|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
1-453 |
0e+00 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 778.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 1 MWVQALDIILEKMKASGFDFSQVLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQC 80
Cdd:cd07776 59 MWVEALDLLLEKLKAAGFDFSRVKAISGSGQQHGSVYWSKGAESALANLDPSKSLAEQLEGAFSVPDSPIWMDSSTTKQC 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 81 RQLEAAVGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQD 160
Cdd:cd07776 139 RELEKAVGGPEALAKLTGSRAYERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGRYAPIDESDGSGMNLMDIRS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 161 KVWSQACL-GACAPHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTL 239
Cdd:cd07776 219 RKWSPELLdAATAPDLKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGLEPGDVAVSLGTSDTV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 240 FLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPE 319
Cdd:cd07776 299 FLVLDEPKPGPEGHVFANPVDPGSYMAMLCYKNGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNLGLYFDEPEITPP 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 320 IIGRHRFNTENHK-VAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVmSKTKILATGGASHNREILQVLADVFDAPVYVID 398
Cdd:cd07776 379 VPGGGRRFFGDDGvDAFFDPAVEVRAVVESQFLSMRLHAERLGSDI-PPTRILATGGASANKAILQVLADVFGAPVYTLD 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370485743 399 TANSACVGSAYRAFHGLAGGTDVPFS--EVVKLAPNPRLAATPSPGASQVYEALLPQ 453
Cdd:cd07776 458 VANSAALGAALRAAHGLLCAGSGDFSpeFVVFSAEEPKLVAEPDPEAAEVYDKLLER 514
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
1-469 |
0e+00 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 546.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 1 MWVQALDIILEKMKASGFDFSQVLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQC 80
Cdd:PLN02669 68 MWVEALDLLLQKLAKEKFPFHKVVAISGSGQQHGSVYWRKGASAVLKSLDPSKSLVAQLQDAFSTKDSPIWMDSSTTKQC 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 81 RQLEAAVGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQD 160
Cdd:PLN02669 148 REIEEAVGGAAELSKLTGSRAYERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYASIDETDGAGMNLMDIEK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 161 KVWSQACLGACAPHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEE-GDIAVSLGTSDTL 239
Cdd:PLN02669 228 RCWSKAALEATAPGLEEKLGKLAPAHAVAGKIHPYFVQRFGFSSNCLVVQWSGDNPNSLAGLTLSTpGDLAISLGTSDTV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 240 FLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPE 319
Cdd:PLN02669 308 FGITREPQPSLEGHVFPNPVDPESYMVMLCYKNGSLTREDIRNRCADGSWDVFNKLLEQTPPLNGGKLGFYYKEHEILPP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 320 I-IGRHRFNTEN-----------HKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKtKILATGGASHNREILQVLA 387
Cdd:PLN02669 388 LpVGFHRYILENfsgealdglveEEVGEFDPPSEVRAIIEGQFLSMRAHAERFGMPVPPK-RIIATGGASANQSILKLIA 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 388 DVFDAPVYVIDTANSACVGSAYRAFHGLA---GGTDVPFSEVVK---LAPNPRLAATPSPGASQV---YEALLPQYAKLE 458
Cdd:PLN02669 467 SIFGCDVYTVQRPDSASLGAALRAAHGWLcneQGSFVPISCLYEgklEATSLSCKLAVKAGDQELlsqYGLLMKKRMEIE 546
|
490
....*....|.
gi 1370485743 459 QRILsQTRGPP 469
Cdd:PLN02669 547 QQLV-EKLGRC 556
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
1-411 |
9.29e-56 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 190.08 E-value: 9.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 1 MWVQALDIILEKMKASGFDFSQVLALSGAGQQHGSIYWKAgAQQALTslspdlrlhqqlqdcfsisDCPVWMDSsttaqc 80
Cdd:cd00366 48 WWQAVVEAIREVLAKAGIDPSDIAAIGISGQMPGVVLVDA-DGNPLR-------------------PAIIWLDR------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 81 rqleaavggaqalscltgsRAyerftgnqiakiyqqnpeayshteRISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQD 160
Cdd:cd00366 102 -------------------RA------------------------KFLQPNDYIVFRLTGEFA-IDYSNASGTGLYDIKT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 161 KVWSQACLGACAPhLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTSDTL 239
Cdd:cd00366 138 GDWSEELLDALGI-PREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVvEPGDAVDSTGTSSVL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 240 FLWLQEPMPAlEGHIFCNP-VDSQHYMALLCFKNGSLMREKIRNESVSRSWSD-----FSKALQSTEMGNGGNLGFYFDV 313
Cdd:cd00366 217 SVCTDEPVPP-DPRLLNRChVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDaeyegLDELAAEVPPGSDGLIFLPYLS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 314 MEITPEIIGRHR---FN-TENHKVAAFpgdveVRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADV 389
Cdd:cd00366 296 GERSPIWDPAARgvfFGlTLSHTRAHL-----IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADV 370
|
410 420
....*....|....*....|..
