|
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 ... |
9-519 |
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: 885.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 9 CCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEYGTKGGVHRDGDGGEVTSPVLMWVEALDLLLEKLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 89 VLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY 168
Cdd:cd07776 81 VKAISGSGQQHGSVYWSKGAESALANLDPSKSLAEQLEGAFSVPDSPIWMDSSTTKQCRELEKAVGGPEALAKLTGSRAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 169 ERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACL-GACAPHLEEKLSP 247
Cdd:cd07776 161 ERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGRYAPIDESDGSGMNLMDIRSRKWSPELLdAATAPDLKEKLGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 248 PVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDS 327
Cdd:cd07776 241 LVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGLEPGDVAVSLGTSDTVFLVLDEPKPGPEGHVFANPVDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 328 QHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHRFNTENHK-VAAFPGDV 406
Cdd:cd07776 321 GSYMAMLCYKNGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNLGLYFDEPEITPPVPGGGRRFFGDDGvDAFFDPAV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 407 EVRALIEGQFMAKRIHAEGLGYRVmSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTD 486
Cdd:cd07776 401 EVRAVVESQFLSMRLHAERLGSDI-PPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGS 479
|
490 500 510
....*....|....*....|....*....|....*
gi 18860918 487 VPFS--EVVKLAPNPRLAATPSPGASQVYEALLPQ 519
Cdd:cd07776 480 GDFSpeFVVFSAEEPKLVAEPDPEAAEVYDKLLER 514
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
11-535 |
0e+00 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 609.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 11 LGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVH--VHKDGlTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:PLN02669 11 LGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHYGTKDGVYrdPKVNG-RIVSPTLMWVEALDLLLQKLAKEKFPFHK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 89 VLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY 168
Cdd:PLN02669 90 VVAISGSGQQHGSVYWRKGASAVLKSLDPSKSLVAQLQDAFSTKDSPIWMDSSTTKQCREIEEAVGGAAELSKLTGSRAY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 169 ERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACLGACAPHLEEKLSPP 248
Cdd:PLN02669 170 ERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYASIDETDGAGMNLMDIEKRCWSKAALEATAPGLEEKLGKL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 249 VPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEE-GDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDS 327
Cdd:PLN02669 250 APAHAVAGKIHPYFVQRFGFSSNCLVVQWSGDNPNSLAGLTLSTpGDLAISLGTSDTVFGITREPQPSLEGHVFPNPVDP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 328 QHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEI-IGRHRFNTEN---------- 396
Cdd:PLN02669 330 ESYMVMLCYKNGSLTREDIRNRCADGSWDVFNKLLEQTPPLNGGKLGFYYKEHEILPPLpVGFHRYILENfsgealdglv 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 397 -HKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKtKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAY 475
Cdd:PLN02669 410 eEEVGEFDPPSEVRAIIEGQFLSMRAHAERFGMPVPPK-RIIATGGASANQSILKLIASIFGCDVYTVQRPDSASLGAAL 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18860918 476 RAFHGLA---GGTDVPFSEVVK---LAPNPRLAATPSPGASQV---YEALLPQYAKLEQRILsQTRGPP 535
Cdd:PLN02669 489 RAAHGWLcneQGSFVPISCLYEgklEATSLSCKLAVKAGDQELlsqYGLLMKKRMEIEQQLV-EKLGRC 556
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
9-477 |
3.20e-66 |
|
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: 219.74 E-value: 3.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 9 CCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPefgtqggvhvhKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYP-----------QPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 89 VLALSGAGQQHGSIYWKAgAQQALTslspdlrlhqqlqdcfsisDCPVWMDSsttaqcrqleaavggaqalscltgsRAy 168
