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Conserved domains on  [gi|1033015322|ref|NP_001314862|]
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tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial [Danio rerio]

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 ...
 155-448 1.76e-64

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: 208.09  E-value: 1.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 155 RKMFELKERQKLYSNWGSVAHDDMEGRPAGSVIRTSKGIPFVIRRVSLEEFVLFMKRGPAIAYPKDASAMLTMMDVTEGD 234
Cdd:COG2519    14 KYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDAGYIIARLDIFPGA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 235 CVLECGSGSGGMSLFLSRAVGYKGSVLSVEIREDHHKRSVLNYQRWLNtwrrrggqewPDNVHFHHGDIISAgtlLAGRG 314
Cdd:COG2519    94 RVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGL----------PDNVELKLGDIREG---IDEGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 315 LNSVALDMINPHLALPVVVPYLHPGSVCAVYQANITQVIDLLEALRcsALPLVCECITEVQHRDWLVVPslkkdgtfnkr 394
Cdd:COG2519   161 VDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALR--ESGFTDIEAVETLLREWKVEG----------- 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1033015322 395 kapyengdqdepslkteevlnsqDAVpfgdvqyiaRPHPEQVGHTAFLVKLRKI 448
Cdd:COG2519   228 -----------------------LAV---------RPEHRMVGHTGFLVFARKL 249
 
Name Accession Description Interval E-value
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 155-448 1.76e-64

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: 208.09  E-value: 1.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 155 RKMFELKERQKLYSNWGSVAHDDMEGRPAGSVIRTSKGIPFVIRRVSLEEFVLFMKRGPAIAYPKDASAMLTMMDVTEGD 234
Cdd:COG2519    14 KYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDAGYIIARLDIFPGA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 235 CVLECGSGSGGMSLFLSRAVGYKGSVLSVEIREDHHKRSVLNYQRWLNtwrrrggqewPDNVHFHHGDIISAgtlLAGRG 314
Cdd:COG2519    94 RVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGL----------PDNVELKLGDIREG---IDEGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 315 LNSVALDMINPHLALPVVVPYLHPGSVCAVYQANITQVIDLLEALRcsALPLVCECITEVQHRDWLVVPslkkdgtfnkr 394
Cdd:COG2519   161 VDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALR--ESGFTDIEAVETLLREWKVEG----------- 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1033015322 395 kapyengdqdepslkteevlnsqDAVpfgdvqyiaRPHPEQVGHTAFLVKLRKI 448
Cdd:COG2519   228 -----------------------LAV---------RPEHRMVGHTGFLVFARKL 249
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 215-442 1.74e-14

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: 72.91  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 215 IAYPKDASAMLTMMDVTEGDCVLECGSGSGGMSLFLSRAVGYKGSVLSVEIredHHKRsvlnYQRWLNTWRRRGGQEWpd 294
Cdd:pfam08704  23 ILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEF---HEQR----ADKAREEFREHGIDQL-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 295 nVHFHHGDIISAGTLLAGRGL-NSVALDMINPHLALPVVVPYL-HPGSVCAVYQANITQVIDLLEALRCSALplvCECIT 372
Cdd:pfam08704  94 -VTVTHRDVCKEGFLTEVSGKaDAVFLDLPSPWEAVPHAWKALkVEGGRFCSFSPCIEQVQRTCQALAELGF---TEIST 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 373 -EVQHRdwlvvpslkkdgTFNKRKAPYENGDQDEPSLKTEEV-----LNSQDAVPFGD----VQYIARPHPEQVGHTAFL 442
Cdd:pfam08704 170 lEVLLR------------VYDVRTVSLPVIDLGIDREKENERtrtegLSNDDKSEDNSgnsmLGTALKPMSEAVGHTGYL 237
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 236-303 9.04e-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: 38.57  E-value: 9.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033015322 236 VLECGSGSGGMSLFLsrAVGYKGSVLSVEIREDHhkrsvlnyqrwLNTWRRRGGQEWPDNVHFHHGDI 303
Cdd:cd02440     2 VLDLGCGTGALALAL--ASGPGARVTGVDISPVA-----------LELARKAAAALLADNVEVLKGDA 56
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 197-264 7.23e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 37.69  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 197 IRRVSLEEFV-LFMKRGPAIAYPKD--------ASAMLTMM----DVTEGDCVLECGSGSGGMSLFLSRAVGYKGSVLSV 263
Cdd:PRK13942   28 LLKVPRHLFVpEYLEEYAYVDTPLEigygqtisAIHMVAIMcellDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTI 107


