|
Name |
Accession |
Description |
Interval |
E-value |
| aroK |
PRK05057 |
shikimate kinase AroK; |
1-170 |
1.72e-112 |
|
shikimate kinase AroK;
Pssm-ID: 235335 [Multi-domain] Cd Length: 172 Bit Score: 317.04 E-value: 1.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 1 MAEKRNIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLST 80
Cdd:PRK05057 1 MAEKRNIFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADIGWVFDVEGEEGFRDREEKVINELTEKQGIVLAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 81 GGGAVLSKENRNHLSARGIVIYLETTVEKQYQRTQRDKKRPLLQeVEDPRQVLEDLAKIRNPLYEEIADITLPTDEQSAK 160
Cdd:PRK05057 81 GGGSVKSRETRNRLSARGVVVYLETTIEKQLARTQRDKKRPLLQ-VDDPREVLEALANERNPLYEEIADVTIRTDDQSAK 159
|
170
....*....|
gi 492014357 161 VMATQIVDLI 170
Cdd:PRK05057 160 VVANQIIHML 169
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
1-174 |
1.84e-92 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 266.28 E-value: 1.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 1 MAEKRNIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLST 80
Cdd:PRK00131 1 MLKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELEEEVLAELLARHNLVIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 81 GGGAVLSKENRNHLSARGIVIYLETTVEKQYQRTQRDKKRPLLQeVEDPRQVLEDLAKIRNPLYEEIADITLPTDEQSAK 160
Cdd:PRK00131 81 GGGAVLREENRALLRERGTVVYLDASFEELLRRLRRDRNRPLLQ-TNDPKEKLRDLYEERDPLYEEVADITVETDGRSPE 159
|
170
....*....|....
gi 492014357 161 VMATQIVDLIDNLH 174
Cdd:PRK00131 160 EVVNEILEKLEAAW 173
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
7-170 |
1.05e-82 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 241.19 E-value: 1.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGAVL 86
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENAVIATGGGAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 87 SKENRNHLSARGIVIYLETTVEKQYQRTQRDKKRPLLQeVEDPRQVLEDLAKIRNPLYEEIADITLPTDEQSAKVMATQI 166
Cdd:COG0703 81 SPENRELLKEHGTVVYLDASPETLLERLRRDDNRPLLQ-GEDPRERLEELLAEREPLYREVADITVDTDGRSPEEVVDEI 159
|
....
gi 492014357 167 VDLI 170
Cdd:COG0703 160 LEAL 163
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
13-170 |
3.17e-71 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 212.06 E-value: 3.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 13 MGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGAVLSKENRN 92
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEHGLVIATGGGAVLSEENRD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492014357 93 HLSARGIVIYLETTVEKQYQRTQRDKKRPLLQEVEDPRQVLEDLAKIRNPLYEEIADITLPTDEQSAKVMATQIVDLI 170
Cdd:pfam01202 81 LLKERGIVIYLDAPLEVLLERLKRDKTRPLLQNKDPEEELLELLFEERDPLYEEAADIVIDTDESSPEEVATEILEAL 158
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
6-158 |
8.89e-69 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 205.87 E-value: 8.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 6 NIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGAV 85
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKENAVIATGGGAV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492014357 86 LSKENRNHLSARGIVIYLETTVEKQYQRTQRDKKRPLLQevEDPRQVLEDLAKIRNPLYEEIADITLPTDEQS 158
Cdd:cd00464 81 LREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQ--DEDPERLRELLEEREPLYREVADLTIDTDELS 151
|
|
| PRK13946 |
PRK13946 |
shikimate kinase; Provisional |
4-172 |
7.06e-51 |
|
shikimate kinase; Provisional
Pssm-ID: 184411 [Multi-domain] Cd Length: 184 Bit Score: 161.25 E-value: 7.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 4 KRNIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGG 83
Cdd:PRK13946 10 KRTVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEIERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGPLVLATGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 84 AVLSKENRNHLSARGIVIYLETTVEKQYQRTQRDKKRPLLQeVEDPRQVLEDLAKIRNPLYEEiADITLPTDEQSAKVMA 163
Cdd:PRK13946 90 AFMNEETRAAIAEKGISVWLKADLDVLWERVSRRDTRPLLR-TADPKETLARLMEERYPVYAE-ADLTVASRDVPKEVMA 167
|
....*....
