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Conserved domains on  [gi|27229019|ref|NP_080149|]
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tRNA dimethylallyltransferase precursor [Mus musculus]

Protein Classification

tRNA (adenosine(37)-N6)-dimethylallyltransferase MiaA; tRNA (adenosine(37)-N6)-dimethylallyltransferase MiaA; tRNA dimethylallyltransferase; tRNA dimethylallyltransferase( domain architecture ID 10001084)

tRNA (adenosine(37)-N6)-dimethylallyltransferase MiaA catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); tRNA (adenosine(37)-N6)-dimethylallyltransferase MiaA catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); tRNA dimethylallyltransferase catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); tRNA dimethylallyltransferase catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
 24-373 6.20e-92

tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; tRNA A37 N6-isopentenylltransferase MiaA is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440093  Cd Length: 306  Bit Score: 281.18  E-value: 6.20e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLvTSYTVVDFRNKAT 103
Cdd:COG0324   3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlittkpQEMGTGKVVDRKV------ELEKEDGHELHKRLSQVDPEMAAKL 177
Cdd:COG0324  82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 178 HPHDKRKVARSLQVFEETGISHSEFLHRQHAeegggplggpLRFPNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELR 257
Cdd:COG0324 153 HPNDPQRIIRALEVYELTGKPLSELQKEKKE----------PPPYDVLKIGLDPDREELYERINRRVDQMLEAGLLDEVR 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 258 GFHRRynlkNISENSQdyqhgIFQSIGFKEFHEYLttEGKCTPETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrp 337
Cdd:COG0324 223 ALLAR----GLDPDLP-----AMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD----- 279

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 27229019 338 gpsvPPVYGLEVSDVSKWEEsvlepALNIVQSFIQG 373
Cdd:COG0324 280 ----PDIHWLDPDEPDLLEE-----ILELIKAFLEE 306
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 395-419 1.42e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


:

Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 35.99  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|....*
gi 27229019   395 HMCDLCDRIIIGDREWAAHLKSKSH 419
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKH 26
 
Name Accession Description Interval E-value
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
 24-373 6.20e-92

tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; tRNA A37 N6-isopentenylltransferase MiaA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440093  Cd Length: 306  Bit Score: 281.18  E-value: 6.20e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLvTSYTVVDFRNKAT 103
Cdd:COG0324   3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlittkpQEMGTGKVVDRKV------ELEKEDGHELHKRLSQVDPEMAAKL 177
Cdd:COG0324  82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 178 HPHDKRKVARSLQVFEETGISHSEFLHRQHAeegggplggpLRFPNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELR 257
Cdd:COG0324 153 HPNDPQRIIRALEVYELTGKPLSELQKEKKE----------PPPYDVLKIGLDPDREELYERINRRVDQMLEAGLLDEVR 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 258 GFHRRynlkNISENSQdyqhgIFQSIGFKEFHEYLttEGKCTPETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrp 337
Cdd:COG0324 223 ALLAR----GLDPDLP-----AMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD----- 279

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 27229019 338 gpsvPPVYGLEVSDVSKWEEsvlepALNIVQSFIQG 373
Cdd:COG0324 280 ----PDIHWLDPDEPDLLEE-----ILELIKAFLEE 306
IPPT pfam01715
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ...
 58-332 2.48e-86

IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2)-isopentenylpyrophosphate transferase. These enzymes modify both cytoplasmic and mitochondrial tRNAs at A(37) to give isopentenyl A(37).


