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Conserved domains on  [gi|31581534|ref|NP_060116|]
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tRNA dimethylallyltransferase isoform 1 precursor [Homo sapiens]

Protein Classification

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 2.22e-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: 282.33  E-value: 2.22e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLvTNYTVVDFRNRAT 103
Cdd:COG0324   3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlvntkpQEMGTEKVIDRKV------ELEKEDGLVLHKRLSQVDPEMAAKL 177
Cdd:COG0324  82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 178 HPHDKRKVARSLQVFEETGISHSEFLHRQHTEEGGgplggplkfsNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELR 257
Cdd:COG0324 153 HPNDPQRIIRALEVYELTGKPLSELQKEKKEPPPY----------DVLKIGLDPDREELYERINRRVDQMLEAGLLDEVR 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 258 DFHRRynqkNVSENSQdyqhgIFQSIGFKEFHEYLitEGKCTLETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrp 337
Cdd:COG0324 223 ALLAR----GLDPDLP-----AMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD----- 279

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 31581534 338 gpivPPVYGLEVSDVSKWEEsvlepALEIVQSFIQG 373
Cdd:COG0324 280 ----PDIHWLDPDEPDLLEE-----ILELIKAFLEE 306
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 395-426 2.25e-04

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: 38.39  E-value: 2.25e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 31581534    395 HLCDLCDRIIIGDREWAAHIKSKSHLNQLKKR 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 2.22e-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: 282.33  E-value: 2.22e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLvTNYTVVDFRNRAT 103
Cdd:COG0324   3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlvntkpQEMGTEKVIDRKV------ELEKEDGLVLHKRLSQVDPEMAAKL 177
Cdd:COG0324  82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 178 HPHDKRKVARSLQVFEETGISHSEFLHRQHTEEGGgplggplkfsNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELR 257
Cdd:COG0324 153 HPNDPQRIIRALEVYELTGKPLSELQKEKKEPPPY----------DVLKIGLDPDREELYERINRRVDQMLEAGLLDEVR 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 258 DFHRRynqkNVSENSQdyqhgIFQSIGFKEFHEYLitEGKCTLETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrp 337
Cdd:COG0324 223 ALLAR----GLDPDLP-----AMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD----- 279

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 31581534 338 gpivPPVYGLEVSDVSKWEEsvlepALEIVQSFIQG 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 1.68e-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: 265.06  E-value: 1.68e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534    58 QVYEGLDIITNKVSAQEQRICRHHMISFVDPLVTnYTVVDFRNRATALIEDIFARDKIPIVVGGTNYYIESLLwKVLVNT 137
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEE-YSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALL-DGLDDF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   138 KPQEMGTEKVIDRkvELEKEDGLVLHKRLSQVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHTEEGGgplgg 217
Cdd:pfam01715  79 PPADPELRAELEA--EAAEEGLEALHAELAEVDPEAAARIHPNDRRRIIRALEVYELTGKPLSEFQEPEKPPPPY----- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   218 plkfsNPCILWLhADQAVLDERLDKRVDDMLAAGLLEELRDFHRRYnqknvsensQDYQHGIFQSIGFKEFHEYLitEGK 297
Cdd:pfam01715 152 -----DTLIIGL-SDREELYERINARVDAMLEAGLLEEVRALLDRG---------YGGDLPAMQAIGYKELLAYL--DGE 214

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 31581534   298 CTLETsnqllkkGIEALKQVTKRYARKQNRWVKNR 332
Cdd:pfam01715 215 ISLEE-------AIELIKRATRQYAKRQLTWFRRD 242
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
 25-333 3.35e-77

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: 242.68  E-value: 3.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534    25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPlVTNYTVVDFRNRATA 104
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDP-SESYSAADFQTQALN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   105 LIEDIFARDKIPIVVGGTNYYIESLLWKvLVNTKPQEMGTEKVIDRKVELEKEDglVLHKRLSQVDPEMAAKLHPHDKRK 184
Cdd:TIGR00174  80 AIADITARGKIPLLVGGTGLYLKALLEG-LSPTPSADKLIREQLEILAEEQGWD--FLYNELKKVDPVAAAKIHPNDTRR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   185 VARSLQVFEETGISHSEFLHRQhteegggplgGPLKFSNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRDFHRRYN 264
Cdd:TIGR00174 157 VQRALEVFYATGKPPSELFKEQ----------KIELFYDIVQIGLASSREPLHQRIEQRVHDMLESGLLAEVKALYAQYD 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31581534   265 QKNVsensqdyqhGIFQSIGFKEFHEYLitEGKCTLEtsnqllkKGIEALKQVTKRYARKQNRWVKNRF 333
Cdd:TIGR00174 227 LCDL---------PSIQAIGYKEFLLYL--EGTVSLE-------DAIERIKCNTRQYAKRQLTWFRKWS 277
PLN02748 PLN02748
tRNA dimethylallyltransferase
 25-419 6.11e-70

