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Conserved domains on  [gi|1032287566|gb|OAP01893|]
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PRMT6 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
83-235 3.21e-45

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 156.74  E-value: 3.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  83 YFHSYAHVGIHEEMIKDRARTETYREAIMQHqsLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDAS-DIAVQAKEVVK 161
Cdd:COG4076     2 YLMQFFVPRWHHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIA 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032287566 162 ANGLSDKVIVLHGRVEDVEIDEEVDVIISEWMGYMLLYESMLGSVITARDRWLKPGGLILPSHATLYMAPISHP 235
Cdd:COG4076    80 ANGLSDRITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESP 153
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
272-337 9.54e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


The actual alignment was detected with superfamily member cd13896:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 115  Bit Score: 36.08  E-value: 9.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032287566 272 SISGEnvlTWPEVvkhidcKTIKIQELDSVTARYKFNSMMRAPMHGFAFWFDVEFSGPASSPAKNT 337
Cdd:cd13896    18 TINGK---AYPDA------DPLRVREGERVRIVFVNDTMMAHPMHLHGHFFQVENGNGEYGPRKDT 74
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
83-235 3.21e-45

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 156.74  E-value: 3.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  83 YFHSYAHVGIHEEMIKDRARTETYREAIMQHqsLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDAS-DIAVQAKEVVK 161
Cdd:COG4076     2 YLMQFFVPRWHHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIA 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032287566 162 ANGLSDKVIVLHGRVEDVEIDEEVDVIISEWMGYMLLYESMLGSVITARDRWLKPGGLILPSHATLYMAPISHP 235
Cdd:COG4076    80 ANGLSDRITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESP 153
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
122-221 1.14e-16

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: 75.54  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 122 VVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQAKEVVKANGLSDKVIVLHGRVEDV--EIDEEVDVIISEW--MGYML 197
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELppEADESFDVIISDPplHHLVE 81
                          90       100
                  ....*....|....*....|....
gi 1032287566 198 LYESMLGSVItardRWLKPGGLIL 221
Cdd:cd02440    82 DLARFLEEAR----RLLKPGGVLV 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
122-218 2.59e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.06  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 122 VVDVGCGTGILSIFCAQAGAKRVYAVDASDIAV-QAKEVVKANGLsdKVIVLHGRVEDVEI-DEEVDVIISeWMGYMLLY 199
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLeRARERAAEAGL--NVEFVQGDAEDLPFpDGSFDLVVS-SGVLHHLP 77
                          90
                  ....*....|....*....
gi 1032287566 200 ESMLGSVITARDRWLKPGG 218
Cdd:pfam13649  78 DPDLEAALREIARVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
118-189 4.42e-15

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 74.80  E-value: 4.42e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032287566 118 EGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGrvedveiDEEVDVII 189
Cdd:PRK00517  119 PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEaARENAELNGVELNVYLPQG-------DLKADVIV 184
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
119-225 9.04e-11

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 62.54  E-value: 9.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 119 GKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGRVEDvEIDEEVDVIISEWMGYML 197
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVEsARKNAELNQVSDRLQVKLIYLEQ-PIEGKADVIVANILAEVI 238
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1032287566 198 LyesMLGSVITardRWLKPGGL-----ILPSHA 225
Cdd:TIGR00406 239 K---ELYPQFS---RLVKPGGWlilsgILETQA 265
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
272-337 9.54e-03

The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 36.08  E-value: 9.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032287566 272 SISGEnvlTWPEVvkhidcKTIKIQELDSVTARYKFNSMMRAPMHGFAFWFDVEFSGPASSPAKNT 337
Cdd:cd13896    18 TINGK---AYPDA------DPLRVREGERVRIVFVNDTMMAHPMHLHGHFFQVENGNGEYGPRKDT 74
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
83-235 3.21e-45

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 156.74  E-value: 3.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  83 YFHSYAHVGIHEEMIKDRARTETYREAIMQHqsLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDAS-DIAVQAKEVVK 161
Cdd:COG4076     2 YLMQFFVPRWHHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIA 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032287566 162 ANGLSDKVIVLHGRVEDVEIDEEVDVIISEWMGYMLLYESMLGSVITARDRWLKPGGLILPSHATLYMAPISHP 235
Cdd:COG4076    80 ANGLSDRITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESP 153
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
108-189 8.22e-18