gi 1370485743 390 FDAPVYVIDTANSACVGSAYRA 411
Cdd:cd00366 371 LGVPVVVPEVAEGAALGAAILA 392
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
1-457 |
1.30e-52 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 184.65 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 1 MWVQAL-DIILEKMKASGFDFSQVLALSGAGQQHGsiYWKAGAQQALtslspdlrlhqqlqdcfsISDCPVWMDSSTTAQ 79
Cdd:COG1070 48 DWWEAVvEAIRELLAKAGVDPEEIAAIGVSGQMHG--LVLLDADGEP------------------LRPAILWNDTRAAAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 80 CRQLEAAVGGAQALScLTGSRAyerFTGNQIAKIY---QQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLL 156
Cdd:COG1070 108 AAELREELGEEALYE-ITGNPL---HPGFTAPKLLwlkENEPEIFARIAKVLLPKDYLRYRLTGEFV-TDYSDASGTGLL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 157 QIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGT 235
Cdd:COG1070 183 DVRTRDWSDELLEALGID-RELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGaVEPGDAAVSLGT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 236 SDTLFLWLQEPM--PALEGHIFCNPVDsQHYMALLCFKNGSLMREKIRNE---SVSRSWSDFSKALQSTEMGNGGnLGFY 310
Cdd:COG1070 262 SGVVFVVSDKPLpdPEGRVHTFCHAVP-GRWLPMGATNNGGSALRWFRDLfadGELDDYEELNALAAEVPPGADG-LLFL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 311 ---------FDVMEITPEIIGRhrfnTENHKVAAFpgdveVRALIEGQFMAKRIHAE---GLGYRVmskTKILATGGASH 378
Cdd:COG1070 340 pylsgertpHWDPNARGAFFGL----TLSHTRAHL-----ARAVLEGVAFALRDGLEaleEAGVKI---DRIRATGGGAR 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370485743 379 NREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDvpFSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKL 457
Cdd:COG1070 408 SPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDD--LEEAAAAMVRVGETIEPDPENVAAYDELYERYREL 484
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
1-411 |
5.45e-42 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 154.63 E-value: 5.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 1 MWVQALDIILEKM-KASGFDFSQVLALSGAGQQHGsiYWKAGAQQALtslspdLRlhqqlqdcfsisdcPV--WMDSSTT 77
Cdd:cd07809 48 DWWDALQAAFAQLlKDAGAELRDVAAIGISGQMHG--LVALDADGKV------LR--------------PAklWCDTRTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 78 AQCRQLEAAVGGAQALSCLTGSRAyeRFTgnqIAKIYQ---QNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMN 154
Cdd:cd07809 106 PEAEELTEALGGKKCLLVGLNIPA--RFT---ASKLLWlkeNEPEHYARIAKILLPHDYLNWKLTGEKV-TGLGDASGTF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 155 LLQIQDKVWSQACL--GACAPHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAV 231
Cdd:cd07809 180 PIDPRTRDYDAELLaaIDPSRDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGvVNPGTVAV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 232 SLGTSDTLFLWLQEPMPALEGHI--FCNPVDsqHYMALLCFKNG--SLMrEKIRnESVSRSWSDFSKALQSTEMGNGGNL 307
Cdd:cd07809 260 SLGTSGTAYGVSDKPVSDPHGRVatFCDSTG--GMLPLINTTNCltAWT-ELFR-ELLGVSYEELDELAAQAPPGAGGLL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 308 GF-YFDVMEIT--PEIIGR-HRFNTENHKVAAFpgdveVRALIEGQFMAKRIhaeglGYRVMSK-----TKILATGGASH 378
Cdd:cd07809 336 LLpFLNGERTPnlPHGRASlVGLTLSNFTRANL-----ARAALEGATFGLRY-----GLDILRElgveiDEIRLIGGGSK 405
|
410 420 430
....*....|....*....|....*....|...
