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Conserved domains on  [gi|1182946175|ref|NP_001337510|]
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tRNA (guanine(10)-N2)-methyltransferase homolog isoform c [Homo sapiens]

Protein Classification

TRM11 family methyltransferase( domain architecture ID 11437146)

TRM11 family SAM-dependent methyltransferase containing a THUMP domain, similar to fungal tRNA (guanine(10)-N2)-methyltransferase, the catalytic subunit of a tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 134-323 1.11e-25

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


:

Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 101.95  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 134 TSMDAGLSFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVHGLgkatrknqkwrgpdeniRANLRQ 213
Cdd:COG1041     8 GSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGA-----------------RENLEH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 214 YGLEKYylDVLVSDASKPSWRKGTyFDAIITDPPYGIRESTRRTGsqkeipkgiekwekcpeshvpvslsyhLSDMFLDL 293
Cdd:COG1041    71 YGYEDA--DVIRGDARDLPLADES-VDAIVTDPPYGRSSKISGEE---------------------------LLELYEKA 120

                         170       180       190
                  ....*....|....*....|....*....|
gi 1182946175 294 LNFAAETLVLGGRLVywlpVYTPEYTEEMV 323
Cdd:COG1041   121 LEEAARVLKPGGRVV----IVTPRDIDELL 146
 
Name Accession Description Interval E-value
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 134-323 1.11e-25

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


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 101.95  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 134 TSMDAGLSFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVHGLgkatrknqkwrgpdeniRANLRQ 213
Cdd:COG1041     8 GSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGA-----------------RENLEH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 214 YGLEKYylDVLVSDASKPSWRKGTyFDAIITDPPYGIRESTRRTGsqkeipkgiekwekcpeshvpvslsyhLSDMFLDL 293
Cdd:COG1041    71 YGYEDA--DVIRGDARDLPLADES-VDAIVTDPPYGRSSKISGEE---------------------------LLELYEKA 120

                         170       180       190
                  ....*....|....*....|....*....|
gi 1182946175 294 LNFAAETLVLGGRLVywlpVYTPEYTEEMV 323
Cdd:COG1041   121 LEEAARVLKPGGRVV----IVTPRDIDELL 146
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 76-269 2.85e-23

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 99.43  E-value: 2.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175  76 KVNLKKPQHVFSVledYGLDPNCipenphniYFGRWIADGQRELIESYSVKKRHFIGNTSMDAGLSFIMANHGKVKENDI 155
Cdd:TIGR01177 117 KVSLRRPDIVVRV---VITEDIF--------YLGRVLEERDKEQFIERKPDRRPFFKPGSMDPKLARAMVNLARVTEGDR 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 156 VFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVHGlgkatrknqkwrgpdenIRANLRQYGLEKYYldVLVSDASKPSWRK 235
Cdd:TIGR01177 186 VLDPFCGTGGFLIEAGLMGAKVIGCDIDWKMVAG-----------------ARINLEHYGIEDFF--VKRGDATKLPLSS 246

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1182946175 236 GTyFDAIITDPPYGIRESTRRTGSQKEIPKGIEK 269
Cdd:TIGR01177 247 ES-VDAIATDPPYGRSTTAAGDGLESLYERSLEE 279
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 127-258 4.74e-12

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 64.30  E-value: 4.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 127 KRHFIGNTSMDAGLSFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYgtdidyntvHGLGKAtRKNQKWRGPDEN 206
Cdd:pfam01170   3 YRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIA---------PGKFDA-RVRAPLYGSDID 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1182946175 207 IRA------NLRQYGLEKyYLDVLVSDASKPSWRKGTYfDAIITDPPYGIRESTRRTG 258
Cdd:pfam01170  73 RRMvqgarlNAENAGVGD-LIEFVQADAADLPLLEGSV-DVIVTNPPYGIRLGSKGAL 128
PRK14968 PRK14968
putative methyltransferase; Provisional
 141-248 1.67e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 47.97  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 141 SFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVhglgKATRKNQKWRGPDENiranlrqyGLEkyy 220
Cdd:PRK14968   12 SFLLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAV----ECAKCNAKLNNIRNN--------GVE--- 76