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 83.30  E-value: 8.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 108 EAIMQHqsLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGrveDVEIDEEVD 186
Cdd:COG2264   140 EALEKL--LKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEaARENAELNGVEDRIEVVLG---DLLEDGPYD 214

                  ...
gi 1032287566 187 VII 189
Cdd:COG2264   215 LVV 217
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
122-221 1.14e-16

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: 75.54  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 122 VVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQAKEVVKANGLSDKVIVLHGRVEDV--EIDEEVDVIISEW--MGYML 197
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELppEADESFDVIISDPplHHLVE 81
                          90       100
                  ....*....|....*....|....
gi 1032287566 198 LYESMLGSVItardRWLKPGGLIL 221
Cdd:cd02440    82 DLARFLEEAR----RLLKPGGVLV 101
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
116-221 3.81e-16

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 75.35  E-value: 3.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 116 LIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGRVEDVEIDEEVDVIIS---- 190
Cdd:COG2230    49 LKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEyARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSigmf 128
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1032287566 191 EWMGYmLLYESMLGSVitarDRWLKPGGLIL 221
Cdd:COG2230   129 EHVGP-ENYPAYFAKV----ARLLKPGGRLL 154
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
122-218 2.59e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.06  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 122 VVDVGCGTGILSIFCAQAGAKRVYAVDASDIAV-QAKEVVKANGLsdKVIVLHGRVEDVEI-DEEVDVIISeWMGYMLLY 199
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLeRARERAAEAGL--NVEFVQGDAEDLPFpDGSFDLVVS-SGVLHHLP 77
                          90
                  ....*....|....*....
gi 1032287566 200 ESMLGSVITARDRWLKPGG 218
Cdd:pfam13649  78 DPDLEAALREIARVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
118-189 4.42e-15

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 74.80  E-value: 4.42e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032287566 118 EGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGrvedveiDEEVDVII 189
Cdd:PRK00517  119 PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEaARENAELNGVELNVYLPQG-------DLKADVIV 184
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
98-221 5.98e-15

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 71.20  E-value: 5.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  98 KDRARTETYREAIMQ--HQSLIEGKVVVDVGCGTGILSIFCAQAGAkRVYAVDASDIAVqakEVVKANGLSDKVIVLHGR 175
Cdd:COG2227     2 SDPDARDFWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEAL---EIARERAAELNVDFVQGD 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1032287566 176 VEDVEIDEE-VDVIISewmGYMLLYESMLGSVITARDRWLKPGGLIL 221
Cdd:COG2227    78 LEDLPLEDGsFDLVIC---SEVLEHLPDPAALLRELARLLKPGGLLL 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
117-190 1.08e-14

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 72.24  E-value: 1.08e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032287566 117 IEGKVVVDVGCGTGILSIFCAQAGAKRVYAVdasDIAVQAKEVVKAN--GLSDKVIVLHGRVEDVEIDEEVDVIIS 190
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGV---DIDPEALEIARENaeRLGVRVDFIRADVTRIPLGGSVDTVVM 116
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
118-223 1.22e-12

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 68.06  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 118 EGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSDKVIV-LHGRVedveIDEEVDVIISEWMGY 195
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRaAKENAELNGVEARLEVyLPGDL----PKEKADVVVANILAD 236
                          90       100
                  ....*....|....*....|....*...
gi 1032287566 196 MLLyesMLGSVITARdrwLKPGGLILPS 223
Cdd:pfam06325 237 PLI---ELAPDIYAL---VKPGGYLILS 258
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
100-190 3.02e-12

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 66.71  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 100 RARTETYREAIMQHQSLIEGKVVVDVGCGTGILSIFCAQAGAK-RVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGRV- 176
Cdd:COG2890    94 RPETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDaRVTAVDISPDALAvARRNAERLGLEDRVRFLQGDLf 173
                          90
                  ....*....|....
gi 1032287566 177 EDVEIDEEVDVIIS 190
Cdd:COG2890   174 EPLPGDGRFDLIVS 187
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
99-221 3.25e-12

