|
Name |
Accession |
Description |
Interval |
E-value |
| Thr-synth_2 |
cd01560 |
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ... |
230-733 |
0e+00 |
|
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.
Pssm-ID: 107203 [Multi-domain] Cd Length: 460 Bit Score: 556.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 230 TFISTRHVClkdhdkkfPPKYFSEAVVEGLASDGGLFVPEKgFPKPSLGEWTNLIGATYIERAQVLLERCIhPADIPAAK 309
Cdd:cd01560 1 KYVSTRGGN--------PGVSFSEALLSGLAPDGGLYVPEE-LPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 310 LGEMIETAYGEsFACSKVAPVRHLSGNQFILELFYGPTGSFKDLSLQLMPHIFAYCIPP-GCNYVLLVATSGDTGSAVLN 388
Cdd:cd01560 71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 389 GFSrlnrsDKERIAVLTFFPENGVSDFQRAEIVGSQRENGWAIGVKSDFDFCQAAIRKIFNDSDFTgfltveYGVVLSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 469 NSINWARLLPQVVYHASAYLELVSQGFisfGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNHVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKRGE---GEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 549 YDLRnRRLAQTFSPSINILKSSNLERHLYLMANKDGQLMADLYNQLESQLHFQIEELLVEKLQQDFVADWCSEGECLEAI 628
Cdd:cd01560 296 YDRR-ESLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 629 STTYNTSGYILDPHTAVAKVVADKMQDK-SCPVVIASTAHYSKFAPVVLQALRIKElnqtsasqlyllssynalPPPHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEP------------------VELPEE 436
|
490 500
....*....|....*....|....*.
gi 60551777 708 LLERMKQKGKmdYQACVADVDVLKSH 733
Cdd:cd01560 437 LEGLEDLEKR--HEDLLADKELLKSH 460
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
251-682 |
3.39e-64 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 218.92 E-value: 3.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 251 FSEAVVEGLASDGGLfVPEKgFPKPSLGEWTNLIG-ATYIEraqVLLERCIHPAdipaaklgemieTAYGESFA----CS 325
Cdd:COG0498 11 FSDALLYLCPDCGGL-LPDS-YPALSREDLASRRGlWRYRE---LLPFDDEEKA------------VSLGEGGTplvkAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 326 KVApvRHLSGNQFILELFYGPTGSFKDLSLQLMPHIFAYCippGCnYVLLVATSGdTGSAVLNGFsrlnrSDKERIAVLT 405
Cdd:COG0498 74 RLA--DELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALER---GA-KTIVCASSG-NGSAALAAY-----AARAGIEVFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 406 FFPENGVSDFQRAEIV--GSQrengwAIGVKSDFDFCQAAIRKIFNDSDFtgfltveygvvlSSANSINWARLLPQVVYh 483
Cdd:COG0498 142 FVPEGKVSPGQLAQMLtyGAH-----VIAVDGNFDDAQRLVKELAADEGL------------YAVNSINPARLEGQKTY- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 484 asaYLELVSQgfisFGSPVD-VCIPTGNFGNILAAVYAKMM----GIPIR--KFI--CASNQNHVLTDFiKTGHYDLRNR 554
Cdd:COG0498 204 ---AFEIAEQ----LGRVPDwVVVPTGNGGNILAGYKAFKElkelGLIDRlpRLIavQATGCNPILTAF-ETGRDEYEPE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 555 RlAQTFSPSINILKSSNLERHLYLMANKDGqlmadlynqlesqlhfqieellveklqqdfVADWCSEGECLEAISTTYNT 634
Cdd:COG0498 276 R-PETIAPSMDIGNPSNGERALFALRESGG------------------------------TAVAVSDEEILEAIRLLARR 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 60551777 635 SGYILDPHTAVA-----KVVADKMQDKSCPVVIASTAHYSKFAPVVLQALRIK 682
Cdd:COG0498 325 EGIFVEPATAVAvaglrKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
57-204 |
2.01e-38 |
|
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: 140.00 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 57 NIVLMGPPGAGKTTVGRILGDKLGCCVIDVDaDVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFAS-GSVISLSGSN 135
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLD-ELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60551777 136 PMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRVDRIVGRNTGTSLRDLLKHGKLHYRKWYDARVFCE 204
Cdd:cd00464 80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD 148
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
64-221 |
3.68e-38 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 139.25 E-value: 3.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 64 PGAGKTTVGRILGDKLGCCVIDVDaDVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFAS-GSVISLSGSNPMHDASM 142
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTD-EEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEhGLVIATGGGAVLSEENR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 143 WHLKKNGIVVYLDVPLTDIISRLKsMRVDRIV--GRNTGTSLRDLLKHGKLH-YRKwYDARVFCESGASAEEVADKVLDV 219
Cdd:pfam01202 80 DLLKERGIVIYLDAPLEVLLERLK-RDKTRPLlqNKDPEEELLELLFEERDPlYEE-AADIVIDTDESSPEEVATEILEA 157
|
..
