|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02840 |
PLN02840 |
tRNA dimethylallyltransferase |
26-457 |
0e+00 |
|
tRNA dimethylallyltransferase
Pssm-ID: 215451 Cd Length: 421 Bit Score: 793.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 26 RRFCAATTACSVPlngnKKKKSEKEKVIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSDRKVV 105
Cdd:PLN02840 1 RRFCAATTALSGS----GASKTKKEKVIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSLSERKEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 106 PHHLIDILHPSQDYSVGQFYDDGRQATKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPKPSPEVIAEAHDMLVGFQTEYN 185
Cdd:PLN02840 77 PHHLIDILHPSDDYSVGAFFDDARRATQDILNRGRVPIVAGGTGLYLRWYIYGKPDVPKSSPEITSEVWSELVDFQKNGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 186 WDAAVELVVNAGDPKASSLPRNDWYRLRRSLEILKSTGSPPSSFRIPYDSFRVNLVAPDADDFLEDGSSAdisiqniETD 265
Cdd:PLN02840 157 WDAAVELVVNAGDPKARSLPRNDWYRLRRSLEIIKSSGSPPSAFSLPYDSFREQLVTEDTDSSLEDGSSA-------ETE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 266 LDYDFLCFFLSSPRVALYRSIDFRCEDMLSGPNGVLSEARWLLDLGLLPNSNPATRAIGYRQAMEYLLQCRRYEGESSPR 345
Cdd:PLN02840 230 LDYDFLCFFLSSPRLDLYRSIDLRCEEMLAGTNGILSEASWLLDLGLLPNSNSATRAIGYRQAMEYLLQCRQNGGESSPQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 346 EFYAFLNKFQTASRNFAKRQMTWFRCEPMYHWLNASKPLDSILQCIYDAYESEAEMVEIPESLRMSKDVRDSREASELKG 425
Cdd:PLN02840 310 EFLAFLSKFQTASRNFAKRQMTWFRNEPIYHWLDASQPLEKILQFIYDAYHSRTARVVVPESLRMKKEVSCSRESSELKT 389
|
410 420 430
....*....|....*....|....*....|..
gi 30687613 426 YRSKNRHFVRREDCSSVLEWIRSEGCKSEASC 457
Cdd:PLN02840 390 YRSKNRHFVSREDCSHVLEWIRRTQCKASASC 421
|
|
| MiaA |
COG0324 |
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ... |
52-391 |
4.48e-105 |
|
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: 314.69 E-value: 4.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSDRKVVPHHLIDILHPSQDYSVGQFYDDGRQA 131
Cdd:COG0324 4 LIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPDEEYSVADFQRDARAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 132 TKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPKPSPEVIAEAHDMLvgfqTEYNWDAAVELVVNAgDPK-ASSLPRNDWY 210
Cdd:COG0324 84 IAEILARGKLPILVGGTGLYIKALLEGLSFLPPADPELRAELEAEA----EELGLEALHAELAEL-DPEaAARIHPNDPQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 211 RLRRSLEILKSTGSPPSSFRipydsfrvnlvapdaddfledgssadisiQNIETDLDYDFLCFFLSSPRVALYRSIDFRC 290
Cdd:COG0324 159 RIIRALEVYELTGKPLSELQ-----------------------------KEKKEPPPYDVLKIGLDPDREELYERINRRV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 291 EDMLSgpNGVLSEARWLLDLGLLPNSnPATRAIGYRQAMEYLlqcrryEGESSPREFYAflnKFQTASRNFAKRQMTWFR 370
Cdd:COG0324 210 DQMLE--AGLLDEVRALLARGLDPDL-PAMRAIGYRELLAYL------DGEISLEEAIE---RIKRATRQYAKRQLTWFR 277
|
330 340
....*....|....*....|...