gi 1370485743 379 NREILQVLADVFDAPVYVIDTANSACVGSAYRA 411
Cdd:cd07809 406 SPVWRQILADVFGVPVVVPETGEGGALGAALQA 438
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
65-417 |
3.39e-36 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 138.87 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 65 ISDCPVWMDSSTTAQCRQLEAAVGgAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSp 144
Cdd:cd07773 90 LGPAIVWFDPRGKEEAEELAERIG-AEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAYRLTGEPV- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 145 IDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVafTG--DNPASLAGM 222
Cdd:cd07773 168 TDYSLASRTMLFDIRKRTWSEELLEAAGID-ASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVV--VGghDHLCAALGA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 223 RL-EEGDIAVSLGTSDTLFLWLQEPMP--ALEGHIFCNP--VDSQHYMALLCFKNGSLMrEKIRNESVSRSWSDFSKALQ 297
Cdd:cd07773 245 GViEPGDVLDSTGTAEALLAVVDEPPLdeMLAEGGLSYGhhVPGGYYYLAGSLPGGALL-EWFRDLFGGDESDLAAADEL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 298 STEMGNGGN-LGF--YFDVMEiTPEIIGRHRFNTENHKVAAFPGDVeVRALIEG-QFMAKRIHA--EGLGYRVmskTKIL 371
Cdd:cd07773 324 AEAAPPGPTgLLFlpHLSGSG-TPDFDPDARGAFLGLTLGTTRADL-LRAILEGlAFELRLNLEalEKAGIPI---DEIR 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1370485743 372 ATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYrafhgLAG 417
Cdd:cd07773 399 AVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAAL-----LAG 439
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
2-457 |
1.00e-33 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 132.66 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 2 WVQAL-DIILEKMKASGFDFSQVLALSGAGQQHGSIYwkagaqqaltslspdlrLHQQLQdcfSISDCPVWMDSSTTAQC 80
Cdd:cd07808 48 WWQATkEALRELLAKAGISPSDIAAIGLTGQMHGLVL-----------------LDKNGR---PLRPAILWNDQRSAAEC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 81 RQLEAAVGGAQALscLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQD 160
Cdd:cd07808 108 EELEARLGDEILI--ITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLRYRLTGELA-TDPSDASGTLLFDVEK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 161 KVWSQACLGACapHL-EEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTSDT 238
Cdd:cd07808 185 REWSEELLEAL--GLdPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGAGVvEPGDALISLGTSGV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 239 LFLWLQEPMPALEG--HIFCNPVDSQHY-MALLCFKNGSL--MREKIRNESVsrSWSDFSKALQSTEMGNGGnLGF---- 309
Cdd:cd07808 263 VFAPTDKPVPDPKGrlHTFPHAVPGKWYaMGVTLSAGLSLrwLRDLFGPDRE--SFDELDAEAAKVPPGSEG-LLFlpyl 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 310 ------YFDvmeitPEIigRHRFN--TENHKVAAFpgdveVRALIEGQFMA-----KRIHAEGLGYRvmsktKILATGGA 376
Cdd:cd07808 340 sgertpYWD-----PNA--RGSFFglSLSHTRAHL-----ARAVLEGVAFSlrdslEVLKELGIKVK-----EIRLIGGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 377 SHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVpfSEVVKLAPNPRLAATPSPGASQVYEALLPQYAK 456
Cdd:cd07808 403 AKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDL--EEAAAACIKIEKTIEPDPERHEAYDELYARYRE 480
|
.
