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Conserved domains on  [gi|2443763600|ref|WP_273305554|]
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tRNA (adenosine(37)-N6)-dimethylallyltransferase MiaA [Barnesiella viscericola]

Protein Classification

tRNA (adenosine(37)-N6)-dimethylallyltransferase( domain architecture ID 10001072)

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)

CATH:  1.10.287.890|3.40.50.300
EC:  2.5.1.-
Gene Ontology:  GO:0005524|GO:0006400|GO:0008033
PubMed:  9012675|19158097
SCOP:  4006480

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]; ...
 4-297 6.30e-135

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: 384.41  E-value: 6.30e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   4 TLLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLR 83
Cdd:COG0324     3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPDEEYSVADFQRDARA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  84 LLDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPTITDEVRREVLADYHRVGLDVLCEELRELDPVYYGEVDLKNHKRVIH 163
Cdd:COG0324    83 AIAEILARGKLPILVGGTGLYIKALLEGLSFLPPADPELRAELEAEAEELGLEALHAELAELDPEAAARIHPNDPQRIIR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 164 AIEICRQTGGRYSDLRTRQVKQRPFHIVKIGLIRPREELFERIARRTDQMIADGLLDEARRVYPL---RHLNSLNTVGYK 240
Cdd:COG0324   163 ALEVYELTGKPLSELQKEKKEPPPYDVLKIGLDPDREELYERINRRVDQMLEAGLLDEVRALLARgldPDLPAMRAIGYR 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 241 ELFAYFDGTMTLDQAIEKIKRNTRVYSKKQVTWYKKDPDMHWFSPDDK---EAIIEYIDE 297
Cdd:COG0324   243 ELLAYLDGEISLEEAIERIKRATRQYAKRQLTWFRRDPDIHWLDPDEPdllEEILELIKA 302
 
Name Accession Description Interval E-value
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
 4-297 6.30e-135

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: 384.41  E-value: 6.30e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   4 TLLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLR 83
Cdd:COG0324     3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPDEEYSVADFQRDARA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  84 LLDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPTITDEVRREVLADYHRVGLDVLCEELRELDPVYYGEVDLKNHKRVIH 163
Cdd:COG0324    83 AIAEILARGKLPILVGGTGLYIKALLEGLSFLPPADPELRAELEAEAEELGLEALHAELAELDPEAAARIHPNDPQRIIR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 164 AIEICRQTGGRYSDLRTRQVKQRPFHIVKIGLIRPREELFERIARRTDQMIADGLLDEARRVYPL---RHLNSLNTVGYK 240
Cdd:COG0324   163 ALEVYELTGKPLSELQKEKKEPPPYDVLKIGLDPDREELYERINRRVDQMLEAGLLDEVRALLARgldPDLPAMRAIGYR 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 241 ELFAYFDGTMTLDQAIEKIKRNTRVYSKKQVTWYKKDPDMHWFSPDDK---EAIIEYIDE 297
Cdd:COG0324   243 ELLAYLDGEISLEEAIERIKRATRQYAKRQLTWFRRDPDIHWLDPDEPdllEEILELIKA 302
IPPT pfam01715
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ...
 38-277 1.92e-93

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: 276.61  E-value: 1.92e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  38 QFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLRLLDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPT 117
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEEYSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALLDGLDDFPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 118 ITDEVRREVLADYHRVGLDVLCEELRELDPVYYGEVDLKNHKRVIHAIEICRQTGGRYSDLRTRQVKQRPFHIVKIGLiR 197
Cdd:pfam01715  81 ADPELRAELEAEAAEEGLEALHAELAEVDPEAAARIHPNDRRRIIRALEVYELTGKPLSEFQEPEKPPPPYDTLIIGL-S 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 198 PREELFERIARRTDQMIADGLLDEARRVYP---LRHLNSLNTVGYKELFAYFDGTMTLDQAIEKIKRNTRVYSKKQVTWY 274
Cdd:pfam01715 160 DREELYERINARVDAMLEAGLLEEVRALLDrgyGGDLPAMQAIGYKELLAYLDGEISLEEAIELIKRATRQYAKRQLTWF 239


