|
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: 570.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 230 TFISTRHVClkdhdkkfPPKYFSEAVVEGLASDGGLFVPEkEFPKLSPGEWNNLIGATYIERAQVLLERCIhPADIPAAK 309
Cdd:cd01560 1 KYVSTRGGN--------PGVSFSEALLSGLAPDGGLYVPE-ELPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 310 LGEMIETAYGEnFACSKVAPVRHLSGNQFILELFYGPTGSFKDLSLQLMPHIFAYCIPP-GCNYVILVATSGDTGSAVLN 388
Cdd:cd01560 71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 389 GFShlnknDKERIAVVTFFPENGVSDFQKAEIIGSQRENGWAIGVRSDFDFCQTAIRKIFNDSDFTgflaveYGTILSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 469 NSINWARLLPQIVYHASAYLELVNQrfiSFGSPVDVCVPTGNFGNVLAAVYAKMMGIPIRKFICASNQNHVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKR---GEGEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 549 YDLRnRKLAQTFSPSIDILKSSNLERHLYLMANKDGQLMANLYHQLESQLHFRIEKMLVEKLQQEFVADWCSEGECLAAI 628
Cdd:cd01560 296 YDRR-ESLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 629 STTYNASGYILDPHTAVAKVVADKMQDK-SCPVLIASTAHYSKFAPAIMQALGIKElnqtsssqlyllssynalPPPHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEP------------------VELPEE 436
|
490 500
....*....|....*....|....*.
gi 29243946 708 LLERMKQKEKmdYQVCVADVDVLKSH 733
Cdd:cd01560 437 LEGLEDLEKR--HEDLLADKELLKSH 460
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
251-682 |
1.35e-66 |
|
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: 225.46 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 251 FSEAVVEGLASDGGLfVPEkEFPKLSPGEWNNLIG-ATYIEraqVLLERCIHPAdipaaklgemieTAYGENFA----CS 325
Cdd:COG0498 11 FSDALLYLCPDCGGL-LPD-SYPALSREDLASRRGlWRYRE---LLPFDDEEKA------------VSLGEGGTplvkAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 326 KVApvRHLSGNQFILELFYGPTGSFKDLSLQLMPHIFAYCippGCnYVILVATSGdTGSAVLNGFShlnknDKERIAVVT 405
Cdd:COG0498 74 RLA--DELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALER---GA-KTIVCASSG-NGSAALAAYA-----ARAGIEVFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 406 FFPENGVSDFQKAEII--GSQrengwAIGVRSDFDFCQTAIRKIFNDSDFtgflaveygtilSSANSINWARLLPQIVYH 483
Cdd:COG0498 142 FVPEGKVSPGQLAQMLtyGAH-----VIAVDGNFDDAQRLVKELAADEGL------------YAVNSINPARLEGQKTYA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 484 ASAYLELVNqrfisfgSPVDVCVPTGNFGNVLAAVYAKMM----GIPIR--KFI--CASNQNHVLTDFiKTGHYDLRNRK 555
Cdd:COG0498 205 FEIAEQLGR-------VPDWVVVPTGNGGNILAGYKAFKElkelGLIDRlpRLIavQATGCNPILTAF-ETGRDEYEPER 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 556 lAQTFSPSIDILKSSNLERHLYLMANKDGqlmanlyhqlesqlhfriekmlveklqqefVADWCSEGECLAAISTTYNAS 635
Cdd:COG0498 277 -PETIAPSMDIGNPSNGERALFALRESGG------------------------------TAVAVSDEEILEAIRLLARRE 325
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 29243946 636 GYILDPHTAVA-----KVVADKMQDKSCPVLIASTAHYSKFAPAIMQALGIK 682
Cdd:COG0498 326 GIFVEPATAVAvaglrKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
64-221 |
5.89e-40 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 144.26 E-value: 5.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 64 PGSGKTTVGRILGDKLGCCVIDVDsDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSAS-GSVISLSGSNPMHDASM 142
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTD-EEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEhGLVIATGGGAVLSEENR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 143 WHLKKNGIVVYLDVPLTDIISRLKsMRIDRIVGQN--TGASLRDSLKHVR--LYYKkwYDARVFCESGASAEEVADKVLD 218
Cdd:pfam01202 80 DLLKERGIVIYLDAPLEVLLERLK-RDKTRPLLQNkdPEEELLELLFEERdpLYEE--AADIVIDTDESSPEEVATEILE 156
|
...
