|
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: 601.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 230 TFISTRHVWPedceqKVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYVERAQILLERCIhPADIPAAR 309
Cdd:cd01560 1 KYVSTRGGNP-----GVS---FSEALLSGLAPDGGLYVPE-ELPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 310 LGEMIETAYGEnFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHCIPP-SCNYMILVATSGDTGSAVLN 388
Cdd:cd01560 71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 389 GFSrlnknDKQRIAVVAFFPENGVSDFQKAQIIGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTgfltveYGTILSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 469 NSINWGRLLPQVVYHASAYLDLVSQGFisfGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNHVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKRGE---GEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 549 YDLRErKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNRLESQHHFQIEKALVEKLQQDFVADWCSEGECLAAI 628
Cdd:cd01560 296 YDRRE-SLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 629 NSTYNTSGYILDPHTAVAKVVADRVQDK-TCPVIISSTAHYSKFAPAIMQALKIKEInetsssqlyllgsynALPPLHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEPV---------------ELPEELEG 439
|
490 500
....*....|....*....|....*.
gi 1034569575 708 LLERTKQQEKMEyqvcaADMNVLKSH 733
Cdd:cd01560 440 LEDLEKRHEDLL-----ADKELLKSH 460
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
251-682 |
1.17e-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: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 251 FSEAVIEGLASDGGLfVPAkEFPKLSCGEWKSLVG-ATYVEraqiLLercihPADIPAARLgemietAYGENFA----CS 325
Cdd:COG0498 11 FSDALLYLCPDCGGL-LPD-SYPALSREDLASRRGlWRYRE----LL-----PFDDEEKAV------SLGEGGTplvkAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 326 KIApvRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHcippSCNYMILVATSGdTGSAVLNGFSrlnknDKQRIAVVA 405
Cdd:COG0498 74 RLA--DELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALE----RGAKTIVCASSG-NGSAALAAYA-----ARAGIEVFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 406 FFPENGVSDFQKAQII--GSQrengwAVGVESDFDFCQTAIKRIFNDSDFtgfltveygtilSSANSINWGRLLPQVVYH 483
Cdd:COG0498 142 FVPEGKVSPGQLAQMLtyGAH-----VIAVDGNFDDAQRLVKELAADEGL------------YAVNSINPARLEGQKTYA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 484 ASAYLDLVSqgfisfgSPVDVCIPTGNFGNILAAVYAKMM----GIPIR--KFI--CASNQNHVLTDFiKTGHyDLRERK 555
Cdd:COG0498 205 FEIAEQLGR-------VPDWVVVPTGNGGNILAGYKAFKElkelGLIDRlpRLIavQATGCNPILTAF-ETGR-DEYEPE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 556 LAQTFSPSIDILKSSNLERHLHLMANKDGqlmtelfnrlesqhhfqiekalveklqqdfVADWCSEGECLAAINSTYNTS 635
Cdd:COG0498 276 RPETIAPSMDIGNPSNGERALFALRESGG------------------------------TAVAVSDEEILEAIRLLARRE 325
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034569575 636 GYILDPHTAVA-----KVVADRVQDKTCPVIISSTAHYSKFAPAIMQALKIK 682
Cdd:COG0498 326 GIFVEPATAVAvaglrKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
64-221 |
2.73e-41 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 148.11 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 64 PGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSNPMHDASM 142
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTDEEI-EKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEhGLVIATGGGAVLSEENR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 143 WHLKKNGIIVYLDVPLLDLICRLKlMKTDRIVGQN--SGTSMKDLLKFRRQY-YKKwYDARVFCESGASPEEVADKVLNA 219
Cdd:pfam01202 80 DLLKERGIVIYLDAPLEVLLERLK-RDKTRPLLQNkdPEEELLELLFEERDPlYEE-AADIVIDTDESSPEEVATEILEA 157
|
..