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 229.77  E-value: 6.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLVtNYTVVDFRNRATA 104
Cdd:PLN02748  24 VVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSV-EFTAKDFRDHAVP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  105 LIEDIFARDKIPIVVGGTNYYIESLLWKVLVNTKPQEM---------GTEKVIDRKVELEKEDGLVLHKRLSQVDPEMAA 175
Cdd:PLN02748 103 LIEEILSRNGLPVIVGGTNYYIQALVSPFLLDDMAEETedctfvvasVLDEHMDVESGLGNDDEDHGYELLKELDPVAAN 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  176 KLHPHDKRKVARSLQVFEETGISHSEFLhrQHTEEGGGPLGGPLKFsNPCILWLHADQAVLDERLDKRVDDMLAAGLLEE 255
Cdd:PLN02748 183 RIHPNNHRKINRYLELYATTGVLPSKLY--QGKAAENWGRISNSRF-DCCFICVDADTAVLDRYVNQRVDCMIDAGLLDE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  256 LRDFHRRYnqknvsensQDYQHGIFQSIGFKEFHEYL---ITE---GKCTLETSNQ---------------------LLK 308
Cdd:PLN02748 260 VYDIYDPG---------ADYTRGLRQAIGVREFEDFLrlyLSRnenGELTSSSNNDkvmkensrkilnfphddklkiLLD 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  309 KGIEALKQVTKRYARKQNRWVknrflSRPGP--------IVPPVYGLEVSDVSkWEESVLEPALEIVQSFIQGHKPTATP 380
Cdd:PLN02748 331 EAIDQVKLNTRRLVRRQKRRL-----HRLNTvfgwnihyIDATEAILCKSEES-WNAKVVKPAVEIVRRFLSDDTSSGPD 404

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 31581534  381 IKMPYNEAENKRSYHLCDLCD-RIIIGDREWAAHIKSKSH 419
Cdd:PLN02748 405 ASSGKSVSRELWTQYVCEACGnKVLRGAHEWEQHKQGRGH 444
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 395-426 2.25e-04

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: 38.39  E-value: 2.25e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 31581534    395 HLCDLCDRIIIGDREWAAHIKSKSHLNQLKKR 426
Cdd:smart00451   4 FYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 397-419 3.20e-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: 34.84  E-value: 3.20e-03
                          10        20
                  ....*....|....*....|...
gi 31581534   397 CDLCDRIIIGDREWAAHIKSKSH 419
Cdd:pfam12171   4 CVLCDKYFKSENALQNHLKSKKH 26
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 25-57 4.44e-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: 4.44e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 31581534  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSM 57
Cdd:cd02021   1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDL 33
 
Name Accession Description Interval E-value
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
 24-373 2.22e-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: 282.33  E-value: 2.22e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLvTNYTVVDFRNRAT 103
Cdd:COG0324   3 PLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPD-EEYSVADFQRDAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 104 ALIEDIFARDKIPIVVGGTNYYIESLLwkvlvntkpQEMGTEKVIDRKV------ELEKEDGLVLHKRLSQVDPEMAAKL 177
Cdd:COG0324  82 AAIAEILARGKLPILVGGTGLYIKALL---------EGLSFLPPADPELraeleaEAEELGLEALHAELAELDPEAAARI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 178 HPHDKRKVARSLQVFEETGISHSEFLHRQHTEEGGgplggplkfsNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELR 257
Cdd:COG0324 153 HPNDPQRIIRALEVYELTGKPLSELQKEKKEPPPY----------DVLKIGLDPDREELYERINRRVDQMLEAGLLDEVR 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534 258 DFHRRynqkNVSENSQdyqhgIFQSIGFKEFHEYLitEGKCTLETSnqllkkgIEALKQVTKRYARKQNRWVKNRflsrp 337
Cdd:COG0324 223 ALLAR----GLDPDLP-----AMRAIGYRELLAYL--DGEISLEEA-------IERIKRATRQYAKRQLTWFRRD----- 279