Cdd:cd00366 70 IAAIGISGQMPGVVLVDA-DGNPLR-------------------PAIIWLDR-------------------------RA- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 169 erftgnqiakiyqqnpeayshteRISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPhLEEKLSPP 248
Cdd:cd00366 104 -----------------------KFLQPNDYIVFRLTGEFA-IDYSNASGTGLYDIKTGDWSEELLDALGI-PREKLPPI 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 249 VPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTSDTLFLWLQEPMPAlEGHIFCNP-VD 326
Cdd:cd00366 159 VESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVvEPGDAVDSTGTSSVLSVCTDEPVPP-DPRLLNRChVV 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 327 SQHYMALLCFKNGSLMREKIRNESVSRSWSD-----FSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHR---FN-TENH 397
Cdd:cd00366 238 PGLWLLEGAINTGGASLRWFRDEFGEEEDSDaeyegLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARgvfFGlTLSH 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 398 KVAAFpgdveVRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRA 477
Cdd:cd00366 318 TRAHL-----IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
11-523 |
1.71e-57 |
|
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: 199.29 E-value: 1.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 11 LGWDFSTQQVKVVAVDAELNVFYEESVHFDrdlpefgtqggVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVL 90
Cdd:COG1070 4 LGIDIGTTSVKAVLFDADGEVVASASAEYP-----------LSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 91 ALSGAGQQHGsiYWKAGAQQALtslspdlrlhqqlqdcfsISDCPVWMDSSTTAQCRQLEAAVGGAQALScLTGSRAyer 170
Cdd:COG1070 73 AIGVSGQMHG--LVLLDADGEP------------------LRPAILWNDTRAAAEAAELREELGEEALYE-ITGNPL--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 171 FTGNQIAKIY---QQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSP 247
Cdd:COG1070 129 HPGFTAPKLLwlkENEPEIFARIAKVLLPKDYLRYRLTGEFV-TDYSDASGTGLLDVRTRDWSDELLEALGID-RELLPE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 248 PVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGTSDTLFLWLQEPM--PALEGHIFCNP 324
Cdd:COG1070 207 LVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGaVEPGDAAVSLGTSGVVFVVSDKPLpdPEGRVHTFCHA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 325 VDsQHYMALLCFKNGSLMREKIRNE---SVSRSWSDFSKALQSTEMGNGGnLGFY---------FDVMEITPEIIGRhrf 392
Cdd:COG1070 287 VP-GRWLPMGATNNGGSALRWFRDLfadGELDDYEELNALAAEVPPGADG-LLFLpylsgertpHWDPNARGAFFGL--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 393 nTENHKVAAFpgdveVRALIEGQFMAKRIHAE---GLGYRVmskTKILATGGASHNREILQVLADVFDAPVYVIDTANSA 469
Cdd:COG1070 362 -TLSHTRAHL-----ARAVLEGVAFALRDGLEaleEAGVKI---DRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGG 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 18860918 470 CVGSAYRAFHGLAGGTDvpFSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKL 523
Cdd:COG1070 433 ALGAALLAAVGLGLYDD--LEEAAAAMVRVGETIEPDPENVAAYDELYERYREL 484
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
11-477 |
1.00e-44 |
|
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: 163.49 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 11 LGWDFSTQQVKVVAVDAELNvfyeESVHFDR-DLPEFGTQGGVHvhkdgltvTSPVLMWVQALDIILEKM-KASGFDFSQ 88
Cdd:cd07809 3 LGIDLGTQSIKAVLIDAETG----RVVASGSaPHENILIDPGWA--------EQDPEDWWDALQAAFAQLlKDAGAELRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 89 VLALSGAGQQHGsiYWKAGAQQALtslspdLRlhqqlqdcfsisdcPV--WMDSSTTAQCRQLEAAVGGAQALSCLTGSR 166
Cdd:cd07809 71 VAAIGISGQMHG--LVALDADGKV------LR--------------PAklWCDTRTAPEAEELTEALGGKKCLLVGLNIP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 167 AyeRFTgnqIAKIYQ---QNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACL--GACAPHL 241
Cdd:cd07809 129 A--RFT---ASKLLWlkeNEPEHYARIAKILLPHDYLNWKLTGEKV-TGLGDASGTFPIDPRTRDYDAELLaaIDPSRDL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 242 EEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGTSDTLFLWLQEPMPALEGHI 320
Cdd:cd07809 203 RDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGvVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 321 --FCNPVDsqHYMALLCFKNG--SLMrEKIRnESVSRSWSDFSKALQSTEMGNGGNLGF-YFDVMEIT--PEIIGR-HRF 392