gi 1034569575 220 IK 221
Cdd:pfam01202 158 LE 159
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
57-211 |
6.61e-41 |
|
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: 146.93 E-value: 6.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 57 NIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSN 135
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELI-EQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034569575 136 PMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKTDRIVGQNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:cd00464 80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD-ELSPEE 154
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
289-670 |
5.85e-37 |
|
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: 141.37 E-value: 5.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 289 VERAQILLErcihPADIPAARLGEMIEtaygENFACSKIaPVRHLSGNQFILELFHGPTGSFKDLSLQLMphiFAHcIPP 368
Cdd:TIGR00260 1 VWRYREFLP----VTEKDLVDLGEGVT----PLFRAPAL-AANVGIKNLYVKELGHNPTLSFKDRGMAVA---LTK-ALE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 369 SCNYMILVATSGDTGSAVLNGFSRLNKNdkqriaVVAFFPENGVSDFQKAQIIGsqrENGWAVGVESDFDFCQTAIKRIF 448
Cdd:TIGR00260 68 LGNDTVLCASTGNTGAAAAAYAGKAGLK------VVVLYPAGKISLGKLAQALG---YNAEVVAIDGNFDDAQRLVKQLF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 449 NDSdftgfltveYGTILSSANSInWGRLLPQvVYHASAYLDLVSQgfisfGSPVDVCIP---TGNFGNILAAVYAKMMG- 524
Cdd:TIGR00260 139 EDK---------PALGLNSANSI-PYRLEGQ-KTYAFEAVEQLGW-----EAPDKVVVPvpnSGNFGAIWKGFKEKKMLg 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 525 ---IPIRKFICASNQNHVLTDFIKTGHYDLRERKlaQTFSPSIDILKSSNLERHLHLMANKDGQlMTELfnrlesqhhfq 601
Cdd:TIGR00260 203 ldsLPVKRGIQAEGAADIVRAFLEGGQWEPIETP--ETLSTAMDIGNPANWPRALEAFRRSNGY-AEDL----------- 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034569575 602 iekalveklqqdfvadwcSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQDKTcpviissTAHYSK 670
Cdd:TIGR00260 269 ------------------SDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKG-------TADPAE 312
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
58-222 |
1.08e-34 |
|
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: 129.48 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSA-SGSVISLTGSNP 136
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEI-EERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 137 MHDASMWHLKKNGIIVYLDVPLLDLICRLKLmKTDR--IVGQNSGTSMKDLLKFRRQYYKKWYDARVFCeSGASPEEVAD 214
Cdd:COG0703 80 LSPENRELLKEHGTVVYLDASPETLLERLRR-DDNRplLQGEDPRERLEELLAEREPLYREVADITVDT-DGRSPEEVVD 157
|
....*...
gi 1034569575 215 KVLNAIKR 222
Cdd:COG0703 158 EILEALEE 165
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
56-223 |
3.67e-33 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 125.69 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEgKAVLNF--SASGSVISLTG 133
Cdd:PRK00131 5 PNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLI-EARAGKSIPEIFEEEGEAAFRELE-EEVLAEllARHNLVISTGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 134 SNPMHDASMWHLKKNGIIVYLDVPLLDLICRLKlMKTDR--IVGQNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:PRK00131 83 GAVLREENRALLRERGTVVYLDASFEELLRRLR-RDRNRplLQTNDPKEKLRDLYEERDPLYEEVADITVETD-GRSPEE 160
|
170
....*....|..
gi 1034569575 212 VADKVLNAIKRY 223
Cdd:PRK00131 161 VVNEILEKLEAA 172
|
|
| Thr_synth_N |
pfam14821 |
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine ... |
231-318 |
3.36e-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: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 231 FISTRhvwpeDCEQKVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYVERAQILLERCIhPADIPAARL 310
Cdd:pfam14821 2 YISTR-----GGAPPLS---FEDALLKGLAPDGGLYVPE-EIPQLSAEELASWRGLSYQELAFEVLSLFI-GDDIPEEDL 71
|
....*...
gi 1034569575 311 GEMIETAY 318
Cdd:pfam14821 72 KALIERAY 79
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
346-672 |
1.29e-11 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 67.53 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 346 PTGSFKDLSLQL------------MPHIFAHCippscnymilvATSGDTGSAVLNGFSRLNkndkqrIAVVAFFPENGVS 413
Cdd:PLN02569 161 HTGSFKDLGMTVlvsqvnrlrkmaKPVVGVGC-----------ASTGDTSAALSAYCAAAG------IPSIVFLPADKIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 414 DFQKAQIIGsqreNGWAV-GVESDFDFCQTAIKRIfndsdftgflTVEYGTILssANSINWGRLLPQvvyhASAYLDLVS 492
Cdd:PLN02569 224 IAQLVQPIA----NGALVlSIDTDFDGCMRLIREV----------TAELPIYL--ANSLNSLRLEGQ----KTAAIEILQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 493 QgfisFGSPVD--VCIPTGNFGNILAAVYA----KMMGI--PIRKFICASNQN-HVLTDFIKTGHYDLRERKLAQTFSPS 563
Cdd:PLN02569 284 Q----FDWEVPdwVIVPGGNLGNIYAFYKGfkmcKELGLvdRLPRLVCAQAANaNPLYRAYKSGWEEFKPVKANPTFASA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 564 IDILKSSNLERHLHLMANKDGqlmtelfnrlesqhhfqiekaLVEKLQQDFVADWCSEGEclaainstynTSGYILDPHT 643
Cdd:PLN02569 360 IQIGDPVSIDRAVYALKESNG---------------------IVEEATEEELMDAQAEAD----------KTGMFLCPHT 408
|
330 340 350
....*....|....*....|....*....|....