gi 492014357 164 TQIVDLIDN 172
Cdd:PRK13946 168 DEVIEALAA 176
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
5-175 |
1.57e-38 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 129.44 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 5 RNIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGA 84
Cdd:PRK13947 2 KNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARLKNLVIATGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 85 VLSKENRNHLSARGIVIYLETTVEKQYQRTQRDKKRPLLQeVEDPRQVLEDLAKIRNPLYeEIADITLPTDEQSAKVMAT 164
Cdd:PRK13947 82 VLNPENVVQLRKNGVVICLKARPEVILRRVGKKKSRPLLM-VGDPEERIKELLKEREPFY-DFADYTIDTGDMTIDEVAE 159
|
170
....*....|.
gi 492014357 165 QIVDLIDNLHG 175
Cdd:PRK13947 160 EIIKAYLKLKN 170
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
7-170 |
8.89e-36 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 122.36 E-value: 8.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQrQGIVLSTGGGAVL 86
Cdd:PRK03731 5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARESAALEAVTA-PSTVIATGGGIIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 87 SKENRNHLSARGIVIYLETTVEKQYQRTQRDKK---------RPLLQEVEDprqVLEDlakiRNPLYEEIADITLPTDeQ 157
Cdd:PRK03731 84 TEENRHFMRNNGIVIYLCAPVSVLANRLEANPEedqrptltgKPISEEVAE---VLAE----REALYREVAHHIIDAT-Q 155
|
170
....*....|...
gi 492014357 158 SAKVMATQIVDLI 170
Cdd:PRK03731 156 PPSQVVSEILSAL 168
|
|
| PRK13948 |
PRK13948 |
shikimate kinase; Provisional |
9-168 |
6.57e-33 |
|
shikimate kinase; Provisional
Pssm-ID: 184413 [Multi-domain] Cd Length: 182 Bit Score: 115.66 E-value: 6.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 9 LIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGAVLSK 88
Cdd:PRK13948 15 LAGFMGTGKSRIGWELSRALMLHFIDTDRYIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLTRLDYAVISLGGGTFMHE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 89 ENRNHLSARGIVIYLETTVEKQYQRTqRDKKRPLLQeVEDPRQVLEDLAKIRNPLYEEiADITLPTDEQSAKVMATQIVD 168
Cdd:PRK13948 95 ENRRKLLSRGPVVVLWASPETIYERT-RPGDRPLLQ-VEDPLGRIRTLLNEREPVYRQ-ATIHVSTDGRRSEEVVEEIVE 171
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
5-173 |
1.30e-30 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 109.05 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 5 RNIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGA 84
Cdd:PRK13949 2 ARIFLVGYMGAGKTTLGKALARELGLSFIDLDFFIENRFHKTVGDIFAERGEAVFRELERNMLHEVAEFEDVVISTGGGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 85 VLSKENRNHLSARGIVIYLETTVEKQYQRTQRDKK-RPLLQEVEDPR---QVLEDLAKiRNPLYEEiADITLPTDEQsak 160
Cdd:PRK13949 82 PCFFDNMELMNASGTTVYLKVSPEVLFVRLRLAKQqRPLLKGKSDEElldFIIEALEK-RAPFYRQ-AKIIFNADKL--- 156
|
170
....*....|...