gi 1370485743 457 L 457
Cdd:cd07808 481 L 481
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
71-457 |
9.26e-32 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 126.90 E-value: 9.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 71 WMDSSTTAQCRQLEAAvggaqalscLTGSRAYERfTG---------NQIAKIYQQNPEAYSHTERISLVSSFAASLFLGS 141
Cdd:cd07770 96 WADTRAAEEAERLRKE---------GDGSELYRR-TGcpihpmyplAKLLWLKEERPELFAKAAKFVSIKEYLLYRLTGE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 142 YsPIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPAS-LA 220
Cdd:cd07770 166 L-VTDYSTASGTGLLNIHTLDWDEEALELLGID-EEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALAnLG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 221 GMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHY---MALlcfKNGSL----MREKIRNESVsrSWSDFS 293
Cdd:cd07770 244 SGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENRWlvgGAI---NNGGNvldwLRDTLLLSGD--DYEELD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 294 KALQSTEMGNGGNLGFYFdvmeITPE------------IIGRhrfnTENHKVAAFpgdveVRALIEGqfMAKRIH--AEG 359
Cdd:cd07770 319 KLAEAVPPGSHGLIFLPY----LAGErapgwnpdargaFFGL----TLNHTRADI-----LRAVLEG--VAFNLKsiYEA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 360 LGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFSEVVKlapnPRLAATP 439
Cdd:cd07770 384 LEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEADELVK----IGKVVEP 459
|
410
....*....|....*...
gi 1370485743 440 SPGASQVYEALLPQYAKL 457
Cdd:cd07770 460 DPENHAIYAELYERFKKL 477
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
67-454 |
7.35e-25 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 106.84 E-value: 7.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 67 DCPVWMDSSTTAQCRQLEAAVGGAqalscltgsRAYERFTGNQ------IAKI--YQQN-PEAYSHTERISLVSSFAASL 137
Cdd:cd07805 94 NAIIWSDTRAAEEAEEIAGGLGGI---------EGYRLGGGNPpsgkdpLAKIlwLKENePEIYAKTHKFLDAKDYLNFR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 138 FLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPA 217
Cdd:cd07805 165 LTGRAA-TDPSTASTTGLMDLRKRRWSEELLRAAGID-PDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDAAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 218 SLAG-MRLEEGDIAVSLGTSDtlflWL----QEPMPALEGHIFCNP-VDSQHYMALLCFKNGSLMREKIRN------ESV 285
Cdd:cd07805 243 AALGaGAVEEGDAHIYLGTSG----WVaahvPKPKTDPDHGIFTLAsADPGRYLLAAEQETAGGALEWARDnlggdeDLG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 286 SRSWSDFSKALQSTEMGNGGnLGFyfdvmeiTPEIIGRhRFNTENHKV-AAF--------PGDVeVRALIEGQFMAKRIH 356
Cdd:cd07805 319 ADDYELLDELAAEAPPGSNG-LLF-------LPWLNGE-RSPVEDPNArGAFiglslehtRADL-ARAVLEGVAFNLRWL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 357 AEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTA-NSACVGSAYRAFHGLagGTDVPFSEVVKLAPnPRL 435
Cdd:cd07805 389 LEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGL--GLLKSFDEAKALVK-VEK 465
|
410
....*....|....*....
gi 1370485743 436 AATPSPGASQVYEALLPQY 454
Cdd:cd07805 466 VFEPDPENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
124-415 |
4.82e-21 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 95.28 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 124 TERISLVSSFAASLFLGSYsPIDYSDGSGMNLLQIQDKVWSQACLGACA-PhlEEKLSPPVPSCSVVGAISSYYVQRYGF 202
Cdd:cd07779 103 TAKFLTVQDYLLYRLTGEF-VTDTTSASRTGLPDIRTRDWSDDLLDAFGiD--RDKLPELVPPGTVIGTLTKEAAEETGL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 203 PPGCKVVAFTGDNP-ASL-AGMrLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNP--VDSQHYMALLCFKNGSLMR- 277