Pssm-ID: 460304  Cd Length: 242  Bit Score: 264.29  E-value: 2.48e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019    58 QVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVTsYTVVDFRNKATALIEDIFARDKIPIVVGGTNYYIESLL--WKVLI 135
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEE-YSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALLdgLDDFP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   136 TTKPQemgtgkvVDRKVE--LEKEDGHELHKRLSQVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHAeeggg 213
Cdd:pfam01715  80 PADPE-------LRAELEaeAAEEGLEALHAELAEVDPEAAARIHPNDRRRIIRALEVYELTGKPLSEFQEPEKP----- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   214 plggpLRFPNPCILWLhADQAVLDERLDKRVDDMLAAGLLEELRGFHRRYnlknisensQDYQHGIFQSIGFKEFHEYLt 293
Cdd:pfam01715 148 -----PPPYDTLIIGL-SDREELYERINARVDAMLEAGLLEEVRALLDRG---------YGGDLPAMQAIGYKELLAYL- 211

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 27229019   294 tEGKCTpetsnqlLKKGIEALKQVTKRYARKQNRWVKNR 332
Cdd:pfam01715 212 -DGEIS-------LEEAIELIKRATRQYAKRQLTWFRRD 242
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
 25-333 6.06e-79

tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate transferase, IPP transferase, 2-methylthio-N6-isopentyladenosine tRNA modification enzyme. Catalyzes the first step in the modification of an adenosine near the anticodon to 2-methylthio-N6-isopentyladenosine. Understanding of substrate specificity has changed. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 213512  Cd Length: 287  Bit Score: 247.30  E-value: 6.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019    25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPlVTSYTVVDFRNKATA 104
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDP-SESYSAADFQTQALN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   105 LIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEMGTGKVvdrKVELEKEDGHELHKRLSQVDPEMAAKLHPHDKRK 184
Cdd:TIGR00174  80 AIADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQL---EILAEEQGWDFLYNELKKVDPVAAAKIHPNDTRR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   185 VARSLQVFEETGISHSEFLHRQhaeegggplgGPLRFPNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRGFHRRYN 264
Cdd:TIGR00174 157 VQRALEVFYATGKPPSELFKEQ----------KIELFYDIVQIGLASSREPLHQRIEQRVHDMLESGLLAEVKALYAQYD 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229019   265 LKNIsensqdyqhGIFQSIGFKEFHEYLttEGKCTpetsnqlLKKGIEALKQVTKRYARKQNRWVKNRF 333
Cdd:TIGR00174 227 LCDL---------PSIQAIGYKEFLLYL--EGTVS-------LEDAIERIKCNTRQYAKRQLTWFRKWS 277
PLN02748 PLN02748
tRNA dimethylallyltransferase
 17-419 8.89e-72

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 234.39  E-value: 8.89e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   17 RGLRRtlpLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVtSYTVV 96
Cdd:PLN02748  19 KGKAK---VVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSV-EFTAK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   97 DFRNKATALIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEM-----GTGKVVDRKV----ELEKEDGHELHKRLS 167
Cdd:PLN02748  95 DFRDHAVPLIEEILSRNGLPVIVGGTNYYIQALVSPFLLDDMAEETedctfVVASVLDEHMdvesGLGNDDEDHGYELLK 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  168 QVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHAeeGGGPLGGPLRFpNPCILWLHADQAVLDERLDKRVDDM 247
Cdd:PLN02748 175 ELDPVAANRIHPNNHRKINRYLELYATTGVLPSKLYQGKAA--ENWGRISNSRF-DCCFICVDADTAVLDRYVNQRVDCM 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  248 LAAGLLEElrgfhrrynLKNISENSQDYQHGIFQSIGFKEFHEYL------TTEGKCTPETSNQ---------------- 305
Cdd:PLN02748 252 IDAGLLDE---------VYDIYDPGADYTRGLRQAIGVREFEDFLrlylsrNENGELTSSSNNDkvmkensrkilnfphd 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  306 -----LLKKGIEALKQVTKRYARKQNRWVkNRFLSRPGPSVPPV----YGLEVSDVSkWEESVLEPALNIVQSFIQGHKP 376
Cdd:PLN02748 323 dklkiLLDEAIDQVKLNTRRLVRRQKRRL-HRLNTVFGWNIHYIdateAILCKSEES-WNAKVVKPAVEIVRRFLSDDTS 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 27229019  377 TAMPVKMAYNESENKRSYHMCDLCD-RIIIGDREWAAHLKSKSH 419
Cdd:PLN02748 401 SGPDASSGKSVSRELWTQYVCEACGnKVLRGAHEWEQHKQGRGH 444
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 25-91 1.12e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 37.32  E-value: 1.12e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229019  25 LVVILGATGTGKSTLALQLGQRLGGEIVSA-DSMQVYEGLDIITNKVSAQEQKmcQHHMISFVDPLVT 91
Cdd:cd02019   1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVlDEIVILEGLYASYKSRDARIRD--LADLKIYLDADLV 66
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 395-419 1.42e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 35.99  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|....*
gi 27229019   395 HMCDLCDRIIIGDREWAAHLKSKSH 419
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKH 26
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 395-426 2.61e-03