gi 30687613 371 CEPMYHWLNASKP--LDSILQCI 391
Cdd:COG0324 278 RDPDIHWLDPDEPdlLEEILELI 300
|
|
| IPPT |
pfam01715 |
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ... |
85-370 |
2.18e-81 |
|
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: 251.57 E-value: 2.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 85 QVYKGLDVGSAKPSDSDRKVVPHHLIDILHPSQDYSVGQFYDDGRQATKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPK 164
Cdd:pfam01715 1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEEYSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALLDGLDDFPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 165 PSPEVIAEAHDMLvgfqTEYNWDAAVELvVNAGDPK-ASSLPRNDWYRLRRSLEILKSTGSPPSSFRipydsfrvnlvap 243
Cdd:pfam01715 81 ADPELRAELEAEA----AEEGLEALHAE-LAEVDPEaAARIHPNDRRRIIRALEVYELTGKPLSEFQ------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 244 daddfledgssadisiQNIETDLDYDFLCFFLsSPRVALYRSIDFRCEDMLSgpNGVLSEARWLLDLGLLPNsNPATRAI 323
Cdd:pfam01715 143 ----------------EPEKPPPPYDTLIIGL-SDREELYERINARVDAMLE--AGLLEEVRALLDRGYGGD-LPAMQAI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 30687613 324 GYRQAMEYLlqcrryEGESSPREfyaFLNKFQTASRNFAKRQMTWFR 370
Cdd:pfam01715 203 GYKELLAYL------DGEISLEE---AIELIKRATRQYAKRQLTWFR 240
|
|
| miaA |
TIGR00174 |
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ... |
52-383 |
6.92e-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: 244.22 E-value: 6.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSDRKVVPHHLIDILHPSQDYSVGQFYDDGRQA 131
Cdd:TIGR00174 1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDPSESYSAADFQTQALNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 132 TKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPKPSPEVIAEAhDMLVGFQTeynWDAAVELVVNAgDP-KASSLPRNDWY 210
Cdd:TIGR00174 81 IADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQL-EILAEEQG---WDFLYNELKKV-DPvAAAKIHPNDTR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 211 RLRRSLEILKSTGSPPSSFripydsfrvnlvapdaddFLEDGSSadisiqnietdLDYDFLCFFLSSPRVALYRSIDFRC 290
Cdd:TIGR00174 156 RVQRALEVFYATGKPPSEL------------------FKEQKIE-----------LFYDIVQIGLASSREPLHQRIEQRV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 291 EDMLSgpNGVLSEARWLLDLGLLPNsNPATRAIGYRQAMEYLlqcrryEGESSPREFYAFLNkfqTASRNFAKRQMTWFR 370
Cdd:TIGR00174 207 HDMLE--SGLLAEVKALYAQYDLCD-LPSIQAIGYKEFLLYL------EGTVSLEDAIERIK---CNTRQYAKRQLTWFR 274
|
330
....*....|...
gi 30687613 371 CEPMYHWLNASKP 383
Cdd:TIGR00174 275 KWSDVLWLDSTDP 287
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
52-84 |
9.55e-04 |
|
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: 39.54 E-value: 9.55e-04
10 20 30
....*....|....*....|....*....|...
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSV 84
Cdd:cd02021 1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDL 33
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02840 |
PLN02840 |
tRNA dimethylallyltransferase |
26-457 |
0e+00 |
|
tRNA dimethylallyltransferase
Pssm-ID: 215451 Cd Length: 421 Bit Score: 793.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 26 RRFCAATTACSVPlngnKKKKSEKEKVIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSDRKVV 105
Cdd:PLN02840 1 RRFCAATTALSGS----GASKTKKEKVIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSLSERKEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 106 PHHLIDILHPSQDYSVGQFYDDGRQATKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPKPSPEVIAEAHDMLVGFQTEYN 185
Cdd:PLN02840 77 PHHLIDILHPSDDYSVGAFFDDARRATQDILNRGRVPIVAGGTGLYLRWYIYGKPDVPKSSPEITSEVWSELVDFQKNGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 186 WDAAVELVVNAGDPKASSLPRNDWYRLRRSLEILKSTGSPPSSFRIPYDSFRVNLVAPDADDFLEDGSSAdisiqniETD 265
Cdd:PLN02840 157 WDAAVELVVNAGDPKARSLPRNDWYRLRRSLEIIKSSGSPPSAFSLPYDSFREQLVTEDTDSSLEDGSSA-------ETE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 266 LDYDFLCFFLSSPRVALYRSIDFRCEDMLSGPNGVLSEARWLLDLGLLPNSNPATRAIGYRQAMEYLLQCRRYEGESSPR 345
Cdd:PLN02840 230 LDYDFLCFFLSSPRLDLYRSIDLRCEEMLAGTNGILSEASWLLDLGLLPNSNSATRAIGYRQAMEYLLQCRQNGGESSPQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 346 EFYAFLNKFQTASRNFAKRQMTWFRCEPMYHWLNASKPLDSILQCIYDAYESEAEMVEIPESLRMSKDVRDSREASELKG 425
Cdd:PLN02840 310 EFLAFLSKFQTASRNFAKRQMTWFRNEPIYHWLDASQPLEKILQFIYDAYHSRTARVVVPESLRMKKEVSCSRESSELKT 389
|
410 420 430
....*....|....*....|....*....|..
