLLAEEVRVIPAPSSFSLAAARLGWALAEVVVVSLLGRALLLLLLALLPGARLLLLLLDGAAPAAAAALLLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 172 TGFGQSRLTVLEALGGARERQRSAVAADFDLVDIDPLNVCAVDVAAGEGARILPfAAGLEDELFEHD-GQITKREIRAMT 250
Cdd:COG2242  161 RGGGGSLLLVLEGLGGGEERRRTGAAAAAAAADAAALNVVALLVVAGPGARLPR-TPGLPDEAFERDkGPITKREVRALT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 251 LSALAPRHGELLWDIGAGSGSIGIEWMLADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGLAPDALKGLPEPDVI 330
Cdd:COG2242  240 LAKLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALADLPDPDAV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 331 FLGGGGSE-PGVIDAAIAALKRGGRLVANAVTLEMEAVLLSEHAKRGGF--LTRIEISRAQPVGGMTGWRPAMPVTQWRW 407
Cdd:COG2242  320 FIGGSGGNlPEILEACWARLRPGGRLVANAVTLETLALALEALAELGYGgeLVQVQVSRLKPLGGGTGFRPANPVTIISA 399


                 ...
gi 517057395 408 TKG 410
Cdd:COG2242  400 EKP 402
 
Name Accession Description Interval E-value
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 12-410 2.68e-126

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: 370.65  E-value: 2.68e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  12 WLTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERLSWQSPFERSVEAILERRGTPVVVLASGDPFLY 91
Cdd:COG2242    1 ALVLVGGGGGGGGGLGAAAAAAAAAAAALVGGGRLLLLLLALLAAAALAWPPPLAALLLLLLARRGVVVVVLASGDPGFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  92 GVGATLSRYVAADEMRAIPAPSAFSLAASRLGWPLQDVASLSLHGRPINLIRPHLHPGRRIIALTSDEKGPGDLAALLTA 171
Cdd:COG2242   81 GGGGTLLRLLLAEEVRVIPAPSSFSLAAARLGWALAEVVVVSLLGRALLLLLLALLPGARLLLLLLDGAAPAAAAALLLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 172 TGFGQSRLTVLEALGGARERQRSAVAADFDLVDIDPLNVCAVDVAAGEGARILPfAAGLEDELFEHD-GQITKREIRAMT 250
Cdd:COG2242  161 RGGGGSLLLVLEGLGGGEERRRTGAAAAAAAADAAALNVVALLVVAGPGARLPR-TPGLPDEAFERDkGPITKREVRALT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 251 LSALAPRHGELLWDIGAGSGSIGIEWMLADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGLAPDALKGLPEPDVI 330
Cdd:COG2242  240 LAKLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALADLPDPDAV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 331 FLGGGGSE-PGVIDAAIAALKRGGRLVANAVTLEMEAVLLSEHAKRGGF--LTRIEISRAQPVGGMTGWRPAMPVTQWRW 407
Cdd:COG2242  320 FIGGSGGNlPEILEACWARLRPGGRLVANAVTLETLALALEALAELGYGgeLVQVQVSRLKPLGGGTGFRPANPVTIISA 399


                 ...
gi 517057395 408 TKG 410
Cdd:COG2242  400 EKP 402
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 16-213 1.11e-63

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: 202.72  E-value: 1.11e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  16 IGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLiTGERLSWQS-PFERSVEAIlERRGTPVVVLASGDPFLYGVG 94
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLLELFPDL-GAEKIPLPSeDIAELLEEI-AEAGKRVVVLASGDPGFYGIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  95 ATLSRYVAADEMRAIPAPSAFSLAASRLGWPLQDVASLSLHGRPINLIRPHLHPGRRIIALTSDEKGPGDLAALLTATGF 174
Cdd:cd11644   79 KTLLRRLGGEEVEVIPGISSVQLAAARLGLPWEDARLVSLHGRDLENLRRALRRGRKVFVLTDGKNTPAEIARLLLERGL 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 517057395 175 GQSRLTVLEALGGARERQRSAVAADFDLVDIDPLNVCAV 213
Cdd:cd11644  159 GDSRVTVGENLGYPDERITEGTAEELAEEEFSDLNVVLI 197
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 15-211 2.64e-49