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 35.31  E-value: 2.61e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 27229019    395 HMCDLCDRIIIGDREWAAHLKSKSHLHQLKKR 426
Cdd:smart00451   4 FYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
 
Name Accession Description Interval E-value
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
 24-373 6.20e-92

tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; tRNA A37 N6-isopentenylltransferase MiaA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440093  Cd Length: 306  Bit Score: 281.18  E-value: 6.20e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLvTSYTVVDFRNKAT 103
Cdd:COG0324   3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlittkpQEMGTGKVVDRKV------ELEKEDGHELHKRLSQVDPEMAAKL 177
Cdd:COG0324  82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 178 HPHDKRKVARSLQVFEETGISHSEFLHRQHAeegggplggpLRFPNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELR 257
Cdd:COG0324 153 HPNDPQRIIRALEVYELTGKPLSELQKEKKE----------PPPYDVLKIGLDPDREELYERINRRVDQMLEAGLLDEVR 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019 258 GFHRRynlkNISENSQdyqhgIFQSIGFKEFHEYLttEGKCTPETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrp 337
Cdd:COG0324 223 ALLAR----GLDPDLP-----AMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD----- 279

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 27229019 338 gpsvPPVYGLEVSDVSKWEEsvlepALNIVQSFIQG 373
Cdd:COG0324 280 ----PDIHWLDPDEPDLLEE-----ILELIKAFLEE 306
IPPT pfam01715
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ...
 58-332 2.48e-86

IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2)-isopentenylpyrophosphate transferase. These enzymes modify both cytoplasmic and mitochondrial tRNAs at A(37) to give isopentenyl A(37).


Pssm-ID: 460304  Cd Length: 242  Bit Score: 264.29  E-value: 2.48e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019    58 QVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVTsYTVVDFRNKATALIEDIFARDKIPIVVGGTNYYIESLL--WKVLI 135
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEE-YSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALLdgLDDFP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   136 TTKPQemgtgkvVDRKVE--LEKEDGHELHKRLSQVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHAeeggg 213
Cdd:pfam01715  80 PADPE-------LRAELEaeAAEEGLEALHAELAEVDPEAAARIHPNDRRRIIRALEVYELTGKPLSEFQEPEKP----- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   214 plggpLRFPNPCILWLhADQAVLDERLDKRVDDMLAAGLLEELRGFHRRYnlknisensQDYQHGIFQSIGFKEFHEYLt 293
Cdd:pfam01715 148 -----PPPYDTLIIGL-SDREELYERINARVDAMLEAGLLEEVRALLDRG---------YGGDLPAMQAIGYKELLAYL- 211