Cdd:cd07809 283 atFCDSTG--GMLPLINTTNCltAWT-ELFR-ELLGVSYEELDELAAQAPPGAGGLLLLpFLNGERTPnlPHGRASlVGL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 393 NTENHKVAAFpgdveVRALIEGQFMAKRIhaeglGYRVMSK-----TKILATGGASHNREILQVLADVFDAPVYVIDTAN 467
Cdd:cd07809 359 TLSNFTRANL-----ARAALEGATFGLRY-----GLDILRElgveiDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGE 428
|
490
....*....|
gi 18860918 468 SACVGSAYRA 477
Cdd:cd07809 429 GGALGAALQA 438
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
11-523 |
2.74e-38 |
|
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: 146.53 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 11 LGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPefgtqggvhvhKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVL 90
Cdd:cd07808 3 LGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSP-----------KPGWAEQDPEDWWQATKEALRELLAKAGISPSDIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 91 ALSGAGQQHGSIYwkagaqqaltslspdlrLHQQLQdcfSISDCPVWMDSSTTAQCRQLEAAVGGAQALscLTGSRAYER 170
Cdd:cd07808 72 AIGLTGQMHGLVL-----------------LDKNGR---PLRPAILWNDQRSAAECEELEARLGDEILI--ITGNPPLPG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 171 FTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACapHL-EEKLSPPV 249
Cdd:cd07808 130 FTLPKLLWLKENEPEIFARIRKILLPKDYLRYRLTGELA-TDPSDASGTLLFDVEKREWSEELLEAL--GLdPSILPPIV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 250 PSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTSDTLFLWLQEPMPALEG--HIFCNPVD 326
Cdd:cd07808 207 ESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGAGVvEPGDALISLGTSGVVFAPTDKPVPDPKGrlHTFPHAVP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 327 SQHY-MALLCFKNGSL--MREKIRNESVsrSWSDFSKALQSTEMGNGGnLGF----------YFDvmeitPEIigRHRFN 393
Cdd:cd07808 287 GKWYaMGVTLSAGLSLrwLRDLFGPDRE--SFDELDAEAAKVPPGSEG-LLFlpylsgertpYWD-----PNA--RGSFF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 394 --TENHKVAAFpgdveVRALIEGQFMA-----KRIHAEGLGYRvmsktKILATGGASHNREILQVLADVFDAPVYVIDTA 466
Cdd:cd07808 357 glSLSHTRAHL-----ARAVLEGVAFSlrdslEVLKELGIKVK-----EIRLIGGGAKSPLWRQILADVLGVPVVVPAEE 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 18860918 467 NSACVGSAYRAFHGLAGGTDVpfSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKL 523
Cdd:cd07808 427 EGSAYGAALLAAVGAGVFDDL--EEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
11-483 |
3.49e-37 |
|
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: 142.73 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 11 LGWDFSTQQVKVVAVDAELNVFYEESvhfdRDLPefgtqggVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDfsQVL 90
Cdd:cd07773 3 LGIDIGTTNVKAVLFDEDGRILASAS----RETP-------LIHPGPGWAELDPEELWEAVKEAIREAAAQAGPD--PIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 91 ALSGAGQqhgsiywkaGaqQALTSLSPDLRlhqqlqdcfSISDCPVWMDSSTTAQCRQLEAAVGgAQALSCLTGSRAYER 170
Cdd:cd07773 70 AISVSSQ---------G--ESGVPVDRDGE---------PLGPAIVWFDPRGKEEAEELAERIG-AEELYRITGLPPSPM 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 171 FTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSPPVP 250
Cdd:cd07773 129 YSLAKLLWLREHEPEIFAKAAKWLSVADYIAYRLTGEPV-TDYSLASRTMLFDIRKRTWSEELLEAAGID-ASLLPELVP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 251 SCSVVGAISSYYVQRYGFPPGCKVVafTG--DNPASLAGMRL-EEGDIAVSLGTSDTLFLWLQEPMP--ALEGHIFCNP- 324
Cdd:cd07773 207 SGTVIGTVTPEAAEELGLPAGTPVV--VGghDHLCAALGAGViEPGDVLDSTGTAEALLAVVDEPPLdeMLAEGGLSYGh 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 325 -VDSQHYMALLCFKNGSLMrEKIRNESVSRSWSDFSKALQSTEMGNGGN-LGF--YFDVMEiTPEIIGRHRFNTENHKVA 400
Cdd:cd07773 285 hVPGGYYYLAGSLPGGALL-EWFRDLFGGDESDLAAADELAEAAPPGPTgLLFlpHLSGSG-TPDFDPDARGAFLGLTLG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 401 AFPGDVeVRALIEG-QFMAKRIHA--EGLGYRVmskTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYra 477
Cdd:cd07773 363 TTRADL-LRAILEGlAFELRLNLEalEKAGIPI---DEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAAL-- 436
|
....*.