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: 165.95  E-value: 2.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   15 IIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERLSW--QSPFERSVEAILERR-GTPVVVLASGDPFLY 91
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIIltYKDLDELLEFIAATRkEKRVVVLASGDPLFY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   92 GVGATLSRYVAADEMRAIPAPSAFSLAASRLGWPLQDVASLSLHGRPINLIRPHLHPG-RRIIALTSDEKGPGDLAALLT 170
Cdd:TIGR02467  81 GIGRTLAERLGKERLEIIPGISSVQYAFARLGLPWQDAVVISLHGRELDELLLALLRGhRKVAVLTDPRNGPAEIARELI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 517057395  171 ATGFGQS-RLTVLEALGGARERQRSAVAADFDLV--DIDPLNVC 211
Cdd:TIGR02467 161 ELGIGGSyELTVGENLGYEDERITEGTLEEIAAAqfDFSPLLVV 204
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
13-191 1.14e-29

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 114.20  E-value: 1.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  13 LTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERLSWQSPFeRSVEAILERRGTP--VVVLASGDPFL 90
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGL-RDLLEWLELAAKGknVVVLSTGDPLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  91 YGVGATLSRYVAADEM-RAIPAPSAFSLAASRLGWPLQDVASLSLHGR-PI-NLIRPHLHPGRRIIALTSDEKGPGDLAA 167
Cdd:PRK05787  81 SGLGKLLKVRRAVAEDvEVIPGISSVQYAAARLGIDMNDVVFTTSHGRgPNfEELEDLLKNGRKVIMLPDPRFGPKEIAA 160

                        170       180
                 ....*....|....*....|....
gi 517057395 168 LLTATGFGQSRLTVLEALGGARER 191
Cdd:PRK05787 161 ELLERGKLERRIVVGENLSYPDER 184
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 13-201 5.00e-17

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: 79.31  E-value: 5.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   13 LTIIGIGEDGPEGLGEEAKRLIATAPAVFG-GARHHALAASLITGERLSWQSPFERSVE----------AILERRGTPVV 81
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGdDSRALEILLDLLPEDLYFPMTEDKEPLEeayeeiaealAAALRAGKDVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   82 VLASGDPFLYGVGATLSRYVAADEM--RAIPAPSAFSLAASRLGWPLQD-------VASLSLHGRPINLIRPHLHPGRRI 152
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIdvEVVPGVSSAQAAAARLGIPLTEggevlsvLFLPGLARIELRLLEALLANGDTV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 517057395  153 IALTSDEKgPGDLAALLTATGFGQSRLTVLEALGGARERQRSAVAADFD 201
Cdd:pfam00590 162 VLLYGPRR-LAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
 
Name Accession Description Interval E-value
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 12-410 2.68e-126

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: 370.65  E-value: 2.68e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  12 WLTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERLSWQSPFERSVEAILERRGTPVVVLASGDPFLY 91
Cdd:COG2242    1 ALVLVGGGGGGGGGLGAAAAAAAAAAAALVGGGRLLLLLLALLAAAALAWPPPLAALLLLLLARRGVVVVVLASGDPGFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  92 GVGATLSRYVAADEMRAIPAPSAFSLAASRLGWPLQDVASLSLHGRPINLIRPHLHPGRRIIALTSDEKGPGDLAALLTA 171
Cdd:COG2242   81 GGGGTLLRLLLAEEVRVIPAPSSFSLAAARLGWALAEVVVVSLLGRALLLLLLALLPGARLLLLLLDGAAPAAAAALLLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 172 TGFGQSRLTVLEALGGARERQRSAVAADFDLVDIDPLNVCAVDVAAGEGARILPfAAGLEDELFEHD-GQITKREIRAMT 250
Cdd:COG2242  161 RGGGGSLLLVLEGLGGGEERRRTGAAAAAAAADAAALNVVALLVVAGPGARLPR-TPGLPDEAFERDkGPITKREVRALT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 251 LSALAPRHGELLWDIGAGSGSIGIEWMLADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGLAPDALKGLPEPDVI 330
Cdd:COG2242  240 LAKLALRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALADLPDPDAV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 331 FLGGGGSE-PGVIDAAIAALKRGGRLVANAVTLEMEAVLLSEHAKRGGF--LTRIEISRAQPVGGMTGWRPAMPVTQWRW 407
Cdd:COG2242  320 FIGGSGGNlPEILEACWARLRPGGRLVANAVTLETLALALEALAELGYGgeLVQVQVSRLKPLGGGTGFRPANPVTIISA 399