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: 63.86  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  99 DRARTETYREAIMQHQSLIEGKVVVDVGCGTGILSIFCAQAGAkRVYAVDASDIAV-QAKEVVKANGLsdKVIVLHGRVE 177
Cdd:COG2226     3 RVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLeLARERAAEAGL--NVEFVVGDAE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1032287566 178 DVEI-DEEVDVIISewmGYMLLYESMLGSVITARDRWLKPGGLIL 221
Cdd:COG2226    80 DLPFpDGSFDLVIS---SFVLHHLPDPERALAEIARVLKPGGRLV 121
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
110-221 8.41e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.17  E-value: 8.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 110 IMQHQSLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSdKVIVLHGRVEDVEI--DEEVD 186
Cdd:COG0500    18 LALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIAlARARAAKAGLG-NVEFLVADLAELDPlpAESFD 96
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1032287566 187 VIIS----EWMGymllyESMLGSVITARDRWLKPGGLIL 221
Cdd:COG0500    97 LVVAfgvlHHLP-----PEEREALLRELARALKPGGVLL 130
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
119-224 2.94e-11

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: 63.24  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 119 GKVVVDVGCGTGILSIFCAQ-AGAKRVYAVDASDIAV-QAKEVVKANGLSDKVIVLHGRVEDVE---IDEEVDVIIS--- 190
Cdd:COG4123    38 GGRVLDLGTGTGVIALMLAQrSPGARITGVEIQPEAAeLARRNVALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSnpp 117
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032287566 191 ---EWMGY--------MLLYESMLG--SVITARDRWLKPGG---LILPSH 224
Cdd:COG4123   118 yfkAGSGRkspdearaIARHEDALTleDLIRAAARLLKPGGrfaLIHPAE 167
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
123-221 3.58e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.22  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 123 VDVGCGTGILSIFCAQAGAkRVYAVDASDIAVqakEVVKANGLSDKVIVLHGRVEDVEI-DEEVDVIISEWmgyMLLYES 201
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEML---ELAREKAPREGLTFVVGDAEDLPFpDNSFDLVLSSE---VLHHVE 73
                          90       100
                  ....*....|....*....|
gi 1032287566 202 MLGSVITARDRWLKPGGLIL 221
Cdd:pfam08241  74 DPERALREIARVLKPGGILI 93
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
119-225 9.04e-11

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 62.54  E-value: 9.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 119 GKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGRVEDvEIDEEVDVIISEWMGYML 197
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVEsARKNAELNQVSDRLQVKLIYLEQ-PIEGKADVIVANILAEVI 238
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1032287566 198 LyesMLGSVITardRWLKPGGL-----ILPSHA 225
Cdd:TIGR00406 239 K---ELYPQFS---RLVKPGGWlilsgILETQA 265
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
77-270 1.21e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 60.40  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  77 TDFDVAYFHSYAHVgiHEEMIKDRARTET---YREAIMQHQSLIEGKVVVDVGCGTGILSIFCAQAGaKRVYAVDASDIA 153
Cdd:COG4976     4 DAYVEALFDQYADS--YDAALVEDLGYEApalLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSEEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 154 VqakEVVKANGLSDKVIvlHGRVEDV-EIDEEVDVIISewmGYMLLYESMLGSVITARDRWLKPGGLILpshATLYMAPI 232
Cdd:COG4976    81 L---AKAREKGVYDRLL--VADLADLaEPDGRFDLIVA---ADVLTYLGDLAAVFAGVARALKPGGLFI---FSVEDADG 149
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1032287566 233 SHpdRYSHSIDFWRnvygidmsammQLAKQCAFEEPSV 270
Cdd:COG4976   150 SG--RYAHSLDYVR-----------DLLAAAGFEVPGL 174
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
100-221 4.89e-10

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 60.18  E-value: 4.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 100 RARTETYREAIMQHQSLIEGKVVVDVGCGTGILSI----FCAQAgakRVYAVDASDIAVqakEVVKAN---GLSDKVIVL 172
Cdd:PRK09328   90 RPETEELVEWALEALLLKEPLRVLDLGTGSGAIALalakERPDA---EVTAVDISPEAL---AVARRNakhGLGARVEFL 163
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032287566 173 HGRVEDVEIDEEVDVIIS--------EW---MGYMLLYE------------SMLGSVITARDRWLKPGGLIL 221
Cdd:PRK09328  164 QGDWFEPLPGGRFDLIVSnppyipeaDIhllQPEVRDHEphlalfggedglDFYRRIIEQAPRYLKPGGWLL 235
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
118-190 6.23e-10