gi 18860918 478 fhgLAG 483
Cdd:cd07773 437 ---LAG 439
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
11-523 |
5.03e-33 |
|
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: 131.52 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 11 LGWDFSTQQVKVVAVDAELNVFYEESvhfdRDLPEFGTQGGVHVHkDGLTVTSPVlmwVQALDIILEKMKASgfdfsQVL 90
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVASSS----AEYPLIRPEPGWAEQ-DPEEILEAV---LEALKEVLAKLGGG-----EVD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 91 ALSGAGQQHGSIywkA--GAQQALTSLSPdlrlhqqlqdcfsisdcpvWMDSSTTAQCRQLEAAvggaqalscLTGSRAY 168
Cdd:cd07770 70 AIGFSSAMHSLL---GvdEDGEPLTPVIT-------------------WADTRAAEEAERLRKE---------GDGSELY 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 169 ERfTG---------NQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYsPIDYSDGSGMNLLQIQDKVWSQACLGACAP 239
Cdd:cd07770 119 RR-TGcpihpmyplAKLLWLKEERPELFAKAAKFVSIKEYLLYRLTGEL-VTDYSTASGTGLLNIHTLDWDEEALELLGI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 240 HlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPAS-LAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEG 318
Cdd:cd07770 197 D-EEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALAnLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 319 HIFCNPVDSQHY---MALlcfKNGSL----MREKIRNESVsrSWSDFSKALQSTEMGNGGNLGFYFdvmeITPE------ 385
Cdd:cd07770 276 RLWCYRLDENRWlvgGAI---NNGGNvldwLRDTLLLSGD--DYEELDKLAEAVPPGSHGLIFLPY----LAGErapgwn 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 386 ------IIGRhrfnTENHKVAAFpgdveVRALIEGqfMAKRIH--AEGLGYRVMSKTKILATGGASHNREILQVLADVFD 457
Cdd:cd07770 347 pdargaFFGL----TLNHTRADI-----LRAVLEG--VAFNLKsiYEALEELAGPVKEIRASGGFLRSPLWLQILADVLG 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18860918 458 APVYVIDTANSACVGSAYRAFHGLAGGTDVPFSEVVKlapnPRLAATPSPGASQVYEALLPQYAKL 523
Cdd:cd07770 416 RPVLVPEEEEASALGAALLALEALGLISSLEADELVK----IGKVVEPDPENHAIYAELYERFKKL 477
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
133-520 |
1.08e-24 |
|
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: 107.22 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 133 DCPVWMDSSTTAQCRQLEAAVGGAqalscltgsRAYERFTGNQ------IAKI--YQQN-PEAYSHTERISLVSSFAASL 203
Cdd:cd07805 94 NAIIWSDTRAAEEAEEIAGGLGGI---------EGYRLGGGNPpsgkdpLAKIlwLKENePEIYAKTHKFLDAKDYLNFR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 204 FLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPA 283
Cdd:cd07805 165 LTGRAA-TDPSTASTTGLMDLRKRRWSEELLRAAGID-PDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDAAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 284 SLAG-MRLEEGDIAVSLGTSDtlflWL----QEPMPALEGHIFCNP-VDSQHYMALLCFKNGSLMREKIRN------ESV 351
Cdd:cd07805 243 AALGaGAVEEGDAHIYLGTSG----WVaahvPKPKTDPDHGIFTLAsADPGRYLLAAEQETAGGALEWARDnlggdeDLG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 352 SRSWSDFSKALQSTEMGNGGnLGFyfdvmeiTPEIIGRhRFNTENHKV-AAF--------PGDVeVRALIEGQFMAKRIH 422
Cdd:cd07805 319 ADDYELLDELAAEAPPGSNG-LLF-------LPWLNGE-RSPVEDPNArGAFiglslehtRADL-ARAVLEGVAFNLRWL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 423 AEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTA-NSACVGSAYRAFHGLagGTDVPFSEVVKLAPnPRL 501
Cdd:cd07805 389 LEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGL--GLLKSFDEAKALVK-VEK 465
|
410
....*....|....*....
gi 18860918 502 AATPSPGASQVYEALLPQY 520
Cdd:cd07805 466 VFEPDPENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
190-481 |
5.86e-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: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 190 TERISLVSSFAASLFLGSYsPIDYSDGSGMNLLQIQDKVWSQACLGACA-PhlEEKLSPPVPSCSVVGAISSYYVQRYGF 268
Cdd:cd07779 103 TAKFLTVQDYLLYRLTGEF-VTDTTSASRTGLPDIRTRDWSDDLLDAFGiD--RDKLPELVPPGTVIGTLTKEAAEETGL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 269 PPGCKVVAFTGDNP-ASL-AGMrLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNP--VDSQHYMALLCFKNGSLMR- 343
Cdd:cd07779 180 PEGTPVVAGGGDQQcAALgAGV-LEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPsaVPGKWVLEGSINTGGSAVRw 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 344 --------EKIRNESVSRSWSDFSKALQSTEMGNGGnlgfyfdVMEItPEIIGRHRFNTENHKVAAF--------PGDVe 407
