|
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
|
| 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
|
| 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
|
| 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
|
|
|