gi 60551777 220 VK 221
Cdd:pfam01202 158 LE 159
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
336-667 |
1.04e-35 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 137.90 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 336 NQFILELFYGPTGSFKDLSLQLMphiFAYCIPPGcNYVLLVATSGDTGSAVLnGFSRlnrsdKERIAVLTFFPENGVSDF 415
Cdd:TIGR00260 39 NLYVKELGHNPTLSFKDRGMAVA---LTKALELG-NDTVLCASTGNTGAAAA-AYAG-----KAGLKVVVLYPAGKISLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 416 QRAEIVGsqrENGWAIGVKSDFDFCQAAIRKIFNDSdftgfltveYGVVLSSANSInWARLLPQVVYhasaYLELVSQgf 495
Cdd:TIGR00260 109 KLAQALG---YNAEVVAIDGNFDDAQRLVKQLFEDK---------PALGLNSANSI-PYRLEGQKTY----AFEAVEQ-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 496 ISFGSPVDVCIP---TGNFGNILAAVYAKMMG----IPIRKFICASNQNHVLTDFIKTGhyDLRNRRLAQTFSPSINILK 568
Cdd:TIGR00260 170 LGWEAPDKVVVPvpnSGNFGAIWKGFKEKKMLgldsLPVKRGIQAEGAADIVRAFLEGG--QWEPIETPETLSTAMDIGN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 569 SSNLERHLYLMANKDGQlmadlynqlesqlhfqIEELlveklqqdfvadwcSEGECLEAISTTYNTSGYILDPHTAVA-- 646
Cdd:TIGR00260 248 PANWPRALEAFRRSNGY----------------AEDL--------------SDEEILEAIKLLAREEGYFVEPHSAVAva 297
|
330 340
....*....|....*....|....
gi 60551777 647 ---KVVADKMQDKSCPVVIASTAH 667
Cdd:TIGR00260 298 allKLVEKGTADPAERVVCALTGN 321
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
58-222 |
9.70e-33 |
|
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: 124.09 E-value: 9.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDaDVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFA-SGSVISLSGSNP 136
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTD-AEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 137 MHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRvDR--IVGRNTGTSLRDLLKHGKLHYRKWYDARVFCeSGASAEEVAD 214
Cdd:COG0703 80 LSPENRELLKEHGTVVYLDASPETLLERLRRDD-NRplLQGEDPRERLEELLAEREPLYREVADITVDT-DGRSPEEVVD 157
|
....*...
gi 60551777 215 KVLDVVKR 222
Cdd:COG0703 158 EILEALEE 165
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
56-223 |
3.54e-31 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 119.91 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVlEKTWNMSVSEKLQDVGNERFLEEEgKAVLN--LFASGSVISLSG 133
Cdd:PRK00131 5 PNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLI-EARAGKSIPEIFEEEGEAAFRELE-EEVLAelLARHNLVISTGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 134 SNPMHDASMWHLKKNGIVVYLDVPLTDIISRLKsmrvdRIVGR------NTGTSLRDLLKHGKLHYRKWYDARVFCEsGA 207
Cdd:PRK00131 83 GAVLREENRALLRERGTVVYLDASFEELLRRLR-----RDRNRpllqtnDPKEKLRDLYEERDPLYEEVADITVETD-GR 156
|
170
....*....|....*.
gi 60551777 208 SAEEVADKVLDVVKRY 223
Cdd:PRK00131 157 SPEEVVNEILEKLEAA 172
|
|
| Thr_synth_N |
pfam14821 |
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine ... |
231-318 |
6.50e-15 |
|
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine synthase enzymes.
Pssm-ID: 464335 [Multi-domain] Cd Length: 79 Bit Score: 70.14 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 231 FISTRhvclkdhdKKFPPKYFSEAVVEGLASDGGLFVPEKgFPKPSLGEWTNLIGATYIERAQVLLERCIhPADIPAAKL 310
Cdd:pfam14821 2 YISTR--------GGAPPLSFEDALLKGLAPDGGLYVPEE-IPQLSAEELASWRGLSYQELAFEVLSLFI-GDDIPEEDL 71
|
....*...
gi 60551777 311 GEMIETAY 318
Cdd:pfam14821 72 KALIERAY 79
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
346-672 |
6.01e-12 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 68.69 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 346 PTGSFKDLSLQL------------MPHIFAYCippgcnyvllvATSGDTGSAVLNGFSRLNrsdkerIAVLTFFPENGVS 413
Cdd:PLN02569 161 HTGSFKDLGMTVlvsqvnrlrkmaKPVVGVGC-----------ASTGDTSAALSAYCAAAG------IPSIVFLPADKIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 414 DFQRAEIVgSQRENGWAIgvKSDFDFCQAAIRKIfndsdftgflTVEYGVVLssANSINWARLLPQvvyhASAYLELVSQ 493
Cdd:PLN02569 224 IAQLVQPI-ANGALVLSI--DTDFDGCMRLIREV----------TAELPIYL--ANSLNSLRLEGQ----KTAAIEILQQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 494 gfisFGSPVD--VCIPTGNFGNILAAVYA----KMMGI--PIRKFICASNQN-HVLTDFIKTGHYDLRNRRLAQTFSPSI 564
Cdd:PLN02569 285 ----FDWEVPdwVIVPGGNLGNIYAFYKGfkmcKELGLvdRLPRLVCAQAANaNPLYRAYKSGWEEFKPVKANPTFASAI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 565 NILKSSNLERHLYLMANKDGqlmadlynqlesqlhfqieelLVEKLQQDFVADWCSEGEcleaisttynTSGYILDPHTA 644
Cdd:PLN02569 361 QIGDPVSIDRAVYALKESNG---------------------IVEEATEEELMDAQAEAD----------KTGMFLCPHTG 409
|
330 340 350
....*....|....*....|....*....|...
gi 60551777 645 VAKVVADKMQD-----KSCPVVIASTAHYSKFA 672
Cdd:PLN02569 410 VALAALKKLRAsgvigPTDRTVVVSTAHGLKFT 442
|
|
| therm_gnt_kin |
TIGR01313 |
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ... |
58-174 |
1.19e-03 |
|
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.