Cdd:cd07779 180 PEGTPVVAGGGDQQcAALgAGV-LEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPsaVPGKWVLEGSINTGGSAVRw 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 278 --------EKIRNESVSRSWSDFSKALQSTEMGNGGnlgfyfdVMEItPEIIGRHRFNTENHKVAAF--------PGDVe 341
Cdd:cd07779 259 frdefgqdEVAEKELGVSPYELLNEEAAKSPPGSDG-------LLFL-PYLAGAGTPYWNPEARGAFigltlshtRAHL- 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370485743 342 VRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 415
Cdd:cd07779 330 ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGA 403
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
71-418 |
1.60e-20 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 93.74 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 71 WMDSSTTAQCRQLEAAVGgAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDG 150
Cdd:cd07804 98 YGDRRATEEIEWLNENIG-EDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYIVYKLTGEYV-IDYSSA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 151 SGMN-LLQIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASL--AGMrLEEG 227
Cdd:cd07804 176 GNEGgLFDIRKRTWDEELLEALGID-PDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDAAASAlsAGV-VEPG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 228 DIAVSLGTSdTLFLWLQEPMPALEGHIFCNPVDSQHYMALLC-FKNGSL---MREKIRNESVSRSWSDFSKALQSTEM-- 301
Cdd:cd07804 254 DLLLMLGTA-GDIGVVTDKLPTDPRLWLDYHDIPGTYVLNGGmATSGSLlrwFRDEFAGEEVEAEKSGGDSAYDLLDEea 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 302 -----GNGGnLGF--YFdvM-EITPE--------IIGRHRFNTenhkvaafPGDVeVRALIEGQFMAKRIHAEGLGYRVM 365
Cdd:cd07804 333 ekippGSDG-LIVlpYF--MgERTPIwdpdargvIFGLTLSHT--------RAHL-YRALLEGVAYGLRHHLEVIREAGL 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1370485743 366 SKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG 418
Cdd:cd07804 401 PIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLA--GVGVG 451
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
230-415 |
3.40e-17 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 79.68 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 230 AVSLGTSDTLFLWLQEPmpALEGHIFCNPVDSQH-----YMALLCFKNGSLM---------REKIRNESVSRSWSDFSKA 295
Cdd:pfam02782 2 AISAGTSSFVLVETPEP--VLSVHGVWGPYTNEMlpgywGLEGGQSAAGSLLawllqfhglREELRDAGNVESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 296 LQSTEMGnggnlGFYFDvmeitPEIIGRHRFNTENHKVAAFPG-------DVEVRALIEGQFMAKRIHAEGL----GYRV 364
Cdd:pfam02782 80 AAVAPAG-----GLLFY-----PDFSGNRAPGADPGARGSITGlsspttlAHLYRAILESLALQLRQILEALtkqeGHPI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370485743 365 MSktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 415
Cdd:pfam02782 150 DT---IHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
2-268 |
2.79e-14 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 74.62 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 2 WVQALDiilEKMKASGFDFS--QVLALSGAGQQHGSiywkagaqqalTSLSPDLRLhqqlqdcfsISDCPVWMDSSTTAQ 79
Cdd:PRK15027 48 WWQATD---RAMKALGDQHSlqDVKALGIAGQMHGA-----------TLLDAQQRV---------LRPAILWNDGRCAQE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 80 CRQLEAAVGGAQALsclTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPiDYSDGSGMNLLQIQ 159
Cdd:PRK15027 105 CALLEARVPQSRVI---TGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRMTGEFAS-DMSDAAGTMWLDVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 160 DKVWSQACLGACapHLEEKLSPPVPSCS-VVGAISSYYVQRYGFpPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTSD 237
Cdd:PRK15027 181 KRDWSDVMLQAC--HLSRDQMPALYEGSeITGALLPEVAKAWGM-ATVPVVAGGGDNAAGAVGVGMvDANQAMLSLGTSG 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370485743 238 TLFL----WLQEPMPALegHIFCNPVDSQ-HYMALL 268