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: 58.28  E-value: 6.23e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032287566 118 EGKVVVDVGCGTGILSIFCAQAGAK-RVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGRVEDVEiDEEVDVIIS 190
Cdd:COG2813    49 LGGRVLDLGCGYGVIGLALAKRNPEaRVTLVDVNARAVElARANAAANGLENVEVLWSDGLSGVP-DGSFDLILS 122
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
118-221 1.06e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.21  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 118 EGKVVVDVGCGTGILS-IFCAQAGAKRVYAVDASDIAVQakevvKANGLSDKVIVLHGRVEDVEIDEEVDVIISewmGYM 196
Cdd:COG4106     1 PPRRVLDLGCGTGRLTaLLAERFPGARVTGVDLSPEMLA-----RARARLPNVRFVVADLRDLDPPEPFDLVVS---NAA 72
                          90       100
                  ....*....|....*....|....*
gi 1032287566 197 LLYESMLGSVITARDRWLKPGGLIL 221
Cdd:COG4106    73 LHWLPDHAALLARLAAALAPGGVLA 97
PRK14968 PRK14968
putative methyltransferase; Provisional
118-221 1.02e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 54.90  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 118 EGKVVVDVGCGTGILSIFCAQAGaKRVYAVDASDIAV-QAKEVVKANGLSDKVIV---------LHGRVEDV-------- 179
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYAVeCAKCNAKLNNIRNNGVEvirsdlfepFRGDKFDVilfnppyl 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032287566 180 --EIDEEVDviisEWMGYML--------LYESMLGSVitarDRWLKPGGLIL 221
Cdd:PRK14968  102 ptEEEEEWD----DWLNYALsggkdgreVIDRFLDEV----GRYLKPGGRIL 145
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
112-190 1.93e-08

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: 53.75  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 112 QHQSLIEGKVVVDVGCGTGILSIFCAQAGAK-RVYAVDASDIAVQ-AKEVVKANGLsDKVIVLHGRV-EDVEiDEEVDVI 188
Cdd:pfam05175  25 EHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARALEsARENLAANGL-ENGEVVASDVySGVE-DGKFDLI 102

                  ..
gi 1032287566 189 IS 190
Cdd:pfam05175 103 IS 104
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
103-189 4.38e-08

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: 54.80  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 103 TETYREAIMQHQSLIEGKVVVDVGCGTGILSIFCAQAgAKRVYAVDASDIAVQ-AKEVVKANGLsDKVIVLHGRVEDV-- 179
Cdd:COG2265   218 AEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARR-AKKVIGVEIVPEAVEdARENARLNGL-KNVEFVAGDLEEVlp 295
                          90
                  ....*....|..
gi 1032287566 180 --EIDEEVDVII 189
Cdd:COG2265   296 elLWGGRPDVVV 307
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
107-189 9.09e-08

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 54.03  E-value: 9.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 107 REAIMQhqsLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAV-QAKEVVKANGLSDKVIVLHGRVEDV-----E 180
Cdd:COG1092   208 RARVAE---LAKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALeWAKENAALNGLDDRHEFVQADAFDWlrelaR 284

                  ....*....
gi 1032287566 181 IDEEVDVII 189
Cdd:COG1092   285 EGERFDLII 293
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
118-220 2.67e-07

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 52.17  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 118 EGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLSDKVIVLHGRVEDV--EIDEEVDVIIsewmg 194
Cdd:COG2520   180 PGERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEyLKENIRLNKVEDRVTPILGDAREVapELEGKADRII----- 254
                          90       100
                  ....*....|....*....|....*.
gi 1032287566 195 yMLLYESMLGSVITARDRwLKPGGLI 220
Cdd:COG2520   255 -MNLPHSADEFLDAALRA-LKPGGVI 278
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
118-221 1.03e-06

