|
Name |
Accession |
Description |
Interval |
E-value |
| TrmD |
COG0336 |
tRNA G37 N-methylase TrmD [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
1-272 |
4.10e-126 |
|
tRNA G37 N-methylase TrmD [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase TrmD is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440105 Cd Length: 242 Bit Score: 366.65 E-value: 4.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 1 MRFQILTIFPEFFE-VLGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARDRLRd 79
Cdd:COG0336 1 MRIDVLTLFPEMFEgPLGHSILGRALEKGLLELEVHNLRDFTTDKHRTVDDTPYGGGAGMVMKPEPLFAAIEAAKAEGP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 80 qsagsdpenrptdlvNPKTILaiPTPSGIPLTQAKVREIAAHaDNVIIACGRYEGIDSRVASHYTDpqlypdlevFEYSL 159
Cdd:COG0336 80 ---------------KPRVIY--LSPQGRPFTQALARELAKE-EHLILLCGRYEGIDERVIEHLVD---------EEISI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 160 GDYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEgTGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERA 239
Cdd:COG0336 133 GDYVLSGGELAAMVLIDAVVRLLPGVLGNEESAEEDSFS-DGLLEYPHYTRPAEFRGLKVPEVLLSGNHAKIARWRREQS 211
|
250 260 270
....*....|....*....|....*....|...
gi 1839392051 240 IEKTCSQRPDLLASLDvglLSKRGREKLASLGW 272
Cdd:COG0336 212 LERTRERRPDLLEKAE---LTKEDRKLLEELKK 241
|
|
| trmD |
PRK00026 |
tRNA (guanine-N(1)-)-methyltransferase; Reviewed |
1-272 |
8.88e-120 |
|
tRNA (guanine-N(1)-)-methyltransferase; Reviewed
Pssm-ID: 234581 Cd Length: 244 Bit Score: 350.55 E-value: 8.88e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 1 MRFQILTIFPEFFE-VLGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARDRLRD 79
Cdd:PRK00026 1 MRIDVLTLFPEMFPgPLEYSILGRALEKGLLELEVHNPRDFTTDKHRTVDDTPYGGGAGMVMKPEPLFDAIDAAKAAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 80 qsagsdpenrptdlvNPKTILaiPTPSGIPLTQAKVREIaAHADNVIIACGRYEGIDSRVASHYTDpqlypdlevFEYSL 159
Cdd:PRK00026 81 ---------------KAKVIL--LSPQGKPFTQADAREL-AKEEHLILLCGRYEGIDERVIEHYVD---------EEISI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 160 GDYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEgTGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERA 239
Cdd:PRK00026 134 GDYVLTGGELAAMVLIDAVVRLLPGVLGNEESAEEDSFS-DGLLEYPHYTRPAEFRGMKVPEVLLSGNHAKIARWRRKQS 212
|
250 260 270
....*....|....*....|....*....|...
gi 1839392051 240 IEKTCSQRPDLLASLDvglLSKRGREKLASLGW 272
Cdd:PRK00026 213 LERTKLRRPDLLEKLA---LTKEDKKLLAELKK 242
|
|
| TrmD-like |
cd18080 |
tRNA-M1G37-methyltransferase TrmD; The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) ... |
2-248 |
1.23e-110 |
|
tRNA-M1G37-methyltransferase TrmD; The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the N1 position of G37 in the anticodon loop of a subset of tRNA that contains a G at position 36. The presence of the modification prevents Watson-Crick base-pairing of this guanosine with cytosine in mRNA and translational frame-shifting. This family of proteins contains members of the SPOUT methyltransferases. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.
