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Conserved domains on  [gi|1907156966|ref|XP_036020248|]
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tRNA dimethylallyltransferase isoform X1 [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]; ...
 24-288 9.67e-63

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: 203.37  E-value: 9.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLvTSYTVVDFRNKAT 103
Cdd:COG0324     3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlittkpQEMGTGKVVDRKV------ELEKEDGHELHKRLSQVDPEMAAKL 177
Cdd:COG0324    82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 178 HPHDKRKV---------------ASQD---------------------------------------------YQHGI--- 194
Cdd:COG0324   153 HPNDPQRIiralevyeltgkplsELQKekkepppydvlkigldpdreelyerinrrvdqmleaglldevralLARGLdpd 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 195 ---FQSIGFKEFHEYLttEGKCTPETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrpgpsvPPVYGLEVSDVSKWE 271
Cdd:COG0324   233 lpaMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD---------PDIHWLDPDEPDLLE 294

                         330
                  ....*....|....*..
gi 1907156966 272 EsvlepALNIVQSFIQG 288
Cdd:COG0324   295 E-----ILELIKAFLEE 306
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 310-334 1.01e-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: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 1907156966 310 HMCDLCDRIIIGDREWAAHLKSKSH 334
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKH 26
 
Name Accession Description Interval E-value
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
 24-288 9.67e-63

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: 203.37  E-value: 9.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLvTSYTVVDFRNKAT 103
Cdd:COG0324     3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlittkpQEMGTGKVVDRKV------ELEKEDGHELHKRLSQVDPEMAAKL 177
Cdd:COG0324    82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 178 HPHDKRKV---------------ASQD---------------------------------------------YQHGI--- 194
Cdd:COG0324   153 HPNDPQRIiralevyeltgkplsELQKekkepppydvlkigldpdreelyerinrrvdqmleaglldevralLARGLdpd 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 195 ---FQSIGFKEFHEYLttEGKCTPETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrpgpsvPPVYGLEVSDVSKWE 271
Cdd:COG0324   233 lpaMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD---------PDIHWLDPDEPDLLE 294

                         330
                  ....*....|....*..
gi 1907156966 272 EsvlepALNIVQSFIQG 288
Cdd:COG0324   295 E-----ILELIKAFLEE 306
IPPT pfam01715
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ...
 58-247 1.56e-53

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: 177.23  E-value: 1.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  58 QVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVTsYTVVDFRNKATALIEDIFARDKIPIVVGGTNYYIESLL--WKVLI 135
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEE-YSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALLdgLDDFP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 136 TTKPQemgtgkvVDRKVE--LEKEDGHELHKRLSQVDPEMAAKLHPHDKRKV---------------------------- 185
Cdd:pfam01715  80 PADPE-------LRAELEaeAAEEGLEALHAELAEVDPEAAARIHPNDRRRIiralevyeltgkplsefqepekppppyd 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 186 -------------------------------------ASQDYQHGIFQSIGFKEFHEYLttEGKCTpetsnqlLKKGIEA 228
Cdd:pfam01715 153 tliiglsdreelyerinarvdamleaglleevralldRGYGGDLPAMQAIGYKELLAYL--DGEIS-------LEEAIEL 223

                         250
                  ....*....|....*....
gi 1907156966 229 LKQVTKRYARKQNRWVKNR 247
Cdd:pfam01715 224 IKRATRQYAKRQLTWFRRD 242
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
 25-248 2.79e-51

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: 172.96  E-value: 2.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPlVTSYTVVDFRNKATA 104
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDP-SESYSAADFQTQALN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 105 LIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEMGTGKVvdrKVELEKEDGHELHKRLSQVDPEMAAKLHPHDKRK 184
Cdd:TIGR00174  80 AIADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQL---EILAEEQGWDFLYNELKKVDPVAAAKIHPNDTRR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 185 VA----------------------------------------------------------------SQDYQH--GIFQSI 198
Cdd:TIGR00174 157 VQralevfyatgkppselfkeqkielfydivqiglassreplhqrieqrvhdmlesgllaevkalyAQYDLCdlPSIQAI 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907156966 199 GFKEFHEYLttEGKCTpetsnqlLKKGIEALKQVTKRYARKQNRWVKNRF 248
Cdd:TIGR00174 237 GYKEFLLYL--EGTVS-------LEDAIERIKCNTRQYAKRQLTWFRKWS 277
PLN02748 PLN02748
tRNA dimethylallyltransferase
 17-334 2.30e-49