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 31581534 338 gpivPPVYGLEVSDVSKWEEsvlepALEIVQSFIQG 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 1.68e-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: 265.06  E-value: 1.68e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534    58 QVYEGLDIITNKVSAQEQRICRHHMISFVDPLVTnYTVVDFRNRATALIEDIFARDKIPIVVGGTNYYIESLLwKVLVNT 137
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEE-YSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALL-DGLDDF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   138 KPQEMGTEKVIDRkvELEKEDGLVLHKRLSQVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHTEEGGgplgg 217
Cdd:pfam01715  79 PPADPELRAELEA--EAAEEGLEALHAELAEVDPEAAARIHPNDRRRIIRALEVYELTGKPLSEFQEPEKPPPPY----- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   218 plkfsNPCILWLhADQAVLDERLDKRVDDMLAAGLLEELRDFHRRYnqknvsensQDYQHGIFQSIGFKEFHEYLitEGK 297
Cdd:pfam01715 152 -----DTLIIGL-SDREELYERINARVDAMLEAGLLEEVRALLDRG---------YGGDLPAMQAIGYKELLAYL--DGE 214

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 31581534   298 CTLETsnqllkkGIEALKQVTKRYARKQNRWVKNR 332
Cdd:pfam01715 215 ISLEE-------AIELIKRATRQYAKRQLTWFRRD 242
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
 25-333 3.35e-77

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: 242.68  E-value: 3.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534    25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPlVTNYTVVDFRNRATA 104
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDP-SESYSAADFQTQALN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   105 LIEDIFARDKIPIVVGGTNYYIESLLWKvLVNTKPQEMGTEKVIDRKVELEKEDglVLHKRLSQVDPEMAAKLHPHDKRK 184
Cdd:TIGR00174  80 AIADITARGKIPLLVGGTGLYLKALLEG-LSPTPSADKLIREQLEILAEEQGWD--FLYNELKKVDPVAAAKIHPNDTRR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   185 VARSLQVFEETGISHSEFLHRQhteegggplgGPLKFSNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRDFHRRYN 264
Cdd:TIGR00174 157 VQRALEVFYATGKPPSELFKEQ----------KIELFYDIVQIGLASSREPLHQRIEQRVHDMLESGLLAEVKALYAQYD 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31581534   265 QKNVsensqdyqhGIFQSIGFKEFHEYLitEGKCTLEtsnqllkKGIEALKQVTKRYARKQNRWVKNRF 333
Cdd:TIGR00174 227 LCDL---------PSIQAIGYKEFLLYL--EGTVSLE-------DAIERIKCNTRQYAKRQLTWFRKWS 277
PLN02748 PLN02748
tRNA dimethylallyltransferase
 25-419 6.11e-70

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 229.77  E-value: 6.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLVtNYTVVDFRNRATA 104
Cdd:PLN02748  24 VVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSV-EFTAKDFRDHAVP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  105 LIEDIFARDKIPIVVGGTNYYIESLLWKVLVNTKPQEM---------GTEKVIDRKVELEKEDGLVLHKRLSQVDPEMAA 175
Cdd:PLN02748 103 LIEEILSRNGLPVIVGGTNYYIQALVSPFLLDDMAEETedctfvvasVLDEHMDVESGLGNDDEDHGYELLKELDPVAAN 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  176 KLHPHDKRKVARSLQVFEETGISHSEFLhrQHTEEGGGPLGGPLKFsNPCILWLHADQAVLDERLDKRVDDMLAAGLLEE 255
Cdd:PLN02748 183 RIHPNNHRKINRYLELYATTGVLPSKLY--QGKAAENWGRISNSRF-DCCFICVDADTAVLDRYVNQRVDCMIDAGLLDE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  256 LRDFHRRYnqknvsensQDYQHGIFQSIGFKEFHEYL---ITE---GKCTLETSNQ---------------------LLK 308
Cdd:PLN02748 260 VYDIYDPG---------ADYTRGLRQAIGVREFEDFLrlyLSRnenGELTSSSNNDkvmkensrkilnfphddklkiLLD 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  309 KGIEALKQVTKRYARKQNRWVknrflSRPGP--------IVPPVYGLEVSDVSkWEESVLEPALEIVQSFIQGHKPTATP 380
Cdd:PLN02748 331 EAIDQVKLNTRRLVRRQKRRL-----HRLNTvfgwnihyIDATEAILCKSEES-WNAKVVKPAVEIVRRFLSDDTSSGPD 404