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 49.38  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 118 EGKVVVDVGCGTG----ILSIFCAQagaKRVYAVDaSD---IAVQaKEVVKANGLSDkVIVLHGRVEDVEIDEEVDVIIS 190
Cdd:COG0357    67 EGARVLDVGSGAGfpgiPLAIARPD---LQVTLVD-SLgkkIAFL-REVVRELGLKN-VTVVHGRAEELAPREKFDVVTA 140
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1032287566 191 -------EWMGYMLlyesmlgsvitardRWLKPGGLIL 221
Cdd:COG0357   141 ravaplpDLLELAL--------------PLLKPGGRLL 164
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
119-189 1.03e-06

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: 49.77  E-value: 1.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032287566 119 GKVVVDVGCGTGILSIFCAQA-GAK-RVYAVDA-SDIAVQAKEVVKANGLSDKVIVLHGRVEDVEIDEEVDVII 189
Cdd:COG2519    92 GARVLEAGTGSGALTLALARAvGPEgKVYSYERrEDFAEIARKNLERFGLPDNVELKLGDIREGIDEGDVDAVF 165
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
114-231 1.80e-06

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 48.00  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 114 QSLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQA-KEVVKANGLSDKVIVlHGRVEDVE----IDEEVDVI 188
Cdd:pfam03602  37 APYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQIlKENLQLLGLPGAVLV-MDALLALLrlagKGPVFDIV 115
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1032287566 189 ISEwMGYML-LYESMLgsVITARDRWLKPGGLIL---PSHATLYMAP 231
Cdd:pfam03602 116 FLD-PPYAKgLIEEVL--DLLAEKGWLKPNALIYvetEKRGELPEQP 159
PRK14967 PRK14967
putative methyltransferase; Provisional
110-190 2.82e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 48.13  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 110 IMQHQSLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQ-AKEVVKANGLsdKVIVLHGRVEDVEIDEEVDVI 188
Cdd:PRK14967   28 ALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRsARLNALLAGV--DVDVRRGDWARAVEFRPFDVV 105

                  ..
gi 1032287566 189 IS 190
Cdd:PRK14967  106 VS 107
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
119-169 2.93e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 48.29  E-value: 2.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032287566 119 GKVVVDVGCGTGILSIFCAQAGAKrvyaVDASDIAVQ----AKEVVKANGLSDKV 169
Cdd:PRK07580   64 GLRILDAGCGVGSLSIPLARRGAK----VVASDISPQmveeARERAPEAGLAGNI 114
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
108-190 4.27e-06

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 46.81  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 108 EAIMQHQSLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDasdiaVQAKEVVKANGlSDKVIVLHGRVEDVEIDEE--- 184
Cdd:pfam01728  11 EIDEKFGLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVD-----LGPMQLWKPRN-DPGVTFIQGDIRDPETLDLlee 84
                          90
                  ....*....|.
gi 1032287566 185 -----VDVIIS 190
Cdd:pfam01728  85 llgrkVDLVLS 95
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
35-190 4.42e-06

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: 48.12  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  35 AKKRSHAGARDPRGGLANVLRVSDqLGEHKSLE----TSESSPPPCTDFD-----------VAYFHSYAHVGIHEEMIKD 99
Cdd:TIGR00536  11 SSALSRAIARENPWLEALLLLEHD-LGRERDLLlaflTEELTPDEKERIFrlvlrrvkgvpVAYLLGSKEFYGLEFFVNE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 100 RA---RTETyrEAIMQ--HQSLIE---GKVVVDVGCGTGILSIFCAQAGAKrvYAVDASDIAVQAKEVVKAN----GLSD 167
Cdd:TIGR00536  90 HVlipRPET--EELVEkaLASLISqppILHILDLGTGSGCIALALAYEFPN--AEVIAVDISPDALAVAEENaeknQLEH 165
                         170       180
                  ....*....|....*....|...
gi 1032287566 168 KVIVLHGRVEDVEIDEEVDVIIS 190
Cdd:TIGR00536 166 RVEFIQSNLFEPLAGQKIDIIVS 188
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
123-220 5.34e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.67  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 123 VDVGCGTGILSIFCAQAGA-KRVYAVDASDIAV-QAKEVVKANGLSDKVIVlHGRVEDVEIDEE--VDVIIS----EWMG 194
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPgLEYTGLDISPAALeAARERLAALGLLNAVRV-ELFQLDLGELDPgsFDVVVAsnvlHHLA 79
                          90       100
                  ....*....|....*....|....*.
gi 1032287566 195 YMllyESMLGSVitarDRWLKPGGLI 220
Cdd:pfam08242  80 DP---RAVLRNI----RRLLKPGGVL 98
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
84-265 5.77e-06