gi 29243946 219 VVK 221
Cdd:pfam01202 157 ALE 159
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
57-204 |
2.27e-37 |
|
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: 136.92 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 57 NIVLMGPPGSGKTTVGRILGDKLGCCVIDVDsDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSAS-GSVISLSGSN 135
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLD-ELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29243946 136 PMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRIDRIVGQNTGASLRDSLKHVRLYYKKWYDARVFCE 204
Cdd:cd00464 80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD 148
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
304-670 |
1.62e-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: 137.13 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 304 DIPAAKLGEMIEtaygENFACSKvaPVRHLSG-NQFILELFYGPTGSFKDLSLQLMphiFAYCIPPGcNYVILVATSGDT 382
Cdd:TIGR00260 12 EKDLVDLGEGVT----PLFRAPA--LAANVGIkNLYVKELGHNPTLSFKDRGMAVA---LTKALELG-NDTVLCASTGNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 383 GSAVLNGFSHLNKNdkeriaVVTFFPENGVSDFQKAEIIGsqrENGWAIGVRSDFDFCQTAIRKIFNDSdftgflaveYG 462
Cdd:TIGR00260 82 GAAAAAYAGKAGLK------VVVLYPAGKISLGKLAQALG---YNAEVVAIDGNFDDAQRLVKQLFEDK---------PA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 463 TILSSANSInWARLLPQIvYHASAYLELVNQRfisfgSPVDVCVP---TGNFGNVLAAVYAKMMG----IPIRKFICASN 535
Cdd:TIGR00260 144 LGLNSANSI-PYRLEGQK-TYAFEAVEQLGWE-----APDKVVVPvpnSGNFGAIWKGFKEKKMLgldsLPVKRGIQAEG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 536 QNHVLTDFIKTGHYDLRNRKlaQTFSPSIDILKSSNLERHLYLMANKDGQlmanlyhqlesqlhfriekmlveklqqefv 615
Cdd:TIGR00260 217 AADIVRAFLEGGQWEPIETP--ETLSTAMDIGNPANWPRALEAFRRSNGY------------------------------ 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 29243946 616 ADWCSEGECLAAISTTYNASGYILDPHTAVAKVVADKMQDKscpvliaSTAHYSK 670
Cdd:TIGR00260 265 AEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEK-------GTADPAE 312
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
58-222 |
5.04e-32 |
|
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: 122.16 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDsDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSA-SGSVISLSGSNP 136
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTD-AEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 137 MHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRiDR--IVGQNTGASLRDSLKHVRLYYKKWYDARVFCeSGASAEEVAD 214
Cdd:COG0703 80 LSPENRELLKEHGTVVYLDASPETLLERLRRDD-NRplLQGEDPRERLEELLAEREPLYREVADITVDT-DGRSPEEVVD 157
|
....*...
gi 29243946 215 KVLDVVKR 222
Cdd:COG0703 158 EILEALEE 165
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
56-223 |
2.03e-30 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 117.98 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDsDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSAS-GSVISLSGS 134
Cdd:PRK00131 5 PNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTD-HLIEARAGKSIPEIFEEEGEAAFRELEEEVLAELLARhNLVISTGGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 135 NPMHDASMWHLKKNGIVVYLDVPLTDIISRLkSMRIDR--IVGQNTGASLRDSLKHVRLYYKKWYDARVFCEsGASAEEV 212
Cdd:PRK00131 84 AVLREENRALLRERGTVVYLDASFEELLRRL-RRDRNRplLQTNDPKEKLRDLYEERDPLYEEVADITVETD-GRSPEEV 161
|
170
....*....|.
gi 29243946 213 ADKVLDVVKRY 223
Cdd:PRK00131 162 VNEILEKLEAA 172
|
|
| Thr_synth_N |
pfam14821 |
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine ... |
231-318 |
3.55e-17 |
|
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: 76.69 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 231 FISTRhvclkdhdKKFPPKYFSEAVVEGLASDGGLFVPEkEFPKLSPGEWNNLIGATYIERAQVLLERCIhPADIPAAKL 310
Cdd:pfam14821 2 YISTR--------GGAPPLSFEDALLKGLAPDGGLYVPE-EIPQLSAEELASWRGLSYQELAFEVLSLFI-GDDIPEEDL 71
|
....*...
gi 29243946 311 GEMIETAY 318
Cdd:pfam14821 72 KALIERAY 79
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
346-672 |
1.74e-11 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 67.15 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 346 PTGSFKDLSLQL------------MPHIFAYCippgcnyvilvATSGDTgSAVLNGFShlnknDKERIAVVTFFPENGVS 413
Cdd:PLN02569 161 HTGSFKDLGMTVlvsqvnrlrkmaKPVVGVGC-----------ASTGDT-SAALSAYC-----AAAGIPSIVFLPADKIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 414 DFQKAEIIgSQRENGWAIGvrSDFDFCQTAIRKIfnDSDFTGFLaveygtilssANSINWARLLPQivyhASAYLELVNQ 493
Cdd:PLN02569 224 IAQLVQPI-ANGALVLSID--TDFDGCMRLIREV--TAELPIYL----------ANSLNSLRLEGQ----KTAAIEILQQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 494 rfisFGSPVD--VCVPTGNFGNVLAAVYA----KMMGI--PIRKFICASNQN-HVLTDFIKTGHYDLRNRKLAQTFSPSI 564
Cdd:PLN02569 285 ----FDWEVPdwVIVPGGNLGNIYAFYKGfkmcKELGLvdRLPRLVCAQAANaNPLYRAYKSGWEEFKPVKANPTFASAI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 565 DILKSSNLERHLYLMANKDGqlmanlyhqlesqlhfriekmLVEKLQQEFVADWCSEGEclaaisttynASGYILDPHTA 644
Cdd:PLN02569 361 QIGDPVSIDRAVYALKESNG---------------------IVEEATEEELMDAQAEAD----------KTGMFLCPHTG 409
|
330 340 350
....*....|....*....|....*....|...