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 31581534  381 IKMPYNEAENKRSYHLCDLCD-RIIIGDREWAAHIKSKSH 419
Cdd:PLN02748 405 ASSGKSVSRELWTQYVCEACGnKVLRGAHEWEQHKQGRGH 444
PLN02165 PLN02165
adenylate isopentenyltransferase
 25-371 1.52e-41

adenylate isopentenyltransferase


Pssm-ID: 177823  Cd Length: 334  Bit Score: 150.75  E-value: 1.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLVTNYTVVDFRNRATA 104
Cdd:PLN02165  45 VVVIMGATGSGKSRLSVDLATRFPSEIINSDKMQVYDGLKITTNQITIQDRRGVPHHLLGELNPDDGELTASEFRSLASL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  105 LIEDIFARDKIPIVVGGTNYYIESLLwkvlvntkpqemgtekvIDRkvelekedglvlhkrlsqVDPEmaakLHPHDkrk 184
Cdd:PLN02165 125 SISEITSRQKLPIVAGGSNSFIHALL-----------------ADR------------------FDPE----IYPFS--- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  185 varslqvfEETGISHSEFLHrqhteegggplggplkfsNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRDFHRryn 264
Cdd:PLN02165 163 --------SGSSLISSDLRY------------------DCCFIWVDVSEPVLFEYLSKRVDEMMDSGMFEELAEFYD--- 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  265 qknvSENSQDYQHGIFQSIGFKEFHEYLIT---EGKCTL--ETSNQLLKKGIEALKQVTKRYARKQNR---------WVK 330
Cdd:PLN02165 214 ----PVKSGSEPLGIRKAIGVPEFDRYFKKyppENKMGKwdQARKAAYEEAVREIKENTCQLAKRQIEkimklksagWDI 289

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 31581534  331 NRFLSRPG-PIVPPVYGLEVSDVSKWEESVLEPALEIVQSFI 371
Cdd:PLN02165 290 KRVDATASfRAVMRKKGKKKKWREIWEKDVLEPSVKIVKRFL 331
PLN02840 PLN02840
tRNA dimethylallyltransferase
 25-331 4.07e-33

tRNA dimethylallyltransferase


Pssm-ID: 215451  Cd Length: 421  Bit Score: 129.94  E-value: 4.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534   25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPlVTNYTVVDFRNRATA 104
Cdd:PLN02840  23 VIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSLSERKEVPHHLIDILHP-SDDYSVGAFFDDARR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  105 LIEDIFARDKIPIVVGGTNYYiesLLWkvLVNTKPQ------EMgTEKVIDRKVELEKE---DGLVlhKRLSQVDPEMAA 175
Cdd:PLN02840 102 ATQDILNRGRVPIVAGGTGLY---LRW--YIYGKPDvpksspEI-TSEVWSELVDFQKNgdwDAAV--ELVVNAGDPKAR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  176 KLHPHDKRKVARSLQVFEETGISHSEF----------LHRQHTEEGGGPLGGPLK---FSNPCIlWLHADQAVLDERLDK 242
Cdd:PLN02840 174 SLPRNDWYRLRRSLEIIKSSGSPPSAFslpydsfreqLVTEDTDSSLEDGSSAETeldYDFLCF-FLSSPRLDLYRSIDL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31581534  243 RVDDMLAA--GLLEELRDFHRRYNQKNVSENSqdyqhgifQSIGFKEFHEYLITEGKCTLETSNQLLKKGIEALKQVTKR 320
Cdd:PLN02840 253 RCEEMLAGtnGILSEASWLLDLGLLPNSNSAT--------RAIGYRQAMEYLLQCRQNGGESSPQEFLAFLSKFQTASRN 324

                        330
                 ....*....|.
gi 31581534  321 YARKQNRWVKN 331
Cdd:PLN02840 325 FAKRQMTWFRN 335
PRK06547 PRK06547
hypothetical protein; Provisional
 3-64 1.11e-04

hypothetical protein; Provisional


Pssm-ID: 235825  Cd Length: 172  Bit Score: 42.81  E-value: 1.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31581534    3 SVAAARAVPVGsglrglqrtLPLVVILGATGTGKSTLALQLGQRLGGEIVSADsmQVYEGLD 64
Cdd:PRK06547   4 ALIAARLCGGG---------MITVLIDGRSGSGKTTLAGALAARTGFQLVHLD--DLYPGWH 54
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
25-55 2.08e-04