gi 30687613 426 YRSKNRHFVRREDCSSVLEWIRSEGCKSEASC 457
Cdd:PLN02840 390 YRSKNRHFVSREDCSHVLEWIRRTQCKASASC 421
|
|
| MiaA |
COG0324 |
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ... |
52-391 |
4.48e-105 |
|
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: 314.69 E-value: 4.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSDRKVVPHHLIDILHPSQDYSVGQFYDDGRQA 131
Cdd:COG0324 4 LIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPDEEYSVADFQRDARAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 132 TKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPKPSPEVIAEAHDMLvgfqTEYNWDAAVELVVNAgDPK-ASSLPRNDWY 210
Cdd:COG0324 84 IAEILARGKLPILVGGTGLYIKALLEGLSFLPPADPELRAELEAEA----EELGLEALHAELAEL-DPEaAARIHPNDPQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 211 RLRRSLEILKSTGSPPSSFRipydsfrvnlvapdaddfledgssadisiQNIETDLDYDFLCFFLSSPRVALYRSIDFRC 290
Cdd:COG0324 159 RIIRALEVYELTGKPLSELQ-----------------------------KEKKEPPPYDVLKIGLDPDREELYERINRRV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 291 EDMLSgpNGVLSEARWLLDLGLLPNSnPATRAIGYRQAMEYLlqcrryEGESSPREFYAflnKFQTASRNFAKRQMTWFR 370
Cdd:COG0324 210 DQMLE--AGLLDEVRALLARGLDPDL-PAMRAIGYRELLAYL------DGEISLEEAIE---RIKRATRQYAKRQLTWFR 277
|
330 340
....*....|....*....|...
gi 30687613 371 CEPMYHWLNASKP--LDSILQCI 391
Cdd:COG0324 278 RDPDIHWLDPDEPdlLEEILELI 300
|
|
| IPPT |
pfam01715 |
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ... |
85-370 |
2.18e-81 |
|
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: 251.57 E-value: 2.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 85 QVYKGLDVGSAKPSDSDRKVVPHHLIDILHPSQDYSVGQFYDDGRQATKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPK 164
Cdd:pfam01715 1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEEYSVADFQRDALAAIEEIHARGKLPILVGGTGLYLKALLDGLDDFPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 165 PSPEVIAEAHDMLvgfqTEYNWDAAVELvVNAGDPK-ASSLPRNDWYRLRRSLEILKSTGSPPSSFRipydsfrvnlvap 243
Cdd:pfam01715 81 ADPELRAELEAEA----AEEGLEALHAE-LAEVDPEaAARIHPNDRRRIIRALEVYELTGKPLSEFQ------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 244 daddfledgssadisiQNIETDLDYDFLCFFLsSPRVALYRSIDFRCEDMLSgpNGVLSEARWLLDLGLLPNsNPATRAI 323
Cdd:pfam01715 143 ----------------EPEKPPPPYDTLIIGL-SDREELYERINARVDAMLE--AGLLEEVRALLDRGYGGD-LPAMQAI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 30687613 324 GYRQAMEYLlqcrryEGESSPREfyaFLNKFQTASRNFAKRQMTWFR 370
Cdd:pfam01715 203 GYKELLAYL------DGEISLEE---AIELIKRATRQYAKRQLTWFR 240
|
|
| miaA |
TIGR00174 |
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ... |
52-383 |
6.92e-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: 244.22 E-value: 6.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSDRKVVPHHLIDILHPSQDYSVGQFYDDGRQA 131