                 ...
gi 517057395 408 TKG 410
Cdd:COG2242  400 EKP 402
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 10-216 3.00e-86

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: 260.85  E-value: 3.00e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  10 QRWLTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLiTGERLSWQSPFERSVEAILER-RGTPVVVLASGDP 88
Cdd:COG2241    1 MPWLTVVGIGPGGPDGLTPAAREAIAEADVVVGGKRHLELFPDL-GAERIVWPSPLSELLEELLALlRGRRVVVLASGDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  89 FLYGVGATLSRYVAADEMRAIPAPSAFSLAASRLGWPLQDVASLSLHGRPINLIRPHLHPGRRIIALTSDEKGPGDLAAL 168
Cdd:COG2241   80 LFYGIGATLARHLPAEEVRVIPGISSLQLAAARLGWPWQDAAVVSLHGRPLERLLPALAPGRRVLVLTDDGNTPAAIARL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 517057395 169 LTATGFGQSRLTVLEALGGARERQRSAVAADFDLVDIDPLNVCAVDVA 216
Cdd:COG2241  160 LLERGFGDSRLTVLENLGGPDERITRGTAEELADADFSDLNVVAIECR 207
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 16-213 1.11e-63

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: 202.72  E-value: 1.11e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  16 IGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLiTGERLSWQS-PFERSVEAIlERRGTPVVVLASGDPFLYGVG 94
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLLELFPDL-GAEKIPLPSeDIAELLEEI-AEAGKRVVVLASGDPGFYGIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  95 ATLSRYVAADEMRAIPAPSAFSLAASRLGWPLQDVASLSLHGRPINLIRPHLHPGRRIIALTSDEKGPGDLAALLTATGF 174
Cdd:cd11644   79 KTLLRRLGGEEVEVIPGISSVQLAAARLGLPWEDARLVSLHGRDLENLRRALRRGRKVFVLTDGKNTPAEIARLLLERGL 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 517057395 175 GQSRLTVLEALGGARERQRSAVAADFDLVDIDPLNVCAV 213
Cdd:cd11644  159 GDSRVTVGENLGYPDERITEGTAEELAEEEFSDLNVVLI 197
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 15-211 2.64e-49

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: 165.95  E-value: 2.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   15 IIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERLSW--QSPFERSVEAILERR-GTPVVVLASGDPFLY 91
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIIltYKDLDELLEFIAATRkEKRVVVLASGDPLFY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   92 GVGATLSRYVAADEMRAIPAPSAFSLAASRLGWPLQDVASLSLHGRPINLIRPHLHPG-RRIIALTSDEKGPGDLAALLT 170
Cdd:TIGR02467  81 GIGRTLAERLGKERLEIIPGISSVQYAFARLGLPWQDAVVISLHGRELDELLLALLRGhRKVAVLTDPRNGPAEIARELI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 517057395  171 ATGFGQS-RLTVLEALGGARERQRSAVAADFDLV--DIDPLNVC 211
Cdd:TIGR02467 161 ELGIGGSyELTVGENLGYEDERITEGTLEEIAAAqfDFSPLLVV 204
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 240-361 2.98e-34

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: 123.59  E-value: 2.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  240 QITKREIRAMTLSALAPRHGELLWDIGAGSGSIGIEWMLADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGLAPD 319
Cdd:TIGR02469   1 GMTKREVRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 517057395  320 AL-KGLPEPDVIFLGGGGSEPGVIDAAI-AALKRGGRLVANAVT 361
Cdd:TIGR02469  81 APeALLPDPDAVFVGGSGGLLQEILEAVeRRLRPGGRIVLNAIT 124
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
13-191 1.14e-29