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 41.82  E-value: 2.08e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 31581534  25 LVVILGATGTGKSTLALQLGQRLGGEIVSAD 55
Cdd:COG0645   1 LILVCGLPGSGKSTLARALAERLGAVRLRSD 31
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 395-426 2.25e-04

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: 38.39  E-value: 2.25e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 31581534    395 HLCDLCDRIIIGDREWAAHIKSKSHLNQLKKR 426
Cdd:smart00451   4 FYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
COG3903 COG3903
Predicted ATPase [General function prediction only];
2-50 2.57e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.47  E-value: 2.57e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 31581534   2 ASVAAARAVPVGSGLRGLQRTLPLVVILGATGTGKSTLALQLGQRLGGE 50
Cdd:COG3903 155 LAALARRAAALAAAARALLSAARLVTLTGPGGVGKTRLALEVAHRLADR 203
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 25-57 2.34e-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: 2.34e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 31581534    25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSM 57
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAVRLSSDDE 33
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 26-52 3.17e-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: 3.17e-03
                        10        20
                ....*....|....*....|....*..
gi 31581534  26 VVILGATGTGKSTLALQLGQRLGGEIV 52
Cdd:COG3172  11 IVLLGAESTGKTTLARALAAHYNTPWV 37
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 397-419 3.20e-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: 34.84  E-value: 3.20e-03
                          10        20
                  ....*....|....*....|...
gi 31581534   397 CDLCDRIIIGDREWAAHIKSKSH 419
Cdd:pfam12171   4 CVLCDKYFKSENALQNHLKSKKH 26
PRK12337 PRK12337
2-phosphoglycerate kinase; Provisional
 16-58 3.22e-03

2-phosphoglycerate kinase; Provisional


Pssm-ID: 183452 [Multi-domain]  Cd Length: 475  Bit Score: 39.76  E-value: 3.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 31581534   16 LRGLQRTL-PLVVILG-ATGTGKSTLALQLGQRLG-GEIVSADSMQ 58
Cdd:PRK12337 246 LRSIRRPPrPLHVLIGgVSGVGKSVLASALAYRLGiTRIVSTDAVR 291
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 25-57 4.44e-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: 4.44e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 31581534  25 LVVILGATGTGKSTLALQLGQRLGGEIVSADSM 57
Cdd:cd02021   1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDL 33
IPT pfam01745
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes ...
 28-60 5.09e-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: 5.09e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 31581534    28 ILGATGTGKSTLALQLGQRLGGEIVSADSMQVY 60
Cdd:pfam01745   6 IWGATCTGKTAEAIALAKETGWPVIVLDRVQCC 38
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 24-55 5.55e-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: 5.55e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 31581534  24 PLVVILGATGTGKSTLALQLGQRLGGEIVSAD 55
Cdd:COG3265   2 MVIVVMGVSGSGKSTVGQALAERLGWPFIDGD 33
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 28-88 5.60e-03

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 38.26  E-value: 5.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31581534  28 ILGATGTGKSTLA---LQLGQRLGGEIvsadsmqVYEGLDIitNKVSAQEQRICRHHmISFV--DP 88
Cdd:cd03257  36 LVGESGSGKSTLAraiLGLLKPTSGSI-------IFDGKDL--LKLSRRLRKIRRKE-IQMVfqDP 91
PRK08118 PRK08118
DNA topology modulation protein;
26-48 6.96e-03

DNA topology modulation protein;


Pssm-ID: 181235  Cd Length: 167  Bit Score: 37.28  E-value: 6.96e-03
                         10        20
                 ....*....|....*....|...
gi 31581534   26 VVILGATGTGKSTLALQLGQRLG 48
Cdd:PRK08118   4 IILIGSGGSGKSTLARQLGEKLN 26
AAA_28 pfam13521
AAA domain;
26-52 7.95e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 37.24  E-value: 7.95e-03
                          10        20
                  ....*....|....*....|....*..
gi 31581534    26 VVILGATGTGKSTLALQLGQRLGGEIV 52
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAARFGYPVV 28
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 25-91 8.92e-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: 35.00  E-value: 8.92e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31581534  25 LVVILGATGTGKSTLALQLGQRLGGEIVSA-DSMQVYEGLDIITNKVSAQEQRIcrHHMISFVDPLVT 91
Cdd:cd02019   1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVlDEIVILEGLYASYKSRDARIRDL--ADLKIYLDADLV 66
 
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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