Cdd:TIGR00174 1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDPSESYSAADFQTQALNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 132 TKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPKPSPEVIAEAhDMLVGFQTeynWDAAVELVVNAgDP-KASSLPRNDWY 210
Cdd:TIGR00174 81 IADITARGKIPLLVGGTGLYLKALLEGLSPTPSADKLIREQL-EILAEEQG---WDFLYNELKKV-DPvAAAKIHPNDTR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 211 RLRRSLEILKSTGSPPSSFripydsfrvnlvapdaddFLEDGSSadisiqnietdLDYDFLCFFLSSPRVALYRSIDFRC 290
Cdd:TIGR00174 156 RVQRALEVFYATGKPPSEL------------------FKEQKIE-----------LFYDIVQIGLASSREPLHQRIEQRV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 291 EDMLSgpNGVLSEARWLLDLGLLPNsNPATRAIGYRQAMEYLlqcrryEGESSPREFYAFLNkfqTASRNFAKRQMTWFR 370
Cdd:TIGR00174 207 HDMLE--SGLLAEVKALYAQYDLCD-LPSIQAIGYKEFLLYL------EGTVSLEDAIERIK---CNTRQYAKRQLTWFR 274
|
330
....*....|...
gi 30687613 371 CEPMYHWLNASKP 383
Cdd:TIGR00174 275 KWSDVLWLDSTDP 287
|
|
| PLN02748 |
PLN02748 |
tRNA dimethylallyltransferase |
52-227 |
1.28e-25 |
|
tRNA dimethylallyltransferase
Pssm-ID: 215399 [Multi-domain] Cd Length: 468 Bit Score: 108.82 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSDRKVVPHHLIDILHPSQDYSVGQFYDDGRQA 131
Cdd:PLN02748 24 VVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSVEFTAKDFRDHAVPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 132 TKDILNRGRVPIVTGGTGLYLRW----FMYGKP-----DVPKPSPEVIAEAHDMLVGFQTEyNWDAAVELVVNAGDPKAS 202
Cdd:PLN02748 104 IEEILSRNGLPVIVGGTNYYIQAlvspFLLDDMaeeteDCTFVVASVLDEHMDVESGLGND-DEDHGYELLKELDPVAAN 182
|
170 180
....*....|....*....|....*
gi 30687613 203 SLPRNDWYRLRRSLEILKSTGSPPS 227
Cdd:PLN02748 183 RIHPNNHRKINRYLELYATTGVLPS 207
|
|
| PLN02165 |
PLN02165 |
adenylate isopentenyltransferase |
15-152 |
2.79e-23 |
|
adenylate isopentenyltransferase
Pssm-ID: 177823 Cd Length: 334 Bit Score: 100.29 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687613 15 LRLQPPSLVLRrrfcaaTTACSVPLNGNKKkksekekVIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGS 94
Cdd:PLN02165 21 RKLPPPRSVVT------MTSVAMEQNCKDK-------VVVIMGATGSGKSRLSVDLATRFPSEIINSDKMQVYDGLKITT 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30687613 95 AKPSDSDRKVVPHHLIDILHPSQ-DYSVGQFYDDGRQATKDILNRGRVPIVTGGTGLYL 152
Cdd:PLN02165 88 NQITIQDRRGVPHHLLGELNPDDgELTASEFRSLASLSISEITSRQKLPIVAGGSNSFI 146
|
|
| IPT |
pfam01745 |
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes ... |
55-101 |
1.16e-05 |
|
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: 46.62 E-value: 1.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 30687613 55 ISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSD 101
Cdd:pfam01745 6 IWGATCTGKTAEAIALAKETGWPVIVLDRVQCCSQLATGSGRPLPAE 52
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
52-84 |
3.20e-05 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 44.13 E-value: 3.20e-05
10 20 30
....*....|....*....|....*....|...