Pssm-ID: 349953 Cd Length: 219 Bit Score: 326.27 E-value: 1.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 2 RFQILTIFPEFFE-VLGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARdrlrdq 80
Cdd:cd18080 1 KIDVLTLFPEMFEgFLNDSILGRALEKGLIEIEVINLRDFATDKHKTVDDYPYGGGAGMVMKPEPLVKALESIK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 81 sagsdpenrpTDLVNPKTILaiPTPSGIPLTQAKVREIAAHaDNVIIACGRYEGIDSRVASHYTDpqlypdlevFEYSLG 160
Cdd:cd18080 75 ----------KKRKKSKVIY--LSPQGKPFNQKLAKELAKE-DHLVLICGRYEGIDERVIEYYVD---------EEISIG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 161 DYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEGtGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERAI 240
Cdd:cd18080 133 DYVLTGGELAAMVLIDAVVRLLPGVLGNEESAEEESFSD-GLLEYPQYTRPAEFRGLKVPEVLLSGNHAKIAKWRREQSL 211
|
....*...
gi 1839392051 241 EKTCSQRP 248
Cdd:cd18080 212 ERTKKRRP 219
|
|
| trmD |
TIGR00088 |
tRNA (guanine-N1)-methyltransferase; This model is specfic for the tRNA modification enzyme ... |
1-251 |
2.06e-81 |
|
tRNA (guanine-N1)-methyltransferase; This model is specfic for the tRNA modification enzyme tRNA (guanine-N1)-methyltransferase (trmD). This enzyme methylates guanosime-37 in a number of tRNAs.The enzyme's catalytic activity is as follows: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 129196 [Multi-domain] Cd Length: 233 Bit Score: 252.33 E-value: 2.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 1 MRFQILTIFPEFFE-VLGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARdrlrd 79
Cdd:TIGR00088 1 MKIGVLTLFPEMFWpYLESSILGRAQKKNLVSFEVVNPRDFSKDKHKTVDDRPYGGGAGMVLKPEPIRDALHSVK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 80 qsagsdpenrptdlvNPKTILAIPTPSGIPLTQAKVREIAAHaDNVIIACGRYEGIDSRVASHYTDpqlypdlevFEYSL 159
Cdd:TIGR00088 76 ---------------APAGTVILLSPQGRKFDQAGARELAQN-EHLILICGRYEGFDERIIQLEVD---------EEISI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 160 GDYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEgTGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERA 239
Cdd:TIGR00088 131 GDFVLTGGELPALTLIDSVVRLIPGVLGKEASLIEESFA-NGLLDCPHYTRPYDLKGLKVPEVLLSGNHAKIEQWRLKQS 209
|
250
....*....|..
gi 1839392051 240 IEKTCSQRPDLL 251
Cdd:TIGR00088 210 LLRTKLRRPDLL 221
|
|
| tRNA_m1G_MT |
pfam01746 |
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ... |
22-248 |
3.52e-46 |
|
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyzes the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA.
Pssm-ID: 396350 Cd Length: 182 Bit Score: 158.66 E-value: 3.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 22 GKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARDRlrdqsagsdpenrptdlvNPKTILa 101
Cdd:pfam01746 1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESVNYE------------------KWKVIL- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 102 iPTPSGIPLTQAKVREIAAHaDNVIIACGRYEGIDSRVASHYtdpqlypdlevfEYSLGDYVLNGGEIAAVALIEAVGRL 181
Cdd:pfam01746 62 -LTPTGKPFFQEGAVDLSQK-EHLVYLCGDYEGVDERVDDDK------------EYSIGDFVDKGGEKGALVLIDLVKRL 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839392051 182 LDGMVgnPESLVEESYegtgLLEYPCYTRPEIWRdlAVPEVLKGGNHaaIEAWrrERAIEKTCSQRP 248
Cdd:pfam01746 128 LPGVL--TASLPIDSF----LLEKPHYTRPLTLN--QVPEILLSGNH--IRNW--KEALLRTIPRRK 182
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
367-484 |
1.55e-09 |
|
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440859 [Multi-domain] Cd Length: 132 Bit Score: 56.15 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 367 RYWVAELGGELVGYtyakVGLgesevdqAGIVAGDAYLSKCYVREALHSTGLSGALLEVAVrDLASTSDAPGVCLGTsiy 446
Cdd:COG1246 29 EFWVAEEDGEIVGC----AAL-------HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALL-AEARELGLKRLFLLT--- 93
|
90 100 110
....*....|....*....|....*....|....*....