gi 1034569575 644 AVA-----KVVADRVQDKTCPVIISSTAHYSKFA 672
Cdd:PLN02569 409 GVAlaalkKLRASGVIGPTDRTVVVSTAHGLKFT 442
|
|
| therm_gnt_kin |
TIGR01313 |
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ... |
58-176 |
9.35e-04 |
|
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: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDdiLEKTWN---MSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGS 134
Cdd:TIGR01313 1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDD--LHPAANiekMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034569575 135 NpmhdasmwhLKK-----------NGIIVYLDVPLLDLICRLK-----LMKTDRIVGQ 176
Cdd:TIGR01313 79 A---------LKRhyrdilreaepNLHFIYLSGDKDVILERMKarkghFMKADMLESQ 127
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
31-93 |
1.04e-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: 42.21 E-value: 1.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034569575 31 RFLSRTFALAELRKSWYSTHSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVD-DDILEK 93
Cdd:COG0464 167 EELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDlSDLVSK 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
56-88 |
4.30e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.51 E-value: 4.30e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKL-----GCCVIDVDD 88
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELgppggGVIYIDGED 40
|
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
58-110 |
4.38e-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: 38.24 E-value: 4.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVdddilektwNMSVSEKLQDVGNEQ 110
Cdd:NF033453 19 ILLVGPPGSGKTALLRELAAKRGAPVINV---------NLELSRRLLELPEKQ 62
|
|
| |
|
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: 601.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 230 TFISTRHVWPedceqKVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYVERAQILLERCIhPADIPAAR 309
Cdd:cd01560 1 KYVSTRGGNP-----GVS---FSEALLSGLAPDGGLYVPE-ELPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 310 LGEMIETAYGEnFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHCIPP-SCNYMILVATSGDTGSAVLN 388
Cdd:cd01560 71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 389 GFSrlnknDKQRIAVVAFFPENGVSDFQKAQIIGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTgfltveYGTILSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 469 NSINWGRLLPQVVYHASAYLDLVSQGFisfGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNHVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKRGE---GEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 549 YDLRErKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNRLESQHHFQIEKALVEKLQQDFVADWCSEGECLAAI 628
Cdd:cd01560 296 YDRRE-SLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 629 NSTYNTSGYILDPHTAVAKVVADRVQDK-TCPVIISSTAHYSKFAPAIMQALKIKEInetsssqlyllgsynALPPLHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEPV---------------ELPEELEG 439
|
490 500
....*....|....*....|....*.
gi 1034569575 708 LLERTKQQEKMEyqvcaADMNVLKSH 733
Cdd:cd01560 440 LEDLEKRHEDLL-----ADKELLKSH 460
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
251-682 |
1.17e-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: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 251 FSEAVIEGLASDGGLfVPAkEFPKLSCGEWKSLVG-ATYVEraqiLLercihPADIPAARLgemietAYGENFA----CS 325
Cdd:COG0498 11 FSDALLYLCPDCGGL-LPD-SYPALSREDLASRRGlWRYRE----LL-----PFDDEEKAV------SLGEGGTplvkAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 326 KIApvRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHcippSCNYMILVATSGdTGSAVLNGFSrlnknDKQRIAVVA 405
Cdd:COG0498 74 RLA--DELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALE----RGAKTIVCASSG-NGSAALAAYA-----ARAGIEVFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 406 FFPENGVSDFQKAQII--GSQrengwAVGVESDFDFCQTAIKRIFNDSDFtgfltveygtilSSANSINWGRLLPQVVYH 483
Cdd:COG0498 142 FVPEGKVSPGQLAQMLtyGAH-----VIAVDGNFDDAQRLVKELAADEGL------------YAVNSINPARLEGQKTYA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 484 ASAYLDLVSqgfisfgSPVDVCIPTGNFGNILAAVYAKMM----GIPIR--KFI--CASNQNHVLTDFiKTGHyDLRERK 555
Cdd:COG0498 205 FEIAEQLGR-------VPDWVVVPTGNGGNILAGYKAFKElkelGLIDRlpRLIavQATGCNPILTAF-ETGR-DEYEPE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 556 LAQTFSPSIDILKSSNLERHLHLMANKDGqlmtelfnrlesqhhfqiekalveklqqdfVADWCSEGECLAAINSTYNTS 635
Cdd:COG0498 276 RPETIAPSMDIGNPSNGERALFALRESGG------------------------------TAVAVSDEEILEAIRLLARRE 325
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034569575 636 GYILDPHTAVA-----KVVADRVQDKTCPVIISSTAHYSKFAPAIMQALKIK 682
Cdd:COG0498 326 GIFVEPATAVAvaglrKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
64-221 |
2.73e-41 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 148.11 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 64 PGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSNPMHDASM 142
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTDEEI-EKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEhGLVIATGGGAVLSEENR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 143 WHLKKNGIIVYLDVPLLDLICRLKlMKTDRIVGQN--SGTSMKDLLKFRRQY-YKKwYDARVFCESGASPEEVADKVLNA 219
Cdd:pfam01202 80 DLLKERGIVIYLDAPLEVLLERLK-RDKTRPLLQNkdPEEELLELLFEERDPlYEE-AADIVIDTDESSPEEVATEILEA 157
|
..