Pssm-ID: 273551 Cd Length: 163 Bit Score: 40.46 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVD----ADVLEKtwnMSVSEKLQDvgNER--FLEEEGKAVLNLFASGSVISL 131
Cdd:TIGR01313 1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDdlhpAANIEK---MSAGIPLND--DDRwpWLQNLNDASTAAAAKNKVGII 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 60551777 132 SGSNpmhdasmwhLKK---------NGIV--VYLDVPLTDIISRLKS-----MRVDRIV 174
Cdd:TIGR01313 76 TCSA---------LKRhyrdilreaEPNLhfIYLSGDKDVILERMKArkghfMKADMLE 125
|
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
58-106 |
2.51e-03 |
|
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.
Pssm-ID: 468038 Cd Length: 149 Bit Score: 39.01 E-value: 2.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVdadvlektwNMSVSEKLQDV 106
Cdd:NF033453 19 ILLVGPPGSGKTALLRELAAKRGAPVINV---------NLELSRRLLEL 58
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Thr-synth_2 |
cd01560 |
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ... |
230-733 |
0e+00 |
|
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.
Pssm-ID: 107203 [Multi-domain] Cd Length: 460 Bit Score: 556.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 230 TFISTRHVClkdhdkkfPPKYFSEAVVEGLASDGGLFVPEKgFPKPSLGEWTNLIGATYIERAQVLLERCIhPADIPAAK 309
Cdd:cd01560 1 KYVSTRGGN--------PGVSFSEALLSGLAPDGGLYVPEE-LPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 310 LGEMIETAYGEsFACSKVAPVRHLSGNQFILELFYGPTGSFKDLSLQLMPHIFAYCIPP-GCNYVLLVATSGDTGSAVLN 388
Cdd:cd01560 71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 389 GFSrlnrsDKERIAVLTFFPENGVSDFQRAEIVGSQRENGWAIGVKSDFDFCQAAIRKIFNDSDFTgfltveYGVVLSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 469 NSINWARLLPQVVYHASAYLELVSQGFisfGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNHVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKRGE---GEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 549 YDLRnRRLAQTFSPSINILKSSNLERHLYLMANKDGQLMADLYNQLESQLHFQIEELLVEKLQQDFVADWCSEGECLEAI 628
Cdd:cd01560 296 YDRR-ESLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 629 STTYNTSGYILDPHTAVAKVVADKMQDK-SCPVVIASTAHYSKFAPVVLQALRIKElnqtsasqlyllssynalPPPHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEP------------------VELPEE 436
|
490 500
....*....|....*....|....*.
gi 60551777 708 LLERMKQKGKmdYQACVADVDVLKSH 733
Cdd:cd01560 437 LEGLEDLEKR--HEDLLADKELLKSH 460
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
251-682 |
3.39e-64 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 218.92 E-value: 3.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 251 FSEAVVEGLASDGGLfVPEKgFPKPSLGEWTNLIG-ATYIEraqVLLERCIHPAdipaaklgemieTAYGESFA----CS 325
Cdd:COG0498 11 FSDALLYLCPDCGGL-LPDS-YPALSREDLASRRGlWRYRE---LLPFDDEEKA------------VSLGEGGTplvkAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 326 KVApvRHLSGNQFILELFYGPTGSFKDLSLQLMPHIFAYCippGCnYVLLVATSGdTGSAVLNGFsrlnrSDKERIAVLT 405
Cdd:COG0498 74 RLA--DELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALER---GA-KTIVCASSG-NGSAALAAY-----AARAGIEVFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 406 FFPENGVSDFQRAEIV--GSQrengwAIGVKSDFDFCQAAIRKIFNDSDFtgfltveygvvlSSANSINWARLLPQVVYh 483
Cdd:COG0498 142 FVPEGKVSPGQLAQMLtyGAH-----VIAVDGNFDDAQRLVKELAADEGL------------YAVNSINPARLEGQKTY- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 484 asaYLELVSQgfisFGSPVD-VCIPTGNFGNILAAVYAKMM----GIPIR--KFI--CASNQNHVLTDFiKTGHYDLRNR 554
Cdd:COG0498 204 ---AFEIAEQ----LGRVPDwVVVPTGNGGNILAGYKAFKElkelGLIDRlpRLIavQATGCNPILTAF-ETGRDEYEPE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 555 RlAQTFSPSINILKSSNLERHLYLMANKDGqlmadlynqlesqlhfqieellveklqqdfVADWCSEGECLEAISTTYNT 634
Cdd:COG0498 276 R-PETIAPSMDIGNPSNGERALFALRESGG------------------------------TAVAVSDEEILEAIRLLARR 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 60551777 635 SGYILDPHTAVA-----KVVADKMQDKSCPVVIASTAHYSKFAPVVLQALRIK 682
Cdd:COG0498 325 EGIFVEPATAVAvaglrKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
57-204 |
2.01e-38 |
|
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: 140.00 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 57 NIVLMGPPGAGKTTVGRILGDKLGCCVIDVDaDVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFAS-GSVISLSGSN 135
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLD-ELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60551777 136 PMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRVDRIVGRNTGTSLRDLLKHGKLHYRKWYDARVFCE 204
Cdd:cd00464 80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD 148
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
64-221 |
3.68e-38 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 139.25 E-value: 3.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 64 PGAGKTTVGRILGDKLGCCVIDVDaDVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFAS-GSVISLSGSNPMHDASM 142
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTD-EEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEhGLVIATGGGAVLSEENR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 143 WHLKKNGIVVYLDVPLTDIISRLKsMRVDRIV--GRNTGTSLRDLLKHGKLH-YRKwYDARVFCESGASAEEVADKVLDV 219
Cdd:pfam01202 80 DLLKERGIVIYLDAPLEVLLERLK-RDKTRPLlqNKDPEEELLELLFEERDPlYEE-AADIVIDTDESSPEEVATEILEA 157
|
..