gi 1839392051 447 NKRAQKFYKHHGFRRIGKRTFTVGDVQNQD-VVMRRVFD 484
Cdd:COG1246 94 TSAAIHFYEKLGFEEIDKEDLPYAKVWQRDsVVMEKDLE 132
|
|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
364-461 |
4.09e-06 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 44.75 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 364 QENRYWVAELGGELVGYTYAKVGLGESEVDQAGIvagdaylskcYVREALHSTGLSGALLEVAVRDLAstsdAPGVCLGT 443
Cdd:pfam13508 1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRL----------AVHPEYRGQGIGRALLEAAEAAAK----EGGIKLLE 66
|
90
....*....|....*...
gi 1839392051 444 SIYNKRAQKFYKHHGFRR 461
Cdd:pfam13508 67 LETTNRAAAFYEKLGFEE 84
|
|
| rimI |
TIGR01575 |
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ... |
366-465 |
4.35e-05 |
|
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273701 [Multi-domain] Cd Length: 131 Bit Score: 43.09 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 366 NRYWVAELGGELVGYTYAKVGLGESEVDQAGivagdaylskcyVREALHSTGLSGALLEVAVRDLAStSDAPGVCLGTSI 445
Cdd:TIGR01575 31 LCYLLARIGGKVVGYAGVQIVLDEAHILNIA------------VKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRV 97
|
90 100
....*....|....*....|
gi 1839392051 446 YNKRAQKFYKHHGFRRIGKR 465
Cdd:TIGR01575 98 SNIAAQALYKKLGFNEIAIR 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TrmD |
COG0336 |
tRNA G37 N-methylase TrmD [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
1-272 |
4.10e-126 |
|
tRNA G37 N-methylase TrmD [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase TrmD is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440105 Cd Length: 242 Bit Score: 366.65 E-value: 4.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 1 MRFQILTIFPEFFE-VLGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARDRLRd 79
Cdd:COG0336 1 MRIDVLTLFPEMFEgPLGHSILGRALEKGLLELEVHNLRDFTTDKHRTVDDTPYGGGAGMVMKPEPLFAAIEAAKAEGP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 80 qsagsdpenrptdlvNPKTILaiPTPSGIPLTQAKVREIAAHaDNVIIACGRYEGIDSRVASHYTDpqlypdlevFEYSL 159
Cdd:COG0336 80 ---------------KPRVIY--LSPQGRPFTQALARELAKE-EHLILLCGRYEGIDERVIEHLVD---------EEISI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 160 GDYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEgTGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERA 239
Cdd:COG0336 133 GDYVLSGGELAAMVLIDAVVRLLPGVLGNEESAEEDSFS-DGLLEYPHYTRPAEFRGLKVPEVLLSGNHAKIARWRREQS 211
|
250 260 270
....*....|....*....|....*....|...
gi 1839392051 240 IEKTCSQRPDLLASLDvglLSKRGREKLASLGW 272
Cdd:COG0336 212 LERTRERRPDLLEKAE---LTKEDRKLLEELKK 241
|
|
| trmD |
PRK00026 |
tRNA (guanine-N(1)-)-methyltransferase; Reviewed |
1-272 |
8.88e-120 |
|
tRNA (guanine-N(1)-)-methyltransferase; Reviewed
Pssm-ID: 234581 Cd Length: 244 Bit Score: 350.55 E-value: 8.88e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 1 MRFQILTIFPEFFE-VLGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARDRLRD 79
Cdd:PRK00026 1 MRIDVLTLFPEMFPgPLEYSILGRALEKGLLELEVHNPRDFTTDKHRTVDDTPYGGGAGMVMKPEPLFDAIDAAKAAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 80 qsagsdpenrptdlvNPKTILaiPTPSGIPLTQAKVREIaAHADNVIIACGRYEGIDSRVASHYTDpqlypdlevFEYSL 159
Cdd:PRK00026 81 ---------------KAKVIL--LSPQGKPFTQADAREL-AKEEHLILLCGRYEGIDERVIEHYVD---------EEISI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 160 GDYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEgTGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERA 239
Cdd:PRK00026 134 GDYVLTGGELAAMVLIDAVVRLLPGVLGNEESAEEDSFS-DGLLEYPHYTRPAEFRGMKVPEVLLSGNHAKIARWRRKQS 212
|
250 260 270
....*....|....*....|....*....|...