                  ...
gi 2443763600 275 KKD 277
Cdd:pfam01715 240 RRD 242
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
 5-287 8.55e-78

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: 238.44  E-value: 8.55e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   5 LLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLRL 84
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDPSESYSAADFQTQALNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  85 LDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPTITDEVRREVLADYHRVGLDVLCEELRELDPVYYGEVDLKNHKRVIHA 164
Cdd:TIGR00174  81 IADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQLEILAEEQGWDFLYNELKKVDPVAAAKIHPNDTRRVQRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 165 IEICRQTGGRYSDLRTRQVKQRPFHIVKIGLIRPREELFERIARRTDQMIADGLLDEARRVY---PLRHLNSLNTVGYKE 241
Cdd:TIGR00174 161 LEVFYATGKPPSELFKEQKIELFYDIVQIGLASSREPLHQRIEQRVHDMLESGLLAEVKALYaqyDLCDLPSIQAIGYKE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2443763600 242 LFAYFDGTMTLDQAIEKIKRNTRVYSKKQVTWYKKDPDMHWFSPDD 287
Cdd:TIGR00174 241 FLLYLEGTVSLEDAIERIKCNTRQYAKRQLTWFRKWSDVLWLDSTD 286
PLN02840 PLN02840
tRNA dimethylallyltransferase
 4-295 1.47e-27

tRNA dimethylallyltransferase


Pssm-ID: 215451  Cd Length: 421  Bit Score: 110.68  E-value: 1.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   4 TLLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLR 83
Cdd:PLN02840   22 KVIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSLSERKEVPHHLIDILHPSDDYSVGAFFDDARR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  84 LLDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPTITDEVRREV---LADYHRVG-LDVLCEELRELDPVYYGEVDLKNHK 159
Cdd:PLN02840  102 ATQDILNRGRVPIVAGGTGLYLRWYIYGKPDVPKSSPEITSEVwseLVDFQKNGdWDAAVELVVNAGDPKARSLPRNDWY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 160 RVIHAIEICRQTGGRYSDLR-----------TRQV-----------KQRPFHIVKIGLIRPREELFERIARRTDQMIAD- 216
Cdd:PLN02840  182 RLRRSLEIIKSSGSPPSAFSlpydsfreqlvTEDTdssledgssaeTELDYDFLCFFLSSPRLDLYRSIDLRCEEMLAGt 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 217 -GLLDEARRVYPLRHLNSLNT----VGYKELFAYF-----DGTMTLDQA----IEKIKRNTRVYSKKQVTWYKKDPDMHW 282
Cdd:PLN02840  262 nGILSEASWLLDLGLLPNSNSatraIGYRQAMEYLlqcrqNGGESSPQEflafLSKFQTASRNFAKRQMTWFRNEPIYHW 341

                         330
                  ....*....|....
gi 2443763600 283 FSPDDK-EAIIEYI 295
Cdd:PLN02840  342 LDASQPlEKILQFI 355
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 6-25 8.00e-04

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 39.47  E-value: 8.00e-04
                          10        20
                  ....*....|....*....|
gi 2443763600   6 LVLTGPTGVGKTELSLQLAE 25
Cdd:cd19499    44 FLFLGPTGVGKTELAKALAE 63
 
Name Accession Description Interval E-value
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
 4-297 6.30e-135

