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Conserved domains on  [gi|1890957514|gb|QNE46695|]
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tRNA (adenine-N1)-methyltransferase [Glaciihabitans sp. INWT7]

Protein Classification

tRNA (adenine-N1)-methyltransferase( domain architecture ID 11457537)

tRNA (adenine-N1)-methyltransferase, such as tRNA (adenine(58)-N(1))-methyltransferase, which is a class I SAM-dependent methyltransferase that catalyzes the methylation of N(1)-adenine at position 58 (m1A58) in tRNA using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 13-268 2.41e-145

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: 410.32  E-value: 2.41e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  13 AGDRVQLTGPKGRLNTITLEAGKVFHTHRGMVDHDALIGLADASVVTATNGDEYLALRPLLNDFVMSMPRGAAIIYPKDA 92
Cdd:COG2519     1 EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  93 AQILSLGDIFPGAKVVEAGVGSGALSLWLLRGIGPTGSLTSFERREEFADVARGNVVSFLgaEPQNWTVTVGDLVEslpt 172
Cdd:COG2519    81 GYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFG--LPDNVELKLGDIRE---- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 173 AVENGSVDRVVLDMLAPWECLGVVADALAPGGVLLCYIATVTQLSRVAEAVRGTGlFTDPDSSETMVRGWHVEGLAVRPD 252
Cdd:COG2519   155 GIDEGDVDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESG-FTDIEAVETLLREWKVEGLAVRPE 233

                         250
                  ....*....|....*.
gi 1890957514 253 HRMVAHTGFLLTARRL 268
Cdd:COG2519   234 HRMVGHTGFLVFARKL 249
 
Name Accession Description Interval E-value
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 13-268 2.41e-145

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: 410.32  E-value: 2.41e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  13 AGDRVQLTGPKGRLNTITLEAGKVFHTHRGMVDHDALIGLADASVVTATNGDEYLALRPLLNDFVMSMPRGAAIIYPKDA 92
Cdd:COG2519     1 EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  93 AQILSLGDIFPGAKVVEAGVGSGALSLWLLRGIGPTGSLTSFERREEFADVARGNVVSFLgaEPQNWTVTVGDLVEslpt 172
Cdd:COG2519    81 GYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFG--LPDNVELKLGDIRE---- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 173 AVENGSVDRVVLDMLAPWECLGVVADALAPGGVLLCYIATVTQLSRVAEAVRGTGlFTDPDSSETMVRGWHVEGLAVRPD 252
Cdd:COG2519   155 GIDEGDVDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESG-FTDIEAVETLLREWKVEGLAVRPE 233

                         250
                  ....*....|....*.
gi 1890957514 253 HRMVAHTGFLLTARRL 268
Cdd:COG2519   234 HRMVGHTGFLVFARKL 249
GCD14_N pfam14801
tRNA methyltransferase complex GCD14 subunit N-term; This is the N-terminal domain of GCD14, ...
 8-58 1.57e-26

tRNA methyltransferase complex GCD14 subunit N-term; This is the N-terminal domain of GCD14, itself a subunit of the tRNA methyltransferase complex that is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. The exact function of the N-terminus is not known but it is necessary for maintaining the overall folding and for full enzymatic activity.


Pssm-ID: 434222  Cd Length: 51  Bit Score: 99.49  E-value: 1.57e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890957514   8 SGPFRAGDRVQLTGPKGRLNTITLEAGKVFHTHRGMVDHDALIGLADASVV 58
Cdd:pfam14801   1 RGPFRAGDRVQLTDPKGRKHTITLEPGGEFHTHRGAIRHDDLIGRPEGSVV 51
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 106-213 1.47e-08

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: 52.05  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 106 KVVEAGVGSGALSLWLLRGIGptGSLTSFERREEFADVARGNVvsfLGAEPQNWTVTVGDLVESLPTAVEngSVDRVVLD 185
Cdd:cd02440     1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKAA---AALLADNVEVLKGDAEELPPEADE--SFDVIISD 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1890957514 186 MLAPWEC------LGVVADALAPGGVLLCYIATV 213
Cdd:cd02440    74 PPLHHLVedlarfLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 13-268 2.41e-145

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: 410.32  E-value: 2.41e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  13 AGDRVQLTGPKGRLNTITLEAGKVFHTHRGMVDHDALIGLADASVVTATNGDEYLALRPLLNDFVMSMPRGAAIIYPKDA 92
Cdd:COG2519     1 EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  93 AQILSLGDIFPGAKVVEAGVGSGALSLWLLRGIGPTGSLTSFERREEFADVARGNVVSFLgaEPQNWTVTVGDLVEslpt 172
Cdd:COG2519    81 GYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFG--LPDNVELKLGDIRE---- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 173 AVENGSVDRVVLDMLAPWECLGVVADALAPGGVLLCYIATVTQLSRVAEAVRGTGlFTDPDSSETMVRGWHVEGLAVRPD 252
Cdd:COG2519   155 GIDEGDVDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESG-FTDIEAVETLLREWKVEGLAVRPE 233