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 172.76  E-value: 2.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  17 RGLRRtlpLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVtSYTVV 96
Cdd:PLN02748   19 KGKAK---VVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSV-EFTAK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  97 DFRNKATALIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEM-----GTGKVVDRKV----ELEKEDGHELHKRLS 167
Cdd:PLN02748   95 DFRDHAVPLIEEILSRNGLPVIVGGTNYYIQALVSPFLLDDMAEETedctfVVASVLDEHMdvesGLGNDDEDHGYELLK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 168 QVDPEMAAKLHPHDKRKV-------------------------------------------------------------- 185
Cdd:PLN02748  175 ELDPVAANRIHPNNHRKInrylelyattgvlpsklyqgkaaenwgrisnsrfdccficvdadtavldryvnqrvdcmida 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 186 -----------ASQDYQHGIFQSIGFKEFHEYL------TTEGKCTPETSNQ---------------------LLKKGIE 227
Cdd:PLN02748  255 glldevydiydPGADYTRGLRQAIGVREFEDFLrlylsrNENGELTSSSNNDkvmkensrkilnfphddklkiLLDEAID 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 228 ALKQVTKRYARKQNRWVkNRFLSRPGPSVPPV----YGLEVSDVSkWEESVLEPALNIVQSFIQGHKPTAMPVKMAYNES 303
Cdd:PLN02748  335 QVKLNTRRLVRRQKRRL-HRLNTVFGWNIHYIdateAILCKSEES-WNAKVVKPAVEIVRRFLSDDTSSGPDASSGKSVS 412

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1907156966 304 ENKRSYHMCDLCD-RIIIGDREWAAHLKSKSH 334
Cdd:PLN02748  413 RELWTQYVCEACGnKVLRGAHEWEQHKQGRGH 444
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 310-334 1.01e-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: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 1907156966 310 HMCDLCDRIIIGDREWAAHLKSKSH 334
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKH 26
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 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSA-DSMQVYEGLDIITNKVSAQEQKmcQHHMISFVDPLVT 91
Cdd:cd02019     1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVlDEIVILEGLYASYKSRDARIRD--LADLKIYLDADLV 66
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 310-341 1.96e-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: 35.69  E-value: 1.96e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907156966  310 HMCDLCDRIIIGDREWAAHLKSKSHLHQLKKR 341
Cdd:smart00451   4 FYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
 
Name Accession Description Interval E-value
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
 24-288 9.67e-63

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: 203.37  E-value: 9.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLvTSYTVVDFRNKAT 103
Cdd:COG0324     3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlittkpQEMGTGKVVDRKV------ELEKEDGHELHKRLSQVDPEMAAKL 177
Cdd:COG0324    82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 178 HPHDKRKV---------------ASQD---------------------------------------------YQHGI--- 194
Cdd:COG0324   153 HPNDPQRIiralevyeltgkplsELQKekkepppydvlkigldpdreelyerinrrvdqmleaglldevralLARGLdpd 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 195 ---FQSIGFKEFHEYLttEGKCTPETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrpgpsvPPVYGLEVSDVSKWE 271
Cdd:COG0324   233 lpaMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD---------PDIHWLDPDEPDLLE 294

                         330
                  ....*....|....*..
gi 1907156966 272 EsvlepALNIVQSFIQG 288
Cdd:COG0324   295 E-----ILELIKAFLEE 306
IPPT pfam01715
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ...
 58-247 1.56e-53

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: 177.23  E-value: 1.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  58 QVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVTsYTVVDFRNKATALIEDIFARDKIPIVVGGTNYYIESLL--WKVLI 135
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEE-YSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALLdgLDDFP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 136 TTKPQemgtgkvVDRKVE--LEKEDGHELHKRLSQVDPEMAAKLHPHDKRKV---------------------------- 185
Cdd:pfam01715  80 PADPE-------LRAELEaeAAEEGLEALHAELAEVDPEAAARIHPNDRRRIiralevyeltgkplsefqepekppppyd 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 186 -------------------------------------ASQDYQHGIFQSIGFKEFHEYLttEGKCTpetsnqlLKKGIEA 228
Cdd:pfam01715 153 tliiglsdreelyerinarvdamleaglleevralldRGYGGDLPAMQAIGYKELLAYL--DGEIS-------LEEAIEL 223

                         250
                  ....*....|....*....
gi 1907156966 229 LKQVTKRYARKQNRWVKNR 247
Cdd:pfam01715 224 IKRATRQYAKRQLTWFRRD 242
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
 25-248 2.79e-51