gi 29243946 645 VAKVVADKMQD-----KSCPVLIASTAHYSKFA 672
Cdd:PLN02569 410 VALAALKKLRAsgvigPTDRTVVVSTAHGLKFT 442
|
|
| therm_gnt_kin |
TIGR01313 |
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ... |
58-176 |
4.05e-05 |
|
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: 44.70 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDSdvLEKAWN---MSASEKLQDvgNER--FLEEEGKTVLNLSASGSVISLS 132
Cdd:TIGR01313 1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDD--LHPAANiekMSAGIPLND--DDRwpWLQNLNDASTAAAAKNKVGIIT 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 133 GSNpmhdasmwhLKK---------NGIV--VYLDVPLTDIISRLKS-----MRIDRIVGQ 176
Cdd:TIGR01313 77 CSA---------LKRhyrdilreaEPNLhfIYLSGDKDVILERMKArkghfMKADMLESQ 127
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
25-93 |
1.79e-04 |
|
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: 44.52 E-value: 1.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 25 VQSRTQLLLPRASARAESGKSWHsthslvgdKNIVLMGPPGSGKTTVGRILGDKLGCCVIDVD-SDVLEK 93
Cdd:COG0464 169 LRELVALPLKRPELREEYGLPPP--------RGLLLYGPPGTGKTLLARALAGELGLPLIEVDlSDLVSK 230
|
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
58-106 |
2.64e-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: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVdsdvlekawNMSASEKLQDV 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: 570.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 230 TFISTRHVClkdhdkkfPPKYFSEAVVEGLASDGGLFVPEkEFPKLSPGEWNNLIGATYIERAQVLLERCIhPADIPAAK 309
Cdd:cd01560 1 KYVSTRGGN--------PGVSFSEALLSGLAPDGGLYVPE-ELPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 310 LGEMIETAYGEnFACSKVAPVRHLSGNQFILELFYGPTGSFKDLSLQLMPHIFAYCIPP-GCNYVILVATSGDTGSAVLN 388
Cdd:cd01560 71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 389 GFShlnknDKERIAVVTFFPENGVSDFQKAEIIGSQRENGWAIGVRSDFDFCQTAIRKIFNDSDFTgflaveYGTILSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 469 NSINWARLLPQIVYHASAYLELVNQrfiSFGSPVDVCVPTGNFGNVLAAVYAKMMGIPIRKFICASNQNHVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKR---GEGEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 549 YDLRnRKLAQTFSPSIDILKSSNLERHLYLMANKDGQLMANLYHQLESQLHFRIEKMLVEKLQQEFVADWCSEGECLAAI 628
Cdd:cd01560 296 YDRR-ESLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 629 STTYNASGYILDPHTAVAKVVADKMQDK-SCPVLIASTAHYSKFAPAIMQALGIKElnqtsssqlyllssynalPPPHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEP------------------VELPEE 436
|
490 500
....*....|....*....|....*.
gi 29243946 708 LLERMKQKEKmdYQVCVADVDVLKSH 733
Cdd:cd01560 437 LEGLEDLEKR--HEDLLADKELLKSH 460
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
251-682 |
1.35e-66 |
|
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: 225.46 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 251 FSEAVVEGLASDGGLfVPEkEFPKLSPGEWNNLIG-ATYIEraqVLLERCIHPAdipaaklgemieTAYGENFA----CS 325
Cdd:COG0498 11 FSDALLYLCPDCGGL-LPD-SYPALSREDLASRRGlWRYRE---LLPFDDEEKA------------VSLGEGGTplvkAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 326 KVApvRHLSGNQFILELFYGPTGSFKDLSLQLMPHIFAYCippGCnYVILVATSGdTGSAVLNGFShlnknDKERIAVVT 405
Cdd:COG0498 74 RLA--DELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALER---GA-KTIVCASSG-NGSAALAAYA-----ARAGIEVFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 406 FFPENGVSDFQKAEII--GSQrengwAIGVRSDFDFCQTAIRKIFNDSDFtgflaveygtilSSANSINWARLLPQIVYH 483
Cdd:COG0498 142 FVPEGKVSPGQLAQMLtyGAH-----VIAVDGNFDDAQRLVKELAADEGL------------YAVNSINPARLEGQKTYA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 484 ASAYLELVNqrfisfgSPVDVCVPTGNFGNVLAAVYAKMM----GIPIR--KFI--CASNQNHVLTDFiKTGHYDLRNRK 555
Cdd:COG0498 205 FEIAEQLGR-------VPDWVVVPTGNGGNILAGYKAFKElkelGLIDRlpRLIavQATGCNPILTAF-ETGRDEYEPER 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 556 lAQTFSPSIDILKSSNLERHLYLMANKDGqlmanlyhqlesqlhfriekmlveklqqefVADWCSEGECLAAISTTYNAS 635
Cdd:COG0498 277 -PETIAPSMDIGNPSNGERALFALRESGG------------------------------TAVAVSDEEILEAIRLLARRE 325
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 29243946 636 GYILDPHTAVA-----KVVADKMQDKSCPVLIASTAHYSKFAPAIMQALGIK 682
Cdd:COG0498 326 GIFVEPATAVAvaglrKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
64-221 |
5.89e-40 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 144.26 E-value: 5.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 64 PGSGKTTVGRILGDKLGCCVIDVDsDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSAS-GSVISLSGSNPMHDASM 142
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTD-EEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEhGLVIATGGGAVLSEENR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 143 WHLKKNGIVVYLDVPLTDIISRLKsMRIDRIVGQN--TGASLRDSLKHVR--LYYKkwYDARVFCESGASAEEVADKVLD 218
Cdd:pfam01202 80 DLLKERGIVIYLDAPLEVLLERLK-RDKTRPLLQNkdPEEELLELLFEERdpLYEE--AADIVIDTDESSPEEVATEILE 156
|
...