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 114.20  E-value: 1.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  13 LTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERLSWQSPFeRSVEAILERRGTP--VVVLASGDPFL 90
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGL-RDLLEWLELAAKGknVVVLSTGDPLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  91 YGVGATLSRYVAADEM-RAIPAPSAFSLAASRLGWPLQDVASLSLHGR-PI-NLIRPHLHPGRRIIALTSDEKGPGDLAA 167
Cdd:PRK05787  81 SGLGKLLKVRRAVAEDvEVIPGISSVQYAAARLGIDMNDVVFTTSHGRgPNfEELEDLLKNGRKVIMLPDPRFGPKEIAA 160

                        170       180
                 ....*....|....*....|....
gi 517057395 168 LLTATGFGQSRLTVLEALGGARER 191
Cdd:PRK05787 161 ELLERGKLERRIVVGENLSYPDER 184
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
229-372 2.98e-28

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


Pssm-ID: 180961  Cd Length: 196  Bit Score: 110.08  E-value: 2.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 229 GLEDELFEHDGQI--TKREIRAMTLSALAPRHGELLWDIGAGSGSIGIEWMLADPSLKAIAVEQSPERAARVARNASAFG 306
Cdd:PRK07402   9 GIPDELFERLPGIplTKREVRLLLISQLRLEPDSVLWDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFG 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057395 307 VPHLAVIEGLAPDALKGL-PEPDVIFLGGGGSEPGVIDAAIAALKRGGRLVANAVTLEmEAVLLSEH 372
Cdd:PRK07402  89 VKNVEVIEGSAPECLAQLaPAPDRVCIEGGRPIKEILQAVWQYLKPGGRLVATASSLE-GLYAISEG 154
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
232-391 1.12e-25

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 102.77  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 232 DELFEHDGQI--TKREIRAMTLSALAPRHGELLWDIGAGSGSIGIEWMLADPSLKAIAVEQSPERAARVARNASAFGVPH 309
Cdd:PRK08287   3 DELFLRGEKVpmTKEEVRALALSKLELHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 310 LAVIEGLAPDALKGlpEPDVIFLGG-GGSEPGVIDAAIAALKRGGRLVANAVTLE--MEAVllsEHAKRGGF----LTRI 382
Cdd:PRK08287  83 IDIIPGEAPIELPG--KADAIFIGGsGGNLTAIIDWSLAHLHPGGRLVLTFILLEnlHSAL---AHLEKCGVseldCVQL 157


                 ....*....
gi 517057395 383 EISRAQPVG 391
Cdd:PRK08287 158 QVSSLTPLG 166
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 229-402 2.12e-24

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 99.49  E-value: 2.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 229 GLEDELFEHDGQI--TKREIRAMTLSALAPRHGELLWDIGAGSGSIGIEW-MLADPSLKAIAVEQSPERAARVARNASAF 305
Cdd:PRK00377   9 GIPDEEFERDEEIpmTKEEIRALALSKLRLRKGDMILDIGCGTGSVTVEAsLLVGETGKVYAVDKDEKAINLTRRNAEKF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 306 GV-PHLAVIEGLAPDALKGL-PEPDVIFLGGGGSE-PGVIDAAIAALKRGGRLVANAVTLEMEAVLLSEHAKRGGFL--T 380
Cdd:PRK00377  89 GVlNNIVLIKGEAPEILFTInEKFDRIFIGGGSEKlKEIISASWEIIKKGGRIVIDAILLETVNNALSALENIGFNLeiT 168

                        170       180
                 ....*....|....*....|..
gi 517057395 381 RIEISRAQPVGGMTGWRPAMPV 402
Cdd:PRK00377 169 EVIIAKGMKTKVGTAMMTRNPI 190
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 13-201 5.00e-17