gi 60551777 220 VK 221
Cdd:pfam01202 158 LE 159
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
336-667 |
1.04e-35 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 137.90 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 336 NQFILELFYGPTGSFKDLSLQLMphiFAYCIPPGcNYVLLVATSGDTGSAVLnGFSRlnrsdKERIAVLTFFPENGVSDF 415
Cdd:TIGR00260 39 NLYVKELGHNPTLSFKDRGMAVA---LTKALELG-NDTVLCASTGNTGAAAA-AYAG-----KAGLKVVVLYPAGKISLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 416 QRAEIVGsqrENGWAIGVKSDFDFCQAAIRKIFNDSdftgfltveYGVVLSSANSInWARLLPQVVYhasaYLELVSQgf 495
Cdd:TIGR00260 109 KLAQALG---YNAEVVAIDGNFDDAQRLVKQLFEDK---------PALGLNSANSI-PYRLEGQKTY----AFEAVEQ-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 496 ISFGSPVDVCIP---TGNFGNILAAVYAKMMG----IPIRKFICASNQNHVLTDFIKTGhyDLRNRRLAQTFSPSINILK 568
Cdd:TIGR00260 170 LGWEAPDKVVVPvpnSGNFGAIWKGFKEKKMLgldsLPVKRGIQAEGAADIVRAFLEGG--QWEPIETPETLSTAMDIGN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 569 SSNLERHLYLMANKDGQlmadlynqlesqlhfqIEELlveklqqdfvadwcSEGECLEAISTTYNTSGYILDPHTAVA-- 646
Cdd:TIGR00260 248 PANWPRALEAFRRSNGY----------------AEDL--------------SDEEILEAIKLLAREEGYFVEPHSAVAva 297
|
330 340
....*....|....*....|....
gi 60551777 647 ---KVVADKMQDKSCPVVIASTAH 667
Cdd:TIGR00260 298 allKLVEKGTADPAERVVCALTGN 321
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
58-222 |
9.70e-33 |
|
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: 124.09 E-value: 9.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDaDVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFA-SGSVISLSGSNP 136
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTD-AEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 137 MHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRvDR--IVGRNTGTSLRDLLKHGKLHYRKWYDARVFCeSGASAEEVAD 214
Cdd:COG0703 80 LSPENRELLKEHGTVVYLDASPETLLERLRRDD-NRplLQGEDPRERLEELLAEREPLYREVADITVDT-DGRSPEEVVD 157
|
....*...
gi 60551777 215 KVLDVVKR 222
Cdd:COG0703 158 EILEALEE 165
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
56-223 |
3.54e-31 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 119.91 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVlEKTWNMSVSEKLQDVGNERFLEEEgKAVLN--LFASGSVISLSG 133
Cdd:PRK00131 5 PNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLI-EARAGKSIPEIFEEEGEAAFRELE-EEVLAelLARHNLVISTGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 134 SNPMHDASMWHLKKNGIVVYLDVPLTDIISRLKsmrvdRIVGR------NTGTSLRDLLKHGKLHYRKWYDARVFCEsGA 207
Cdd:PRK00131 83 GAVLREENRALLRERGTVVYLDASFEELLRRLR-----RDRNRpllqtnDPKEKLRDLYEERDPLYEEVADITVETD-GR 156
|
170
....*....|....*.
