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Conserved domains on  [gi|123173772|ref|NP_689520|]
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tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A [Homo sapiens]

Protein Classification

GCD14_N and GCD14 domain-containing protein( domain architecture ID 13573464)

GCD14_N and GCD14 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 64-286 3.61e-159

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: 442.70  E-value: 3.61e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772   64 GWVYVLHPTPELWTLNLPHRTQILYSTDIALITMMLELRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEK 143
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  144 AREEFQEHRVGRWVTVRTQDVCRSGF--GVSHVADAVFLDIPSPWEAVGHAWDALKVEGGRFCSFSPCIEQVQRTCQALA 221
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFltEVSGKADAVFLDLPSPWEAVPHAWKALKVEGGRFCSFSPCIEQVQRTCQALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  222 ARGFSELSTLEVLPQVYNVRTVSLPPPDLG---------TGTDGPAGSDTSPFRSGT--------PMKEAVGHTGYLTFA 284
Cdd:pfam08704 161 ELGFTEISTLEVLLRVYDVRTVSLPVIDLGidrekenerTRTEGLSNDDKSEDNSGNsmlgtalkPMSEAVGHTGYLTFA 240


                  ..
gi 123173772  285 TK 286
Cdd:pfam08704 241 TK 242
GCD14_N super family cl37887
tRNA methyltransferase complex GCD14 subunit N-term; This is the N-terminal domain of GCD14, ...
 23-58 8.47e-03

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.


The actual alignment was detected with superfamily member pfam14801:

Pssm-ID: 434222  Cd Length: 51  Bit Score: 33.63  E-value: 8.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 123173772   23 GAMVAVRVQRGAQTQTRHGVLRHSvDLIGRPFGSKV 58
Cdd:pfam14801  17 GRKHTITLEPGGEFHTHRGAIRHD-DLIGRPEGSVV 51
 
Name Accession Description Interval E-value
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 64-286 3.61e-159

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: 442.70  E-value: 3.61e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772   64 GWVYVLHPTPELWTLNLPHRTQILYSTDIALITMMLELRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEK 143
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  144 AREEFQEHRVGRWVTVRTQDVCRSGF--GVSHVADAVFLDIPSPWEAVGHAWDALKVEGGRFCSFSPCIEQVQRTCQALA 221
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFltEVSGKADAVFLDLPSPWEAVPHAWKALKVEGGRFCSFSPCIEQVQRTCQALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  222 ARGFSELSTLEVLPQVYNVRTVSLPPPDLG---------TGTDGPAGSDTSPFRSGT--------PMKEAVGHTGYLTFA 284
Cdd:pfam08704 161 ELGFTEISTLEVLLRVYDVRTVSLPVIDLGidrekenerTRTEGLSNDDKSEDNSGNsmlgtalkPMSEAVGHTGYLTFA 240


                  ..
gi 123173772  285 TK 286
Cdd:pfam08704 241 TK 242
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 12-287 1.25e-67

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: 210.79  E-value: 1.25e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  12 EGDTAILSLGHGAMVAVRVQRGAQTQTRHGVLRHSvDLIGRPFGSKVTCGRGGWVYVLHPTPELWTLNLPHRTQILYSTD 91
Cdd:COG2519    1 EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHD-DLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  92 IALITMMLELRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRWVTVRTQDVcRSGFGV 171
Cdd:COG2519   80 AGYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDI-REGIDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772 172 sHVADAVFLDIPSPWEAVGHAWDALKVeGGRFCSFSPCIEQVQRTCQALAARGFSELSTLEVLPQVYNVRTVSLPPPDLG 251
Cdd:COG2519  159 -GDVDAVFLDMPDPWEALEAVAKALKP-GGVLVAYVPTVNQVSKLVEALRESGFTDIEAVETLLREWKVEGLAVRPEHRM 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 123173772 252 tgtdgpagsdtspfrsgtpmkeaVGHTGYLTFATKT 287
Cdd:COG2519  237 -----------------------VGHTGFLVFARKL 249
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
92-150 1.65e-03

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 39.03  E-value: 1.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 123173772  92 IALITMMLELRPGSVVCESGTGSGSVShAIIRTIAptGHLHTVEFHQQRAEKAREEFQE 150
Cdd:PRK00312  67 VARMTELLELKPGDRVLEIGTGSGYQA-AVLAHLV--RRVFSVERIKTLQWEAKRRLKQ 122
GCD14_N pfam14801
tRNA methyltransferase complex GCD14 subunit N-term; This is the N-terminal domain of GCD14, ...
 23-58 8.47e-03

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: 33.63  E-value: 8.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 123173772   23 GAMVAVRVQRGAQTQTRHGVLRHSvDLIGRPFGSKV 58
Cdd:pfam14801  17 GRKHTITLEPGGEFHTHRGAIRHD-DLIGRPEGSVV 51
 
Name Accession Description Interval E-value
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 64-286 3.61e-159