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 47.78  E-value: 5.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  84 FHSYahvGIHeemIKDRARTETYREAIMQHQSLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDI-AVQAKEVVKA 162
Cdd:pfam08003  87 FHLF---GVH---IDTEWRSDWKWDRVLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELfLCQFEAVRKL 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 163 NGLSDKVIVLHGRVEDVEIDEEVDVIISewMGYMLLYESMLGSVITARDRWLKPGGLILPS-------HATLYMApishp 235
Cdd:pfam08003 161 LGNDQRAHLLPLGIEQLPALAAFDTVFS--MGVLYHRRSPLDHLLQLKDQLVKGGELVLETlvidgdeNTVLVPG----- 233
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1032287566 236 DRYSHSidfwRNVYGI-DMSAMMQLAKQCAF 265
Cdd:pfam08003 234 DRYAQM----RNVYFIpSAAALINWLEKCGF 260
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
117-162 9.49e-06

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 47.16  E-value: 9.49e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032287566 117 IEGKVVVDVGCGTGILSIFCAQAGAkrvyAVDASDI--------AVQAKEVVKA 162
Cdd:PLN02585  143 LAGVTVCDAGCGTGSLAIPLALEGA----IVSASDIsaamvaeaERRAKEALAA 192
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
116-188 9.51e-06

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 46.33  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 116 LIEGKVVVDVGCGTGILSIFCAQ-AGAK-RVYAVDASDIAVqakEVVKAN----GLSDKVIVLHGRVEDV--EIDEEVDV 187
Cdd:PRK00377   38 LRKGDMILDIGCGTGSVTVEASLlVGETgKVYAVDKDEKAI---NLTRRNaekfGVLNNIVLIKGEAPEIlfTINEKFDR 114

                  .
gi 1032287566 188 I 188
Cdd:PRK00377  115 I 115
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
116-221 1.62e-05

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


Pssm-ID: 443298  Cd Length: 173  Bit Score: 45.18  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 116 LIEGKVVVDVGCGTGILSIFCAQAGAK--RVYAVDAS-DIAVQAKEVVKANGLSDKVIVLHGRVEDVE---IDEEVDVII 189
Cdd:COG4122    14 LLGAKRILEIGTGTGYSTLWLARALPDdgRLTTIEIDpERAAIARENFARAGLADRIRLILGDALEVLprlADGPFDLVF 93
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1032287566 190 --SEWMGYMLLYESMLgsvitardRWLKPGGLIL 221
Cdd:COG4122    94 idADKSNYPDYLELAL--------PLLRPGGLIV 119
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
119-221 1.96e-05

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: 43.86  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 119 GKVVVDVGCGTGILSIFCA-QAGAKRVYAVDASDIAV-QAKEVVKANGLSDKVIVLHGRVEDVE-IDEEVDVIISEWMGy 195
Cdd:TIGR02469  20 GDVLWDIGAGTGSVTIEAArLVPNGRVYAIERNPEALdLIERNLRRFGVSNIVIVEGDAPEAPEaLLPDPDAVFVGGSG- 98
                          90       100
                  ....*....|....*....|....*.
gi 1032287566 196 mllyeSMLGSVITARDRWLKPGGLIL 221
Cdd:TIGR02469  99 -----GLLQEILEAVERRLRPGGRIV 119
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
118-221 2.10e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.33  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 118 EGKVVVDVGCGTGILSIFCAQ--AGAKRVYAVDASDIAVQ-AKEVVKANGLSDkVIVLHGRVEDVEI---DEEVDVIIS- 190
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEkARENAQKLGFDN-VEFEQGDIEELPElleDDKFDVVISn 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1032287566 191 EWMGYMLLYESMLGSVItardRWLKPGGLIL 221
Cdd:pfam13847  82 CVLNHIPDPDKVLQEIL----RVLKPGGRLI 108
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
118-221 5.86e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 43.19  E-value: 5.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 118 EGKVVVDVGCGTGILSIFCAQAGAKrVYAVDASDIAVQAkevvkanGLSDKVIVLHGRVEDVEIDEEVDVIISeWMgyml 197
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGFS-VTGVDPSPIAIER-------ALLNVRFDQFDEQEAAVPAGKFDVIVA-RE---- 88
                          90       100       110
                  ....*....|....*....|....*....|
gi 1032287566 198 lyesMLGSV------ITARDRWLKPGGLIL 221
Cdd:pfam13489  89 ----VLEHVpdppalLRQIAALLKPGGLLL 114
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
117-221 1.15e-04