gi 60551777 208 SAEEVADKVLDVVKRY 223
Cdd:PRK00131 157 SPEEVVNEILEKLEAA 172
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
335-667 |
8.98e-24 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 101.05 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 335 GNQFILELFYGPTGSFKDLSLQLMPHIFAYCIPPGcNYVLLVATSGDTGSAVLNGFSRLNrsdkerIAVLTFFPEnGVSD 414
Cdd:cd00640 15 ANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLP-KGVIIESTGGNTGIALAAAAARLG------LKCTIVMPE-GASP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 415 FQRAEIvgsqRENG-WAIGVKSDFDFCQAAIRKIFNDSDFTGFLtveygvvlssANSINWARLLPQVVYHASAYLELVSQ 493
Cdd:cd00640 87 EKVAQM----RALGaEVVLVPGDFDDAIALAKELAEEDPGAYYV----------NQFDNPANIAGQGTIGLEILEQLGGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 494 gfisfgSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQnhvltdfiktghydlrnrrlaqtfspsinilkssnle 573
Cdd:cd00640 153 ------KPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE------------------------------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 574 rhlylmankdgqlmadlynqlesqlhfqieellveklqqdfvADWCSEGECLEAISTTYNTSGYILDPHTAVAKVVADKM 653
Cdd:cd00640 190 ------------------------------------------VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKL 227
|
330
....*....|....*..
gi 60551777 654 QDKSCP---VVIASTAH 667
Cdd:cd00640 228 AKKLGKgktVVVILTGG 244
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
56-217 |
1.22e-16 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 78.21 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDAdVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFA-SGSVISLSGS 134
Cdd:PRK13947 2 KNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDK-EIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARlKNLVIATGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 135 NPMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRVDRIVGR-NTGTSLRDLLKHgKLHYrkwYDARVFC--ESGASAEE 211
Cdd:PRK13947 81 VVLNPENVVQLRKNGVVICLKARPEVILRRVGKKKSRPLLMVgDPEERIKELLKE-REPF---YDFADYTidTGDMTIDE 156
|
....*.
gi 60551777 212 VADKVL 217
Cdd:PRK13947 157 VAEEII 162
|
|
| PRK00625 |
PRK00625 |
shikimate kinase; Provisional |
56-165 |
1.61e-15 |
|
shikimate kinase; Provisional
Pssm-ID: 134335 [Multi-domain] Cd Length: 173 Bit Score: 75.18 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVLEKTWNM---SVSEKLQDVGNERFLEEEGKAVLNLFASGSVISLS 132
Cdd:PRK00625 1 MQIFLCGLPTVGKTSFGKALAKFLSLPFFDTDDLIVSNYHGAlysSPKEIYQAYGEEGFCREEFLALTSLPVIPSIVALG 80
|
90 100 110
....*....|....*....|....*....|...
gi 60551777 133 GSNPMHDASMWHLKKNGIVVYLDVPLTDIISRL 165
Cdd:PRK00625 81 GGTLMIEPSYAHIRNRGLLVLLSLPIATIYQRL 113
|
|
| Thr_synth_N |
pfam14821 |
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine ... |
231-318 |
6.50e-15 |
|
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine synthase enzymes.
Pssm-ID: 464335 [Multi-domain] Cd Length: 79 Bit Score: 70.14 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 231 FISTRhvclkdhdKKFPPKYFSEAVVEGLASDGGLFVPEKgFPKPSLGEWTNLIGATYIERAQVLLERCIhPADIPAAKL 310
Cdd:pfam14821 2 YISTR--------GGAPPLSFEDALLKGLAPDGGLYVPEE-IPQLSAEELASWRGLSYQELAFEVLSLFI-GDDIPEEDL 71
|
....*...
gi 60551777 311 GEMIETAY 318
Cdd:pfam14821 72 KALIERAY 79
|
|
| PRK13946 |
PRK13946 |
shikimate kinase; Provisional |
50-230 |
4.51e-14 |
|
shikimate kinase; Provisional
Pssm-ID: 184411 [Multi-domain] Cd Length: 184 Bit Score: 71.11 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 50 HSLVGDKNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVlEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFASGS-V 128
Cdd:PRK13946 5 RAALGKRTVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEI-ERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGPlV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 129 ISLSGSNPMHDASMWHLKKNGIVVYLDVPLtDIISRlksmRVDRivgRNTgtslRDLLKHG--KLHYRKWYDAR------ 200
Cdd:PRK13946 84 LATGGGAFMNEETRAAIAEKGISVWLKADL-DVLWE----RVSR---RDT----RPLLRTAdpKETLARLMEERypvyae 151
|
170 180 190
....*....|....*....|....*....|...
gi 60551777 201 --VFCESGA-SAEEVADKVLDVVKRYQDVDSET 230
Cdd:PRK13946 152 adLTVASRDvPKEVMADEVIEALAAYLEKEEAA 184
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
58-166 |
3.55e-12 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 65.35 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVLEKTwNMSVSEKLQDVGNERFLEEEGKAVLNLFASGSVISLSGSNPM 137
Cdd:PRK03731 5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTS-NMTVAEIVEREGWAGFRARESAALEAVTAPSTVIATGGGIIL 83
|
90 100
....*....|....*....|....*....