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: 172.96  E-value: 2.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPlVTSYTVVDFRNKATA 104
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDP-SESYSAADFQTQALN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 105 LIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEMGTGKVvdrKVELEKEDGHELHKRLSQVDPEMAAKLHPHDKRK 184
Cdd:TIGR00174  80 AIADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQL---EILAEEQGWDFLYNELKKVDPVAAAKIHPNDTRR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 185 VA----------------------------------------------------------------SQDYQH--GIFQSI 198
Cdd:TIGR00174 157 VQralevfyatgkppselfkeqkielfydivqiglassreplhqrieqrvhdmlesgllaevkalyAQYDLCdlPSIQAI 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907156966 199 GFKEFHEYLttEGKCTpetsnqlLKKGIEALKQVTKRYARKQNRWVKNRF 248
Cdd:TIGR00174 237 GYKEFLLYL--EGTVS-------LEDAIERIKCNTRQYAKRQLTWFRKWS 277
PLN02748 PLN02748
tRNA dimethylallyltransferase
 17-334 2.30e-49

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 172.76  E-value: 2.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  17 RGLRRtlpLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVtSYTVV 96
Cdd:PLN02748   19 KGKAK---VVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSV-EFTAK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  97 DFRNKATALIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEM-----GTGKVVDRKV----ELEKEDGHELHKRLS 167
Cdd:PLN02748   95 DFRDHAVPLIEEILSRNGLPVIVGGTNYYIQALVSPFLLDDMAEETedctfVVASVLDEHMdvesGLGNDDEDHGYELLK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 168 QVDPEMAAKLHPHDKRKV-------------------------------------------------------------- 185
Cdd:PLN02748  175 ELDPVAANRIHPNNHRKInrylelyattgvlpsklyqgkaaenwgrisnsrfdccficvdadtavldryvnqrvdcmida 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 186 -----------ASQDYQHGIFQSIGFKEFHEYL------TTEGKCTPETSNQ---------------------LLKKGIE 227
Cdd:PLN02748  255 glldevydiydPGADYTRGLRQAIGVREFEDFLrlylsrNENGELTSSSNNDkvmkensrkilnfphddklkiLLDEAID 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 228 ALKQVTKRYARKQNRWVkNRFLSRPGPSVPPV----YGLEVSDVSkWEESVLEPALNIVQSFIQGHKPTAMPVKMAYNES 303
Cdd:PLN02748  335 QVKLNTRRLVRRQKRRL-HRLNTVFGWNIHYIdateAILCKSEES-WNAKVVKPAVEIVRRFLSDDTSSGPDASSGKSVS 412

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1907156966 304 ENKRSYHMCDLCD-RIIIGDREWAAHLKSKSH 334
Cdd:PLN02748  413 RELWTQYVCEACGnKVLRGAHEWEQHKQGRGH 444
PLN02165 PLN02165
adenylate isopentenyltransferase
 25-286 7.44e-35

adenylate isopentenyltransferase


Pssm-ID: 177823  Cd Length: 334  Bit Score: 131.10  E-value: 7.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVTSYTVVDFRNKATA 104
Cdd:PLN02165   45 VVVIMGATGSGKSRLSVDLATRFPSEIINSDKMQVYDGLKITTNQITIQDRRGVPHHLLGELNPDDGELTASEFRSLASL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 105 LIEDIFARDKIPIVVGGTNYYIESLLWKVL-ITTKPQEMGTGKV------------VDRKVELEKEdghELHKRLSQ-VD 170
Cdd:PLN02165  125 SISEITSRQKLPIVAGGSNSFIHALLADRFdPEIYPFSSGSSLIssdlrydccfiwVDVSEPVLFE---YLSKRVDEmMD 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966 171 PEMAAKLHP-HDKRKVASQdyQHGIFQSIGFKEFHEYLTtegKCTPETS----NQLLK----KGIEALKQVTKRYARKQN 241
Cdd:PLN02165  202 SGMFEELAEfYDPVKSGSE--PLGIRKAIGVPEFDRYFK---KYPPENKmgkwDQARKaayeEAVREIKENTCQLAKRQI 276

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907156966 242 R---------WVKNRFLSRPG-PSVPPVYGLEVSDVSKWEESVLEPALNIVQSFI 286
Cdd:PLN02165  277 EkimklksagWDIKRVDATASfRAVMRKKGKKKKWREIWEKDVLEPSVKIVKRFL 331
PLN02840 PLN02840
tRNA dimethylallyltransferase
 25-139 7.44e-29

tRNA dimethylallyltransferase


Pssm-ID: 215451  Cd Length: 421  Bit Score: 116.07  E-value: 7.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPlVTSYTVVDFRNKATA 104
Cdd:PLN02840   23 VIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSLSERKEVPHHLIDILHP-SDDYSVGAFFDDARR 101

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907156966 105 LIEDIFARDKIPIVVGGTNYYiesLLWkvLITTKP 139
Cdd:PLN02840  102 ATQDILNRGRVPIVAGGTGLY---LRW--YIYGKP 131
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
25-55 8.25e-05