gi 29243946 219 VVK 221
Cdd:pfam01202 157 ALE 159
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
57-204 |
2.27e-37 |
|
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: 136.92 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 57 NIVLMGPPGSGKTTVGRILGDKLGCCVIDVDsDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSAS-GSVISLSGSN 135
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLD-ELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29243946 136 PMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRIDRIVGQNTGASLRDSLKHVRLYYKKWYDARVFCE 204
Cdd:cd00464 80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD 148
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
304-670 |
1.62e-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: 137.13 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 304 DIPAAKLGEMIEtaygENFACSKvaPVRHLSG-NQFILELFYGPTGSFKDLSLQLMphiFAYCIPPGcNYVILVATSGDT 382
Cdd:TIGR00260 12 EKDLVDLGEGVT----PLFRAPA--LAANVGIkNLYVKELGHNPTLSFKDRGMAVA---LTKALELG-NDTVLCASTGNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 383 GSAVLNGFSHLNKNdkeriaVVTFFPENGVSDFQKAEIIGsqrENGWAIGVRSDFDFCQTAIRKIFNDSdftgflaveYG 462
Cdd:TIGR00260 82 GAAAAAYAGKAGLK------VVVLYPAGKISLGKLAQALG---YNAEVVAIDGNFDDAQRLVKQLFEDK---------PA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 463 TILSSANSInWARLLPQIvYHASAYLELVNQRfisfgSPVDVCVP---TGNFGNVLAAVYAKMMG----IPIRKFICASN 535
Cdd:TIGR00260 144 LGLNSANSI-PYRLEGQK-TYAFEAVEQLGWE-----APDKVVVPvpnSGNFGAIWKGFKEKKMLgldsLPVKRGIQAEG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 536 QNHVLTDFIKTGHYDLRNRKlaQTFSPSIDILKSSNLERHLYLMANKDGQlmanlyhqlesqlhfriekmlveklqqefv 615
Cdd:TIGR00260 217 AADIVRAFLEGGQWEPIETP--ETLSTAMDIGNPANWPRALEAFRRSNGY------------------------------ 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 29243946 616 ADWCSEGECLAAISTTYNASGYILDPHTAVAKVVADKMQDKscpvliaSTAHYSK 670
Cdd:TIGR00260 265 AEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEK-------GTADPAE 312
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
58-222 |
5.04e-32 |
|
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: 122.16 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDsDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSA-SGSVISLSGSNP 136
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTD-AEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 137 MHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRiDR--IVGQNTGASLRDSLKHVRLYYKKWYDARVFCeSGASAEEVAD 214
Cdd:COG0703 80 LSPENRELLKEHGTVVYLDASPETLLERLRRDD-NRplLQGEDPRERLEELLAEREPLYREVADITVDT-DGRSPEEVVD 157
|
....*...
gi 29243946 215 KVLDVVKR 222
Cdd:COG0703 158 EILEALEE 165
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
56-223 |
2.03e-30 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 117.98 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDsDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSAS-GSVISLSGS 134
Cdd:PRK00131 5 PNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTD-HLIEARAGKSIPEIFEEEGEAAFRELEEEVLAELLARhNLVISTGGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 135 NPMHDASMWHLKKNGIVVYLDVPLTDIISRLkSMRIDR--IVGQNTGASLRDSLKHVRLYYKKWYDARVFCEsGASAEEV 212
Cdd:PRK00131 84 AVLREENRALLRERGTVVYLDASFEELLRRL-RRDRNRplLQTNDPKEKLRDLYEERDPLYEEVADITVETD-GRSPEEV 161
|
170
....*....|.
gi 29243946 213 ADKVLDVVKRY 223
Cdd:PRK00131 162 VNEILEKLEAA 172
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
335-667 |
4.27e-23 |
|
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: 98.74 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 335 GNQFILELFYGPTGSFKDLSLQLMPHIFAYCIPPGcNYVILVATSGDTGSAVLNGFSHLNkndkerIAVVTFFPEnGVSD 414
Cdd:cd00640 15 ANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLP-KGVIIESTGGNTGIALAAAAARLG------LKCTIVMPE-GASP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 415 FQKAEIigsqRENG-WAIGVRSDFDFCQTAIRKIFNDSDftgflaveygtILSSANS-INWARLLPQIVYHASAYLELVN 492
Cdd:cd00640 87 EKVAQM----RALGaEVVLVPGDFDDAIALAKELAEEDP-----------GAYYVNQfDNPANIAGQGTIGLEILEQLGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 493 QRfisfgsPVDVCVPTGNFGNVLAAVYAKMMGIPIRKFICASNQnhvltdfiktghydlrnrklaqtfspsidilkssnl 572
Cdd:cd00640 152 QK------PDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE------------------------------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 573 erhlylmankdgqlmanlyhqlesqlhfriekmlveklqqefvADWCSEGECLAAISTTYNASGYILDPHTAVAKVVADK 652
Cdd:cd00640 190 -------------------------------------------VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALK 226
|
330
....*....|....*...