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: 79.31  E-value: 5.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   13 LTIIGIGEDGPEGLGEEAKRLIATAPAVFG-GARHHALAASLITGERLSWQSPFERSVE----------AILERRGTPVV 81
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGdDSRALEILLDLLPEDLYFPMTEDKEPLEeayeeiaealAAALRAGKDVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   82 VLASGDPFLYGVGATLSRYVAADEM--RAIPAPSAFSLAASRLGWPLQD-------VASLSLHGRPINLIRPHLHPGRRI 152
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIdvEVVPGVSSAQAAAARLGIPLTEggevlsvLFLPGLARIELRLLEALLANGDTV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 517057395  153 IALTSDEKgPGDLAALLTATGFGQSRLTVLEALGGARERQRSAVAADFD 201
Cdd:pfam00590 162 VLLYGPRR-LAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
 13-134 1.27e-10

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: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   13 LTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITG---ERLSWQSPFERSVEAI-LERRGTPVVVLASGDP 88
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLDLIEDLIPGkevVTSGMREEIARAELAIeLAAEGRTVALVSSGDP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517057395   89 FLYGVGA----TLSRYVAADEMRAIPAPSAFSLAASRLGWPL-QDVASLSL 134
Cdd:TIGR01466  81 GIYGMAAlvfeALEKKGAEVDIEVIPGITAASAAASLLGAPLgHDFCVISL 131
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 13-134 1.38e-08

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: 55.11  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  13 LTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITG-ERLSwqSPF----ERSVEAI-LERRGTPVVVLASG 86
Cdd:cd11646    1 LYVVGIGPGSADLMTPRAREALEEADVIVGYKTYLDLIEDLLPGkEVIS--SGMgeevERAREALeLALEGKRVALVSSG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517057395  87 DPFLYGVGA----TLSRYVAADEMRAIPAPSAFSLAASRLGWPL-QDVASLSL 134
Cdd:cd11646   79 DPGIYGMAGlvleLLDERWDDIEVEVVPGITAALAAAALLGAPLgHDFAVISL 131
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
248-357 2.86e-06

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 47.75  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  248 AMTLSALAPRHGELLWDIGAGSGSI-GIEWMLADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGlapDALKGLPE 326
Cdd:pfam01135  63 AMMLELLELKPGMRVLEIGSGSGYLtACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIVVVG---DGRQGWPE 139

                          90       100       110
                  ....*....|....*....|....*....|....
gi 517057395  327 --P-DVIFLGGGGsePGVIDAAIAALKRGGRLVA 357
Cdd:pfam01135 140 faPyDAIHVGAAA--PEIPEALIDQLKEGGRLVI 171
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 248-357 6.99e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 46.62  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 248 AMTLSALAPRHGELLWDIGAGSGsigieWM---LADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGlapDALKGL 324
Cdd:COG2518   56 ARMLEALDLKPGDRVLEIGTGSG-----YQaavLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVG---DGALGW 127

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 517057395 325 PE--P-DVIFLGGGGsePGVIDAAIAALKRGGRLVA 357
Cdd:COG2518  128 PEhaPfDRIIVTAAA--PEVPEALLEQLAPGGRLVA 161
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 251-359 1.37e-05

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 45.57  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 251 LSAL-APRHGELLwDIGAGSGSIGIEWMLADPSLKAIAVEQSpERAARVAR-NASAFGVPHLAVIeglAPDALKGLPEP- 327
Cdd:COG2813   42 LEHLpEPLGGRVL-DLGCGYGVIGLALAKRNPEARVTLVDVN-ARAVELARaNAAANGLENVEVL---WSDGLSGVPDGs 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 517057395 328 -DVI-----FLGGGGSEPGV----IDAAIAALKRGGRL--VANA 359
Cdd:COG2813  117 fDLIlsnppFHAGRAVDKEVahalIADAARHLRPGGELwlVANR 160
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 16-140 2.85e-05

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: 45.08  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  16 IGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGE--------RLSWQSPFERSVEAILERR--GTPVVVLAS 85
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAIlkdgkriyDLHDPNVEEEMAELLLEEArqGKDVAFLSP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  86 GDPFLYGVGATLSRyvAADEM----RAIPAPSAFSLAASRLGWPL-QDVASLSLHGRPIN 140
Cdd:cd09815   81 GDPGVAGTGAELVE--RAEREgvevKVIPGVSAADAAAAALGIDLgESFLFVTASDLLEN 138
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 251-390 3.87e-05