                  .
gi 1033015322 264 E 264
Cdd:PRK13942  108 E 108
rADc smart00650
Ribosomal RNA adenine dimethylases;
229-303 9.18e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 9.18e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033015322  229 DVTEGDCVLECGSGSGGMSLFLSRAVgykGSVLSVEIreDhhkrsvlnyQRWLNTWRRRGgqEWPDNVHFHHGDI 303
Cdd:smart00650  10 NLRPGDTVLEIGPGKGALTEELLERA---KRVTAIEI--D---------PRLAPRLREKF--AAADNLTVIHGDA 68
 
Name Accession Description Interval E-value
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 155-448 1.76e-64

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: 208.09  E-value: 1.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 155 RKMFELKERQKLYSNWGSVAHDDMEGRPAGSVIRTSKGIPFVIRRVSLEEFVLFMKRGPAIAYPKDASAMLTMMDVTEGD 234
Cdd:COG2519    14 KYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDAGYIIARLDIFPGA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 235 CVLECGSGSGGMSLFLSRAVGYKGSVLSVEIREDHHKRSVLNYQRWLNtwrrrggqewPDNVHFHHGDIISAgtlLAGRG 314
Cdd:COG2519    94 RVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGL----------PDNVELKLGDIREG---IDEGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 315 LNSVALDMINPHLALPVVVPYLHPGSVCAVYQANITQVIDLLEALRcsALPLVCECITEVQHRDWLVVPslkkdgtfnkr 394
Cdd:COG2519   161 VDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALR--ESGFTDIEAVETLLREWKVEG----------- 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1033015322 395 kapyengdqdepslkteevlnsqDAVpfgdvqyiaRPHPEQVGHTAFLVKLRKI 448
Cdd:COG2519   228 -----------------------LAV---------RPEHRMVGHTGFLVFARKL 249
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 215-442 1.74e-14

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: 72.91  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 215 IAYPKDASAMLTMMDVTEGDCVLECGSGSGGMSLFLSRAVGYKGSVLSVEIredHHKRsvlnYQRWLNTWRRRGGQEWpd 294
Cdd:pfam08704  23 ILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEF---HEQR----ADKAREEFREHGIDQL-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 295 nVHFHHGDIISAGTLLAGRGL-NSVALDMINPHLALPVVVPYL-HPGSVCAVYQANITQVIDLLEALRCSALplvCECIT 372
Cdd:pfam08704  94 -VTVTHRDVCKEGFLTEVSGKaDAVFLDLPSPWEAVPHAWKALkVEGGRFCSFSPCIEQVQRTCQALAELGF---TEIST 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 373 -EVQHRdwlvvpslkkdgTFNKRKAPYENGDQDEPSLKTEEV-----LNSQDAVPFGD----VQYIARPHPEQVGHTAFL 442
Cdd:pfam08704 170 lEVLLR------------VYDVRTVSLPVIDLGIDREKENERtrtegLSNDDKSEDNSgnsmLGTALKPMSEAVGHTGYL 237
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
206-302 4.84e-07

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 50.06  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 206 VLFMKRGPAIAYPKDASAMLTMMDVTEGDCVLECGSGSGGMSLFLSRAVGYKGSVLSVEIREDHHKRSVLNYqrwlntwR 285
Cdd:pfam01135  47 PLSIGYGQTISAPHMHAMMLELLELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNL-------E 119

                          90
                  ....*....|....*..
gi 1033015322 286 RRGgqewPDNVHFHHGD 302
Cdd:pfam01135 120 KLG----LENVIVVVGD 132
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 224-302 2.17e-04