gi 1034569575 220 IK 221
Cdd:pfam01202 158 LE 159
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
57-211 |
6.61e-41 |
|
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: 146.93 E-value: 6.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 57 NIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSN 135
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELI-EQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034569575 136 PMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKTDRIVGQNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:cd00464 80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD-ELSPEE 154
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
289-670 |
5.85e-37 |
|
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: 141.37 E-value: 5.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 289 VERAQILLErcihPADIPAARLGEMIEtaygENFACSKIaPVRHLSGNQFILELFHGPTGSFKDLSLQLMphiFAHcIPP 368
Cdd:TIGR00260 1 VWRYREFLP----VTEKDLVDLGEGVT----PLFRAPAL-AANVGIKNLYVKELGHNPTLSFKDRGMAVA---LTK-ALE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 369 SCNYMILVATSGDTGSAVLNGFSRLNKNdkqriaVVAFFPENGVSDFQKAQIIGsqrENGWAVGVESDFDFCQTAIKRIF 448
Cdd:TIGR00260 68 LGNDTVLCASTGNTGAAAAAYAGKAGLK------VVVLYPAGKISLGKLAQALG---YNAEVVAIDGNFDDAQRLVKQLF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 449 NDSdftgfltveYGTILSSANSInWGRLLPQvVYHASAYLDLVSQgfisfGSPVDVCIP---TGNFGNILAAVYAKMMG- 524
Cdd:TIGR00260 139 EDK---------PALGLNSANSI-PYRLEGQ-KTYAFEAVEQLGW-----EAPDKVVVPvpnSGNFGAIWKGFKEKKMLg 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 525 ---IPIRKFICASNQNHVLTDFIKTGHYDLRERKlaQTFSPSIDILKSSNLERHLHLMANKDGQlMTELfnrlesqhhfq 601
Cdd:TIGR00260 203 ldsLPVKRGIQAEGAADIVRAFLEGGQWEPIETP--ETLSTAMDIGNPANWPRALEAFRRSNGY-AEDL----------- 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034569575 602 iekalveklqqdfvadwcSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQDKTcpviissTAHYSK 670
Cdd:TIGR00260 269 ------------------SDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKG-------TADPAE 312
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
58-222 |
1.08e-34 |
|
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: 129.48 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSA-SGSVISLTGSNP 136
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEI-EERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 137 MHDASMWHLKKNGIIVYLDVPLLDLICRLKLmKTDR--IVGQNSGTSMKDLLKFRRQYYKKWYDARVFCeSGASPEEVAD 214
Cdd:COG0703 80 LSPENRELLKEHGTVVYLDASPETLLERLRR-DDNRplLQGEDPRERLEELLAEREPLYREVADITVDT-DGRSPEEVVD 157
|
....*...
gi 1034569575 215 KVLNAIKR 222
Cdd:COG0703 158 EILEALEE 165
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
56-223 |
3.67e-33 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 125.69 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEgKAVLNF--SASGSVISLTG 133
Cdd:PRK00131 5 PNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLI-EARAGKSIPEIFEEEGEAAFRELE-EEVLAEllARHNLVISTGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 134 SNPMHDASMWHLKKNGIIVYLDVPLLDLICRLKlMKTDR--IVGQNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:PRK00131 83 GAVLREENRALLRERGTVVYLDASFEELLRRLR-RDRNRplLQTNDPKEKLRDLYEERDPLYEEVADITVETD-GRSPEE 160
|
170
....*....|..
gi 1034569575 212 VADKVLNAIKRY 223
Cdd:PRK00131 161 VVNEILEKLEAA 172
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
335-667 |
6.47e-26 |
|
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: 107.22 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 335 GNQFILELFHGPTGSFKDLSLQLMPHIFAHCIPPScNYMILVATSGDTGSAVLNGFSRLNkndkqrIAVVAFFPEnGVSD 414
Cdd:cd00640 15 ANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLP-KGVIIESTGGNTGIALAAAAARLG------LKCTIVMPE-GASP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 415 FQKAQIigsqRENG-WAVGVESDFDFCQTAIKRIFNDSDftgfltveygtILSSANS-INWGRLLPQVVYHASAYLDLVS 492
Cdd:cd00640 87 EKVAQM----RALGaEVVLVPGDFDDAIALAKELAEEDP-----------GAYYVNQfDNPANIAGQGTIGLEILEQLGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 493 QgfisfgSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQnhvltdfiktghydlrerklaqtfspsidilkssnl 572
Cdd:cd00640 152 Q------KPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE------------------------------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 573 erhlhlmankdgqlmtelfnrlesqhhfqiekalveklqqdfvADWCSEGECLAAINSTYNTSGYILDPHTAVAKVVADR 652
Cdd:cd00640 190 -------------------------------------------VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALK 226
|
330
....*....|....*...