Cdd:cd07779 259 frdefgqdEVAEKELGVSPYELLNEEAAKSPPGSDG-------LLFL-PYLAGAGTPYWNPEARGAFigltlshtRAHL- 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18860918 408 VRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 481
Cdd:cd07779 330 ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGA 403
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
137-484 |
1.99e-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: 94.13 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 137 WMDSSTTAQCRQLEAAVGgAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDG 216
Cdd:cd07804 98 YGDRRATEEIEWLNENIG-EDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYIVYKLTGEYV-IDYSSA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 217 SGMN-LLQIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASL--AGMrLEEG 293
Cdd:cd07804 176 GNEGgLFDIRKRTWDEELLEALGID-PDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDAAASAlsAGV-VEPG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 294 DIAVSLGTSdTLFLWLQEPMPALEGHIFCNPVDSQHYMALLC-FKNGSL---MREKIRNESVSRSWSDFSKALQSTEM-- 367
Cdd:cd07804 254 DLLLMLGTA-GDIGVVTDKLPTDPRLWLDYHDIPGTYVLNGGmATSGSLlrwFRDEFAGEEVEAEKSGGDSAYDLLDEea 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 368 -----GNGGnLGF--YFdvM-EITPE--------IIGRHRFNTenhkvaafPGDVeVRALIEGQFMAKRIHAEGLGYRVM 431
Cdd:cd07804 333 ekippGSDG-LIVlpYF--MgERTPIwdpdargvIFGLTLSHT--------RAHL-YRALLEGVAYGLRHHLEVIREAGL 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 18860918 432 SKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG 484
Cdd:cd07804 401 PIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLA--GVGVG 451
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
296-481 |
2.39e-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: 80.45 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 296 AVSLGTSDTLFLWLQEPmpALEGHIFCNPVDSQH-----YMALLCFKNGSLM---------REKIRNESVSRSWSDFSKA 361
Cdd:pfam02782 2 AISAGTSSFVLVETPEP--VLSVHGVWGPYTNEMlpgywGLEGGQSAAGSLLawllqfhglREELRDAGNVESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 362 LQSTEMGnggnlGFYFDvmeitPEIIGRHRFNTENHKVAAFPG-------DVEVRALIEGQFMAKRIHAEGL----GYRV 430
Cdd:pfam02782 80 AAVAPAG-----GLLFY-----PDFSGNRAPGADPGARGSITGlsspttlAHLYRAILESLALQLRQILEALtkqeGHPI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18860918 431 MSktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 481
Cdd:pfam02782 150 DT---IHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
11-287 |
5.56e-15 |
|
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: 74.68 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 11 LGWDFSTQQVKVVAVDAELNVfyeesvhfdrdlpefgtqggVHVHKDGLTVTSPVLMWV--------QALDIILEK-MKA 81
Cdd:pfam00370 3 LGIDCGTTSTKAILFNEQGKI--------------------IAVAQLENPQITPHPGWAeqdpdeiwQAVAQCIAKtLSQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 82 SGFDFSQVLALSGAGQQHGSIYWKAGAQQaltslspdlrlhqqlqdcfsISDCPVWMDSSTTAQCRQLEAAvGGAQALSC 161
Cdd:pfam00370 63 LGISLKQIKGIGISNQGHGTVLLDKNDKP--------------------LYNAILWKDRRTAEIVENLKEE-GNNQKLYE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 162 LTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHl 241
Cdd:pfam00370 122 ITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYLRWRLTGVFV-TDHTNASRSMMFNIHKLDWDPELLAALGIP- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 18860918 242 EEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAG 287
Cdd:pfam00370 200 RDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
49-334 |
6.58e-15 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 77.31 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 49 QGGV-HVHKDGLTVTSPVLMWV--------QALDiilEKMKASGFDFS--QVLALSGAGQQHGSiywkagaqqalTSLSP 117
Cdd:PRK15027 20 QGEVvASQTEKLTVSRPHPLWSeqdpeqwwQATD---RAMKALGDQHSlqDVKALGIAGQMHGA-----------TLLDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 118 DLRLhqqlqdcfsISDCPVWMDSSTTAQCRQLEAAVGGAQALsclTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVS 197
Cdd:PRK15027 86 QQRV---------LRPAILWNDGRCAQECALLEARVPQSRVI---TGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 198 SFAASLFLGSYSPiDYSDGSGMNLLQIQDKVWSQACLGACapHLEEKLSPPVPSCS-VVGAISSYYVQRYGFpPGCKVVA 276