Cdd:PRK15027 258 VYFAvsegFLSKPESAV--HSFCHALPQRwHLMSVM 291
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
2-221 |
9.88e-14 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 70.83 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 2 WVQALDIILEK-MKASGFDFSQVLALSGAGQQHGSIYWKAGAQQaltslspdlrlhqqlqdcfsISDCPVWMDSSTTAQC 80
Cdd:pfam00370 48 IWQAVAQCIAKtLSQLGISLKQIKGIGISNQGHGTVLLDKNDKP--------------------LYNAILWKDRRTAEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 81 RQLEAAvGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQD 160
Cdd:pfam00370 108 ENLKEE-GNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYLRWRLTGVFV-TDHTNASRSMMFNIHK 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370485743 161 KVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAG 221
Cdd:pfam00370 186 LDWDPELLAALGIP-RDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
70-408 |
1.62e-13 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 72.20 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 70 VWMDSSTTAQCRQLEAAvGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYshtERISLVssFAASLFL-----GSYSp 144
Cdd:cd07802 97 LSNDSRAADIVDRWEED-GTLEKVYPLTGQPLWPGQPVALLRWLKENEPERY---DRIRTV--LFCKDWIryrltGEIS- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 145 IDYSDGSGmNLLQIQDKVWSQACLGAC-APHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGM- 222
Cdd:cd07802 170 TDYTDAGS-SLLDLDTGEYDDELLDLLgIEELKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVVASALGAg 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 223 RLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGS----------LMREKIRNESVSRSWSDF 292
Cdd:cd07802 249 AVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSAsnldwfldtlLGEEKEAGGSDYDELDEL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 293 SKALQSTEMG-------NGGNL------GFYfdvmEITPEiigrHRfntenhkvaafPGDVeVRALIEGQFMAKRIHAEG 359
Cdd:cd07802 329 IAAVPPGSSGviflpylYGSGAnpnargGFF----GLTAW----HT-----------RAHL-LRAVYEGIAFSHRDHLER 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1370485743 360 LGYRVMSKTkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 408
Cdd:cd07802 389 LLVARKPET-IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAA 436
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
111-408 |
3.08e-10 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 61.86 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 111 AKIY---QQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGAC-APHleEKLSPPVPSC 186
Cdd:cd07798 134 ARLLwfkENRPEIFERIATVLSISDWIGYRLTGELV-SEPSQASETQLFDIKKREWSQELLEALgLPP--EILPEIVPSG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 187 SVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNP-VDSQHY 264
Cdd:cd07798 211 TVLGTVSEEAARELGLPEGTPVVVGGADTQCALLGSGaIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGChLVPGKW 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 265 M----ALLCFKNGSLMREKIRnESVSRSWSDFSKALQSTEMGNGGNLGFY----FDvMEITPEIIGRHRFNTENHKVAAF 336
Cdd:cd07798 291 VlesnAGVTGLNYQWLKELLY-GDPEDSYEVLEEEASEIPPGANGVLAFLgpqiFD-ARLSGLKNGGFLFPTPLSASELT 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370485743 337 PGDVeVRALIEGQFMAKRIHAEGLgyRVMSKT---KILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 408
Cdd:cd07798 369 RGDF-ARAILENIAFAIRANLEQL--EEVSGReipYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAA 440
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
118-456 |
1.51e-09 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 60.04 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 118 PEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAphLEEKLSPPV-PSCSVVGAISSYY 196