gi 1839392051 240 IEKTCSQRPDLLASLDvglLSKRGREKLASLGW 272
Cdd:PRK00026 213 LERTKLRRPDLLEKLA---LTKEDKKLLAELKK 242
|
|
| TrmD-like |
cd18080 |
tRNA-M1G37-methyltransferase TrmD; The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) ... |
2-248 |
1.23e-110 |
|
tRNA-M1G37-methyltransferase TrmD; The bacterial tRNA-(N(1)G37) methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the N1 position of G37 in the anticodon loop of a subset of tRNA that contains a G at position 36. The presence of the modification prevents Watson-Crick base-pairing of this guanosine with cytosine in mRNA and translational frame-shifting. This family of proteins contains members of the SPOUT methyltransferases. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.
Pssm-ID: 349953 Cd Length: 219 Bit Score: 326.27 E-value: 1.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 2 RFQILTIFPEFFE-VLGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARdrlrdq 80
Cdd:cd18080 1 KIDVLTLFPEMFEgFLNDSILGRALEKGLIEIEVINLRDFATDKHKTVDDYPYGGGAGMVMKPEPLVKALESIK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 81 sagsdpenrpTDLVNPKTILaiPTPSGIPLTQAKVREIAAHaDNVIIACGRYEGIDSRVASHYTDpqlypdlevFEYSLG 160
Cdd:cd18080 75 ----------KKRKKSKVIY--LSPQGKPFNQKLAKELAKE-DHLVLICGRYEGIDERVIEYYVD---------EEISIG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 161 DYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEGtGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERAI 240
Cdd:cd18080 133 DYVLTGGELAAMVLIDAVVRLLPGVLGNEESAEEESFSD-GLLEYPQYTRPAEFRGLKVPEVLLSGNHAKIAKWRREQSL 211
|
....*...
gi 1839392051 241 EKTCSQRP 248
Cdd:cd18080 212 ERTKKRRP 219
|
|
| trmD |
TIGR00088 |
tRNA (guanine-N1)-methyltransferase; This model is specfic for the tRNA modification enzyme ... |
1-251 |
2.06e-81 |
|
tRNA (guanine-N1)-methyltransferase; This model is specfic for the tRNA modification enzyme tRNA (guanine-N1)-methyltransferase (trmD). This enzyme methylates guanosime-37 in a number of tRNAs.The enzyme's catalytic activity is as follows: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 129196 [Multi-domain] Cd Length: 233 Bit Score: 252.33 E-value: 2.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 1 MRFQILTIFPEFFE-VLGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARdrlrd 79
Cdd:TIGR00088 1 MKIGVLTLFPEMFWpYLESSILGRAQKKNLVSFEVVNPRDFSKDKHKTVDDRPYGGGAGMVLKPEPIRDALHSVK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 80 qsagsdpenrptdlvNPKTILAIPTPSGIPLTQAKVREIAAHaDNVIIACGRYEGIDSRVASHYTDpqlypdlevFEYSL 159
Cdd:TIGR00088 76 ---------------APAGTVILLSPQGRKFDQAGARELAQN-EHLILICGRYEGFDERIIQLEVD---------EEISI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 160 GDYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEgTGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERA 239
Cdd:TIGR00088 131 GDFVLTGGELPALTLIDSVVRLIPGVLGKEASLIEESFA-NGLLDCPHYTRPYDLKGLKVPEVLLSGNHAKIEQWRLKQS 209
|
250
....*....|..