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: 384.41  E-value: 6.30e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   4 TLLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLR 83
Cdd:COG0324     3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPDEEYSVADFQRDARA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  84 LLDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPTITDEVRREVLADYHRVGLDVLCEELRELDPVYYGEVDLKNHKRVIH 163
Cdd:COG0324    83 AIAEILARGKLPILVGGTGLYIKALLEGLSFLPPADPELRAELEAEAEELGLEALHAELAELDPEAAARIHPNDPQRIIR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 164 AIEICRQTGGRYSDLRTRQVKQRPFHIVKIGLIRPREELFERIARRTDQMIADGLLDEARRVYPL---RHLNSLNTVGYK 240
Cdd:COG0324   163 ALEVYELTGKPLSELQKEKKEPPPYDVLKIGLDPDREELYERINRRVDQMLEAGLLDEVRALLARgldPDLPAMRAIGYR 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 241 ELFAYFDGTMTLDQAIEKIKRNTRVYSKKQVTWYKKDPDMHWFSPDDK---EAIIEYIDE 297
Cdd:COG0324   243 ELLAYLDGEISLEEAIERIKRATRQYAKRQLTWFRRDPDIHWLDPDEPdllEEILELIKA 302
IPPT pfam01715
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ...
 38-277 1.92e-93

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: 276.61  E-value: 1.92e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  38 QFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLRLLDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPT 117
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEEYSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALLDGLDDFPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 118 ITDEVRREVLADYHRVGLDVLCEELRELDPVYYGEVDLKNHKRVIHAIEICRQTGGRYSDLRTRQVKQRPFHIVKIGLiR 197
Cdd:pfam01715  81 ADPELRAELEAEAAEEGLEALHAELAEVDPEAAARIHPNDRRRIIRALEVYELTGKPLSEFQEPEKPPPPYDTLIIGL-S 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 198 PREELFERIARRTDQMIADGLLDEARRVYP---LRHLNSLNTVGYKELFAYFDGTMTLDQAIEKIKRNTRVYSKKQVTWY 274
Cdd:pfam01715 160 DREELYERINARVDAMLEAGLLEEVRALLDrgyGGDLPAMQAIGYKELLAYLDGEISLEEAIELIKRATRQYAKRQLTWF 239


                  ...
gi 2443763600 275 KKD 277
Cdd:pfam01715 240 RRD 242
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
 5-287 8.55e-78

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: 238.44  E-value: 8.55e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   5 LLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLRL 84
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDPSESYSAADFQTQALNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  85 LDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPTITDEVRREVLADYHRVGLDVLCEELRELDPVYYGEVDLKNHKRVIHA 164
Cdd:TIGR00174  81 IADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQLEILAEEQGWDFLYNELKKVDPVAAAKIHPNDTRRVQRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 165 IEICRQTGGRYSDLRTRQVKQRPFHIVKIGLIRPREELFERIARRTDQMIADGLLDEARRVY---PLRHLNSLNTVGYKE 241
Cdd:TIGR00174 161 LEVFYATGKPPSELFKEQKIELFYDIVQIGLASSREPLHQRIEQRVHDMLESGLLAEVKALYaqyDLCDLPSIQAIGYKE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2443763600 242 LFAYFDGTMTLDQAIEKIKRNTRVYSKKQVTWYKKDPDMHWFSPDD 287
Cdd:TIGR00174 241 FLLYLEGTVSLEDAIERIKCNTRQYAKRQLTWFRKWSDVLWLDSTD 286
PLN02840 PLN02840
tRNA dimethylallyltransferase
 4-295 1.47e-27

tRNA dimethylallyltransferase


Pssm-ID: 215451  Cd Length: 421  Bit Score: 110.68  E-value: 1.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   4 TLLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVLR 83
Cdd:PLN02840   22 KVIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSLSERKEVPHHLIDILHPSDDYSVGAFFDDARR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  84 LLDSLFQTHEYVLLTGGSMMYIDAVCKGIDEIPTITDEVRREV---LADYHRVG-LDVLCEELRELDPVYYGEVDLKNHK 159
Cdd:PLN02840  102 ATQDILNRGRVPIVAGGTGLYLRWYIYGKPDVPKSSPEITSEVwseLVDFQKNGdWDAAVELVVNAGDPKARSLPRNDWY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 160 RVIHAIEICRQTGGRYSDLR-----------TRQV-----------KQRPFHIVKIGLIRPREELFERIARRTDQMIAD- 216
Cdd:PLN02840  182 RLRRSLEIIKSSGSPPSAFSlpydsfreqlvTEDTdssledgssaeTELDYDFLCFFLSSPRLDLYRSIDLRCEEMLAGt 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 217 -GLLDEARRVYPLRHLNSLNT----VGYKELFAYF-----DGTMTLDQA----IEKIKRNTRVYSKKQVTWYKKDPDMHW 282
Cdd:PLN02840  262 nGILSEASWLLDLGLLPNSNSatraIGYRQAMEYLlqcrqNGGESSPQEflafLSKFQTASRNFAKRQMTWFRNEPIYHW 341