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 27229019   294 tEGKCTpetsnqlLKKGIEALKQVTKRYARKQNRWVKNR 332
Cdd:pfam01715 212 -DGEIS-------LEEAIELIKRATRQYAKRQLTWFRRD 242
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
 25-333 6.06e-79

tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate transferase, IPP transferase, 2-methylthio-N6-isopentyladenosine tRNA modification enzyme. Catalyzes the first step in the modification of an adenosine near the anticodon to 2-methylthio-N6-isopentyladenosine. Understanding of substrate specificity has changed. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 213512  Cd Length: 287  Bit Score: 247.30  E-value: 6.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019    25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPlVTSYTVVDFRNKATA 104
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDP-SESYSAADFQTQALN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   105 LIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEMGTGKVvdrKVELEKEDGHELHKRLSQVDPEMAAKLHPHDKRK 184
Cdd:TIGR00174  80 AIADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQL---EILAEEQGWDFLYNELKKVDPVAAAKIHPNDTRR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   185 VARSLQVFEETGISHSEFLHRQhaeegggplgGPLRFPNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRGFHRRYN 264
Cdd:TIGR00174 157 VQRALEVFYATGKPPSELFKEQ----------KIELFYDIVQIGLASSREPLHQRIEQRVHDMLESGLLAEVKALYAQYD 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229019   265 LKNIsensqdyqhGIFQSIGFKEFHEYLttEGKCTpetsnqlLKKGIEALKQVTKRYARKQNRWVKNRF 333
Cdd:TIGR00174 227 LCDL---------PSIQAIGYKEFLLYL--EGTVS-------LEDAIERIKCNTRQYAKRQLTWFRKWS 277
PLN02748 PLN02748
tRNA dimethylallyltransferase
 17-419 8.89e-72

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 234.39  E-value: 8.89e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   17 RGLRRtlpLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVtSYTVV 96
Cdd:PLN02748  19 KGKAK---VVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSV-EFTAK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   97 DFRNKATALIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEM-----GTGKVVDRKV----ELEKEDGHELHKRLS 167
Cdd:PLN02748  95 DFRDHAVPLIEEILSRNGLPVIVGGTNYYIQALVSPFLLDDMAEETedctfVVASVLDEHMdvesGLGNDDEDHGYELLK 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  168 QVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHAeeGGGPLGGPLRFpNPCILWLHADQAVLDERLDKRVDDM 247
Cdd:PLN02748 175 ELDPVAANRIHPNNHRKINRYLELYATTGVLPSKLYQGKAA--ENWGRISNSRF-DCCFICVDADTAVLDRYVNQRVDCM 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  248 LAAGLLEElrgfhrrynLKNISENSQDYQHGIFQSIGFKEFHEYL------TTEGKCTPETSNQ---------------- 305
Cdd:PLN02748 252 IDAGLLDE---------VYDIYDPGADYTRGLRQAIGVREFEDFLrlylsrNENGELTSSSNNDkvmkensrkilnfphd 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  306 -----LLKKGIEALKQVTKRYARKQNRWVkNRFLSRPGPSVPPV----YGLEVSDVSkWEESVLEPALNIVQSFIQGHKP 376
Cdd:PLN02748 323 dklkiLLDEAIDQVKLNTRRLVRRQKRRL-HRLNTVFGWNIHYIdateAILCKSEES-WNAKVVKPAVEIVRRFLSDDTS 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 27229019  377 TAMPVKMAYNESENKRSYHMCDLCD-RIIIGDREWAAHLKSKSH 419
Cdd:PLN02748 401 SGPDASSGKSVSRELWTQYVCEACGnKVLRGAHEWEQHKQGRGH 444
PLN02165 PLN02165
adenylate isopentenyltransferase
 25-371 6.43e-43