Cdd:PRK15027 154 DYLRLRMTGEFAS-DMSDAAGTMWLDVAKRDWSDVMLQAC--HLSRDQMPALYEGSeITGALLPEVAKAWGM-ATVPVVA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18860918 277 FTGDNPASLAGMRL-EEGDIAVSLGTSDTLFL----WLQEPMPALegHIFCNPVDSQ-HYMALL 334
Cdd:PRK15027 230 GGGDNAAGAVGVGMvDANQAMLSLGTSGVYFAvsegFLSKPESAV--HSFCHALPQRwHLMSVM 291
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
136-474 |
2.14e-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: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 136 VWMDSSTTAQCRQLEAAvGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYshtERISLVssFAASLFL-----GSYSp 210
Cdd:cd07802 97 LSNDSRAADIVDRWEED-GTLEKVYPLTGQPLWPGQPVALLRWLKENEPERY---DRIRTV--LFCKDWIryrltGEIS- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 211 IDYSDGSGmNLLQIQDKVWSQACLGAC-APHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGM- 288
Cdd:cd07802 170 TDYTDAGS-SLLDLDTGEYDDELLDLLgIEELKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVVASALGAg 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 289 RLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGS----------LMREKIRNESVSRSWSDF 358
Cdd:cd07802 249 AVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSAsnldwfldtlLGEEKEAGGSDYDELDEL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 359 SKALQSTEMG-------NGGNL------GFYfdvmEITPEiigrHRfntenhkvaafPGDVeVRALIEGQFMAKRIHAEG 425
Cdd:cd07802 329 IAAVPPGSSGviflpylYGSGAnpnargGFF----GLTAW----HT-----------RAHL-LRAVYEGIAFSHRDHLER 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 18860918 426 LGYRVMSKTkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 474
Cdd:cd07802 389 LLVARKPET-IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAA 436
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
11-474 |
2.82e-12 |
|
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: 68.79 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 11 LGWDFSTQQVKVVAVDAELNVFYEESvhfdRDLPEFGTQGGVHVHkdgltvtSPvLMWVQALDIILEKMKASGfDFSQVL 90
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTVLASAS----EPYPTSRPGPGWVEQ-------DP-EDWWEALRSLLRELPAEL-RPRRVV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 91 ALSGAGQQhGSIywkAGAQQALTSLSPDLrlhqqlqdcfsisdcpVWMDSSTTAQCRQLEAAVGGAQalscltgSRAYER 170
Cdd:cd07783 70 AIAVDGTS-GTL---VLVDREGEPLRPAI----------------MYNDARAVAEAEELAEAAGAVA-------PRTGLA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 171 FTGNQ-IAKI---YQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDG--SGMNLlqiQDKVWSQAcLGACAPHLEEK 244
Cdd:cd07783 123 VSPSSsLAKLlwlKRHEPEVLAKTAKFLHQADWLAGRLTGDRGVTDYNNAlkLGYDP---ETGRWPSW-LLALLGIPPDL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 245 LSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGD-NPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCN 323
Cdd:cd07783 199 LPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDsIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSH 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 324 PVDSQHYM----------ALLCFKNGSLMREKIRnesvsrswsdfskalQSTEMGNGGnLGFY--------FDVmeITPE 385
Cdd:cd07783 279 RHGDGYWLvggasntggaVLRWFFSDDELAELSA---------------QADPPGPSG-LIYYplplrgerFPF--WDPD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 386 IIGrhRFNTENHKVAAFpgdveVRALIEGqfMAkriHAEGLGYRVMSK------TKILATGGASHNREILQVLADVFDAP 459
Cdd:cd07783 341 ARG--FLLPRPHDRAEF-----LRALLEG--IA---FIERLGYERLEElgappvEEVRTAGGGARNDLWNQIRADVLGVP 408
|
490
....*....|....*
gi 18860918 460 VYVIDTaNSACVGSA 474
Cdd:cd07783 409 VVIAEE-EEAALGAA 422
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
177-474 |
2.99e-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: 62.24 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 177 AKIY---QQNPEAYshtERISLV---SSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGAC-APHleEKLSPPV 249
Cdd:cd07798 134 ARLLwfkENRPEIF---ERIATVlsiSDWIGYRLTGELV-SEPSQASETQLFDIKKREWSQELLEALgLPP--EILPEIV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 250 PSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNP-VDS 327