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 42.59  E-value: 8.25e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSAD 55
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLGAVRLRSD 31
PRK06547 PRK06547
hypothetical protein; Provisional
 17-64 6.68e-04

hypothetical protein; Provisional


Pssm-ID: 235825  Cd Length: 172  Bit Score: 40.11  E-value: 6.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907156966  17 RGLRRTLPLVVILGATGTGKSTLALQLGQRLGGEIVSADsmQVYEGLD 64
Cdd:PRK06547    9 RLCGGGMITVLIDGRSGSGKTTLAGALAARTGFQLVHLD--DLYPGWH 54
PRK12337 PRK12337
2-phosphoglycerate kinase; Provisional
 17-58 1.01e-03

2-phosphoglycerate kinase; Provisional


Pssm-ID: 183452 [Multi-domain]  Cd Length: 475  Bit Score: 40.91  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907156966  17 RGLRRTL-PLVVILG-ATGTGKSTLALQLGQRLG-GEIVSADSMQ 58
Cdd:PRK12337  247 RSIRRPPrPLHVLIGgVSGVGKSVLASALAYRLGiTRIVSTDAVR 291
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 310-334 1.01e-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: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 1907156966 310 HMCDLCDRIIIGDREWAAHLKSKSH 334
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKH 26
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 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSA-DSMQVYEGLDIITNKVSAQEQKmcQHHMISFVDPLVT 91
Cdd:cd02019     1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVlDEIVILEGLYASYKSRDARIRD--LADLKIYLDADLV 66
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 25-57 1.23e-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: 38.83  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSM 57
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAVRLSSDDE 33
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 20-52 1.70e-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: 39.03  E-value: 1.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907156966  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 ...
 310-341 1.96e-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: 35.69  E-value: 1.96e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907156966  310 HMCDLCDRIIIGDREWAAHLKSKSHLHQLKKR 341
Cdd:smart00451   4 FYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 25-57 2.59e-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: 38.00  E-value: 2.59e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907156966  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSM 57
Cdd:cd02021     1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDL 33
IPT pfam01745
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes ...
 28-60 3.57e-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: 3.57e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907156966  28 ILGATGTGKSTLALQLGQRLGGEIVSADSMQVY 60
Cdd:pfam01745   6 IWGATCTGKTAEAIALAKETGWPVIVLDRVQCC 38
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 24-55 3.64e-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: 37.80  E-value: 3.64e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907156966  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSAD 55
Cdd:COG3265     2 MVIVVMGVSGSGKSTVGQALAERLGWPFIDGD 33
PRK04220 PRK04220
2-phosphoglycerate kinase; Provisional
 19-48 4.17e-03

2-phosphoglycerate kinase; Provisional


Pssm-ID: 179793 [Multi-domain]  Cd Length: 301  Bit Score: 38.79  E-value: 4.17e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907156966  19 LRRTLPLVVILG-ATGTGKSTLALQLGQRLG 48
Cdd:PRK04220   87 RKSKEPIIILIGgASGVGTSTIAFELASRLG 117
PRK08118 PRK08118
DNA topology modulation protein;
26-48 4.28e-03

DNA topology modulation protein;


Pssm-ID: 181235  Cd Length: 167  Bit Score: 37.67  E-value: 4.28e-03
                          10        20
                  ....*....|....*....|...
gi 1907156966  26 VVILGATGTGKSTLALQLGQRLG 48
Cdd:PRK08118    4 IILIGSGGSGKSTLARQLGEKLN 26
AAA_28 pfam13521
AAA domain;
26-52 4.53e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 37.63  E-value: 4.53e-03
                          10        20
                  ....*....|....*....|....*..
gi 1907156966  26 VVILGATGTGKSTLALQLGQRLGGEIV 52
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAARFGYPVV 28
Pgk2 COG2074
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ...
 20-56 5.37e-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: 38.01  E-value: 5.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907156966  20 RRTLPLVVIL--GATGTGKSTLALQLGQRLG-GEIVSADS 56
Cdd:COG2074     1 RRMKRPRIILigGASGVGKSTIAAELARRLGiPRVISTDS 40
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
12-42 6.89e-03

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 37.59  E-value: 6.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907156966  12 VSSGFRGLRRTLP-------LVVILGATGTGKSTLALQ 42
Cdd:COG0467     2 VPTGIPGLDELLGgglprgsSTLLSGPPGTGKTTLALQ 39
COG3903 COG3903
Predicted ATPase [General function prediction only];
17-50 7.96e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 38.46  E-value: 7.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907156966  17 RGLRRTLPLVVILGATGTGKSTLALQLGQRLGGE 50
Cdd:COG3903   170 RALLSAARLVTLTGPGGVGKTRLALEVAHRLADR 203
 
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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