adenylate isopentenyltransferase


Pssm-ID: 177823  Cd Length: 334  Bit Score: 154.60  E-value: 6.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVTSYTVVDFRNKATA 104
Cdd:PLN02165  45 VVVIMGATGSGKSRLSVDLATRFPSEIINSDKMQVYDGLKITTNQITIQDRRGVPHHLLGELNPDDGELTASEFRSLASL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  105 LIEDIFARDKIPIVVGGTNYYIESLLwkvlittkpqemgtgkvVDRkvelekedghelhkrlsqVDPEmaakLHPHDKRK 184
Cdd:PLN02165 125 SISEITSRQKLPIVAGGSNSFIHALL-----------------ADR------------------FDPE----IYPFSSGS 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  185 VARSLQVfeetgishseflhrqhaeegggplggplRFpNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRGFHRryn 264
Cdd:PLN02165 166 SLISSDL----------------------------RY-DCCFIWVDVSEPVLFEYLSKRVDEMMDSGMFEELAEFYD--- 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  265 lkniSENSQDYQHGIFQSIGFKEFHEYLTtegKCTPETS----NQLLK----KGIEALKQVTKRYARKQNR--------- 327
Cdd:PLN02165 214 ----PVKSGSEPLGIRKAIGVPEFDRYFK---KYPPENKmgkwDQARKaayeEAVREIKENTCQLAKRQIEkimklksag 286

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 27229019  328 WVKNRFLSRPG-PSVPPVYGLEVSDVSKWEESVLEPALNIVQSFI 371
Cdd:PLN02165 287 WDIKRVDATASfRAVMRKKGKKKKWREIWEKDVLEPSVKIVKRFL 331
PLN02840 PLN02840
tRNA dimethylallyltransferase
 25-331 3.86e-34

tRNA dimethylallyltransferase


Pssm-ID: 215451  Cd Length: 421  Bit Score: 132.63  E-value: 3.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019   25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPlVTSYTVVDFRNKATA 104
Cdd:PLN02840  23 VIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSLSERKEVPHHLIDILHP-SDDYSVGAFFDDARR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  105 LIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEMGTGKVVDRKVELEKE-DGHELHKRLSQVDPEMAAKLHPHDKR 183
Cdd:PLN02840 102 ATQDILNRGRVPIVAGGTGLYLRWYIYGKPDVPKSSPEITSEVWSELVDFQKNgDWDAAVELVVNAGDPKARSLPRNDWY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  184 KVARSLQVFEETGISHSEF------LHRQHAEEGGGPLGGPLRFPNP-------CIlWLHADQAVLDERLDKRVDDMLAA 250
Cdd:PLN02840 182 RLRRSLEIIKSSGSPPSAFslpydsFREQLVTEDTDSSLEDGSSAETeldydflCF-FLSSPRLDLYRSIDLRCEEMLAG 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229019  251 --GLLEELRGFHRRYNLKNISENSqdyqhgifQSIGFKEFHEYLTT----EGKCTPETSNQLLKKgieaLKQVTKRYARK 324
Cdd:PLN02840 261 tnGILSEASWLLDLGLLPNSNSAT--------RAIGYRQAMEYLLQcrqnGGESSPQEFLAFLSK----FQTASRNFAKR 328


                 ....*..
gi 27229019  325 QNRWVKN 331
Cdd:PLN02840 329 QMTWFRN 335
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
25-55 1.72e-04

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 42.21  E-value: 1.72e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 27229019  25 LVVILGATGTGKSTLALQLGQRLGGEIVSAD 55
Cdd:COG0645   1 LILVCGLPGSGKSTLARALAERLGAVRLRSD 31
PRK06547 PRK06547
hypothetical protein; Provisional
 17-64 8.64e-04

hypothetical protein; Provisional


Pssm-ID: 235825  Cd Length: 172  Bit Score: 40.11  E-value: 8.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 27229019   17 RGLRRTLPLVVILGATGTGKSTLALQLGQRLGGEIVSADsmQVYEGLD 64
Cdd:PRK06547   9 RLCGGGMITVLIDGRSGSGKTTLAGALAARTGFQLVHLD--DLYPGWH 54
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 25-91 1.12e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 37.32  E-value: 1.12e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229019  25 LVVILGATGTGKSTLALQLGQRLGGEIVSA-DSMQVYEGLDIITNKVSAQEQKmcQHHMISFVDPLVT 91
Cdd:cd02019   1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVlDEIVILEGLYASYKSRDARIRD--LADLKIYLDADLV 66
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 395-419 1.42e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 35.99  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|....*
gi 27229019   395 HMCDLCDRIIIGDREWAAHLKSKSH 419
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKH 26
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 25-57 1.93e-03