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSV 84
Cdd:COG0645 1 LILVCGLPGSGKSTLARALAERLGAVRLRSDVV 33
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
52-114 |
1.39e-04 |
|
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: 41.91 E-value: 1.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSV--QVYkGLDVGSAKPSDSDRKVVPHHLIDILH 114
Cdd:pfam13671 1 LILLVGLPGSGKSTLARRLLEELGAVRLSSDDErkRLF-GEGRPSISYYTDATDRTYERLHELAR 64
|
|
| Pgk2 |
COG2074 |
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ... |
52-84 |
2.68e-04 |
|
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 441677 Cd Length: 207 Bit Score: 42.24 E-value: 2.68e-04
10 20 30
....*....|....*....|....*....|....
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLN-GEIISADSV 84
Cdd:COG2074 8 IILIGGASGVGKSTIAAELARRLGiPRVISTDSI 41
|
|
| cyt_kin_arch |
TIGR02173 |
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ... |
52-81 |
7.90e-04 |
|
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.
Pssm-ID: 274012 [Multi-domain] Cd Length: 171 Bit Score: 40.10 E-value: 7.90e-04
10 20 30
....*....|....*....|....*....|
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISA 81
Cdd:TIGR02173 2 IITISGPPGSGKTTVAKILAEKLSLKLISA 31
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
52-84 |
9.55e-04 |
|
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: 39.54 E-value: 9.55e-04
10 20 30
....*....|....*....|....*....|...
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSV 84
Cdd:cd02021 1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDL 33
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
52-82 |
1.11e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 39.39 E-value: 1.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLN------GEIISAD 82
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLAKKLGlpyldtGGIRTEE 37
|
|
| Dck |
COG1428 |
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]; |
52-79 |
2.00e-03 |
|
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
Pssm-ID: 441037 [Multi-domain] Cd Length: 205 Bit Score: 39.38 E-value: 2.00e-03
10 20
....*....|....*....|....*...
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEII 79
Cdd:COG1428 5 YIAVEGNIGAGKTTLARLLAEHLGAELL 32
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
52-79 |
2.31e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 39.04 E-value: 2.31e-03
10 20 30
....*....|....*....|....*....|...
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLN-----GEII 79
Cdd:COG1102 2 VITISREPGSGGTTIAKRLAEKLGlplydGEIL 34
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
52-84 |
2.89e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 38.63 E-value: 2.89e-03
10 20 30
....*....|....*....|....*....|...
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISADSV 84
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEI 34
|
|
| HprK_C |
cd01918 |
HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the ... |
53-112 |
3.96e-03 |
|
HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of Ser-46 of HPr and its dephosphorylation by phosphorolysis. The latter reaction uses inorganic phosphate as substrate and produces pyrophosphate. Phosphoenolpyruvate carboxykinase (PEPCK) and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting these two phosphotransferases have related functions. The HprK/P N-terminal domain is structurally similar to the N-terminal domains of the MurE and MurF amino acid ligases.
Pssm-ID: 238899 Cd Length: 149 Bit Score: 37.60 E-value: 3.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30687613 53 IVISGPTGAGKSRLAMELAKRlNGEIISADSVQVYKGLD--VGSAKPsdsdrkvVPHHLIDI 112
Cdd:cd01918 17 VLITGPSGIGKSELALELIKR-GHRLVADDRVVVKREGGrlVGRAPE-------ALKGLIEI 70
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
52-83 |
5.38e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 38.28 E-value: 5.38e-03
10 20 30
....*....|....*....|....*....|....*
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGE---IISADS 83
Cdd:COG0572 9 IIGIAGPSGSGKTTFARRLAEQLGADkvvVISLDD 43
|
|
| PRK04220 |
PRK04220 |
2-phosphoglycerate kinase; Provisional |
52-84 |
6.33e-03 |
|
2-phosphoglycerate kinase; Provisional
Pssm-ID: 179793 [Multi-domain] Cd Length: 301 Bit Score: 38.41 E-value: 6.33e-03
10 20 30
....*....|....*....|....*....|....
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLN-GEIISADSV 84
Cdd:PRK04220 94 IILIGGASGVGTSTIAFELASRLGiRSVIGTDSI 127
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
52-93 |
9.02e-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: 9.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 30687613 52 VIVISGPTGAGKSRLAMELAKRLNGEIISA-DSVQVYKGLDVG 93
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVlDEIVILEGLYAS 43
|
|
| |