                         330
                  ....*....|....
gi 2443763600 283 FSPDDK-EAIIEYI 295
Cdd:PLN02840  342 LDASQPlEKILQFI 355
PLN02748 PLN02748
tRNA dimethylallyltransferase
 3-226 2.73e-16

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 78.77  E-value: 2.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   3 GTLLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTDYYSASCYEEEVL 82
Cdd:PLN02748   22 AKVVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSVEFTAKDFRDHAV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  83 RLLDSLFQTHEYVLLTGGSMMYIDAV---------CKGIDEIPTITDEVRREVLAD---YHRVGLDVLCEELRELDPVYY 150
Cdd:PLN02748  102 PLIEEILSRNGLPVIVGGTNYYIQALvspfllddmAEETEDCTFVVASVLDEHMDVesgLGNDDEDHGYELLKELDPVAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 151 GEVDLKNHKRVIHAIEICRQTGGRYSDLRTRQVKQ---RP----FHIVKIGLIRPREELFERIARRTDQMIADGLLDEAR 223
Cdd:PLN02748  182 NRIHPNNHRKINRYLELYATTGVLPSKLYQGKAAEnwgRIsnsrFDCCFICVDADTAVLDRYVNQRVDCMIDAGLLDEVY 261


                  ...
gi 2443763600 224 RVY 226
Cdd:PLN02748  262 DIY 264
PLN02165 PLN02165
adenylate isopentenyltransferase
 5-272 4.82e-10

adenylate isopentenyltransferase


Pssm-ID: 177823  Cd Length: 334  Bit Score: 59.45  E-value: 4.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   5 LLVLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTD-YYSASCYEEEVLR 83
Cdd:PLN02165   45 VVVIMGATGSGKSRLSVDLATRFPSEIINSDKMQVYDGLKITTNQITIQDRRGVPHHLLGELNPDDgELTASEFRSLASL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  84 LLDSLFQTHEYVLLTGGSMMYIDAvckgideiptitdevrreVLADyhrvgldvlceelrELDPVYYGEVDLKNhkrvih 163
Cdd:PLN02165  125 SISEITSRQKLPIVAGGSNSFIHA------------------LLAD--------------RFDPEIYPFSSGSS------ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600 164 aiEICrqtggrySDLRTRQVkqrpFHIVKIGLirprEELFERIARRTDQMIADGLLDEARRVY-----PLRHLNSLNTVG 238
Cdd:PLN02165  167 --LIS-------SDLRYDCC----FIWVDVSE----PVLFEYLSKRVDEMMDSGMFEELAEFYdpvksGSEPLGIRKAIG 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2443763600 239 YKELFAYF-----DGTM---------TLDQAIEKIKRNTRVYSKKQVT 272
Cdd:PLN02165  230 VPEFDRYFkkyppENKMgkwdqarkaAYEEAVREIKENTCQLAKRQIE 277
IPT pfam01745
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes ...
 10-209 6.01e-09