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 38.44  E-value: 1.93e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 27229019    25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSM 57
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAVRLSSDDE 33
PRK12337 PRK12337
2-phosphoglycerate kinase; Provisional
 17-58 1.94e-03

2-phosphoglycerate kinase; Provisional


Pssm-ID: 183452 [Multi-domain]  Cd Length: 475  Bit Score: 40.53  E-value: 1.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 27229019   17 RGLRRTL-PLVVILG-ATGTGKSTLALQLGQRLG-GEIVSADSMQ 58
Cdd:PRK12337 247 RSIRRPPrPLHVLIGgVSGVGKSVLASALAYRLGiTRIVSTDAVR 291
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 20-52 2.51e-03

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 38.65  E-value: 2.51e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 27229019  20 RRTLPL-VVILGATGTGKSTLALQLGQRLGGEIV 52
Cdd:COG3172   4 RPSFVKkIVLLGAESTGKTTLARALAAHYNTPWV 37
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 395-426 2.61e-03

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 35.31  E-value: 2.61e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 27229019    395 HMCDLCDRIIIGDREWAAHLKSKSHLHQLKKR 426
Cdd:smart00451   4 FYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 25-57 4.28e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 37.62  E-value: 4.28e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 27229019  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSM 57
Cdd:cd02021   1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDL 33
PRK04220 PRK04220
2-phosphoglycerate kinase; Provisional
 19-48 5.13e-03

2-phosphoglycerate kinase; Provisional


Pssm-ID: 179793 [Multi-domain]  Cd Length: 301  Bit Score: 38.79  E-value: 5.13e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 27229019   19 LRRTLPLVVILG-ATGTGKSTLALQLGQRLG 48
Cdd:PRK04220  87 RKSKEPIIILIGgASGVGTSTIAFELASRLG 117
IPT pfam01745
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes ...
 28-60 5.14e-03

Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes isopentenyladensosine 5'-monophosphate, a cytokinin that induces shoot formation on host plants infected with the Ti plasmid.


Pssm-ID: 366786  Cd Length: 232  Bit Score: 38.53  E-value: 5.14e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 27229019    28 ILGATGTGKSTLALQLGQRLGGEIVSADSMQVY 60
Cdd:pfam01745   6 IWGATCTGKTAEAIALAKETGWPVIVLDRVQCC 38
PRK08118 PRK08118
DNA topology modulation protein;
26-48 5.61e-03

DNA topology modulation protein;


Pssm-ID: 181235  Cd Length: 167  Bit Score: 37.67  E-value: 5.61e-03
                         10        20
                 ....*....|....*....|...
gi 27229019   26 VVILGATGTGKSTLALQLGQRLG 48
Cdd:PRK08118   4 IILIGSGGSGKSTLARQLGEKLN 26
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 24-55 5.66e-03

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 37.42  E-value: 5.66e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 27229019  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSAD 55
Cdd:COG3265   2 MVIVVMGVSGSGKSTVGQALAERLGWPFIDGD 33
AAA_28 pfam13521
AAA domain;
26-52 7.04e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 37.24  E-value: 7.04e-03
                          10        20
                  ....*....|....*....|....*..
gi 27229019    26 VVILGATGTGKSTLALQLGQRLGGEIV 52
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAARFGYPVV 28
Pgk2 COG2074
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ...
 20-56 8.89e-03

2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 441677  Cd Length: 207  Bit Score: 37.62  E-value: 8.89e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27229019  20 RRTLPLVVIL--GATGTGKSTLALQLGQRLG-GEIVSADS 56
Cdd:COG2074   1 RRMKRPRIILigGASGVGKSTIAAELARRLGiPRVISTDS 40
 
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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