gi 1839392051 240 IEKTCSQRPDLL 251
Cdd:TIGR00088 210 LLRTKLRRPDLL 221
|
|
| trmD |
PRK14599 |
tRNA (guanine-N(1)-)-methyltransferase/unknown domain fusion protein; Provisional |
1-237 |
1.31e-52 |
|
tRNA (guanine-N(1)-)-methyltransferase/unknown domain fusion protein; Provisional
Pssm-ID: 173063 Cd Length: 222 Bit Score: 177.04 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 1 MRFQILTIFPE----FFEVlglSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARDR 76
Cdd:PRK14599 1 MKFNFITLFPEkiqsYFSE---GLQQKAIESGVFSINPIQLRDFSGNKHNRVDDTIYGGGPGMLLRVEPIHKALLSLGEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 77 lrdqsagsdpenrptdlvnpKTILAIPTPSGIPLTQAKVREIAAHADNVIIACGRYEGIDSRVASHYTDpqlypdlevFE 156
Cdd:PRK14599 78 --------------------KGIVILTSPSGIPFNQTIARELKESGKPLTFISGYYEGVDHRVTEHLVD---------ME 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 157 YSLGDYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEGTGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRR 236
Cdd:PRK14599 129 MSLGNYVISAGDLASICIADAVSRLLPGFLGAEESLLDESHNEPDELEYPQFTKPSEYNGWKVPDVLLSGNHASILAWRE 208
|
.
gi 1839392051 237 E 237
Cdd:PRK14599 209 Q 209
|
|
| trmD |
PRK01037 |
tRNA (guanine-N(1)-)-methyltransferase/unknown domain fusion protein; Reviewed |
1-250 |
3.68e-47 |
|
tRNA (guanine-N(1)-)-methyltransferase/unknown domain fusion protein; Reviewed
Pssm-ID: 234892 [Multi-domain] Cd Length: 357 Bit Score: 166.92 E-value: 3.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 1 MRFQILTIFPEFFEV-LGLSLLGKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGaGMVMRADIWGKAIDAARDRlrd 79
Cdd:PRK01037 1 MEIDILSLFPDYFDSpLQASILGRAIKQGLLSVQSRDIREFGLGKWKQVDDAPFNGE-GMLLMAEPVVQAIRSVRRE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 80 qsagsdpenrptdlvNPKTILAipTPSGIPLTQAKVREIAAhADNVIIACGRYEGIDSRVASHYTDPqlypdlevfEYSL 159
Cdd:PRK01037 77 ---------------KSKVIYL--SPQGQLLTAKKSRELAS-CSHLILLCGHYEGIDERALESEVDE---------EISI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 160 GDYVLNGGEIAAVALIEAVGRLLDGMVGNPESLVEESYEgTGLLEYPCYTRPEIWRDLAVPEVLKGGNHAAIEAWRRERA 239
Cdd:PRK01037 130 GDYVLTNGGIAALVLIDALSRFIPGVLGNQESAEYDSLE-NGLLEGPQYTRPRVFEGKEVPEVLLQGDHQAIADWRKQVS 208
|
250
....*....|.
gi 1839392051 240 IEKTCSQRPDL 250
Cdd:PRK01037 209 LERTRERRPDL 219
|
|
| tRNA_m1G_MT |
pfam01746 |
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC: ... |
22-248 |
3.52e-46 |
|
tRNA (Guanine-1)-methyltransferase; This is a family of tRNA (Guanine-1)-methyltransferases EC:2.1.1.31. In E.coli K12 this enzyme catalyzes the conversion of a guanosine residue to N1-methylguanine in position 37, next to the anticodon, in tRNA.