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: 55.48  E-value: 6.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  10 GPTGVGKTELSLQLAEHYGCPIVSADSRQFYRDIPIGTAAPTASELARVKHYFVGQLALTD-YYSASCYEE----EVLRL 84
Cdd:pfam01745   8 GATCTGKTAEAIALAKETGWPVIVLDRVQCCSQLATGSGRPLPAELQGTRRIYLDNRPLSEgIIDAEEAHDrliaEVTSH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  85 LDSlfqthEYVLLTGGSMMYIDAVCKGIDEIPTITDEVRREVLADyHRVGLDVLCEELREL------DPVYYGE-VDLKN 157
Cdd:pfam01745  88 KDE-----GGVILEGGSISLLKRMAQSPYWNAGFPWHVKRMRLPD-RDVFLAQAKARVRQMlrpdsgGPSLLDElAELWV 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2443763600 158 HKRVIHAIE-ICrqtGGRYSdLRTRQVKQRPFHIVKIGLIRPREELFERIARR 209
Cdd:pfam01745 162 LPAARPILEdID---GYRCA-IDFARKHQLTIDQLTNIDADQLEELIEGIAQE 210
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 2-88 1.50e-05

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 44.72  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   2 AGTLLVLTGPTGVGKTELSLQLA-EHY--GCPIV---SADSRQFYRDIPIGTaaPTASELARVKHYFVGQLALTDYYS-- 73
Cdd:COG4088     3 SPMLLILTGPPGSGKTTFAKALAqRLYaeGIAVAllhSDDFRRFLVNESFPK--ETYEEVVEDVRTTTADNALDNGYSvi 80

                          90
                  ....*....|....*..
gi 2443763600  74 --ASCYEEEVLRLLDSL 88
Cdd:COG4088    81 vdGTFYYRSWQRDFRNL 97
AAA_28 pfam13521
AAA domain;
7-146 9.95e-05

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 41.87  E-value: 9.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600   7 VLTGPTGVGKTELSLQLAEHYGCPIVSADSRQFYRD--IPIGTAAPTASELARVKHYFVgQLALTDYYSAS--------- 75
Cdd:pfam13521   3 VITGGPSTGKTTLAEALAARFGYPVVPEAAREILEElgADGGDALPWVEDLLAFARGVL-EAQLEDEAAAAandllffdr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763600  76 ----------CYEEEVLRLLDSLFQTHEY--VLLTGgsmmyidavckgiDEIPTITDEVRREVLADYHRVGlDVLCEELR 143
Cdd:pfam13521  82 gpldtlaysrAYGGPCPPELEAAARASRYdlVFLLP-------------PDPEIVQDGERREDPEERERFH-ERLREALR 147


                  ...
gi 2443763600 144 ELD 146
Cdd:pfam13521 148 ELG 150
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 6-25 8.00e-04

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 39.47  E-value: 8.00e-04
                          10        20
                  ....*....|....*....|
gi 2443763600   6 LVLTGPTGVGKTELSLQLAE 25
Cdd:cd19499    44 FLFLGPTGVGKTELAKALAE 63
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 3-25 1.14e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 1.14e-03
                          10        20
                  ....*....|....*....|...
gi 2443763600   3 GTLLVLtGPTGVGKTELSLQLAE 25
Cdd:COG0542   580 GSFLFL-GPTGVGKTELAKALAE 601
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 7-32 3.60e-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: 37.49  E-value: 3.60e-03
                          10        20
                  ....*....|....*....|....*.
gi 2443763600   7 VLTGPTGVGKTELSLQLAEHYGCPIV 32
Cdd:COG3172    12 VLLGAESTGKTTLARALAAHYNTPWV 37
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-38 7.30e-03

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 36.97  E-value: 7.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2443763600   3 GTLLVLTGPTGVGKTELSLQLAEHYG--CPIVSADSRQ 38
Cdd:COG0194     2 GKLIVLSGPSGAGKTTLVKALLERDPdlRFSVSATTRP 39
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
5-58 8.35e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 36.43  E-value: 8.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2443763600   5 LLVLTGPTGVGKTELSLQLAEHYGCPIVSADS-RQFYRDIPIGTAAPTASELARV 58
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLGAVRLRSDVvRKRLFGAGLAPLERSPEATART 55
 
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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