Cdd:cd07798 208 PSGTVLGTVSEEAARELGLPEGTPVVVGGADTQCALLGSGaIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGChLVP 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 328 QHYM----ALLCFKNGSLMREKIRnESVSRSWSDFSKALQSTEMGNGGNLGFY----FDvMEITPEIIGRHRFNTENHKV 399
Cdd:cd07798 288 GKWVlesnAGVTGLNYQWLKELLY-GDPEDSYEVLEEEASEIPPGANGVLAFLgpqiFD-ARLSGLKNGGFLFPTPLSAS 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18860918 400 AAFPGDVeVRALIEGQFMAKRIHAEGLgyRVMSKT---KILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 474
Cdd:cd07798 366 ELTRGDF-ARAILENIAFAIRANLEQL--EEVSGReipYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAA 440
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
10-477 |
1.16e-09 |
|
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: 60.31 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 10 CLGWDFSTQQVKVVAVDAE-LNVFYEESVHFDRDLPefGTQGGVHVhkdgltvTSPVLMWvQALDIILEKMKAsgFDFSQ 88
Cdd:cd07777 2 VLGIDIGTTSIKAALLDLEsGRILESVSRPTPAPIS--SDDPGRSE-------QDPEKIL-EAVRNLIDELPR--EYLSD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 89 VLALSGAGQQHGSIYWKAGaQQALTSLspdlrlhqqlqdcfsISdcpvWMDSSTTAQCRQleaavggaqalSCLTGSRAY 168
Cdd:cd07777 70 VTGIGITGQMHGIVLWDED-GNPVSPL---------------IT----WQDQRCSEEFLG-----------GLSTYGEEL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 169 ERFTGNQIAKIY--------QQNPEAYSHTERISLVSSFAASLFLGSYSP-IDYSDGSGMNLLQIQDKVWSQACLGAcAP 239
Cdd:cd07777 119 LPKSGMRLKPGYglatlfwlLRNGPLPSKADRAGTIGDYIVARLTGLPKPvMHPTNAASWGLFDLETGTWNKDLLEA-LG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 240 HLEEKLSPPVPSCSVVGAISSyyvqryGFPPGCKVVAFTGDNPASLAG-MRLEEGDIAVSLGTSDTL-FLwlqEPMPALE 317
Cdd:cd07777 198 LPVILLPEIVPSGEIVGTLSS------ALPKGIPVYVALGDNQASVLGsGLNEENDAVLNIGTGAQLsFL---TPKFELS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 318 GHIFCNPVDSQHYMALLCFKNG------------SLMREKIRNESVSRSWSDFSKALQSTEMGNggnlgfyfdvMEITPE 385
Cdd:cd07777 269 GSVEIRPFFDGRYLLVAASLPGgralavlvdflrEWLRELGGSLSDDEIWEKLDELAESEESSD----------LSVDPT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 386 IIG-RHRFNT---------ENhkvaaF-PGDVeVRALIEGqfMAKRIH--AEGLGYRVMSKTKILATGGAS-HNREILQV 451
Cdd:cd07777 339 FFGeRHDPEGrgsitnigeSN-----FtLGNL-FRALCRG--IAENLHemLPRLDLDLSGIERIVGSGGALrKNPVLRRI 410
|
490 500
....*....|....*....|....*.
gi 18860918 452 LADVFDAPVYVIDTANSACVGSAYRA 477
Cdd:cd07777 411 IEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
184-522 |
1.81e-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: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 184 PEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAphLEEKLSPPV-PSCSVVGAISSYY 262
Cdd:cd07775 146 PEIYRKAAKITMLSDWIAYKLSGELA-VEPSNGSTTGLFDLKTRDWDPEILEMAG--LKADILPPVvESGTVIGKVTKEA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 263 VQRYGFPPGCKVVAFTGDNPASLAGM-RLEEGDIAVSLGTsdtlfLWLQE-----PMPALEGHIFCNP-VDSQHYMALLC 335
Cdd:cd07775 223 AEETGLKEGTPVVVGGGDVQLGCLGLgVVRPGQTAVLGGS-----FWQQEvntaaPVTDPAMNIRVNChVIPDMWQAEGI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 336 -FKNGSLMR---------EKIRNESVSRSWSDF-SKALQSTEMGNGGNLGFYFDVMEI------TPEIIGrHRFNTENHK 398
Cdd:cd07775 298 sFFPGLVMRwfrdafcaeEKEIAERLGIDAYDLlEEMAKDVPPGSYGIMPIFSDVMNYknwrhaAPSFLN-LDIDPEKCN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 399 VAAFpgdveVRALIEGQFMAKRIH----AEGLGYRVMSktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 474
Cdd:cd07775 377 KATF-----FRAIMENAAIVSAGNleriAEFSGIFPDS---LVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAA 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 18860918 475 YRAfhGLAGGTDVPFSEVVKlapnpRLAA-----TPSPGASQVYEALlpqYAK 522
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; ... |
137-523 |
2.31e-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: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 137 WMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY--ERFtgnqIAKI---YQQNPEAYSHTERI---------SLVSSFAAS 202
Cdd:cd07781 101 WMDHRAQEEAAEINETAHPALEYYLAYYGGVYssEWM----WPKAlwlKRNAPEVYDAAYTIveacdwinaRLTGRWVRS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 203 L----FLGSYSPidysDGSGmnllqiqdkvWSQACLGACAPHL---EEKLSPPV-PSCSVVGAISSYYVQRYGFPPGCKV 274