Pssm-ID: 396350 Cd Length: 182 Bit Score: 158.66 E-value: 3.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 22 GKAAQNGVLSWDVTNLRDFTDDPHRSVDDTPYGGGAGMVMRADIWGKAIDAARDRlrdqsagsdpenrptdlvNPKTILa 101
Cdd:pfam01746 1 GLAQEKGLVSLVVQNLRDYTANRRNTVDDEPYGGGFGMVLKPEPEFEALESVNYE------------------KWKVIL- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 102 iPTPSGIPLTQAKVREIAAHaDNVIIACGRYEGIDSRVASHYtdpqlypdlevfEYSLGDYVLNGGEIAAVALIEAVGRL 181
Cdd:pfam01746 62 -LTPTGKPFFQEGAVDLSQK-EHLVYLCGDYEGVDERVDDDK------------EYSIGDFVDKGGEKGALVLIDLVKRL 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839392051 182 LDGMVgnPESLVEESYegtgLLEYPCYTRPEIWRdlAVPEVLKGGNHaaIEAWrrERAIEKTCSQRP 248
Cdd:pfam01746 128 LPGVL--TASLPIDSF----LLEKPHYTRPLTLN--QVPEILLSGNH--IRNW--KEALLRTIPRRK 182
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
367-484 |
1.55e-09 |
|
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440859 [Multi-domain] Cd Length: 132 Bit Score: 56.15 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 367 RYWVAELGGELVGYtyakVGLgesevdqAGIVAGDAYLSKCYVREALHSTGLSGALLEVAVrDLASTSDAPGVCLGTsiy 446
Cdd:COG1246 29 EFWVAEEDGEIVGC----AAL-------HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALL-AEARELGLKRLFLLT--- 93
|
90 100 110
....*....|....*....|....*....|....*....
gi 1839392051 447 NKRAQKFYKHHGFRRIGKRTFTVGDVQNQD-VVMRRVFD 484
Cdd:COG1246 94 TSAAIHFYEKLGFEEIDKEDLPYAKVWQRDsVVMEKDLE 132
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
341-483 |
3.71e-09 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 55.09 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 341 DAIAQFVAVEFDTTA----VKARLNTPQENRYWVAELGGELVGYtyakVGLGESEVDQAGivaGDAYLSKCYVREALHST 416
Cdd:COG3153 10 EAIAALLRAAFGPGReaelVDRLREDPAAGLSLVAEDDGEIVGH----VALSPVDIDGEG---PALLLGPLAVDPEYRGQ 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839392051 417 GLSGALLEvAVRDLASTSDAPGVCLGTsiyNKRAQKFYKHHGFRRIGKRTFTVGDvqnQDVVMRRVF 483
Cdd:COG3153 83 GIGRALMR-AALEAARERGARAVVLLG---DPSLLPFYERFGFRPAGELGLTLGP---DEVFLAKEL 142
|
|
| RimI |
COG0456 |
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ... |
400-481 |
4.65e-09 |
|
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440224 [Multi-domain] Cd Length: 92 Bit Score: 53.51 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 400 GDAYLSKCYVREALHSTGLSGALLEvAVRDLASTSDAPGVCLGTSIYNKRAQKFYKHHGFRRIGKRTFTVGDvqnQDVVM 479
Cdd:COG0456 12 DEAEIEDLAVDPEYRGRGIGRALLE-AALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD---DALVM 87
|
..
gi 1839392051 480 RR 481
Cdd:COG0456 88 EK 89
|
|
| PhnO |
COG0454 |
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ... |
356-471 |
1.90e-08 |
|
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];
Pssm-ID: 440222 [Multi-domain] Cd Length: 136 Bit Score: 53.13 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 356 VKARLNTPQENRYWVAELGGELVGYtyakvgLGESEVDQAGIvagdaYLSKCYVREALHSTGLSGALLEvAVRDLASTSD 435
Cdd:COG0454 24 LKAMEGSLAGAEFIAVDDKGEPIGF------AGLRRLDDKVL-----ELKRLYVLPEYRGKGIGKALLE-ALLEWARERG 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1839392051 436 APGVCLGTSIYNKRAQKFYKHHGFRRIGKRTFTVGD 471
Cdd:COG0454 92 CTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGG 127
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
340-481 |
1.75e-07 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 50.76 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 340 NDAIAQFVAV----EFDTTAVKARLNTPQENRY--WVAELGGELVGYTYAKVGLGESEVDQAGIVAgdaylskCYVREAL 413
Cdd:COG1247 20 NEAIAEGTATfetePPSEEEREAWFAAILAPGRpvLVAEEDGEVVGFASLGPFRPRPAYRGTAEES-------IYVDPDA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 414 HSTGLSGALLEvAVRDLASTSDAPGVCLGTSIYNKRAQKFYKHHGFRRIG--KRTFTVGDVQNQDVVMRR 481
Cdd:COG1247 93 RGRGIGRALLE-ALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGtlPEVGFKFGRWLDLVLMQK 161
|
|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
364-461 |
4.09e-06 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 44.75 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 364 QENRYWVAELGGELVGYTYAKVGLGESEVDQAGIvagdaylskcYVREALHSTGLSGALLEVAVRDLAstsdAPGVCLGT 443
Cdd:pfam13508 1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRL----------AVHPEYRGQGIGRALLEAAEAAAK----EGGIKLLE 66
|
90
....*....|....*...