                         250
                  ....*....|....*.
gi 1890957514 253 HRMVAHTGFLLTARRL 268
Cdd:COG2519   234 HRMVGHTGFLVFARKL 249
GCD14_N pfam14801
tRNA methyltransferase complex GCD14 subunit N-term; This is the N-terminal domain of GCD14, ...
 8-58 1.57e-26

tRNA methyltransferase complex GCD14 subunit N-term; This is the N-terminal domain of GCD14, itself a subunit of the tRNA methyltransferase complex that is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. The exact function of the N-terminus is not known but it is necessary for maintaining the overall folding and for full enzymatic activity.


Pssm-ID: 434222  Cd Length: 51  Bit Score: 99.49  E-value: 1.57e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890957514   8 SGPFRAGDRVQLTGPKGRLNTITLEAGKVFHTHRGMVDHDALIGLADASVV 58
Cdd:pfam14801   1 RGPFRAGDRVQLTDPKGRKHTITLEPGGEFHTHRGAIRHDDLIGRPEGSVV 51
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 78-266 1.67e-22

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 94.48  E-value: 1.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  78 MSMPRGAAIIYPKDAAQILSLGDIFPGAKVVEAGVGSGALSLWLLRGIGPTGSLTSFERREEFADVARGNvvsFLGAEPQ 157
Cdd:pfam08704  15 LNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADKAREE---FREHGID 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 158 NW-TVTVGDLV-ESLPTAVeNGSVDRVVLDMLAPWECLGVVADALA-PGGVLLCYIATVTQLSRVAEAVRGTGlFTDPDS 234
Cdd:pfam08704  92 QLvTVTHRDVCkEGFLTEV-SGKADAVFLDLPSPWEAVPHAWKALKvEGGRFCSFSPCIEQVQRTCQALAELG-FTEIST 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890957514 235 SETMVRGWHVE----------------------------------------GLAVRPDHRMVAHTGFLLTAR 266
Cdd:pfam08704 170 LEVLLRVYDVRtvslpvidlgidrekenertrteglsnddksednsgnsmlGTALKPMSEAVGHTGYLTFAT 241
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 106-213 1.47e-08

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: 52.05  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 106 KVVEAGVGSGALSLWLLRGIGptGSLTSFERREEFADVARGNVvsfLGAEPQNWTVTVGDLVESLPTAVEngSVDRVVLD 185
Cdd:cd02440     1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKAA---AALLADNVEVLKGDAEELPPEADE--SFDVIISD 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1890957514 186 MLAPWEC------LGVVADALAPGGVLLCYIATV 213
Cdd:cd02440    74 PPLHHLVedlarfLEEARRLLKPGGVLVLTLVLA 107
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 106-208 1.95e-08

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: 53.26  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 106 KVVEAGVGSGALSLWLLRGIGPTGSLTSFERREEFADVARGNVVSFlGAEPQnWTVTVGDLVESLPTaVENGSVDRVVLD 185
Cdd:COG4122    19 RILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARA-GLADR-IRLILGDALEVLPR-LADGPFDLVFID 95

                          90       100
                  ....*....|....*....|....*.
gi 1890957514 186 ---MLAPwECLGVVADALAPGGVLLC 208
Cdd:COG4122    96 adkSNYP-DYLELALPLLRPGGLIVA 120
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 92-228 2.25e-07

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: 49.61  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  92 AAQILSLGDIFPGAKVVEAGVGSGALSLWLLRgigPTGSLTSFERREEFADVARGNvvsfLGAEPQNWTVTVGDlVESLP 171
Cdd:COG2226    11 REALLAALGLRPGARVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELARER----AAEAGLNVEFVVGD-AEDLP 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890957514 172 taVENGSVDRV----VLDMLA-PWECLGVVADALAPGGVLLCYIATVTQLSRVAEAVRGTGL 228
Cdd:COG2226    83 --FPDGSFDLVissfVLHHLPdPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAGF 142
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
75-207 2.23e-06

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 47.75  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  75 DFVMSMPRGAAIIYPKDAAQILSLGDIFPGAKVVEAGVGSGALSLWLLRGIGPTGSLTSFERREEFADVARGNVVSfLGA 154
Cdd:pfam01135  45 DIPLSIGYGQTISAPHMHAMMLELLELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEK-LGL 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1890957514 155 EpqNWTVTVGDLVESLPtavENGSVDRVVLDMLAPwECLGVVADALAPGGVLL 207
Cdd:pfam01135 124 E--NVIVVVGDGRQGWP---EFAPYDAIHVGAAAP-EIPEALIDQLKEGGRLV 170
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 108-208 4.03e-06