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: 45.55  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 251 LSALAPRHGELLWDIGAGSGSIGIewMLADPSLKAIAVEQSPE--RAARvaRNASAFGVPHLAVIEGLAPDALKGLPE-- 326
Cdd:COG2265  226 LEWLDLTGGERVLDLYCGVGTFAL--PLARRAKKVIGVEIVPEavEDAR--ENARLNGLKNVEFVAGDLEEVLPELLWgg 301

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 327 -PDVIFLgg--gGSEPGVIDaAIAALKRgGRLVA---NAVTLEMEAVLLSEhakrGGFltriEISRAQPV 390
Cdd:COG2265  302 rPDVVVLdppraGAGPEVLE-ALAALGP-RRIVYvscNPATLARDLALLVE----GGY----RLEKVQPV 361
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 13-126 4.82e-05

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: 44.32  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  13 LTIIGIGEDGPEGLGEEAKRLIATAPAVF-----GGARHHAL--AASLITGERL----------------SWqspfERSV 69
Cdd:COG2243    5 LYGVGVGPGDPELLTLKAVRALREADVIAypakgAGKASLAReiVAPYLPPARIvelvfpmttdyealvaAW----DEAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057395  70 EAILE--RRGTPVVVLASGDPFLYGVGATLSRYVAAD--EMRAIPAPSAFSLAASRLGWPL 126
Cdd:COG2243   81 ARIAEelEAGRDVAFLTEGDPSLYSTFMYLLERLRERgfEVEVIPGITSFSAAAAALGIPL 141
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 267-383 5.33e-05

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 43.53  E-value: 5.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 267 AGSGSIGIEwmladpSL-----KAIAVEQSPERAARVARNASAFGVPHLA-VIEGLAPDALKGLPEP--DVIFLGgggse 338
Cdd:COG0742   50 AGSGALGLE------ALsrgaaSVVFVEKDRKAAAVIRKNLEKLGLEDRArVIRGDALRFLKRLAGEpfDLVFLD----- 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 517057395 339 P----GVIDAAIAALKRGGRLVANAVtlemeAVLlsEHAKRGGFLTRIE 383
Cdd:COG0742  119 PpyakGLLEKALELLAENGLLAPGGL-----IVV--EHSKREELPELPA 160
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 30-126 9.35e-05

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: 43.27  E-value: 9.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  30 AKRLIATAPAVF--------GGARHHALAASLITGERL----------------SWQspfeRSVEAILE--RRGTPVVVL 83
Cdd:cd11645   15 AVRILKEADVIFvpvskggeGSAALIIAAALLIPDKEIiplefpmtkdreeleeAWD----EAAEEIAEelKEGKDVAFL 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 517057395  84 ASGDPFLYGVGATLSRYVAADEMRA--IPAPSAFSLAASRLGWPL 126
Cdd:cd11645   91 TLGDPSLYSTFSYLLERLRAPGVEVeiIPGITSFSAAAARLGIPL 135
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
264-367 2.42e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 42.33  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 264 DIGAGSGSIGiewMLADPSL--KAIAVEQSPERAARVARNASAFGVPH-LAVIEGLAPDALkgLPEP-DVI---FLGGGG 336
Cdd:COG4076   41 DIGTGSGLLS---MLAARAGakKVYAVEVNPDIAAVARRIIAANGLSDrITVINADATDLD--LPEKaDVIiseMLDTAL 115

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 517057395 337 SEPGVIDAAIAA----LKRGGRLVANAVTLEMEAV 367
Cdd:COG4076  116 LDEGQVPILNHArkrlLKPGGRIIPERITNAAQPV 150
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 262-356 2.61e-04

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: 40.11  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 262 LWDIGAGSGSIGIEwMLADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGLAPDALKGLPEP-DVIFLGG-----G 335
Cdd:cd02440    2 VLDLGCGTGALALA-LASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESfDVIISDPplhhlV 80

                         90       100
                 ....*....|....*....|.
gi 517057395 336 GSEPGVIDAAIAALKRGGRLV 356
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLV 101
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
 15-123 4.10e-04