Cdd:cd07781 177 RcaagHKWMYNE----WGGG----------PPREFLAALDPGLlklREKLPGEVvPVGEPAGTLTAEAAERLGLPAGIPV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 275 VAFTGDNPASLAGMR-LEEGDIAVSLGTSdTLFLwLQEPMP-ALEGhiFCNPVDS----QHYMA----------LLCFKN 338
Cdd:cd07781 243 AQGGIDAHMGAIGAGvVEPGTLALIMGTS-TCHL-MVSPKPvDIPG--ICGPVPDavvpGLYGLeagqsavgdiFAWFVR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 339 GSLMREKIRNESVSRSWSDFSKALQSTEMG------NGGNLGFYFDvMEITPEIIGRhrfnTENHKvaafPGDVeVRALI 412
Cdd:cd07781 319 LFVPPAEERGDSIYALLSEEAAKLPPGESGlvaldwFNGNRTPLVD-PRLRGAIVGL----TLGTT----PAHI-YRALL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 413 EG-QFMAKRI--HAEGLGYRVmskTKILATGG-ASHNREILQVLADVFDAPVYVIDTANSACVGSAyrAFHGLAGG--TD 486
Cdd:cd07781 389 EAtAFGTRAIieRFEEAGVPV---NRVVACGGiAEKNPLWMQIYADVLGRPIKVPKSDQAPALGAA--ILAAVAAGvyAD 463
|
410 420 430
....*....|....*....|....*....|....*..
gi 18860918 487 VPfSEVVKLAPNPRLaATPSPGASQVYEALLPQYAKL 523
Cdd:cd07781 464 IE-EAADAMVRVDRV-YEPDPENHAVYEELYALYKEL 498
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
409-523 |
6.45e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 48.69 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 409 RALIEGQ-FMAKRI----HAEGlgyrvMSKTKILATGG-ASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFhgLA 482
Cdd:PRK04123 415 RALIEATaFGTRAImecfEDQG-----VPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAA--VA 487
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 18860918 483 GGT--DVPfSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKL 523
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 ... |
408-484 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 408 VRALIEGqfMAKRIHA--EGLGYRVMSK-TKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG 484
Cdd:cd07793 387 VRAILES--IAFRVKQllETMEKETSIKiSSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLA--GLASG 462
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
249-529 |
5.64e-03 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 39.19 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 249 VPSCSVVGAISSYYVQRYgfpPGCKVVAFTGDNPASLAG-MRLEEGDIAVSLGTSdtLFLWL---QEPMP---------- 314
Cdd:PTZ00294 219 KSSSENFGTISGEAVPLL---EGVPITGCIGDQQAALIGhGCFEKGDAKNTYGTG--CFLLMntgTEIVFskhgllttvc 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 315 -----------ALEGHIFCNpvdsqhymallcfknGSLMREKIRNESVSRSWSDFSKALQSTEmgngGNLGFYFdvmeit 383
Cdd:PTZ00294 294 yqlgpngptvyALEGSIAVA---------------GAGVEWLRDNMGLISHPSEIEKLARSVK----DTGGVVF------ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 384 peiigrhrfntenhkVAAFPG------DVEVRALIEG-QFMAKRIHA-----EGLGYRV------MSK------TKILAT 439
Cdd:PTZ00294 349 ---------------VPAFSGlfapywRPDARGTIVGmTLKTTRAHIvraalEAIALQTndviesMEKdagielNSLRVD 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 440 GGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG--TDVpfSEVVKLAPNPRLAATPSPGASQvYEALL 517
Cdd:PTZ00294 414 GGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLA--GLAVGvwKSL--EEVKKLIRRSNSTFSPQMSAEE-RKAIY 488
|
330
....*....|..
gi 18860918 518 PQYAKLEQRILS 529
Cdd:PTZ00294 489 KEWNKAVERSLK 500
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
184-311 |
7.95e-03 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 38.83 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860918 184 PEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAphLEEKLSPPV-PSCSVVGAISSYY 262
Cdd:PRK10939 149 PDIYRQAHTITMISDWIAYMLSGELA-VDPSNAGTTGLLDLVTRDWDPALLEMAG--LRADILPPVkETGTVLGHVTAKA 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18860918 263 VQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTsdtlfLWLQE 311
Cdd:PRK10939 226 AAETGLRAGTPVVMGGGDVQLGCLGLGVvRPGQTAVLGGT-----FWQQV 270
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
409-480 |
9.10e-03 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 38.47 E-value: 9.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18860918 409 RALIEGqfMAKRIHAeglGYRVMSK------TKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHG 480
Cdd:PRK10331 365 RAALEG--LTAQLKR---NLQVLEKighfkaSELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYG 437
|
|
| |