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 44.99  E-value: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 108 VEAGVGSGALSLWLLRGIGP--TGSLTSFERREEFADVARGNVVSFLGAepqNWTVTVGDLVESLPTaVENGSVDRVVLD 185
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAALRDngLGRLTAVDPDPGAEEAGALLRKAGLDD---RVRLIVGDSREALPS-LADGPIDLLFID 76

                          90       100
                  ....*....|....*....|....*..
gi 1890957514 186 ML----APWECLGVVADALAPGGVLLC 208
Cdd:pfam13578  77 GDhtyeAVLNDLELWLPRLAPGGVILF 103
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 101-208 4.51e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.87  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 101 IFPGAKVVEAGVGSGALSLWLLRGIGPTGSLTSFERREEFADVARGNVVSFlgaEPQNWTVTVGDlVESLPTAVENGSVD 180
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKL---GFDNVEFEQGD-IEELPELLEDDKFD 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1890957514 181 -----RVVLDMLAPWECLGVVADALAPGGVLLC 208
Cdd:pfam13847  77 vvisnCVLNHIPDPDKVLQEILRVLKPGGRLII 109
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 107-204 7.64e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 41.01  E-value: 7.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 107 VVEAGVGSGALSLWLLRGIGptGSLTSFERREEFADVARGNvvsfLGAEPQNWTVTVGDlVESLPtaVENGSVDRVV--- 183
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARER----AAEAGLNVEFVQGD-AEDLP--FPDGSFDLVVssg 71

                          90       100
                  ....*....|....*....|....*
gi 1890957514 184 ----LDMLAPWECLGVVADALAPGG 204
Cdd:pfam13649  72 vlhhLPDPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 103-207 9.93e-05

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: 41.54  E-value: 9.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 103 PGAKVVEAGVGSGALSLWLLR-GIgptgSLTSFERREEFADVARGNvvsflgAEPQNWTVTVGDLvESLPtaVENGSVDR 181
Cdd:COG2227    24 AGGRVLDVGCGTGRLALALARrGA----DVTGVDISPEALEIARER------AAELNVDFVQGDL-EDLP--LEDGSFDL 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1890957514 182 VV-LDMLA----PWECLGVVADALAPGGVLL 207
Cdd:COG2227    91 VIcSEVLEhlpdPAALLRELARLLKPGGLLL 121
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 91-207 1.14e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.14  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  91 DAAQ------ILSLGDIFPGAKVVEAGVGSGALSLWLLRGIGptGSLTSFERREEFADVARGNVVSFLGAEPqnwtVTVg 164
Cdd:COG2230    33 EEAQeakldlILRKLGLKPGMRVLDIGCGWGGLALYLARRYG--VRVTGVTLSPEQLEYARERAAEAGLADR----VEV- 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1890957514 165 dLVESLPTAVENGSVDRVV-LDML-----APW-ECLGVVADALAPGGVLL 207
Cdd:COG2230   106 -RLADYRDLPADGQFDAIVsIGMFehvgpENYpAYFAKVARLLKPGGRLL 154
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 89-229 6.55e-03

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 37.38  E-value: 6.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  89 PKDAAQILSLGDIFPGAKVVEAGVGSG---ALslwlLRGIGptGSLTSFERREEFADVARGNvvsFLGAEPQNWTVTVGD 165
Cdd:COG2518    52 PYIVARMLEALDLKPGDRVLEIGTGSGyqaAV----LARLA--GRVYSVERDPELAERARER---LAALGYDNVTVRVGD 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890957514 166 LVESLPtavENGSVDRVVL-----DMLAPWeclgvvADALAPGGVLLC-----YIATVTQLSRVAEAVRGTGLF 229
Cdd:COG2518   123 GALGWP---EHAPFDRIIVtaaapEVPEAL------LEQLAPGGRLVApvgegGVQRLVLITRTGDGFERESLF 187
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 82-283 6.65e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.20  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514  82 RGAAIIYPKDAAQILSLGDIFPGAKVVEAGVGSGALSLWLLRGIGptGSLTSFERREEFADVARGNVVSflgAEPQNWTV 161
Cdd:COG0500     5 YYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAK---AGLGNVEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890957514 162 TVGDLVESLPtaVENGSVDRVVLDMLAPW-------ECLGVVADALAPGGVLLCYIATVTQLSRVAEAVRGTGLFTDPDS 234
Cdd:COG0500    80 LVADLAELDP--LPAESFDLVVAFGVLHHlppeereALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1890957514 235 SETMvrgwhveGLAVRPDHRMVAHTGFLLTARRLAPDTVLPQLKRRLSK 283
Cdd:COG0500   158 LLLR-------LLALELYLRALLAAAATEDLRSDALLESANALEYLLSK 199
 
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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