gi 1034569575 653 VQDKTCP---VIISSTAH 667
Cdd:cd00640 227 LAKKLGKgktVVVILTGG 244
|
|
| Thr_synth_N |
pfam14821 |
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine ... |
231-318 |
3.36e-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: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 231 FISTRhvwpeDCEQKVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYVERAQILLERCIhPADIPAARL 310
Cdd:pfam14821 2 YISTR-----GGAPPLS---FEDALLKGLAPDGGLYVPE-EIPQLSAEELASWRGLSYQELAFEVLSLFI-GDDIPEEDL 71
|
....*...
gi 1034569575 311 GEMIETAY 318
Cdd:pfam14821 72 KALIERAY 79
|
|
| PRK00625 |
PRK00625 |
shikimate kinase; Provisional |
56-165 |
5.91e-16 |
|
shikimate kinase; Provisional
Pssm-ID: 134335 [Multi-domain] Cd Length: 173 Bit Score: 76.33 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNM---SVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLT 132
Cdd:PRK00625 1 MQIFLCGLPTVGKTSFGKALAKFLSLPFFDTDDLIVSNYHGAlysSPKEIYQAYGEEGFCREEFLALTSLPVIPSIVALG 80
|
90 100 110
....*....|....*....|....*....|...
gi 1034569575 133 GSNPMHDASMWHLKKNGIIVYLDVPLLDLICRL 165
Cdd:PRK00625 81 GGTLMIEPSYAHIRNRGLLVLLSLPIATIYQRL 113
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
56-223 |
1.65e-15 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 74.74 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSA-SGSVISLTGS 134
Cdd:PRK13947 2 KNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEI-EKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARlKNLVIATGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 135 NPMHDASMWHLKKNGIIVYLDVPlLDLICRLKLMKTDR--IVGQNSGTSMKDLLKfRRQYYkkwYDARVFC--ESGASPE 210
Cdd:PRK13947 81 VVLNPENVVQLRKNGVVICLKAR-PEVILRRVGKKKSRplLMVGDPEERIKELLK-EREPF---YDFADYTidTGDMTID 155
|
170
....*....|...
gi 1034569575 211 EVADKVlnaIKRY 223
Cdd:PRK13947 156 EVAEEI---IKAY 165
|
|
| PRK13946 |
PRK13946 |
shikimate kinase; Provisional |
50-230 |
3.19e-14 |
|
shikimate kinase; Provisional
Pssm-ID: 184411 [Multi-domain] Cd Length: 184 Bit Score: 71.49 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 50 HSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGS-V 128
Cdd:PRK13946 5 RAALGKRTVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEI-ERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGPlV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 129 ISLTGSNPMHDASMWHLKKNGIIVYLDVPLLDLICRLK------LMKTDrivgqNSGTSMKDLLKFRRQYYKKwydARVF 202
Cdd:PRK13946 84 LATGGGAFMNEETRAAIAEKGISVWLKADLDVLWERVSrrdtrpLLRTA-----DPKETLARLMEERYPVYAE---ADLT 155
|
170 180
....*....|....*....|....*....