gi 29243946 653 MQDKSCP---VLIASTAH 667
Cdd:cd00640 227 LAKKLGKgktVVVILTGG 244
|
|
| PRK00625 |
PRK00625 |
shikimate kinase; Provisional |
56-165 |
2.96e-17 |
|
shikimate kinase; Provisional
Pssm-ID: 134335 [Multi-domain] Cd Length: 173 Bit Score: 80.19 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVD---SDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSASGSVISLS 132
Cdd:PRK00625 1 MQIFLCGLPTVGKTSFGKALAKFLSLPFFDTDdliVSNYHGALYSSPKEIYQAYGEEGFCREEFLALTSLPVIPSIVALG 80
|
90 100 110
....*....|....*....|....*....|...
gi 29243946 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 |
3.55e-17 |
|
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: 76.69 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 231 FISTRhvclkdhdKKFPPKYFSEAVVEGLASDGGLFVPEkEFPKLSPGEWNNLIGATYIERAQVLLERCIhPADIPAAKL 310
Cdd:pfam14821 2 YISTR--------GGAPPLSFEDALLKGLAPDGGLYVPE-EIPQLSAEELASWRGLSYQELAFEVLSLFI-GDDIPEEDL 71
|
....*...
gi 29243946 311 GEMIETAY 318
Cdd:pfam14821 72 KALIERAY 79
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
56-217 |
1.94e-15 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 74.74 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDSdVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSA-SGSVISLSGS 134
Cdd:PRK13947 2 KNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDK-EIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARlKNLVIATGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 135 NPMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRiDR--IVGQNTGASLRDSLKHvRLYYkkwYDARVFC--ESGASAE 210
Cdd:PRK13947 81 VVLNPENVVQLRKNGVVICLKARPEVILRRVGKKK-SRplLMVGDPEERIKELLKE-REPF---YDFADYTidTGDMTID 155
|
....*..
gi 29243946 211 EVADKVL 217
Cdd:PRK13947 156 EVAEEII 162
|
|
| PRK13946 |
PRK13946 |
shikimate kinase; Provisional |
50-230 |
1.57e-13 |
|
shikimate kinase; Provisional
Pssm-ID: 184411 [Multi-domain] Cd Length: 184 Bit Score: 69.57 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 50 HSLVGDKNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDSDVlEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSASGS-V 128
Cdd:PRK13946 5 RAALGKRTVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEI-ERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGPlV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 129 ISLSGSNPMHDASMWHLKKNGIVVYLDVPLtDIISRLKSMRIDR--IVGQNTGASLRDsLKHVRlyYKKWYDARVFCESG 206
Cdd:PRK13946 84 LATGGGAFMNEETRAAIAEKGISVWLKADL-DVLWERVSRRDTRplLRTADPKETLAR-LMEER--YPVYAEADLTVASR 159
|
170 180
....*....|....*....|....*
gi 29243946 207 A-SAEEVADKVLDVVKRYQDVDSET 230
Cdd:PRK13946 160 DvPKEVMADEVIEALAAYLEKEEAA 184
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
346-672 |
1.74e-11 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 67.15 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 346 PTGSFKDLSLQL------------MPHIFAYCippgcnyvilvATSGDTgSAVLNGFShlnknDKERIAVVTFFPENGVS 413
Cdd:PLN02569 161 HTGSFKDLGMTVlvsqvnrlrkmaKPVVGVGC-----------ASTGDT-SAALSAYC-----AAAGIPSIVFLPADKIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 414 DFQKAEIIgSQRENGWAIGvrSDFDFCQTAIRKIfnDSDFTGFLaveygtilssANSINWARLLPQivyhASAYLELVNQ 493
Cdd:PLN02569 224 IAQLVQPI-ANGALVLSID--TDFDGCMRLIREV--TAELPIYL----------ANSLNSLRLEGQ----KTAAIEILQQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 494 rfisFGSPVD--VCVPTGNFGNVLAAVYA----KMMGI--PIRKFICASNQN-HVLTDFIKTGHYDLRNRKLAQTFSPSI 564
Cdd:PLN02569 285 ----FDWEVPdwVIVPGGNLGNIYAFYKGfkmcKELGLvdRLPRLVCAQAANaNPLYRAYKSGWEEFKPVKANPTFASAI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 565 DILKSSNLERHLYLMANKDGqlmanlyhqlesqlhfriekmLVEKLQQEFVADWCSEGEclaaisttynASGYILDPHTA 644
Cdd:PLN02569 361 QIGDPVSIDRAVYALKESNG---------------------IVEEATEEELMDAQAEAD----------KTGMFLCPHTG 409
|
330 340 350
....*....|....*....|....*....|...
gi 29243946 645 VAKVVADKMQD-----KSCPVLIASTAHYSKFA 672
Cdd:PLN02569 410 VALAALKKLRAsgvigPTDRTVVVSTAHGLKFT 442
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
58-166 |
4.21e-11 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 62.27 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDSDVLEKAwNMSASEKLQDVGNERFLEEEGKTVLNLSASGSVISLSGSNPM 137
Cdd:PRK03731 5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTS-NMTVAEIVEREGWAGFRARESAALEAVTAPSTVIATGGGIIL 83
|
90 100
....*....|....*....|....*....