gi 60551777 138 HDASMWHLKKNGIVVYLDVPLTDIISRLK 166
Cdd:PRK03731 84 TEENRHFMRNNGIVIYLCAPVSVLANRLE 112
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
346-672 |
6.01e-12 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 68.69 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 346 PTGSFKDLSLQL------------MPHIFAYCippgcnyvllvATSGDTGSAVLNGFSRLNrsdkerIAVLTFFPENGVS 413
Cdd:PLN02569 161 HTGSFKDLGMTVlvsqvnrlrkmaKPVVGVGC-----------ASTGDTSAALSAYCAAAG------IPSIVFLPADKIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 414 DFQRAEIVgSQRENGWAIgvKSDFDFCQAAIRKIfndsdftgflTVEYGVVLssANSINWARLLPQvvyhASAYLELVSQ 493
Cdd:PLN02569 224 IAQLVQPI-ANGALVLSI--DTDFDGCMRLIREV----------TAELPIYL--ANSLNSLRLEGQ----KTAAIEILQQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 494 gfisFGSPVD--VCIPTGNFGNILAAVYA----KMMGI--PIRKFICASNQN-HVLTDFIKTGHYDLRNRRLAQTFSPSI 564
Cdd:PLN02569 285 ----FDWEVPdwVIVPGGNLGNIYAFYKGfkmcKELGLvdRLPRLVCAQAANaNPLYRAYKSGWEEFKPVKANPTFASAI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 565 NILKSSNLERHLYLMANKDGqlmadlynqlesqlhfqieelLVEKLQQDFVADWCSEGEcleaisttynTSGYILDPHTA 644
Cdd:PLN02569 361 QIGDPVSIDRAVYALKESNG---------------------IVEEATEEELMDAQAEAD----------KTGMFLCPHTG 409
|
330 340 350
....*....|....*....|....*....|...
gi 60551777 645 VAKVVADKMQD-----KSCPVVIASTAHYSKFA 672
Cdd:PLN02569 410 VALAALKKLRAsgvigPTDRTVVVSTAHGLKFT 442
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
56-184 |
4.37e-11 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 62.05 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDAdVLEKTWNMSVSEKLQDVGNERFLEEEgKAVLNLFA--SGSVISLSG 133
Cdd:PRK13949 2 ARIFLVGYMGAGKTTLGKALARELGLSFIDLDF-FIENRFHKTVGDIFAERGEAVFRELE-RNMLHEVAefEDVVISTGG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 60551777 134 SNPMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRVDR-IVGRNTGTSLRD 184
Cdd:PRK13949 80 GAPCFFDNMELMNASGTTVYLKVSPEVLFVRLRLAKQQRpLLKGKSDEELLD 131
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
343-664 |
3.24e-10 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 61.94 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 343 FYGPTGSFKDLSLQlmpHIFAYCIPPGCNYVLLVATSGDTGSAVLNGFSRLNrsdkerIAVLTFFPENGVSDFQR----- 417
Cdd:pfam00291 30 SLNPTGSFKDRGAL---NLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLG------LKVTIVVPEDAPPGKLLlmral 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 418 -AEIvgsqrengwaIGVKSDFDFCQAAIRKIFNDSDftgfltvEYGVVLSSANSINWArllpqvvYHASAYLELVSQgfi 496
Cdd:pfam00291 101 gAEV----------VLVGGDYDEAVAAARELAAEGP-------GAYYINQYDNPLNIE-------GYGTIGLEILEQ--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 497 sFGSPVD-VCIPTGNFGNILA-AVYAKMMGIPIRKFICASNQNHVLTDFIKTGHYDlrNRRLAQTFSPSINILKSSnler 574
Cdd:pfam00291 154 -LGGDPDaVVVPVGGGGLIAGiARGLKELGPDVRVIGVEPEGAPALARSLAAGRPV--PVPVADTIADGLGVGDEP---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 575 hlylmankdgqlmadlynqleSQLHFQieelLVEKLQQDFVAdwCSEGECLEAISTTYNTSGYILDPHTAVA-----KVV 649
Cdd:pfam00291 227 ---------------------GALALD----LLDEYVGEVVT--VSDEEALEAMRLLARREGIVVEPSSAAAlaalkLAL 279
|
330
....*....|....*
gi 60551777 650 ADKMQDKSCPVVIAS 664
Cdd:pfam00291 280 AGELKGGDRVVVVLT 294
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
56-186 |
1.29e-08 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 57.01 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFASGSVISLSGSN 135
Cdd:PLN02199 103 RSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQAMNGTSVAEIFVHHGENFFRGKETDALKKLSSRYQVVVSTGGG 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 60551777 136 PMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMrvdrivgrntGTSLRDLL 186
Cdd:PLN02199 183 AVIRPINWKYMHKGISIWLDVPLEALAHRIAAV----------GTDSRPLL 223
|
|
| aroK |
PRK05057 |
shikimate kinase AroK; |
56-166 |
6.24e-07 |
|
shikimate kinase AroK;
Pssm-ID: 235335 [Multi-domain] Cd Length: 172 Bit Score: 50.10 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVLEKT-----WNMSVS------EKLQDVGNErfLEEEGKAVLNLfA 124
Cdd:PRK05057 5 RNIFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTgadigWVFDVEgeegfrDREEKVINE--LTEKQGIVLAT-G 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 60551777 125 SGSVISLSGSNpmhdasmwHLKKNGIVVYLDVPLTDIISRLK 166
Cdd:PRK05057 82 GGSVKSRETRN--------RLSARGVVVYLETTIEKQLARTQ 115