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: 442.70  E-value: 3.61e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772   64 GWVYVLHPTPELWTLNLPHRTQILYSTDIALITMMLELRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEK 143
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  144 AREEFQEHRVGRWVTVRTQDVCRSGF--GVSHVADAVFLDIPSPWEAVGHAWDALKVEGGRFCSFSPCIEQVQRTCQALA 221
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFltEVSGKADAVFLDLPSPWEAVPHAWKALKVEGGRFCSFSPCIEQVQRTCQALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  222 ARGFSELSTLEVLPQVYNVRTVSLPPPDLG---------TGTDGPAGSDTSPFRSGT--------PMKEAVGHTGYLTFA 284
Cdd:pfam08704 161 ELGFTEISTLEVLLRVYDVRTVSLPVIDLGidrekenerTRTEGLSNDDKSEDNSGNsmlgtalkPMSEAVGHTGYLTFA 240


                  ..
gi 123173772  285 TK 286
Cdd:pfam08704 241 TK 242
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 12-287 1.25e-67

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: 210.79  E-value: 1.25e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  12 EGDTAILSLGHGAMVAVRVQRGAQTQTRHGVLRHSvDLIGRPFGSKVTCGRGGWVYVLHPTPELWTLNLPHRTQILYSTD 91
Cdd:COG2519    1 EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHD-DLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  92 IALITMMLELRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRWVTVRTQDVcRSGFGV 171
Cdd:COG2519   80 AGYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDI-REGIDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772 172 sHVADAVFLDIPSPWEAVGHAWDALKVeGGRFCSFSPCIEQVQRTCQALAARGFSELSTLEVLPQVYNVRTVSLPPPDLG 251
Cdd:COG2519  159 -GDVDAVFLDMPDPWEALEAVAKALKP-GGVLVAYVPTVNQVSKLVEALRESGFTDIEAVETLLREWKVEGLAVRPEHRM 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 123173772 252 tgtdgpagsdtspfrsgtpmkeaVGHTGYLTFATKT 287
Cdd:COG2519  237 -----------------------VGHTGFLVFARKL 249
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 93-202 3.73e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 46.62  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  93 ALITMMLELRPGSVVCESGTGSGSVShAIIRTIAptGHLHTVEFHQQRAEKAREEFQEHRVGRwVTVRTQDVCRsgfGVS 172
Cdd:COG2518   56 ARMLEALDLKPGDRVLEIGTGSGYQA-AVLARLA--GRVYSVERDPELAERARERLAALGYDN-VTVRVGDGAL---GWP 128

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 123173772 173 HVA--DAVFL-----DIPSPWeavghaWDALKvEGGR 202
Cdd:COG2518  129 EHApfDRIIVtaaapEVPEAL------LEQLA-PGGR 158
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 98-226 1.86e-05

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: 43.83  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  98 MLELRPGSVVCESGTGSGSVSHAIIRTiapTGHLHTVEFHQQRAEKAREEFQEHrvGRWVTVRTQDVCRSGFGvSHVADA 177
Cdd:COG2226   17 ALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEA--GLNVEFVVGDAEDLPFP-DGSFDL 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 123173772 178 VFL-----DIPSPWEAVGHAWDALKvEGGRFCSFSPCIEQVQRTCQALAARGFS 226
Cdd:COG2226   91 VISsfvlhHLPDPERALAEIARVLK-PGGRLVVVDFSPPDLAELEELLAEAGFE 143
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 93-163 2.52e-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: 43.63  E-value: 2.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123173772  93 ALITMMLELRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRWVTVRTQD 163
Cdd:COG4122    6 RLLYLLARLLGAKRILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGD 76
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 99-203 9.31e-05

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: 43.62  E-value: 9.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  99 LELRPGSVVCESGTGSGSVSHAIIRtIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRwVTVrtqdvcrsgfgVSHVADAV 178
Cdd:COG2242  243 LALRPGDVLWDIGAGSGSVSIEAAR-LAPGGRVYAIERDPERAALIRANARRFGVPN-VEV-----------VEGEAPEA 309

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 123173772 179 FLDIPSP------------WEAVGHAWDALKvEGGRF 203
Cdd:COG2242  310 LADLPDPdavfiggsggnlPEILEACWARLR-PGGRL 345
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 101-212 1.88e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.86  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123173772  101 LRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRwVTVRTQDV-------CRSGFGVSh 173
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIeelpellEDDKFDVV- 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 123173772  174 VADAVFLDIPSPWEAVGHAWDALKvEGGRFCSFSPCIEQ 212
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLK-PGGRLIISDPDSLA 116
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
92-150 1.65e-03

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 39.03  E-value: 1.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 123173772  92 IALITMMLELRPGSVVCESGTGSGSVShAIIRTIAptGHLHTVEFHQQRAEKAREEFQE 150
Cdd:PRK00312  67 VARMTELLELKPGDRVLEIGTGSGYQA-AVLAHLV--RRVFSVERIKTLQWEAKRRLKQ 122
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 92-150 1.72e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 38.84  E-value: 1.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 123173772  92 IALITMMLELRPGSVVCESGTGSGSVSHAIIRTIAPTGHLHTVEFHQQRAEKAREEFQE 150
Cdd:PRK13942  65 VAIMCELLDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKK 123
GCD14_N pfam14801
tRNA methyltransferase complex GCD14 subunit N-term; This is the N-terminal domain of GCD14, ...
 23-58 8.47e-03

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: 33.63  E-value: 8.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 123173772   23 GAMVAVRVQRGAQTQTRHGVLRHSvDLIGRPFGSKV 58
Cdd:pfam14801  17 GRKHTITLEPGGEFHTHRGAIRHD-DLIGRPEGSVV 51
 
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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