                          90       100
                  ....*....|....*....|....*...
gi 1182946175 221 ldVLVSDASKPSwrKGTYFDAIITDPPY 248
Cdd:PRK14968   77 --VIRSDLFEPF--RGDKFDVILFNPPY 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 156-314 1.10e-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: 41.26  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 156 VFDPFVGTGGLLIACAHF-GAYVYGTDIDyntvhglgkatrknqkwrgPDENIRANLRQYGLEKYYLDVLVSDASKPSWR 234
Cdd:cd02440     2 VLDLGCGTGALALALASGpGARVTGVDIS-------------------PVALELARKAAAALLADNVEVLKGDAEELPPE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 235 KGTYFDAIITDPPYgirestrrtgsqkeipkgiekwekcpeshvpvslsYHLSDMFLDLLNFAAETLVLGGRLVYWLPVY 314
Cdd:cd02440    63 ADESFDVIISDPPL-----------------------------------HHLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 134-323 1.11e-25

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


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 101.95  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 134 TSMDAGLSFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVHGLgkatrknqkwrgpdeniRANLRQ 213
Cdd:COG1041     8 GSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGA-----------------RENLEH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 214 YGLEKYylDVLVSDASKPSWRKGTyFDAIITDPPYGIRESTRRTGsqkeipkgiekwekcpeshvpvslsyhLSDMFLDL 293
Cdd:COG1041    71 YGYEDA--DVIRGDARDLPLADES-VDAIVTDPPYGRSSKISGEE---------------------------LLELYEKA 120

                         170       180       190
                  ....*....|....*....|....*....|
gi 1182946175 294 LNFAAETLVLGGRLVywlpVYTPEYTEEMV 323
Cdd:COG1041   121 LEEAARVLKPGGRVV----IVTPRDIDELL 146
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 76-269 2.85e-23

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 99.43  E-value: 2.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175  76 KVNLKKPQHVFSVledYGLDPNCipenphniYFGRWIADGQRELIESYSVKKRHFIGNTSMDAGLSFIMANHGKVKENDI 155
Cdd:TIGR01177 117 KVSLRRPDIVVRV---VITEDIF--------YLGRVLEERDKEQFIERKPDRRPFFKPGSMDPKLARAMVNLARVTEGDR 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 156 VFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVHGlgkatrknqkwrgpdenIRANLRQYGLEKYYldVLVSDASKPSWRK 235
Cdd:TIGR01177 186 VLDPFCGTGGFLIEAGLMGAKVIGCDIDWKMVAG-----------------ARINLEHYGIEDFF--VKRGDATKLPLSS 246

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1182946175 236 GTyFDAIITDPPYGIRESTRRTGSQKEIPKGIEK 269
Cdd:TIGR01177 247 ES-VDAIATDPPYGRSTTAAGDGLESLYERSLEE 279
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 127-258 4.74e-12

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 64.30  E-value: 4.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 127 KRHFIGNTSMDAGLSFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYgtdidyntvHGLGKAtRKNQKWRGPDEN 206
Cdd:pfam01170   3 YRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIA---------PGKFDA-RVRAPLYGSDID 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1182946175 207 IRA------NLRQYGLEKyYLDVLVSDASKPSWRKGTYfDAIITDPPYGIRESTRRTG 258
Cdd:pfam01170  73 RRMvqgarlNAENAGVGD-LIEFVQADAADLPLLEGSV-DVIVTNPPYGIRLGSKGAL 128
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
151-253 1.88e-07