|
|
| PRK13948 |
PRK13948 |
shikimate kinase; Provisional |
58-225 |
8.72e-07 |
|
shikimate kinase; Provisional
Pssm-ID: 184413 [Multi-domain] Cd Length: 182 Bit Score: 49.79 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDAdVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFASG-SVISLSGSNP 136
Cdd:PRK13948 13 VALAGFMGTGKSRIGWELSRALMLHFIDTDR-YIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLTRLDyAVISLGGGTF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 137 MHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRVDRIVGRNTGTSLRDLLKHGKLHYRKwydARVFCES-GASAEEVADK 215
Cdd:PRK13948 92 MHEENRRKLLSRGPVVVLWASPETIYERTRPGDRPLLQVEDPLGRIRTLLNEREPVYRQ---ATIHVSTdGRRSEEVVEE 168
|
170
....*....|
gi 60551777 216 VLDVVKRYQD 225
Cdd:PRK13948 169 IVEKLWAWAE 178
|
|
| PRK03839 |
PRK03839 |
putative kinase; Provisional |
58-222 |
2.00e-06 |
|
putative kinase; Provisional
Pssm-ID: 179660 Cd Length: 180 Bit Score: 48.56 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVLEKTWNMSVSEKLQ-DVGN-ERFLEEEgkavlnlfasgsvisLSGSN 135
Cdd:PRK03839 3 IAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEiDFDKlAYFIEEE---------------FKEKN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 136 PMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRVDR-IVGRNTGTSLRD------LLKHGKLhyrkwYDARVfceSGAS 208
Cdd:PRK03839 68 VVLDGHLSHLLPVDYVIVLRAHPKIIKERLKERGYSKkKILENVEAELVDvclceaLEEKEKV-----IEVDT---TGKT 139
|
170
....*....|....
gi 60551777 209 AEEVADKVLDVVKR 222
Cdd:PRK03839 140 PEEVVEEILELIKS 153
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
62-224 |
3.62e-06 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 48.28 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 62 GPPGAGKTTVGRILGDKLGCCVIDVD--ADVLEKTwNMSVSE------------KLQDVGNERFLEEEGKAVLNLFASGS 127
Cdd:COG1102 7 REPGSGGTTIAKRLAEKLGLPLYDGEilREAAKER-GLSEEEfekldekapsllYRDTAEEDEIDRALDKVIRELARKGN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 128 VISLS-GSNpmhdasmWHLK--KNGIVVYLDVPLTDiisrlksmRVDRIVGRNtGTSLRDLLK-----------HGKLHY 193
Cdd:COG1102 86 CVIVGrLAD-------WILRdrPNVLKVFLTAPLEV--------RVKRIAERE-GISEEEAEKeikkrdksrakYYKYYY 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 60551777 194 -RKWYDAR----VFCESGASAEEVADKVLDVVKRYQ 224
Cdd:COG1102 150 gIDWGDPSnydlVINTSRLGIEEAVDLILAAIEARE 185
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
59-164 |
4.17e-06 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 50.24 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 59 VLMGPPGAGKTTVGRILGDKLGCCVIDVDADVlEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFAS-GSVISLSGSNPM 137
Cdd:PRK14021 10 VIIGMMGAGKTRVGKEVAQMMRLPFADADVEI-EREIGMSIPSYFEEYGEPAFREVEADVVADMLEDfDGIFSLGGGAPM 88
|
90 100 110
....*....|....*....|....*....|.
gi 60551777 138 HDASMWHLKK----NGIVVYLDVPLTDIISR 164
Cdd:PRK14021 89 TPSTQHALASyiahGGRVVYLDADPKEAMER 119
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
58-105 |
8.63e-06 |
|
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: 46.09 E-value: 8.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIdvDADVLEKTWN---MSVSEKLQD 105
Cdd:cd02021 2 IVVMGVSGSGKSTVGKALAERLGAPFI--DGDDLHPPANiakMAAGIPLND 50
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
58-89 |
1.24e-05 |
|
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: 45.89 E-value: 1.24e-05
10 20 30
....*....|....*....|....*....|..
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDAD 89
Cdd:COG3265 4 IVVMGVSGSGKSTVGQALAERLGWPFIDGDDF 35
|
|
| PRK08118 |
PRK08118 |
DNA topology modulation protein; |
56-115 |
1.45e-05 |
|
DNA topology modulation protein;
Pssm-ID: 181235 Cd Length: 167 Bit Score: 46.14 E-value: 1.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVLEKTWNMSVSEKLQDVGNERFLEEE 115
Cdd:PRK08118 2 KKIILIGSGGSGKSTLARQLGEKLNIPVHHLDALFWKPNWEGVPKEEQITVQNELVKEDE 61
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
57-80 |
1.91e-05 |
|
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440329 [Multi-domain] Cd Length: 212 Bit Score: 46.27 E-value: 1.91e-05
10 20
....*....|....*....|....
gi 60551777 57 NIVLMGPPGAGKTTVGRILGDKLG 80
Cdd:COG0563 2 RIILLGPPGAGKGTQAKRLAEKYG 25
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
57-84 |
2.01e-05 |
|
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.