gi 492014357 161 VMATQIVDLIDNL 173
Cdd:PRK13949 157 EDESQIEQLVQRL 169
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
7-162 |
1.66e-27 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 106.91 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGAVL 86
Cdd:PRK13951 3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEIERREGRSVRRIFEEDGEEYFRLKEKELLRELVERDNVVVATGGGVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 87 SKENRNHLSARGiVIYLETTVEKQYQRTQRDkKRPLLQE-VEDPRQVLEDlakiRNPLYEEI--ADITLPTD-EQSAKVM 162
Cdd:PRK13951 83 DPENRELLKKEK-TLFLYAPPEVLMERVTTE-NRPLLREgKERIREIWER----RKQFYTEFrgIDTSKLNEwETTALVV 156
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
9-171 |
3.41e-26 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 103.79 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 9 LIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGAVLSK 88
Cdd:PRK14021 11 IIGMMGAGKTRVGKEVAQMMRLPFADADVEIEREIGMSIPSYFEEYGEPAFREVEADVVADMLEDFDGIFSLGGGAPMTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 89 ENRNHLSAR----GIVIYLETTVEKQYQRTQRDKKRPLLQevEDPRQVLEDLAKIRNPLYEEIADITLPTDEQSAKVMAT 164
Cdd:PRK14021 91 STQHALASYiahgGRVVYLDADPKEAMERANRGGGRPMLN--GDANKRWKKLFKQRDPVFRQVANVHVHTRGLTPQAAAK 168
|
....*..
gi 492014357 165 QIVDLID 171
Cdd:PRK14021 169 KLIDMVA 175
|
|
| PRK08154 |
PRK08154 |
anaerobic benzoate catabolism transcriptional regulator; Reviewed |
2-170 |
9.93e-26 |
|
anaerobic benzoate catabolism transcriptional regulator; Reviewed
Pssm-ID: 236167 [Multi-domain] Cd Length: 309 Bit Score: 100.03 E-value: 9.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 2 AEKRNIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQG-IVLST 80
Cdd:PRK08154 131 ARRRRIALIGLRGAGKSTLGRMLAARLGVPFVELNREIEREAGLSVSEIFALYGQEGYRRLERRALERLIAEHEeMVLAT 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 81 GGGAVLSKENRNHLSARGIVIYLETTVEKQYQRT--QRDkKRPLlqevEDPRQVLEDLAKI---RNPLYEEiADITLPTD 155
Cdd:PRK08154 211 GGGIVSEPATFDLLLSHCYTVWLKASPEEHMARVraQGD-LRPM----ADNREAMEDLRRIlasREPLYAR-ADAVVDTS 284
|
170
....*....|....*
gi 492014357 156 EQSAKVMATQIVDLI 170
Cdd:PRK08154 285 GLTVAQSLARLRELV 299
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
5-125 |
1.34e-19 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 83.59 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 5 RNIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRA-GADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGG 83
Cdd:PLN02199 103 RSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQAMnGTSVAEIFVHHGENFFRGKETDALKKLSSRYQVVVSTGGG 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 492014357 84 AVLSKENRNHLSaRGIVIYLETTVEKQYQRTQR--DKKRPLLQE 125
Cdd:PLN02199 183 AVIRPINWKYMH-KGISIWLDVPLEALAHRIAAvgTDSRPLLHD 225
|
|
| PRK00625 |
PRK00625 |
shikimate kinase; Provisional |
6-156 |
2.18e-14 |
|
shikimate kinase; Provisional
Pssm-ID: 134335 [Multi-domain] Cd Length: 173 Bit Score: 67.09 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 6 NIFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADI----SWIFDVEGEDGFRKREERIINELTQRQGIVlSTG 81
Cdd:PRK00625 2 QIFLCGLPTVGKTSFGKALAKFLSLPFFDTDDLIVSNYHGALysspKEIYQAYGEEGFCREEFLALTSLPVIPSIV-ALG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492014357 82 GGAVLSKENRNHLSARGIVIYLETTVEKQYQRTQrdkKRPLLQEVEDPRQvLEDLAKIRNPLYEEIADITLPTDE 156