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 43.51  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 117 IEGKVVVDVGCGTGIlsiF--CA-QAGAKRVYAVD----------ASDiavqakevvkanglsDKVIVLHG---R-VEDV 179
Cdd:COG1189    76 VAGKVCLDIGASTGG---FtdCLlQRGAAKVYAVDvgygqlawklRQD---------------PRVVVLERtnaRyLTPE 137
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1032287566 180 EIDEEVDVI------ISewmgymllyesmLGSVITARDRWLKPGGLIL 221
Cdd:COG1189   138 DLPEPPDLVvidvsfIS------------LTLVLPALLALLKPGGELV 173
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
121-190 1.53e-04

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 41.53  E-value: 1.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032287566 121 VVVDVGCGTGILSIFCAQAGAK-RVYAVDAS-DIAVQAKEVVKANGLsDKVIVLHGRVEDveIDEEVDVIIS 190
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLpDAYEILEENVKLNNL-PNVVLLNAAVGD--RDGELEFNVS 69
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
109-228 2.10e-04

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 42.66  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 109 AIMQHQSLIEGKVVVDVGCGTGILSIFCAQAGAK-RVYAVDASDIA-VQAKEVVKANglsdkVIVLHGRVEDVEI-DEEV 185
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQaEFIALDISAGMlAQAKTKLSEN-----VQFICGDAEKLPLeDSSF 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032287566 186 DVIIS----EWMGymllyesMLGSVITARDRWLKPGGLIL---PSHATLY 228
Cdd:TIGR02072 100 DLIVSnlalQWCD-------DLSQALSELARVLKPGGLLAfstFGPGTLH 142
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
116-179 3.86e-04

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: 42.46  E-value: 3.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032287566 116 LIEGKVVVDVGCGTGILSIFCAQAGAK-RVYAVDASDIAVqakEVVKAN----GLSDkVIVLHGRVEDV 179
Cdd:COG2242   245 LRPGDVLWDIGAGSGSVSIEAARLAPGgRVYAIERDPERA---ALIRANarrfGVPN-VEVVEGEAPEA 309
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
123-221 5.14e-04

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 39.21  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 123 VDVGCGTGILSIFCAQA----GAKRVYAVDASDIAVQAKEVVKANGLSDKVIVLHGRVEDVE---IDEEVDVII--SEwm 193
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAAlrdnGLGRLTAVDPDPGAEEAGALLRKAGLDDRVRLIVGDSREALpslADGPIDLLFidGD-- 78
                          90       100
                  ....*....|....*....|....*...
gi 1032287566 194 gymLLYESMLGSVITARDRwLKPGGLIL 221
Cdd:pfam13578  79 ---HTYEAVLNDLELWLPR-LAPGGVIL 102
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
119-246 6.72e-04