gi 29243946 138 HDASMWHLKKNGIVVYLDVPLTDIISRLK 166
Cdd:PRK03731 84 TEENRHFMRNNGIVIYLCAPVSVLANRLE 112
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
56-184 |
1.95e-10 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 60.13 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDSdVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSA-SGSVISLSGS 134
Cdd:PRK13949 2 ARIFLVGYMGAGKTTLGKALARELGLSFIDLDF-FIENRFHKTVGDIFAERGEAVFRELERNMLHEVAEfEDVVISTGGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 29243946 135 NPMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRIDR-IVGQNTGASLRD 184
Cdd:PRK13949 81 APCFFDNMELMNASGTTVYLKVSPEVLFVRLRLAKQQRpLLKGKSDEELLD 131
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
343-646 |
1.05e-09 |
|
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: 60.40 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 343 FYGPTGSFKDLSLQlmpHIFAYCIPPGCNYVILVATSGDTGSAVLNGFSHLNkndkerIAVVTFFPENGVSDFQK----- 417
Cdd:pfam00291 30 SLNPTGSFKDRGAL---NLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLG------LKVTIVVPEDAPPGKLLlmral 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 418 -AEIigsqrengwaIGVRSDFDFCQTAIRKIFNDSDftgflavEYGTILSSANSINWArllpqivYHASAYLELVNQrfi 496
Cdd:pfam00291 101 gAEV----------VLVGGDYDEAVAAARELAAEGP-------GAYYINQYDNPLNIE-------GYGTIGLEILEQ--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 497 sFGSPVD-VCVPTGNFGNVLA-AVYAKMMGIPIRKFICASNQNHVLTDFIKTGHYDlrNRKLAQTFSPSIDILKSSnler 574
Cdd:pfam00291 154 -LGGDPDaVVVPVGGGGLIAGiARGLKELGPDVRVIGVEPEGAPALARSLAAGRPV--PVPVADTIADGLGVGDEP---- 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29243946 575 hlylmankdgqlmanlyhqleSQLHFRiekmLVEKLQQEFVAdwCSEGECLAAISTTYNASGYILDPHTAVA 646
Cdd:pfam00291 227 ---------------------GALALD----LLDEYVGEVVT--VSDEEALEAMRLLARREGIVVEPSSAAA 271
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
56-168 |
1.90e-09 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 59.71 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDSdVLEKAWN-MSASEKLQDVGNERFLEEEGKTVLNLSASGSVISLSGS 134
Cdd:PLN02199 103 RSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDT-LIEQAMNgTSVAEIFVHHGENFFRGKETDALKKLSSRYQVVVSTGG 181
|
90 100 110
....*....|....*....|....*....|....
gi 29243946 135 NPMHDASMWHLKKNGIVVYLDVPLTDIISRLKSM 168
Cdd:PLN02199 182 GAVIRPINWKYMHKGISIWLDVPLEALAHRIAAV 215
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
62-224 |
1.46e-08 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 55.22 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 62 GPPGSGKTTVGRILGDKLGCCVidVDSDVLEKAW---NMSASE------------KLQDVGNERFLEEEGKTVLNLSASG 126
Cdd:COG1102 7 REPGSGGTTIAKRLAEKLGLPL--YDGEILREAAkerGLSEEEfekldekapsllYRDTAEEDEIDRALDKVIRELARKG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 127 SVISLS-GSNpmhdasmWHLK--KNGIVVYLDVPLTDiisrlksmRIDRIVgQNTGASLRDSLKHV-------RLYYKK- 195
Cdd:COG1102 85 NCVIVGrLAD-------WILRdrPNVLKVFLTAPLEV--------RVKRIA-EREGISEEEAEKEIkkrdksrAKYYKYy 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 29243946 196 ----WYDAR----VFCESGASAEEVADKVLDVVKRYQ 224
Cdd:COG1102 149 ygidWGDPSnydlVINTSRLGIEEAVDLILAAIEARE 185
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
58-105 |
5.36e-08 |
|
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: 52.64 E-value: 5.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIdvDSDVLEKAWN---MSASEKLQD 105
Cdd:cd02021 2 IVVMGVSGSGKSTVGKALAERLGAPFI--DGDDLHPPANiakMAAGIPLND 50
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
58-167 |
1.25e-06 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 49.14 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIdvDSDVLEKA---WNMSASEKLQDVGNERFLEEEGKTVLNLSASGSVIsLSGS 134
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRL--RSDVVRKRlfgAGLAPLERSPEATARTYARLLALARELLAAGRSVI-LDAT 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 29243946 135 NPMHDA-SMWH--LKKNGI---VVYLDVPLTDIISRLKS 167
Cdd:COG0645 79 FLRRAQrEAFRalAEEAGApfvLIWLDAPEEVLRERLEA 117
|
|
| aroK |
PRK05057 |
shikimate kinase AroK; |
56-166 |
1.61e-06 |
|
shikimate kinase AroK;
Pssm-ID: 235335 [Multi-domain] Cd Length: 172 Bit Score: 48.94 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDsDVLEK------AWnmsasekLQDV-GNERFLEEEGKTVLNLS----- 123
Cdd:PRK05057 5 RNIFLVGPMGAGKSTIGRQLAQQLNMEFYDSD-QEIEKrtgadiGW-------VFDVeGEEGFRDREEKVINELTekqgi 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 29243946 124 ----ASGSVISLSGSNpmhdasmwHLKKNGIVVYLDVPLTDIISRLK 166