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: 41.54  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395   15 IIGIGEDGPEGLGEEAKRLIATAPAVFggarhhaLAASLITGERLSWQSP-------FERSVEAILE------RRGTPVV 81
Cdd:TIGR01465   3 FIGAGPGDPDLITVKGRKLIESADVIL-------YAGSLVPPELLAHCRPgaevvnsAGMSLEEIVDimsdahREGKDVA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 517057395   82 VLASGDPFLYGVGATLSRYVAADEM--RAIPAPSAFSLAASRLG 123
Cdd:TIGR01465  76 RLHSGDPSIYGAIAEQMRLLEALGIpyEVVPGVSSFFAAAAALG 119
PRK04457 PRK04457
polyamine aminopropyltransferase;
247-398 5.51e-04

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 41.56  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 247 RAMT---LSALAPRHgelLWDIGAGSGSIG--IEWMLadPSLKAIAVEQSPeRAARVARNAsaFGVPH----LAVIEGLA 317
Cdd:PRK04457  55 RAMMgflLFNPRPQH---ILQIGLGGGSLAkfIYTYL--PDTRQTAVEINP-QVIAVARNH--FELPEngerFEVIEADG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 318 PDALKGLPEP-DVIFLGGGGSEpGVIDA---------AIAALKRGGRLVANavtlemeavLLSEHAKRGGFLTRIEISRA 387
Cdd:PRK04457 127 AEYIAVHRHStDVILVDGFDGE-GIIDAlctqpffddCRNALSSDGIFVVN---------LWSRDKRYDRYLERLESSFE 196

                        170
                 ....*....|.
gi 517057395 388 QPVGGMTGWRP 398
Cdd:PRK04457 197 GRVLELPAESH 207
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 251-356 5.54e-04

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


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 41.28  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 251 LSALAP-RHGELLWDIGAGSGSIGIewMLAD--PSLKAIAVEQSPERAARVARNASAFGV-PHLAVIEGLAPDALKGLPE 326
Cdd:COG4123   29 LAAFAPvKKGGRVLDLGTGTGVIAL--MLAQrsPGARITGVEIQPEAAELARRNVALNGLeDRITVIHGDLKEFAAELPP 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517057395 327 P--DVI------FLGGGGSEPG-----------------VIDAAIAALKRGGRLV 356
Cdd:COG4123  107 GsfDLVvsnppyFKAGSGRKSPdearaiarhedaltledLIRAAARLLKPGGRFA 161
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 245-356 6.59e-04

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: 39.59  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 245 EIRAMTLSALAPRHGELLWDIGAGSGSIGIEwmLADPSLKAIAVEQSPERAARVARNASAFGVpHLAVIEGlapDALKgL 324
Cdd:COG2226    9 DGREALLAALGLRPGARVLDLGCGTGRLALA--LAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVG---DAED-L 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 517057395 325 PEP----DVIFLGGG----GSEPGVIDAAIAALKRGGRLV 356
Cdd:COG2226   82 PFPdgsfDLVISSFVlhhlPDPERALAEIARVLKPGGRLV 121
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
 13-134 6.68e-04

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 40.92  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  13 LTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERL----SWQSPF--ERSVEAILErrGTPVVVLASG 86
Cdd:PRK05765   4 LYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYLRLISDLLDGKEVigarMKEEIFraNTAIEKALE--GNIVALVSSG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517057395  87 DPFLYGVGA----TLSRYVAADEMRAIPAPSAFSLAASRLGWPL-QDVASLSL 134
Cdd:PRK05765  82 DPQVYGMAGlvfeLISRRKLDVDVEVIPGVTAALAAAARLGSPLsLDFVVISL 134
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
13-154 9.37e-04