Cdd:PRK00625 81 GGTLMIEPSYAHIRNRGLLVLLSLPIATIYQRLQ---KRGLPERLKHAPS-LEEILSQRIDRMRSIADYIFSLDH 151
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
7-136 |
2.79e-07 |
|
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: 47.30 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISWIfdvegeDGFRKREERIINELTQRQGIVLSTGGGAV- 85
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEGRPSI------SYYTDATDRTYERLHELARIALRAGRPVIl 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492014357 86 ----LSKENR-------NHLSARGIVIYLETTVEKQYQRT-QRDKKRPLLQEVedPRQVLEDL 136
Cdd:pfam13671 76 datnLRRDERarllalaREYGVPVRIVVFEAPEEVLRERLaARARAGGDPSDV--PEEVLDRQ 136
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
11-95 |
1.34e-06 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 46.36 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 11 GPMGAGKSTIGRQLAQLLSMDFVDSD--NEIEQRAGADISWI------------FDVEGEDGFRKREERIINELTQRQGI 76
Cdd:COG1102 7 REPGSGGTTIAKRLAEKLGLPLYDGEilREAAKERGLSEEEFekldekapsllyRDTAEEDEIDRALDKVIRELARKGNC 86
|
90
....*....|....*....
gi 492014357 77 VLSTGGGAVLSKENRNHLS 95
Cdd:COG1102 87 VIVGRLADWILRDRPNVLK 105
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
7-132 |
2.55e-06 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 44.73 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEqragADISWIFDVEGEDGFRKREERIINELTQRQGIVLSTGGGAVL 86
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALE----NGLVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGNLI 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 492014357 87 SKENRNHLSARGIV----IYLETTVEKQYQR-TQRDKKRPLLQEVEDPRQV 132
Cdd:pfam13238 77 IDGHLAELEPERAKdlvgIVLRASPEELLERlEKRGYEEAKIKENEEAEIL 127
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
7-121 |
5.26e-06 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 44.13 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLAQLLSMDFVDSDNEIEQRAGADISwifdveGEDGFRKREERIINELTQRQGIVLSTGGGAVL 86
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRLRSDVVRKRLFGAGLA------PLERSPEATARTYARLLALARELLAAGRSVIL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 492014357 87 -----SKENRNHL----SARGI---VIYLETTVEKQYQR-TQRDKKRP 121
Cdd:COG0645 76 datflRRAQREAFralaEEAGApfvLIWLDAPEEVLRERlEARNAEGG 123
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
7-36 |
2.15e-05 |
|
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: 42.24 E-value: 2.15e-05
10 20 30
....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLAQLLSMDFVDSD 36
Cdd:cd02021 2 IVVMGVSGSGKSTVGKALAERLGAPFIDGD 31
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
11-155 |
8.13e-05 |
|
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: 40.55 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 11 GPMGAGKSTIGRQLAQLLSMDFVDS----DNEIEQRAGAdISWIFDVegedgfRKREERIINELTQRQGIVL-STGGGAV 85
Cdd:cd02020 6 GPAGSGKSTVAKLLAKKLGLPYLDTggirTEEVGKLASE-VAAIPEV------RKALDERQRELAKKPGIVLeGRDIGTV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492014357 86 LSKENRnhlsargIVIYLETTVEKQYQRtqRDKKRPLLQEVEDPRQVLEDLAKiR---------NPLYEEIADITLPTD 155
Cdd:cd02020 79 VFPDAD-------LKIFLTASPEVRAKR--RAKQLQAKGEGVDLEEILAEIIE-RderdstryvAPLKLAEDAIVIDTS 147
|
|
| Cytidylate_kin2 |
pfam13189 |
Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase. |
13-97 |
1.91e-04 |
|
Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase.