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 51.73  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 151 KENDIVFDPFVGTGGLLIACAHFGA----------YVYGTDIDYNTV---------HGLGKAtrknqkwrgpdeNIRanl 211
Cdd:COG0286    42 KPGETVYDPACGSGGFLVEAAEYLKehggderkklSLYGQEINPTTYrlakmnlllHGIGDP------------NIE--- 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1182946175 212 rqyglekyYLDVLVSDaskpsWRKGTYFDAIITDPPYGIRES 253
Cdd:COG0286   107 --------LGDTLSND-----GDELEKFDVVLANPPFGGKWK 135
PRK14968 PRK14968
putative methyltransferase; Provisional
 141-248 1.67e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 47.97  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 141 SFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVhglgKATRKNQKWRGPDENiranlrqyGLEkyy 220
Cdd:PRK14968   12 SFLLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAV----ECAKCNAKLNNIRNN--------GVE--- 76

                          90       100
                  ....*....|....*....|....*...
gi 1182946175 221 ldVLVSDASKPSwrKGTYFDAIITDPPY 248
Cdd:PRK14968   77 --VIRSDLFEPF--RGDKFDVILFNPPY 100
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 141-259 1.20e-05

HemK-related putative methylase; 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. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 45.62  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 141 SFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYVYGTDIDYNTVhglgKATRKNQKWRGPDeniranlrqyglekyy 220
Cdd:TIGR00537   8 SLLLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAV----KELRENAKLNNVG---------------- 67

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1182946175 221 LDVLVSDASKPSWRKgtyFDAIITDPPYGIRESTRRTGS 259
Cdd:TIGR00537  68 LDVVMTDLFKGVRGK---FDVILFNPPYLPLEDDLRRGD 103
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
152-252 1.86e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 45.28  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 152 ENDIVFDPFVGTGGLLIACAHFGA-YVYGTDIDYNTVhglgkatrknqkwrgpdENIRANLRQYGLEkyyLDVLVSDASK 230
Cdd:COG2263    45 EGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEAL-----------------EIARENAERLGVR---VDFIRADVTR 104

                          90       100
                  ....*....|....*....|..
gi 1182946175 231 PSWRKGtyFDAIITDPPYGIRE 252
Cdd:COG2263   105 IPLGGS--VDTVVMNPPFGAQR 124
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 136-225 2.88e-05

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: 45.33  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 136 MDAGLSFIMANHGK-----------VKENDIVFDPFVGTGGLLIACAHFGA-YVYGTDIDYNTVhglgKATRKNQKWRGP 203
Cdd:pfam06325 134 LDPGMAFGTGTHPTtklclealerlVKPGESVLDVGCGSGILAIAALKLGAkKVVGVDIDPVAV----RAAKENAELNGV 209

                          90       100
                  ....*....|....*....|..
gi 1182946175 204 DENIRANLRQYGLEKYYlDVLV 225
Cdd:pfam06325 210 EARLEVYLPGDLPKEKA-DVVV 230
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 156-314 1.10e-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: 41.26  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 156 VFDPFVGTGGLLIACAHF-GAYVYGTDIDyntvhglgkatrknqkwrgPDENIRANLRQYGLEKYYLDVLVSDASKPSWR 234
Cdd:cd02440     2 VLDLGCGTGALALALASGpGARVTGVDIS-------------------PVALELARKAAAALLADNVEVLKGDAEELPPE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 235 KGTYFDAIITDPPYgirestrrtgsqkeipkgiekwekcpeshvpvslsYHLSDMFLDLLNFAAETLVLGGRLVYWLPVY 314
Cdd:cd02440    63 ADESFDVIISDPPL-----------------------------------HHLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
150-197 1.37e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 43.22  E-value: 1.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1182946175 150 VKENDIVFDpfVGTG-GLL-IACAHFGA-YVYGTDIDYNTVhglgKATRKN 197
Cdd:PRK00517  117 VLPGKTVLD--VGCGsGILaIAAAKLGAkKVLAVDIDPQAV----EAAREN 161
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
 128-257 1.00e-03

N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.


