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Conserved domains on  [gi|119569152|gb|EAW48767|]
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mitochondrial translation optimization 1 homolog (S. cerevisiae), isoform CRA_h [Homo sapiens]

Protein Classification

MnmG/GidA family protein( domain architecture ID 1003581)

MnmG family protein similar to bacterial tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG and eukaryotic protein MTO1 homolog

CATH:  1.10.10.1800
Gene Ontology:  GO:0030488|GO:0002098|GO:0050660
SCOP:  4006485

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MnmG super family cl33878
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
5-362 1.91e-168

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


The actual alignment was detected with superfamily member COG0445:

Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 484.51  E-value: 1.91e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152   5 RYCPSIESKVLRFPNRL-HQVWLEPEGMDSDLIYPQGLSMTLPAELQEKMITCIRGLEKAKVIQPGYGVQYDYLDPRQIT 83
Cdd:COG0445  274 RYCPSIEDKIVRFADKDrHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLK 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  84 PSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSRKPPFVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVE 163
Cdd:COG0445  354 PTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAE 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152 164 FRLSLRPDNADSRLTLRGYKdAGCVSQQRYERACWMKSSLEEGISVLKSIEFLSSKWKKLIPEASISTSRSLPVRALDVL 243
Cdd:COG0445  434 YRLLLRQDNADLRLTEKGYE-LGLVSDERYERFEEKKEAIEEEIERLKSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLL 512
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152 244 KYEEVDMDSLAKAVPEpLKKYTkcRELAERLKIEATYESVLFHQLQEIKGVQQDEALQLPKDLDYLTIRdvSLSHEVREK 323
Cdd:COG0445  513 RRPEITYEDLAELDPE-LPDLD--PEVAEQVEIEIKYEGYIERQEEEIEKLKRLENLKIPEDFDYDAIP--GLSNEAREK 587
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 119569152 324 LHFSRPQTIGAASRIPGVTPAAIINLLRFVKTTQRRQSA 362
Cdd:COG0445  588 LKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
5-362 1.91e-168

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 484.51  E-value: 1.91e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152   5 RYCPSIESKVLRFPNRL-HQVWLEPEGMDSDLIYPQGLSMTLPAELQEKMITCIRGLEKAKVIQPGYGVQYDYLDPRQIT 83
Cdd:COG0445  274 RYCPSIEDKIVRFADKDrHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLK 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  84 PSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSRKPPFVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVE 163
Cdd:COG0445  354 PTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAE 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152 164 FRLSLRPDNADSRLTLRGYKdAGCVSQQRYERACWMKSSLEEGISVLKSIEFLSSKWKKLIPEASISTSRSLPVRALDVL 243
Cdd:COG0445  434 YRLLLRQDNADLRLTEKGYE-LGLVSDERYERFEEKKEAIEEEIERLKSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLL 512
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152 244 KYEEVDMDSLAKAVPEpLKKYTkcRELAERLKIEATYESVLFHQLQEIKGVQQDEALQLPKDLDYLTIRdvSLSHEVREK 323
Cdd:COG0445  513 RRPEITYEDLAELDPE-LPDLD--PEVAEQVEIEIKYEGYIERQEEEIEKLKRLENLKIPEDFDYDAIP--GLSNEAREK 587
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 119569152 324 LHFSRPQTIGAASRIPGVTPAAIINLLRFVKTTQRRQSA 362
Cdd:COG0445  588 LKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
5-355 6.29e-139

glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272927 [Multi-domain]  Cd Length: 616  Bit Score: 409.06  E-value: 6.29e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152    5 RYCPSIESKVLRFPNR-LHQVWLEPEGMDSDLIYPQGLSMTLPAELQEKMITCIRGLEKAKVIQPGYGVQYDYLDPRQIT 83
Cdd:TIGR00136 269 RYCPSIEDKVVRFADKeRHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIRSIPGLENAEILRPGYAIEYDYFDPTQLK 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152   84 PSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSRKPPFVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVE 163
Cdd:TIGR00136 349 PTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRNEAYIGVLIDDLVTKGTKEPYRMFTSRAE 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  164 FRLSLRPDNADSRLTLRGYkDAGCVSQQRYERACWMKSSLEEGISVLKSIEFLSSKWKKLIPEASISTSRSLPVRALDVL 243
Cdd:TIGR00136 429 YRLLLREDNADFRLTEIGR-ELGLIDEDRYARFLKKKQNIEEEIERLKSTRLSPSKEVKEELKNLAQSPLKDEVSGYDLL 507
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  244 KYEEVDMDSLAKAVPE--PLKKytkcrELAERLKIEATYESVLFHQLQEIKGVQQDEALQLPKDLDYLTIRdvSLSHEVR 321
Cdd:TIGR00136 508 KRPEMNLDKLTKLLPFlpPLDE-----EVLEQVEIEIKYEGYIKKQQQYIKKLDRLENVKIPADFDYRKIP--GLSTEAR 580
                         330       340       350
                  ....*....|....*....|....*....|....
gi 119569152  322 EKLHFSRPQTIGAASRIPGVTPAAIINLLRFVKT 355
Cdd:TIGR00136 581 EKLSKFRPLSLGQASRISGINPADISALLVYLKK 614
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
130-350 1.60e-91

tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA and to be responsible for the interaction with protein MnmE. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, pfam12631.


Pssm-ID: 464049 [Multi-domain]  Cd Length: 214  Bit Score: 273.87  E-value: 1.60e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  130 FVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVEFRLSLRPDNADSRLTLRGYKdAGCVSQQRYERACWMKSSLEEGISV 209
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRE-LGLVSDERYERFEEKKEAIEEEIER 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  210 LKSIEFLSSKWKKLIPEASISTSRSlPVRALDVLKYEEVDMDSLAKAVPEPLKKYtkcRELAERLKIEATYESVLFHQLQ 289
Cdd:pfam13932  80 LKSTRLSPSEWNNALLELGSAPLGT-GRSAFDLLRRPEVTYEDLAALIPELAPLD---PEVLEQVEIEAKYEGYIERQEA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119569152  290 EIKGVQQDEALQLPKDLDYLTIRdvSLSHEVREKLHFSRPQTIGAASRIPGVTPAAIINLL 350
Cdd:pfam13932 156 EIEKFKRLENLKIPEDLDYDAIP--GLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
50-148 7.70e-13

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 69.40  E-value: 7.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  50 QEKMITCIRGLEKAKVIQpgYGVQY--DYLD-PRQITPSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSR 126
Cdd:PRK05335 288 QKRVFRMIPGLENAEFVR--YGVMHrnTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALG 365
                         90       100
                 ....*....|....*....|..
gi 119569152 127 KPPFVVSRTEGyIGVLIDDLTT 148
Cdd:PRK05335 366 KEPVIPPPTTA-LGALLNYITG 386
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
5-362 1.91e-168

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 484.51  E-value: 1.91e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152   5 RYCPSIESKVLRFPNRL-HQVWLEPEGMDSDLIYPQGLSMTLPAELQEKMITCIRGLEKAKVIQPGYGVQYDYLDPRQIT 83
Cdd:COG0445  274 RYCPSIEDKIVRFADKDrHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLK 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  84 PSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSRKPPFVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVE 163
Cdd:COG0445  354 PTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAE 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152 164 FRLSLRPDNADSRLTLRGYKdAGCVSQQRYERACWMKSSLEEGISVLKSIEFLSSKWKKLIPEASISTSRSLPVRALDVL 243
Cdd:COG0445  434 YRLLLRQDNADLRLTEKGYE-LGLVSDERYERFEEKKEAIEEEIERLKSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLL 512
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152 244 KYEEVDMDSLAKAVPEpLKKYTkcRELAERLKIEATYESVLFHQLQEIKGVQQDEALQLPKDLDYLTIRdvSLSHEVREK 323
Cdd:COG0445  513 RRPEITYEDLAELDPE-LPDLD--PEVAEQVEIEIKYEGYIERQEEEIEKLKRLENLKIPEDFDYDAIP--GLSNEAREK 587
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 119569152 324 LHFSRPQTIGAASRIPGVTPAAIINLLRFVKTTQRRQSA 362
Cdd:COG0445  588 LKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
5-355 6.29e-139

glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272927 [Multi-domain]  Cd Length: 616  Bit Score: 409.06  E-value: 6.29e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152    5 RYCPSIESKVLRFPNR-LHQVWLEPEGMDSDLIYPQGLSMTLPAELQEKMITCIRGLEKAKVIQPGYGVQYDYLDPRQIT 83
Cdd:TIGR00136 269 RYCPSIEDKVVRFADKeRHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIRSIPGLENAEILRPGYAIEYDYFDPTQLK 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152   84 PSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSRKPPFVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVE 163
Cdd:TIGR00136 349 PTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRNEAYIGVLIDDLVTKGTKEPYRMFTSRAE 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  164 FRLSLRPDNADSRLTLRGYkDAGCVSQQRYERACWMKSSLEEGISVLKSIEFLSSKWKKLIPEASISTSRSLPVRALDVL 243
Cdd:TIGR00136 429 YRLLLREDNADFRLTEIGR-ELGLIDEDRYARFLKKKQNIEEEIERLKSTRLSPSKEVKEELKNLAQSPLKDEVSGYDLL 507
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  244 KYEEVDMDSLAKAVPE--PLKKytkcrELAERLKIEATYESVLFHQLQEIKGVQQDEALQLPKDLDYLTIRdvSLSHEVR 321
Cdd:TIGR00136 508 KRPEMNLDKLTKLLPFlpPLDE-----EVLEQVEIEIKYEGYIKKQQQYIKKLDRLENVKIPADFDYRKIP--GLSTEAR 580
                         330       340       350
                  ....*....|....*....|....*....|....
gi 119569152  322 EKLHFSRPQTIGAASRIPGVTPAAIINLLRFVKT 355
Cdd:TIGR00136 581 EKLSKFRPLSLGQASRISGINPADISALLVYLKK 614
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
130-350 1.60e-91

tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA and to be responsible for the interaction with protein MnmE. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, pfam12631.


Pssm-ID: 464049 [Multi-domain]  Cd Length: 214  Bit Score: 273.87  E-value: 1.60e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  130 FVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVEFRLSLRPDNADSRLTLRGYKdAGCVSQQRYERACWMKSSLEEGISV 209
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRE-LGLVSDERYERFEEKKEAIEEEIER 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  210 LKSIEFLSSKWKKLIPEASISTSRSlPVRALDVLKYEEVDMDSLAKAVPEPLKKYtkcRELAERLKIEATYESVLFHQLQ 289
Cdd:pfam13932  80 LKSTRLSPSEWNNALLELGSAPLGT-GRSAFDLLRRPEVTYEDLAALIPELAPLD---PEVLEQVEIEAKYEGYIERQEA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119569152  290 EIKGVQQDEALQLPKDLDYLTIRdvSLSHEVREKLHFSRPQTIGAASRIPGVTPAAIINLL 350
Cdd:pfam13932 156 EIEKFKRLENLKIPEDLDYDAIP--GLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
GIDA pfam01134
Glucose inhibited division protein A;
5-128 1.34e-65

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 213.18  E-value: 1.34e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152    5 RYCPSIESKVLRFPNRL-HQVWLEPEGMDSDLIYPQGLSMTLPAELQEKMITCIRGLEKAKVIQPGYGVQYDYLDPRQIT 83
Cdd:pfam01134 267 RYCPSIEDKPVRFADKPyHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTIPGLENAEIVRPGYAIEYDYIDPPQLL 346
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 119569152   84 PSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSRKP 128
Cdd:pfam01134 347 PTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
50-148 7.70e-13

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 69.40  E-value: 7.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  50 QEKMITCIRGLEKAKVIQpgYGVQY--DYLD-PRQITPSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSR 126
Cdd:PRK05335 288 QKRVFRMIPGLENAEFVR--YGVMHrnTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALG 365
                         90       100
                 ....*....|....*....|..
gi 119569152 127 KPPFVVSRTEGyIGVLIDDLTT 148
Cdd:PRK05335 366 KEPVIPPPTTA-LGALLNYITG 386
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
50-148 6.56e-12

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 66.62  E-value: 6.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569152  50 QEKMITCIRGLEKAKVIQpgYGVQY--DYLD-PRQITPSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSR 126
Cdd:COG1206  288 QKRVFRMIPGLENAEFVR--YGVMHrnTFINsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAARLLLG 365
                         90       100
                 ....*....|....*....|..
gi 119569152 127 KPPFVVSRTEGyIGVLIDDLTT 148
Cdd:COG1206  366 KEPVPPPPTTA-LGALLNYITG 386
 
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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