gi 1034569575 203 CESGASPEEV-ADKVLNAIKRYQDVDSET 230
Cdd:PRK13946 156 VASRDVPKEVmADEVIEALAAYLEKEEAA 184
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
56-195 |
1.28e-12 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 66.68 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSA-SGSVISLTGS 134
Cdd:PRK13949 2 ARIFLVGYMGAGKTTLGKALARELGLSFIDLDFFI-ENRFHKTVGDIFAERGEAVFRELERNMLHEVAEfEDVVISTGGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034569575 135 NPMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKTDR-IVGQNSGTSMKDL----LKFRRQYYKK 195
Cdd:PRK13949 81 APCFFDNMELMNASGTTVYLKVSPEVLFVRLRLAKQQRpLLKGKSDEELLDFiieaLEKRAPFYRQ 146
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
58-167 |
5.76e-12 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 64.58 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTwNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGSNPM 137
Cdd:PRK03731 5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTS-NMTVAEIVEREGWAGFRARESAALEAVTAPSTVIATGGGIIL 83
|
90 100 110
....*....|....*....|....*....|
gi 1034569575 138 HDASMWHLKKNGIIVYLDVPLLDLICRLKL 167
Cdd:PRK03731 84 TEENRHFMRNNGIVIYLCAPVSVLANRLEA 113
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
346-672 |
1.29e-11 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 67.53 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 346 PTGSFKDLSLQL------------MPHIFAHCippscnymilvATSGDTGSAVLNGFSRLNkndkqrIAVVAFFPENGVS 413
Cdd:PLN02569 161 HTGSFKDLGMTVlvsqvnrlrkmaKPVVGVGC-----------ASTGDTSAALSAYCAAAG------IPSIVFLPADKIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 414 DFQKAQIIGsqreNGWAV-GVESDFDFCQTAIKRIfndsdftgflTVEYGTILssANSINWGRLLPQvvyhASAYLDLVS 492
Cdd:PLN02569 224 IAQLVQPIA----NGALVlSIDTDFDGCMRLIREV----------TAELPIYL--ANSLNSLRLEGQ----KTAAIEILQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 493 QgfisFGSPVD--VCIPTGNFGNILAAVYA----KMMGI--PIRKFICASNQN-HVLTDFIKTGHYDLRERKLAQTFSPS 563
Cdd:PLN02569 284 Q----FDWEVPdwVIVPGGNLGNIYAFYKGfkmcKELGLvdRLPRLVCAQAANaNPLYRAYKSGWEEFKPVKANPTFASA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 564 IDILKSSNLERHLHLMANKDGqlmtelfnrlesqhhfqiekaLVEKLQQDFVADWCSEGEclaainstynTSGYILDPHT 643
Cdd:PLN02569 360 IQIGDPVSIDRAVYALKESNG---------------------IVEEATEEELMDAQAEAD----------KTGMFLCPHT 408
|
330 340 350
....*....|....*....|....*....|....
gi 1034569575 644 AVA-----KVVADRVQDKTCPVIISSTAHYSKFA 672
Cdd:PLN02569 409 GVAlaalkKLRASGVIGPTDRTVVVSTAHGLKFT 442
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
15-171 |
5.34e-10 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 61.25 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 15 QKCFSSIHVKTDKHAQRFLSR----TFALAELRKSWYSTHSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDI 90
Cdd:PLN02199 58 RRAVSPAVSCSDNNSSALLETgsvyPFDEDILKRKAEEVKPYLNGRSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 91 LEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGSNPMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKT 170
Cdd:PLN02199 138 EQAMNGTSVAEIFVHHGENFFRGKETDALKKLSSRYQVVVSTGGGAVIRPINWKYMHKGISIWLDVPLEALAHRIAAVGT 217
|
.
gi 1034569575 171 D 171
Cdd:PLN02199 218 D 218
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
340-656 |
3.28e-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: 58.86 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 340 LELFHgPTGSFKDLSLQlmpHIFAHCIPPSCNYMILVATSGDTGSAVLNGFSRLNkndkqrIAVVAFFPENGVSdfQKAQ 419
Cdd:pfam00291 28 LESLN-PTGSFKDRGAL---NLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLG------LKVTIVVPEDAPP--GKLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 420 IIgsqRENGwA--VGVESDFDFCQTAIKRIFNDSDftgfltvEYGTILSSANSINWgrllpqvVYHASAYLDLVSQgfis 497
Cdd:pfam00291 96 LM---RALG-AevVLVGGDYDEAVAAARELAAEGP-------GAYYINQYDNPLNI-------EGYGTIGLEILEQ---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 498 FGSPVD-VCIPTGNFGNILA-AVYAKMMGIPIRKFICASNQNHVLTDFIKTGHYDlrERKLAQTFSPSIDIlkssnlerh 575
Cdd:pfam00291 154 LGGDPDaVVVPVGGGGLIAGiARGLKELGPDVRVIGVEPEGAPALARSLAAGRPV--PVPVADTIADGLGV--------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 576 lhlmankDGQLMTELFnrlesqhhfqiekALVEKLQQDFVAdwCSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQD 655
Cdd:pfam00291 223 -------GDEPGALAL-------------DLLDEYVGEVVT--VSDEEALEAMRLLARREGIVVEPSSAAALAALKLALA 280
|
.
gi 1034569575 656 K 656
Cdd:pfam00291 281 G 281
|
|
| aroK |
PRK05057 |
shikimate kinase AroK; |
56-155 |
1.06e-07 |
|
shikimate kinase AroK;
Pssm-ID: 235335 [Multi-domain] Cd Length: 172 Bit Score: 52.41 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKT-----WNMSVS------EKLQDVGNEqfLEEEGKAVLNfSA 124
Cdd:PRK05057 5 RNIFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTgadigWVFDVEgeegfrDREEKVINE--LTEKQGIVLA-TG 81
|
90 100 110
....*....|....*....|....*....|.