Pssm-ID: 426749 [Multi-domain]  Cd Length: 310  Bit Score: 40.77  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 128 RHFIGNTSMDAG-------LSFIMANHGKVKENDIVFDPFVGTGGLLIaCAHfgAYVYGTDIDYN--TVHGLgkatrknQ 198
Cdd:pfam02384  14 RKFAPNAGKSGGefftpreVSKLIVELLDPKPGESIYDPACGSGGFLI-QAE--KFVKEHDGDTNdlSIYGQ-------E 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 199 KWRGPDENIRANLRQYGLEKYYLDVLVSDA-SKPSWRKGTYFDAIITDPPYGIRESTRRT 257
Cdd:pfam02384  84 KNPTTYRLARMNMILHGIEYDDFHIRHGDTlTSPKFEDDKKFDVVVANPPFSDKWDANDT 143
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 151-269 1.59e-03

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: 40.16  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 151 KENDIVFDPFVGTGGLLIACAHFGAYVYGTDIDyntvhglgkatrknqkwrgPD--ENIRANLRQYGLEKyyLDVLVSDA 228
Cdd:COG2265   232 TGGERVLDLYCGVGTFALPLARRAKKVIGVEIV-------------------PEavEDARENARLNGLKN--VEFVAGDL 290

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1182946175 229 SK--PSWRKGTYFDAIITDPPygirestrRTGSQKEIPKGIEK 269
Cdd:COG2265   291 EEvlPELLWGGRPDVVVLDPP--------RAGAGPEVLEALAA 325
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
151-183 2.90e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 39.14  E-value: 2.90e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1182946175 151 KENDIVFDPFVGTGGLLIACAHFGAYVYGTDID 183
Cdd:COG0863   181 NPGDIVLDPFAGSGTTLVAAERLGRRFIGIEID 213
N6_N4_Mtase pfam01555
DNA methylase; Members of this family are DNA methylases. The family contains both N-4 ...
 151-183 3.34e-03

DNA methylase; Members of this family are DNA methylases. The family contains both N-4 cytosine-specific DNA methylases and N-6 Adenine-specific DNA methylases.


Pssm-ID: 396230 [Multi-domain]  Cd Length: 221  Bit Score: 38.53  E-value: 3.34e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1182946175 151 KENDIVFDPFVGTGGLLIACAHFGAYVYGTDID 183
Cdd:pfam01555 180 NPGDIVLDPFAGSGTTGAAAKELGRNFIGIEIE 212
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 150-252 5.90e-03

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: 38.30  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 150 VKENDIVFDPFVGTGGL-LIACAHFGAYVYGTDIDYNTVHGLGkatrknqkwrgpdENIRANlrqyGLEKyYLDVLVSDA 228
Cdd:COG2520   178 VKPGERVLDMFAGVGPFsIPIAKRSGAKVVAIDINPDAVEYLK-------------ENIRLN----KVED-RVTPILGDA 239

                          90       100
                  ....*....|....*....|....*
gi 1182946175 229 SK-PSWRKGTyFDAIITDPPYGIRE 252
Cdd:COG2520   240 REvAPELEGK-ADRIIMNLPHSADE 263
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 148-243 6.39e-03

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 38.38  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182946175 148 GKVKENDIVFdpFVGTGGL-----LIAcAHFGAYVYGTDIdyntvhglgkatrknqkwrgpDENIRANLRQYGLEKYYLD 222
Cdd:cd08254   161 GEVKPGETVL--VIGLGGLglnavQIA-KAMGAAVIAVDI---------------------KEEKLELAKELGADEVLNS 216

                          90       100
                  ....*....|....*....|.
gi 1182946175 223 VLVSDASKPSWRKGTYFDAII 243
Cdd:cd08254   217 LDDSPKDKKAAGLGGGFDVIF 237
 
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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