Cdd:cd07775 146 PEIYRKAAKITMLSDWIAYKLSGELA-VEPSNGSTTGLFDLKTRDWDPEILEMAG--LKADILPPVvESGTVIGKVTKEA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 197 VQRYGFPPGCKVVAFTGDNPASLAGM-RLEEGDIAVSLGTsdtlfLWLQE-----PMPALEGHIFCNP-VDSQHYMALLC 269
Cdd:cd07775 223 AEETGLKEGTPVVVGGGDVQLGCLGLgVVRPGQTAVLGGS-----FWQQEvntaaPVTDPAMNIRVNChVIPDMWQAEGI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 270 -FKNGSLMR---------EKIRNESVSRSWSDF-SKALQSTEMGNGGNLGFYFDVMEI------TPEIIGrHRFNTENHK 332
Cdd:cd07775 298 sFFPGLVMRwfrdafcaeEKEIAERLGIDAYDLlEEMAKDVPPGSYGIMPIFSDVMNYknwrhaAPSFLN-LDIDPEKCN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 333 VAAFpgdveVRALIEGQFMAKRIH----AEGLGYRVMSktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 408
Cdd:cd07775 377 KATF-----FRAIMENAAIVSAGNleriAEFSGIFPDS---LVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAA 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1370485743 409 YRAfhGLAGGTDVPFSEVVKlapnpRLAA-----TPSPGASQVYEALlpqYAK 456
Cdd:cd07775 449 IAA--GVGAGIYSSLEEAVE-----SLVKwereyLPNPENHEVYQDL---YEK 491
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
71-457 |
1.83e-09 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 59.86 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 71 WMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY--ERFtgnqIAKI---YQQNPEAYSHTERI---------SLVSSFAAS 136
Cdd:cd07781 101 WMDHRAQEEAAEINETAHPALEYYLAYYGGVYssEWM----WPKAlwlKRNAPEVYDAAYTIveacdwinaRLTGRWVRS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 137 L----FLGSYSPidysDGSGmnllqiqdkvWSQACLGACAPHL---EEKLSPPV-PSCSVVGAISSYYVQRYGFPPGCKV 208
Cdd:cd07781 177 RcaagHKWMYNE----WGGG----------PPREFLAALDPGLlklREKLPGEVvPVGEPAGTLTAEAAERLGLPAGIPV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 209 VAFTGDNPASLAGMR-LEEGDIAVSLGTSdTLFLwLQEPMP-ALEGhiFCNPVDS----QHYMA----------LLCFKN 272
Cdd:cd07781 243 AQGGIDAHMGAIGAGvVEPGTLALIMGTS-TCHL-MVSPKPvDIPG--ICGPVPDavvpGLYGLeagqsavgdiFAWFVR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 273 GSLMREKIRNESVSRSWSDFSKALQSTEMG------NGGNLGFYFDvMEITPEIIGRhrfnTENHKvaafPGDVeVRALI 346
Cdd:cd07781 319 LFVPPAEERGDSIYALLSEEAAKLPPGESGlvaldwFNGNRTPLVD-PRLRGAIVGL----TLGTT----PAHI-YRALL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 347 EG-QFMAKRI--HAEGLGYRVmskTKILATGG-ASHNREILQVLADVFDAPVYVIDTANSACVGSAyrAFHGLAGG--TD 420
Cdd:cd07781 389 EAtAFGTRAIieRFEEAGVPV---NRVVACGGiAEKNPLWMQIYADVLGRPIKVPKSDQAPALGAA--ILAAVAAGvyAD 463
|
410 420 430
....*....|....*....|....*....|....*..
gi 1370485743 421 VPfSEVVKLAPNPRLaATPSPGASQVYEALLPQYAKL 457
Cdd:cd07781 464 IE-EAADAMVRVDRV-YEPDPENHAVYEELYALYKEL 498
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
176-408 |
8.15e-09 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 57.62 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 176 EEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGD-NPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHI 254
Cdd:cd07783 196 PDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDsIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 255 FCNPVDSQHYM----------ALLCFKNGSLMREKIRnesvsrswsdfskalQSTEMGNGGnLGFY--------FDVmeI 316
Cdd:cd07783 276 YSHRHGDGYWLvggasntggaVLRWFFSDDELAELSA---------------QADPPGPSG-LIYYplplrgerFPF--W 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 317 TPEIIGrhRFNTENHKVAAFpgdveVRALIEGqfMAkriHAEGLGYRVMSK------TKILATGGASHNREILQVLADVF 390
Cdd:cd07783 338 DPDARG--FLLPRPHDRAEF-----LRALLEG--IA---FIERLGYERLEElgappvEEVRTAGGGARNDLWNQIRADVL 405
|
250
....*....|....*...