gi 1034569575 125 SGSVISLTGSNpmhdasmwHLKKNGIIVYLD 155
Cdd:PRK05057 82 GGSVKSRETRN--------RLSARGVVVYLE 104
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
62-224 |
8.16e-07 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 49.82 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 62 GPPGAGKTTVGRIIGQKLGCCVidVDDDILEKTW---NMSVSE------------KLQDVGNEQFLEEEGKAVLNFSASG 126
Cdd:COG1102 7 REPGSGGTTIAKRLAEKLGLPL--YDGEILREAAkerGLSEEEfekldekapsllYRDTAEEDEIDRALDKVIRELARKG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 127 SVIsLTGsnpmHDASmWHLK--KNGIIVYLDVPLLDlicRLKlmktdRIVGQNsGTSMKDLLKF-------RRQYYKK-- 195
Cdd:COG1102 85 NCV-IVG----RLAD-WILRdrPNVLKVFLTAPLEV---RVK-----RIAERE-GISEEEAEKEikkrdksRAKYYKYyy 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034569575 196 ---WYDAR----VFCESGASPEEVADKVLNAIKRYQ 224
Cdd:COG1102 150 gidWGDPSnydlVINTSRLGIEEAVDLILAAIEARE 185
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
59-220 |
8.81e-07 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 52.17 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 59 ILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSNPM 137
Cdd:PRK14021 10 VIIGMMGAGKTRVGKEVAQMMRLPFADADVEI-EREIGMSIPSYFEEYGEPAFREVEADVVADMLEDfDGIFSLGGGAPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 138 HDASMWHLKK----NGIIVYLDVPLLDLICRLKLMKTDRIVGQNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEEVA 213
Cdd:PRK14021 89 TPSTQHALASyiahGGRVVYLDADPKEAMERANRGGGRPMLNGDANKRWKKLFKQRDPVFRQVANVHVHTR-GLTPQAAA 167
|
....*..
gi 1034569575 214 DKVLNAI 220
Cdd:PRK14021 168 KKLIDMV 174
|
|
| PRK03839 |
PRK03839 |
putative kinase; Provisional |
58-222 |
3.75e-06 |
|
putative kinase; Provisional
Pssm-ID: 179660 Cd Length: 180 Bit Score: 47.79 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSVSEKLQ-DVGN-EQFLEEEGKavlnfsasgsvisltGSN 135
Cdd:PRK03839 3 IAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEiDFDKlAYFIEEEFK---------------EKN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 136 PMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKTDR-IVGQNSGTSMKDLlkfrrqyykkwydarVFCES--------- 205
Cdd:PRK03839 68 VVLDGHLSHLLPVDYVIVLRAHPKIIKERLKERGYSKkKILENVEAELVDV---------------CLCEAleekekvie 132
|
170 180
....*....|....*....|.
gi 1034569575 206 ----GASPEEVADKVLNAIKR 222
Cdd:PRK03839 133 vdttGKTPEEVVEEILELIKS 153
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
58-196 |
4.13e-06 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 49.90 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGSNPM 137
Cdd:PRK13951 3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEI-ERREGRSVRRIFEEDGEEYFRLKEKELLRELVERDNVVVATGGGVV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034569575 138 HDASMWHLKKNGIIVYLDVPLLDLICRLKLmkTDRIVGQNSGTSMKDLLKFRRQYYKKW 196
Cdd:PRK13951 82 IDPENRELLKKEKTLFLYAPPEVLMERVTT--ENRPLLREGKERIREIWERRKQFYTEF 138
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
57-88 |
5.99e-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: 5.99e-06
10 20 30
....*....|....*....|....*....|..
gi 1034569575 57 NIILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGD 32
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
58-89 |
7.19e-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: 46.66 E-value: 7.19e-06
10 20 30
....*....|....*....|....*....|..
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDD 89
Cdd:COG3265 4 IVVMGVSGSGKSTVGQALAERLGWPFIDGDDF 35
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
58-88 |
9.84e-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: 9.84e-06
10 20 30
....*....|....*....|....*....|.
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:cd02021 2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDD 32
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
57-80 |
1.06e-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: 47.04 E-value: 1.06e-05
|
| PRK08118 |
PRK08118 |
DNA topology modulation protein; |
56-185 |
1.34e-05 |
|
DNA topology modulation protein;
Pssm-ID: 181235 Cd Length: 167 Bit Score: 46.14 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAsgsvislTGSN 135
Cdd:PRK08118 2 KKIILIGSGGSGKSTLARQLGEKLNIPVHHLDALFWKPNWEGVPKEEQITVQNELVKEDEWIIDGNYGG-------TMDI 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1034569575 136 PMHDASMwhlkkngiIVYLDVPllDLICRLKLMKtdRIVgQNSGTSMKDL 185
Cdd:PRK08118 75 RLNAADT--------IIFLDIP--RTICLYRAFK--RRV-QYRGKTRPDM 111
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
58-88 |
2.53e-05 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 45.29 E-value: 2.53e-05
10 20 30
....*....|....*....|....*....|.