Pssm-ID: 238713 [Multi-domain] Cd Length: 194 Bit Score: 46.08 E-value: 2.01e-05
10 20
....*....|....*....|....*...
gi 60551777 57 NIVLMGPPGAGKTTVGRILGDKLGCCVI 84
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHI 28
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
58-88 |
2.18e-05 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 45.29 E-value: 2.18e-05
10 20 30
....*....|....*....|....*....|.
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDA 88
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRLRSDV 32
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
58-87 |
1.73e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 42.03 E-value: 1.73e-04
10 20 30
....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVD 87
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDNVRD 30
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
58-94 |
1.88e-04 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 43.13 E-value: 1.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 60551777 58 IVLMGPPGAGKTTV----GRILGDKLGCCVI------DVDADVLEKT 94
Cdd:COG0378 16 VNLMGSPGSGKTTLlektIRALKDRLRIAVIegdiytTEDAERLRAA 62
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
58-200 |
2.10e-04 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 44.51 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDaDVLEKTWNMSVSEKLQDVGNERFLEEEGKAVLNLFASGSVISLSGSNPM 137
Cdd:PRK13951 3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMD-EEIERREGRSVRRIFEEDGEEYFRLKEKELLRELVERDNVVVATGGGVV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60551777 138 HDASMWHLKKNGIVVYLDVPltdiisrlKSMRVDRIVGRNtgtslRDLLKHGKLHYRKWYDAR 200
Cdd:PRK13951 82 IDPENRELLKKEKTLFLYAP--------PEVLMERVTTEN-----RPLLREGKERIREIWERR 131
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
56-80 |
1.14e-03 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 40.90 E-value: 1.14e-03
10 20
....*....|....*....|....*
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLG 80
Cdd:PRK00279 1 MRLILLGPPGAGKGTQAKFIAEKYG 25
|
|
| therm_gnt_kin |
TIGR01313 |
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ... |
58-174 |
1.19e-03 |
|
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.
Pssm-ID: 273551 Cd Length: 163 Bit Score: 40.46 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVD----ADVLEKtwnMSVSEKLQDvgNER--FLEEEGKAVLNLFASGSVISL 131
Cdd:TIGR01313 1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDdlhpAANIEK---MSAGIPLND--DDRwpWLQNLNDASTAAAAKNKVGII 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 60551777 132 SGSNpmhdasmwhLKK---------NGIV--VYLDVPLTDIISRLKS-----MRVDRIV 174
Cdd:TIGR01313 76 TCSA---------LKRhyrdilreaEPNLhfIYLSGDKDVILERMKArkghfMKADMLE 125
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
56-103 |
1.48e-03 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This 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: 410917 [Multi-domain] Cd Length: 163 Bit Score: 40.03 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVLEKTWnMSVSEKL 103
Cdd:cd19509 33 RGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKW-VGESEKI 79
|
|
| PRK08154 |
PRK08154 |
anaerobic benzoate catabolism transcriptional regulator; Reviewed |
22-120 |
1.70e-03 |
|
anaerobic benzoate catabolism transcriptional regulator; Reviewed
Pssm-ID: 236167 [Multi-domain] Cd Length: 309 Bit Score: 41.09 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60551777 22 LVKVQTPTQLSLPRaLACAESGKSWHSTHSlvgDKNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVlEKTWNMSVSE 101
Cdd:PRK08154 104 LLEQASPAQLARVR-DALSGMLGAGRRAAR---RRRIALIGLRGAGKSTLGRMLAARLGVPFVELNREI-EREAGLSVSE 178
|
90 100 110
....*....|....*....|....*....|
gi 60551777 102 KLQDVGN-----------ERFLEEEGKAVL 120
Cdd:PRK08154 179 IFALYGQegyrrlerralERLIAEHEEMVL 208
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
58-88 |
2.15e-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: 39.22 E-value: 2.15e-03
10 20 30
....*....|....*....|....*....|.
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVDA 88
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDD 32
|
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
58-106 |
2.51e-03 |
|
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.
Pssm-ID: 468038 Cd Length: 149 Bit Score: 39.01 E-value: 2.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGCCVIDVdadvlektwNMSVSEKLQDV 106
Cdd:NF033453 19 ILLVGPPGSGKTALLRELAAKRGAPVINV---------NLELSRRLLEL 58
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
56-95 |
2.67e-03 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This 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: 410933 [Multi-domain] Cd Length: 186 Bit Score: 39.59 E-value: 2.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 60551777 56 KNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVLEKTW 95
Cdd:cd19525 56 KGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
50-91 |
4.06e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 40.28 E-value: 4.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 60551777 50 HSLVGDKNIVLMGPPGAGKTTVGRILGDKLGCCVIDVDADVL 91
Cdd:COG0464 186 YGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL 227
|
|
| cyt_kin_arch |
TIGR02173 |
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ... |
58-80 |
4.07e-03 |
|
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: 38.94 E-value: 4.07e-03
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
58-81 |
4.56e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 38.63 E-value: 4.56e-03
10 20
....*....|....*....|....
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLGC 81
Cdd:PRK04182 3 ITISGPPGSGKTTVARLLAEKLGL 26
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
58-80 |
4.81e-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: 38.24 E-value: 4.81e-03
10 20
....*....|....*....|...
gi 60551777 58 IVLMGPPGAGKTTVGRILGDKLG 80
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLAKKLG 24
|
|
| |