gi 1370485743 391 DAPVYVIDTaNSACVGSA 408
Cdd:cd07783 406 GVPVVIAEE-EEAALGAA 422
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-411 |
1.18e-07 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 53.76 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 3 VQALDIILEKMKAsgFDFSQVLALSGAGQQHGSIYWKAGaQQALTSLspdlrlhqqlqdcfsISdcpvWMDSSTTAQCRQ 82
Cdd:cd07777 52 LEAVRNLIDELPR--EYLSDVTGIGITGQMHGIVLWDED-GNPVSPL---------------IT----WQDQRCSEEFLG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 83 leaavggaqalSCLTGSRAYERFTGNQIAKIY--------QQNPEAYSHTERISLVSSFAASLFLGSYSP-IDYSDGSGM 153
Cdd:cd07777 110 -----------GLSTYGEELLPKSGMRLKPGYglatlfwlLRNGPLPSKADRAGTIGDYIVARLTGLPKPvMHPTNAASW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 154 NLLQIQDKVWSQACLGAcAPHLEEKLSPPVPSCSVVGAISSyyvqryGFPPGCKVVAFTGDNPASLAG-MRLEEGDIAVS 232
Cdd:cd07777 179 GLFDLETGTWNKDLLEA-LGLPVILLPEIVPSGEIVGTLSS------ALPKGIPVYVALGDNQASVLGsGLNEENDAVLN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 233 LGTSDTL-FLwlqEPMPALEGHIFCNPVDSQHYMALLCFKNG------------SLMREKIRNESVSRSWSDFSKALQST 299
Cdd:cd07777 252 IGTGAQLsFL---TPKFELSGSVEIRPFFDGRYLLVAASLPGgralavlvdflrEWLRELGGSLSDDEIWEKLDELAESE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 300 EMGNggnlgfyfdvMEITPEIIG-RHRFNT---------ENHKvaafPGDVeVRALIEGqfMAKRIH--AEGLGYRVMSK 367
Cdd:cd07777 329 ESSD----------LSVDPTFFGeRHDPEGrgsitnigeSNFT----LGNL-FRALCRG--IAENLHemLPRLDLDLSGI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1370485743 368 TKILATGGAS-HNREILQVLADVFDAPVYVIDTANSACVGSAYRA 411
Cdd:cd07777 392 ERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
343-457 |
5.06e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 48.69 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 343 RALIEGQ-FMAKRI----HAEGlgyrvMSKTKILATGG-ASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFhgLA 416
Cdd:PRK04123 415 RALIEATaFGTRAImecfEDQG-----VPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAA--VA 487
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370485743 417 GGT--DVPfSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKL 457
Cdd:PRK04123 488 AGAypDIP-EAQQAMASPVEKTYQPDPENVARYEQLYQEYKQL 529
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
342-418 |
1.79e-03 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 40.62 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 342 VRALIEGqfMAKRIHA--EGLGYRVMSK-TKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG 418
Cdd:cd07793 387 VRAILES--IAFRVKQllETMEKETSIKiSSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLA--GLASG 462
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
183-463 |
4.70e-03 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 39.19 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 183 VPSCSVVGAISSYYVQRYgfpPGCKVVAFTGDNPASLAG-MRLEEGDIAVSLGTSdtLFLWL---QEPMP---------- 248
Cdd:PTZ00294 219 KSSSENFGTISGEAVPLL---EGVPITGCIGDQQAALIGhGCFEKGDAKNTYGTG--CFLLMntgTEIVFskhgllttvc 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 249 -----------ALEGHIFCNpvdsqhymallcfknGSLMREKIRNESVSRSWSDFSKALQSTEmgngGNLGFYFdvmeit 317
Cdd:PTZ00294 294 yqlgpngptvyALEGSIAVA---------------GAGVEWLRDNMGLISHPSEIEKLARSVK----DTGGVVF------ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 318 peiigrhrfntenhkVAAFPG------DVEVRALIEG-QFMAKRIHA-----EGLGYRV------MSK------TKILAT 373
Cdd:PTZ00294 349 ---------------VPAFSGlfapywRPDARGTIVGmTLKTTRAHIvraalEAIALQTndviesMEKdagielNSLRVD 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 374 GGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG--TDVpfSEVVKLAPNPRLAATPSPGASQvYEALL 451
Cdd:PTZ00294 414 GGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLA--GLAVGvwKSL--EEVKKLIRRSNSTFSPQMSAEE-RKAIY 488
|
330
....*....|..
gi 1370485743 452 PQYAKLEQRILS 463
Cdd:PTZ00294 489 KEWNKAVERSLK 500
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
118-245 |
6.75e-03 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 38.83 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485743 118 PEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAphLEEKLSPPV-PSCSVVGAISSYY 196
Cdd:PRK10939 149 PDIYRQAHTITMISDWIAYMLSGELA-VDPSNAGTTGLLDLVTRDWDPALLEMAG--LRADILPPVkETGTVLGHVTAKA 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1370485743 197 VQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTsdtlfLWLQE 245
Cdd:PRK10939 226 AAETGLRAGTPVVMGGGDVQLGCLGLGVvRPGQTAVLGGT-----FWQQV 270
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
343-414 |
8.59e-03 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 38.47 E-value: 8.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370485743 343 RALIEGqfMAKRIHAeglGYRVMSK------TKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHG 414
Cdd:PRK10331 365 RAALEG--LTAQLKR---NLQVLEKighfkaSELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYG 437
|
|
| |