Pssm-ID: 433023 [Multi-domain] Cd Length: 176 Bit Score: 39.92 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 13 MGAGKSTIGRQLAQLLSMDFVDSD--NEIEQRAGADISWI----------------------FDVEGEDGFRKREERIIN 68
Cdd:pfam13189 8 YGSGGTTIAKKLAEKLGYPFYDREilDEIAKELGISEEEFelfdeksrlssflyslaggrvrGDALSDDRLFDAQSKVIR 87
|
90 100 110
....*....|....*....|....*....|
gi 492014357 69 ELT-QRQGIVLSTGGGAVLsKENRNHLSAR 97
Cdd:pfam13189 88 ELAaEDNCVIVGRGADYIL-KDIPNVLRVF 116
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
7-36 |
1.97e-04 |
|
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: 39.73 E-value: 1.97e-04
10 20 30
....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLAQLLSMDFVDSD 36
Cdd:COG3265 4 IVVMGVSGSGKSTVGQALAERLGWPFIDGD 33
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
4-78 |
8.14e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 4 KRNIFLIGPMGAGKSTIGRQLAQLLSMD-----FVDSDNEIEQRAGADISWIFDVEGEDGFRKREERIINELTQRQGIVL 78
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgggviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
7-28 |
9.00e-04 |
|
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: 36.16 E-value: 9.00e-04
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
5-56 |
1.03e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 38.77 E-value: 1.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 492014357 5 RNIFLIGPMGAGKSTigrqLAQLLSMDFvdsdneieQRAGADIsWIFDVEGE 56
Cdd:COG3451 205 GNTLILGPSGSGKSF----LLKLLLLQL--------LRYGARI-VIFDPGGS 243
|
|
| Cmk |
COG0283 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
11-35 |
1.27e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440052 [Multi-domain] Cd Length: 220 Bit Score: 38.08 E-value: 1.27e-03
10 20
....*....|....*....|....*
gi 492014357 11 GPMGAGKSTIGRQLAQLLSMDFVDS 35
Cdd:COG0283 7 GPAGSGKSTVAKALAKRLGYHYLDT 31
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
1-78 |
2.61e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 36.88 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 1 MAEKRnIFLIGPMGAGKSTIGRQLAQllsmDFVDSDNE---IeqraGADIS-------------WIFDVEGEDGFRKREE 64
Cdd:COG1100 1 MGEKK-IVVVGTGGVGKTSLVNRLVG----DIFSLEKYlstN----GVTIDkkelkldgldvdlVIWDTPGQDEFRETRQ 71
|
90
....*....|....
gi 492014357 65 RIINELTQRQGIVL 78
Cdd:COG1100 72 FYARQLTGASLYLF 85
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
5-33 |
3.85e-03 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU 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: 410906 [Multi-domain] Cd Length: 183 Bit Score: 36.20 E-value: 3.85e-03
10 20
....*....|....*....|....*....
gi 492014357 5 RNIFLIGPMGAGKSTIGRQLAQLLSMDFV 33
Cdd:cd19498 47 KNILMIGPTGVGKTEIARRLAKLAGAPFI 75
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
7-146 |
4.95e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 35.58 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492014357 7 IFLIGPMGAGKSTIGRQLA---QLLSMDFVD---SDNEIEQRAGADIswifdvegedgFRKREERIINELTQRQGIVL-S 79
Cdd:COG4639 5 VVLIGLPGSGKSTFARRLFaptEVVSSDDIRallGGDENDQSAWGDV-----------FQLAHEIARARLRAGRLTVVdA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492014357 80 TGggavLSKENRNHL-------SARGIVIYLETTVEKQYQRtQRDKKRPLlqevedPRQVLEDLAKI--RNPLYEE 146
Cdd:COG4639 74 TN----LQREARRRLlalarayGALVVAVVLDVPLEVCLAR-NAARDRQV------PEEVIRRMLRRlrRPPLPEE 138
|
|
|