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 42.00  E-value: 2.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033015322 224 MLTMMDVTEGDCVLECGSGSGGMSLFLSRAVgykGSVLSVEIREDHHKRSVLNyqrwlntWRRRGgqewPDNVHFHHGD 302
Cdd:COG2518    58 MLEALDLKPGDRVLEIGTGSGYQAAVLARLA---GRVYSVERDPELAERARER-------LAALG----YDNVTVRVGD 122
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 236-344 2.61e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 41.25  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 236 VLECGSGSGGMSLFLSRAVGYKGSVLSVEIREDHHKRSvlnyqrwlntwRRRGGQEWPDNVHFHHGDIISAGTLLAGRG- 314
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKA-----------RENAQKLGFDNVEFEQGDIEELPELLEDDKf 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1033015322 315 ----LNSVALDMINPHLALPVVVPYLHPGSVCAV 344
Cdd:pfam13847  76 dvviSNCVLNHIPDPDKVLQEILRVLKPGGRLII 109
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 224-303 5.74e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 40.30  E-value: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 224 MLTMMDVTEGDCVLECGSGSGGMSLFLSRAVGYKgsVLSVEIREDHHKRSvlnyQRWLntwRRRGGQewpDNVHFHHGDI 303
Cdd:COG2230    43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVR--VTGVTLSPEQLEYA----RERA---AEAGLA---DRVEVRLADY 110
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 236-341 6.37e-04

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: 40.55  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 236 VLECGSGSGGMSLFLSRAVGYKGSVLSVEIREDHHKRSVLNyqrwlntWRRRGgqeWPDNVHFHHGDiisAGTLLagRGL 315
Cdd:COG4122    20 ILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIAREN-------FARAG---LADRIRLILGD---ALEVL--PRL 84

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1033015322 316 NSVALDMI--------NPHlALPVVVPYLHPGSV 341
Cdd:COG4122    85 ADGPFDLVfidadksnYPD-YLELALPLLRPGGL 117
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 236-303 9.04e-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: 38.57  E-value: 9.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033015322 236 VLECGSGSGGMSLFLsrAVGYKGSVLSVEIREDHhkrsvlnyqrwLNTWRRRGGQEWPDNVHFHHGDI 303
Cdd:cd02440     2 VLDLGCGTGALALAL--ASGPGARVTGVDISPVA-----------LELARKAAAALLADNVEVLKGDA 56
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 236-303 1.71e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.54  E-value: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033015322 236 VLECGSGSGGMSLFLSRAVGYKgsVLSVEIREDHHKRSvlnyqrwlntwRRRGGQEWPdNVHFHHGDI 303
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR--VTGVDLSPEMLERA-----------RERAAEAGL-NVEFVQGDA 54
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 223-303 2.57e-03

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: 38.05  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 223 AMLTMMDVTEGDCVLECGSGSGGMSLFLSRAVgykGSVLSVEIREDHHKRSvlnyqrwlntwRRRgGQEWPDNVHFHHGD 302
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAERG---ARVTGVDISPEMLELA-----------RER-AAEAGLNVEFVVGD 77


                  .
gi 1033015322 303 I 303
Cdd:COG2226    78 A 78
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 197-264 7.23e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 37.69  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 197 IRRVSLEEFV-LFMKRGPAIAYPKD--------ASAMLTMM----DVTEGDCVLECGSGSGGMSLFLSRAVGYKGSVLSV 263
Cdd:PRK13942   28 LLKVPRHLFVpEYLEEYAYVDTPLEigygqtisAIHMVAIMcellDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTI 107


                  .
gi 1033015322 264 E 264
Cdd:PRK13942  108 E 108
arsM PRK11873
arsenite methyltransferase;
216-303 8.79e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 38.01  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015322 216 AYPKDASAML------TMMDVTEGDCVLECGSGsGGMSLFLS-RAVGYKGSVLSVEIREDHHKRSVLNyqrwlntwRRRG 288
Cdd:PRK11873   55 AVPEGANLGLgcgnptALAELKPGETVLDLGSG-GGFDCFLAaRRVGPTGKVIGVDMTPEMLAKARAN--------ARKA 125

                          90
                  ....*....|....*
gi 1033015322 289 GQEwpdNVHFHHGDI 303
Cdd:PRK11873  126 GYT---NVEFRLGEI 137
rADc smart00650
Ribosomal RNA adenine dimethylases;
229-303 9.18e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 9.18e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033015322  229 DVTEGDCVLECGSGSGGMSLFLSRAVgykGSVLSVEIreDhhkrsvlnyQRWLNTWRRRGgqEWPDNVHFHHGDI 303
Cdd:smart00650  10 NLRPGDTVLEIGPGKGALTEELLERA---KRVTAIEI--D---------PRLAPRLREKF--AAADNLTVIHGDA 68
 
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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