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 40.64  E-value: 9.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  13 LTIIGIGEDGPEGLGEEAKRLIATAPAVFGGARHHALAASLITGERL---SWQSPFERSVEAI-LERRGTPVVVLASGDP 88
Cdd:PRK15478   2 LSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAFTGDKQViktGMCKEIERCQAAIeLAQAGHNVALISSGDA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057395  89 FLYGVGATLSRYVAAD----EMRAIPAPSAFSLAASRLGWPL-QDVASLSLHgrpiNLIRPHLHPGRRIIA 154
Cdd:PRK15478  82 GIYGMAGLVLELVSKQkldvEVRLIPGMTASIAAASLLGAPLmHDFCHISLS----DLLTPWPVIEKRIVA 148
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 251-330 1.30e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 251 LSALAPRHGELLWDIGAGSGSIGIewMLAD--PSLKAIAVEQSPErAARVAR-NASAFGVPHLAVIEGlapDALKGLPEP 327
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIAL--ALAKerPDAEVTAVDISPE-ALAVARrNAKHGLGARVEFLQG---DWFEPLPGG 174


                 ....*
gi 517057395 328 --DVI 330
Cdd:PRK09328 175 rfDLI 179
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 251-330 1.95e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.75  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 251 LSALAPRHGELLWDIGAGSGSIGIewMLAD--PSLKAIAVEQSPErAARVAR-NASAFGVPH-LAVIEGlapDALKGLPE 326
Cdd:COG2890  105 LALLPAGAPPRVLDLGTGSGAIAL--ALAKerPDARVTAVDISPD-ALAVARrNAERLGLEDrVRFLQG---DLFEPLPG 178


                 ....*..
gi 517057395 327 P---DVI 330
Cdd:COG2890  179 DgrfDLI 185
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 264-355 2.32e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.35  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  264 DIGAGSGSIGIEWMLADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGLAPDALKGLPEP-DVIFLGGGGSEPGVI 342
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSfDVVVASNVLHHLADP 81

                          90
                  ....*....|....*..
gi 517057395  343 DAAI----AALKRGGRL 355
Cdd:pfam08242  82 RAVLrnirRLLKPGGVL 98
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 264-385 2.50e-03

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: 39.37  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395 264 DIGAGSG--SIGIEWMLAdPSLKAIAVEQSPERAARVARNASAFGVPHlAVIEGLApDALKGLPEPDV--IFLGGGgsEP 339
Cdd:COG2519   97 EAGTGSGalTLALARAVG-PEGKVYSYERREDFAEIARKNLERFGLPD-NVELKLG-DIREGIDEGDVdaVFLDMP--DP 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 517057395 340 G-VIDAAIAALKRGGRLVA-NAVTLEMEAVLlsEHAKRGGFlTRIEIS 385
Cdd:COG2519  172 WeALEAVAKALKPGGVLVAyVPTVNQVSKLV--EALRESGF-TDIEAV 216
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 251-309 3.58e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 3.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  251 LSALAPRHGELLW-DIGAGSGSIGIEWMLADPSLKAIAVEQSPERAARVARNASAFGVPH 309
Cdd:TIGR00536 106 LASLISQPPILHIlDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEH 165
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
264-383 3.61e-03

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 37.99  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  264 DIGAGSGSIGIEwMLADPSLKAIAVEQSPERAARVARNASAFGVPHLAVIEGLAPDALK---GLPEPDVIFLggggsEP- 339
Cdd:pfam03602  47 DLFAGSGALGLE-ALSRGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDALLALLRlagKGPVFDIVFL-----DPp 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 517057395  340 ---GVIDAAIAALKRGGRlvanavtLEMEAVLLSEHAKRGGFLTRIE 383
Cdd:pfam03602 121 yakGLIEEVLDLLAEKGW-------LKPNALIYVETEKRGELPEQPG 160
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 251-358 6.24e-03

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 37.18  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057395  251 LSALAPRHGELLWDIGAGSGSIGIEWMLADPSLKAIAVEQSpERAARVAR-NASAFGVPHLAVIEGlapDALKGLPEP-- 327
Cdd:pfam05175  24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDIN-ARALESAReNLAANGLENGEVVAS---DVYSGVEDGkf 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 517057395  328 DVI-----FLGGGGSEPGVIDAAIA----ALKRGGRL--VAN 358
Cdd:pfam05175 100 DLIisnppFHAGLATTYNVAQRFIAdakrHLRPGGELwiVAN 141
 
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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