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 41.44  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 119 GKVVVDVGCGT-GILSIFCAQA-GAKRVYAVDASDiavQAKEVVKANGLSDkviVLHGRVEDVEIDEE------VDVIIs 190
Cdd:cd08236   160 GDTVVVIGAGTiGLLAIQWLKIlGAKRVIAVDIDD---EKLAVARELGADD---TINPKEEDVEKVREltegrgADLVI- 232
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032287566 191 ewmgymllyESMlGSVITARD--RWLKPGGLILpshatlyMAPISHPDRYSHSIDFWR 246
Cdd:cd08236   233 ---------EAA-GSPATIEQalALARPGGKVV-------LVGIPYGDVTLSEEAFEK 273
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
94-220 1.80e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.50  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566  94 EEMIKDRARTETYREAIMQHQSLI---EGKVVVDVGCGTGILSIFCAQAgAKRVYAVDASDIAVQAKEVVkaNGLSDKVI 170
Cdd:PLN02336   10 EAMMLDSKASDLDKEERPEILSLLppyEGKSVLELGAGIGRFTGELAKK-AGQVIALDFIESVIKKNESI--NGHYKNVK 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032287566 171 VLHGRV--EDVEI-DEEVDVIISEWMgYMLLYESMLGSVITARDRWLKPGGLI 220
Cdd:PLN02336   87 FMCADVtsPDLNIsDGSVDLIFSNWL-LMYLSDKEVENLAERMVKWLKVGGYI 138
PRK08317 PRK08317
hypothetical protein; Provisional
106-236 1.97e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 39.53  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 106 YREAIMQHQSLIEGKVVVDVGCGTGILSIFCAQA--GAKRVYAVDAS-DIAVQAKEVVKANGLsdKVIVLHGRVEDVEI- 181
Cdd:PRK08317    7 YRARTFELLAVQPGDRVLDVGCGPGNDARELARRvgPEGRVVGIDRSeAMLALAKERAAGLGP--NVEFVRGDADGLPFp 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032287566 182 DEEVDVIISEwmgYMLLYESMLGSVITARDRWLKPGGLILpshatlymapISHPD 236
Cdd:PRK08317   85 DGSFDAVRSD---RVLQHLEDPARALAEIARVLRPGGRVV----------VLDTD 126
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
117-190 2.05e-03

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 39.92  E-value: 2.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032287566 117 IEGKVVvDVGCGTGILSIFCAQAGAK-RVYAVDASDIAVQA-KEVVKANGLSDKVIvlhgrVEDV--EIDEEVDVIIS 190
Cdd:PRK09489  196 TKGKVL-DVGCGAGVLSAVLARHSPKiRLTLSDVSAAALESsRATLAANGLEGEVF-----ASNVfsDIKGRFDMIIS 267
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
116-190 2.43e-03

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 39.62  E-value: 2.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032287566 116 LIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASD-IAVQAKEVVKANGLSDKVIVLHGRVEDveIDEEVDVIIS 190
Cdd:pfam02353  59 LKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKnQYKLARKRVAAEGLARKVEVLLQDYRD--FDEPFDRIVS 132
arsM PRK11873
arsenite methyltransferase;
112-190 2.82e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 39.55  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 112 QHQSLIEGKVVVDVGCGTGILSIFCAQA-GAK-RVYAVDASDIAVQ-AKEVVKANGLSDkVIVLHGRVEDVEI-DEEVDV 187
Cdd:PRK11873   71 ALAELKPGETVLDLGSGGGFDCFLAARRvGPTgKVIGVDMTPEMLAkARANARKAGYTN-VEFRLGEIEALPVaDNSVDV 149

                  ...
gi 1032287566 188 IIS 190
Cdd:PRK11873  150 IIS 152
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
122-221 3.64e-03

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 39.17  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032287566 122 VVDVGCGTGILSIFCAQA--GAKRVYAVDASDIAVQA-KEVVKA--NGLSDKVIVLHGRVEDVEIDEEVDVIIsewMGYM 196
Cdd:COG5459    84 VLDVGAGPGTAAWAAADAwpSLLDATLLERSAAALALgRRLARAaaNPALETAEWRLADLAAALPAPPADLVV---ASYV 160
                          90       100
                  ....*....|....*....|....*..
gi 1032287566 197 L--LYESMLGSVitARDRWLKPGGLIL 221
Cdd:COG5459   161 LneLADAARAAL--VDRLWLAPDGALL 185
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
272-337 9.54e-03

The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 36.08  E-value: 9.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032287566 272 SISGEnvlTWPEVvkhidcKTIKIQELDSVTARYKFNSMMRAPMHGFAFWFDVEFSGPASSPAKNT 337
Cdd:cd13896    18 TINGK---AYPDA------DPLRVREGERVRIVFVNDTMMAHPMHLHGHFFQVENGNGEYGPRKDT 74
 
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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