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRLRSDV 32
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
56-80 |
1.80e-04 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 43.60 E-value: 1.80e-04
|
| AAA_18 |
pfam13238 |
AAA domain; |
58-87 |
3.62e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 40.87 E-value: 3.62e-04
10 20 30
....*....|....*....|....*....|
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVD 87
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDNVRD 30
|
|
| PRK13948 |
PRK13948 |
shikimate kinase; Provisional |
60-154 |
4.96e-04 |
|
shikimate kinase; Provisional
Pssm-ID: 184413 [Multi-domain] Cd Length: 182 Bit Score: 41.70 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 60 LMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAV-----LNFsasgSVISLTGS 134
Cdd:PRK13948 15 LAGFMGTGKSRIGWELSRALMLHFIDTDRYI-ERVTGKSIPEIFRHLGEAYFRRCEAEVVrrltrLDY----AVISLGGG 89
|
90 100
....*....|....*....|
gi 1034569575 135 NPMHDASMWHLKKNGIIVYL 154
Cdd:PRK13948 90 TFMHEENRRKLLSRGPVVVL 109
|
|
| therm_gnt_kin |
TIGR01313 |
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ... |
58-176 |
9.35e-04 |
|
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: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDdiLEKTWN---MSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGS 134
Cdd:TIGR01313 1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDD--LHPAANiekMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034569575 135 NpmhdasmwhLKK-----------NGIIVYLDVPLLDLICRLK-----LMKTDRIVGQ 176
Cdd:TIGR01313 79 A---------LKRhyrdilreaepNLHFIYLSGDKDVILERMKarkghFMKADMLESQ 127
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
31-93 |
1.04e-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: 42.21 E-value: 1.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034569575 31 RFLSRTFALAELRKSWYSTHSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVD-DDILEK 93
Cdd:COG0464 167 EELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDlSDLVSK 230
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
43-105 |
1.85e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. 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: 410928 [Multi-domain] Cd Length: 166 Bit Score: 39.72 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034569575 43 RKSWYSTHSLVG-DKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWnMSVSEKLQD 105
Cdd:cd19520 22 RPELFDNSRLLQpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKW-YGESQKLVA 84
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
58-88 |
2.00e-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: 2.00e-03
10 20 30
....*....|....*....|....*....|.
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDD 32
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
35-106 |
2.26e-03 |
|
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: 39.19 E-value: 2.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034569575 35 RTFALAELRKSWYSTHSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVD-DDILEKtWNMSVSEKLQDV 106
Cdd:cd19481 6 REAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKlSSLLSK-YVGESEKNLRKI 77
|
|
| PRK14528 |
PRK14528 |
adenylate kinase; Provisional |
56-108 |
2.50e-03 |
|
adenylate kinase; Provisional
Pssm-ID: 172994 [Multi-domain] Cd Length: 186 Bit Score: 39.61 E-value: 2.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSV----SEKLQDVGN 108
Cdd:PRK14528 2 KNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAmgieAKRYMDAGD 58
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
56-88 |
4.30e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.51 E-value: 4.30e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKL-----GCCVIDVDD 88
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELgppggGVIYIDGED 40
|
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
58-110 |
4.38e-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: 38.24 E-value: 4.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034569575 58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVdddilektwNMSVSEKLQDVGNEQ 110
Cdd:NF033453 19 ILLVGPPGSGKTALLRELAAKRGAPVINV---------NLELSRRLLELPEKQ 62
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
58-94 |
4.60e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 38.89 E-value: 4.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034569575 58 IILMGPPGAGKTTV----GRIIGQKLGCCVI------DVDDDILEKT 94
Cdd:COG0378 16 VNLMGSPGSGKTTLlektIRALKDRLRIAVIegdiytTEDAERLRAA 62
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
56-129 |
4.64e-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: 38.28 E-value: 4.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLG-----CCVIDVDDDIlektwnmsvsEKLQDVGNEQFLEEEGKAVLNFSASGSVI 129
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFrpgapFLYLNASDLL----------EGLVVAELFGHFLVRLLFELAEKAKPGVL 88
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
56-103 |
4.79e-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: 38.49 E-value: 4.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1034569575 56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWnMSVSEKL 103
Cdd:cd19509 33 RGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKW-VGESEKI 79
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
62-80 |
5.07e-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: 5.07e-03
|
| cyt_kin_arch |
TIGR02173 |
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ... |
58-80 |
8.42e-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: 37.79 E-value: 8.42e-03
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
57-81 |
9.72e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 38.91 E-value: 9.72e-03
|
| |