Cdd:PRK05057 77 vlatGGGSVKSRETRN--------RLSARGVVVYLETTIEKQLARTQ 115
|
|
| PRK03839 |
PRK03839 |
putative kinase; Provisional |
58-222 |
2.29e-06 |
|
putative kinase; Provisional
Pssm-ID: 179660 Cd Length: 180 Bit Score: 48.56 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDSDVLEKAWNMSASEKLQ-DVGN-ERFLEEEgktvlnlsasgsvisLSGSN 135
Cdd:PRK03839 3 IAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEiDFDKlAYFIEEE---------------FKEKN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 136 PMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRIDR-IVGQNTGASLRDslkhVRLYYKKWYDARVF--CESGASAEEV 212
Cdd:PRK03839 68 VVLDGHLSHLLPVDYVIVLRAHPKIIKERLKERGYSKkKILENVEAELVD----VCLCEALEEKEKVIevDTTGKTPEEV 143
|
170
....*....|
gi 29243946 213 ADKVLDVVKR 222
Cdd:PRK03839 144 VEEILELIKS 153
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
58-89 |
3.55e-06 |
|
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: 47.82 E-value: 3.55e-06
10 20 30
....*....|....*....|....*....|..
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDSD 89
Cdd:COG3265 4 IVVMGVSGSGKSTVGQALAERLGWPFIDGDDF 35
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
57-94 |
5.59e-06 |
|
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: 47.62 E-value: 5.59e-06
10 20 30
....*....|....*....|....*....|....*...
gi 29243946 57 NIVLMGPPGSGKTTVGRILGDKLGCCVIDVdSDVLEKA 94
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHIST-GDLLREE 37
|
|
| PRK08118 |
PRK08118 |
DNA topology modulation protein; |
56-115 |
6.63e-06 |
|
DNA topology modulation protein;
Pssm-ID: 181235 Cd Length: 167 Bit Score: 46.91 E-value: 6.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDSDVLEKAWNMSASEKLQDVGNERFLEEE 115
Cdd:PRK08118 2 KKIILIGSGGSGKSTLARQLGEKLNIPVHHLDALFWKPNWEGVPKEEQITVQNELVKEDE 61
|
|
| Fap7 |
COG1936 |
Broad-specificity NMP kinase [Nucleotide transport and metabolism]; |
58-93 |
1.23e-05 |
|
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
Pssm-ID: 441539 [Multi-domain] Cd Length: 173 Bit Score: 46.35 E-value: 1.23e-05
10 20 30
....*....|....*....|....*....|....*.
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVdSDVLEK 93
Cdd:COG1936 3 IAITGTPGTGKTTVAKLLAERLGLEVIHL-NDLVKE 37
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
57-80 |
3.25e-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: 45.50 E-value: 3.25e-05
10 20
....*....|....*....|....
gi 29243946 57 NIVLMGPPGSGKTTVGRILGDKLG 80
Cdd:COG0563 2 RIILLGPPGAGKGTQAKRLAEKYG 25
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
59-164 |
3.30e-05 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 59 VLMGPPGSGKTTVGRILGDKLGCCVIDVDSDVlEKAWNMSASEKLQDVGNERFLEEEGKTVLN-LSASGSVISLSGSNPM 137
Cdd:PRK14021 10 VIIGMMGAGKTRVGKEVAQMMRLPFADADVEI-EREIGMSIPSYFEEYGEPAFREVEADVVADmLEDFDGIFSLGGGAPM 88
|
90 100 110
....*....|....*....|....*....|.
gi 29243946 138 HDASMWHLKK----NGIVVYLDVPLTDIISR 164
Cdd:PRK14021 89 TPSTQHALASyiahGGRVVYLDADPKEAMER 119
|
|
| therm_gnt_kin |
TIGR01313 |
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ... |
58-176 |
4.05e-05 |
|
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: 44.70 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDSdvLEKAWN---MSASEKLQDvgNER--FLEEEGKTVLNLSASGSVISLS 132
Cdd:TIGR01313 1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDD--LHPAANiekMSAGIPLND--DDRwpWLQNLNDASTAAAAKNKVGIIT 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 133 GSNpmhdasmwhLKK---------NGIV--VYLDVPLTDIISRLKS-----MRIDRIVGQ 176
Cdd:TIGR01313 77 CSA---------LKRhyrdilreaEPNLhfIYLSGDKDVILERMKArkghfMKADMLESQ 127
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
58-87 |
1.12e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 42.42 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVD 87
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDNVRD 30
|
|
| PRK13948 |
PRK13948 |
shikimate kinase; Provisional |
58-154 |
1.63e-04 |
|
shikimate kinase; Provisional
Pssm-ID: 184413 [Multi-domain] Cd Length: 182 Bit Score: 43.24 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDSdVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSASG-SVISLSGSNP 136
Cdd:PRK13948 13 VALAGFMGTGKSRIGWELSRALMLHFIDTDR-YIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLTRLDyAVISLGGGTF 91
|
90
....*....|....*...