gi 1839392051 444 SIYNKRAQKFYKHHGFRR 461
Cdd:pfam13508 67 LETTNRAAAFYEKLGFEE 84
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
367-459 |
4.82e-06 |
|
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
Pssm-ID: 395465 [Multi-domain] Cd Length: 116 Bit Score: 45.59 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 367 RYWVAELGGELVGYTYAKVGLGESEVdqagivagdAYLSKCYVREALHSTGLSGALLEvAVRDLASTSDAPGVCLGTSIY 446
Cdd:pfam00583 34 GFFVAEEDGELVGFASLSIIDDEPPV---------GEIEGLAVAPEYRGKGIGTALLQ-ALLEWARERGCERIFLEVAAD 103
|
90
....*....|...
gi 1839392051 447 NKRAQKFYKHHGF 459
Cdd:pfam00583 104 NLAAIALYEKLGF 116
|
|
| Acetyltransf_10 |
pfam13673 |
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ... |
341-463 |
8.55e-06 |
|
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
Pssm-ID: 463953 [Multi-domain] Cd Length: 128 Bit Score: 44.95 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 341 DAIAQFVavEFDTTAVKARLNTPQENRYWVAELGGELVGYTyakvglgesEVDQAGivagdaYLSKCYVREALHSTGLSG 420
Cdd:pfam13673 8 EGIETFY--EFISPEALRERIDQGEYFFFVAFEGGQIVGVI---------ALRDRG------HISLLFVDPDYQGQGIGK 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1839392051 421 ALLEvAVRDLASTsDAPGVCLGT---SIYnkrAQKFYKHHGFRRIG 463
Cdd:pfam13673 71 ALLE-AVEDYAEK-DGIKLSELTvnaSPY---AVPFYEKLGFRATG 111
|
|
| COG3393 |
COG3393 |
Predicted acetyltransferase, GNAT family [General function prediction only]; |
399-469 |
2.67e-05 |
|
Predicted acetyltransferase, GNAT family [General function prediction only];
Pssm-ID: 442620 [Multi-domain] Cd Length: 86 Bit Score: 42.59 E-value: 2.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1839392051 399 AGDAYLSKCYVREALHSTGLSGALLEVAVRDLAStSDAPGVCLGTSIYNKRAQKFYKHHGFRRIGKRTFTV 469
Cdd:COG3393 13 PGVAEISGVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRPVGEYATVL 82
|
|
| rimI |
TIGR01575 |
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ... |
366-465 |
4.35e-05 |
|
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273701 [Multi-domain] Cd Length: 131 Bit Score: 43.09 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839392051 366 NRYWVAELGGELVGYTYAKVGLGESEVDQAGivagdaylskcyVREALHSTGLSGALLEVAVRDLAStSDAPGVCLGTSI 445
Cdd:TIGR01575 31 LCYLLARIGGKVVGYAGVQIVLDEAHILNIA------------VKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRV 97
|
90 100
....*....|....*....|
gi 1839392051 446 YNKRAQKFYKHHGFRRIGKR 465
Cdd:TIGR01575 98 SNIAAQALYKKLGFNEIAIR 117
|
|
| |