gi 29243946 137 MHDASMWHLKKNGIVVYL 154
Cdd:PRK13948 92 MHEENRRKLLSRGPVVVL 109
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
25-93 |
1.79e-04 |
|
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: 44.52 E-value: 1.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 25 VQSRTQLLLPRASARAESGKSWHsthslvgdKNIVLMGPPGSGKTTVGRILGDKLGCCVIDVD-SDVLEK 93
Cdd:COG0464 169 LRELVALPLKRPELREEYGLPPP--------RGLLLYGPPGTGKTLLARALAGELGLPLIEVDlSDLVSK 230
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
56-103 |
1.92e-04 |
|
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: 42.72 E-value: 1.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDSDVLEKAWnMSASEKL 103
Cdd:cd19509 33 RGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKW-VGESEKI 79
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
58-81 |
4.49e-04 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 41.72 E-value: 4.49e-04
10 20
....*....|....*....|....
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGC 81
Cdd:PRK04182 3 ITISGPPGSGKTTVARLLAEKLGL 26
|
|
| cyt_kin_arch |
TIGR02173 |
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ... |
58-80 |
7.86e-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: 40.87 E-value: 7.86e-04
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
58-80 |
1.35e-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: 39.78 E-value: 1.35e-03
10 20
....*....|....*....|...
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLG 80
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLAKKLG 24
|
|
| adk |
TIGR01351 |
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ... |
57-84 |
1.67e-03 |
|
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 273569 [Multi-domain] Cd Length: 210 Bit Score: 40.68 E-value: 1.67e-03
10 20
....*....|....*....|....*...
gi 29243946 57 NIVLMGPPGSGKTTVGRILGDKLGCCVI 84
Cdd:TIGR01351 1 RLVLLGPPGSGKGTQAKRIAEKYGLPHI 28
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
58-87 |
1.78e-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: 1.78e-03
10 20 30
....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVD 87
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSSD 31
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
58-87 |
2.26e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 40.04 E-value: 2.26e-03
10 20 30
....*....|....*....|....*....|....
gi 29243946 58 IVLMGPPGSGKTTV----GRILGDKLGCCVIDVD 87
Cdd:COG0378 16 VNLMGSPGSGKTTLlektIRALKDRLRIAVIEGD 49
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
56-117 |
2.62e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 39.05 E-value: 2.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCC---VIDVDSDVLEKAWNMSASEKLQDVGNERFLEEEGK 117
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPgapFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAK 84
|
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
58-106 |
2.64e-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: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVdsdvlekawNMSASEKLQDV 106
Cdd:NF033453 19 ILLVGPPGSGKTALLRELAAKRGAPVINV---------NLELSRRLLEL 58
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
56-80 |
2.80e-03 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 39.75 E-value: 2.80e-03
10 20
....*....|....*....|....*
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLG 80
Cdd:PRK00279 1 MRLILLGPPGAGKGTQAKFIAEKYG 25
|
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| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
56-103 |
3.51e-03 |
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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: 39.20 E-value: 3.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 29243946 56 KNIVLMGPPGSGKTTVGRILGDKLGCCVIDVDSDVLEKAWnMSASEKL 103
Cdd:cd19525 56 KGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW-VGEGEKM 102
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| TIGR00152 |
TIGR00152 |
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ... |
58-158 |
3.61e-03 |
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dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 272931 Cd Length: 190 Bit Score: 39.30 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDS---DVLEKawNMSASEKLQDVGNERFLEEEGKtvLNLSASGSVI----- 129
Cdd:TIGR00152 2 IALTGGIGSGKSTVLQYLADKYHFPVIDADKiahQVVEP--GQPAYHAIADHFGANILNQDGE--LDRKALGNYVfndpe 77
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90 100 110
....*....|....*....|....*....|....*..
gi 29243946 130 ---SLSG-SNPMHDASMWHLK----KNGIVVYLDVPL 158
Cdd:TIGR00152 78 elkWLNAlTHPLIRQWMKKLIaqfqSKYALVLLDVPL 114
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| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
58-165 |
5.48e-03 |
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bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 39.89 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 58 IVLMGPPGSGKTTVGRILGDKLGCCVIDVDSDVlEKAWNMSASEKLQDVGNERFLEEEGKTVLNLSASGSVISLSGSNPM 137
Cdd:PRK13951 3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEI-ERREGRSVRRIFEEDGEEYFRLKEKELLRELVERDNVVVATGGGVV 81
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90 100
....*....|....*....|....*...
gi 29243946 138 HDASMWHLKKNGIVVYLDVPLTDIISRL 165
Cdd:PRK13951 82 IDPENRELLKKEKTLFLYAPPEVLMERV 109
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| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
48-106 |
6.84e-03 |
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proteases similar to RecA; RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 38.03 E-value: 6.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243946 48 STHSLVGDKNIVLMGPPGSGKTTVGRILGDKLGCCVIDVD-SDVLEKAWNMSAsEKLQDV 106
Cdd:cd19481 19 RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKlSSLLSKYVGESE-KNLRKI 77
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