|
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 ... |
5-508 |
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: 729.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHekLKKFGTENGVHKNGS--VITSPVIMWIEAIDILFNDLRENGWT-D 81
Cdd:cd07776 2 YLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSD--LPEYGTKGGVHRDGDggEVTSPVLMWVEALDLLLEKLKAAGFDfS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 82 KLRGISGCAQQHGTVYWKNGAENSLKGLDESRSLAEQLEMCFSVQKSPIWMDSSTEKQCQELETFVGGDQEMAKLTGSRA 161
Cdd:cd07776 80 RVKAISGSGQQHGSVYWSKGAESALANLDPSKSLAEQLEGAFSVPDSPIWMDSSTTKQCRELEKAVGGPEALAKLTGSRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 162 HHRFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYALIELTDGSGMNLMNIKTENWHKPLFD-FISSDLESKLG 240
Cdd:cd07776 160 YERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGRYAPIDESDGSGMNLMDIRSRKWSPELLDaATAPDLKEKLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 241 TLVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSLLPTDIGISLGTSDTVFFFTPTFEPNIDAHVFSHFAP 320
Cdd:cd07776 240 ELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGLEPGDVAVSLGTSDTVFLVLDEPKPGPEGHVFANPVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 321 NSGYMAMVCFKNGSLTRERARNL-NNSSWDKWDKIMKKTPAGNDNYIGFFFDEDEIVPRKPKGDYTFECSEEELKNKHPE 399
Cdd:cd07776 320 PGSYMAMLCYKNGSLARERVRDRyAGGSWEKFNELLESTPPGNNGNLGLYFDEPEITPPVPGGGRRFFGDDGVDAFFDPA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 400 KFARAVFESQCLFKLLYTQKMGFkKSDCSRILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALGGAMRSRYVH---- 475
Cdd:cd07776 400 VEVRAVVESQFLSMRLHAERLGS-DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLlcag 478
|
490 500 510
....*....|....*....|....*....|...
gi 392895951 476 SKTTKTYSQYYPCDNVSLACQPISANVEVYSNL 508
Cdd:cd07776 479 SGDFSPEFVVFSAEEPKLVAEPDPEAAEVYDKL 511
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
5-471 |
7.53e-161 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 468.48 E-value: 7.53e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTheKLKKFGTENGVHKNGSV---ITSPVIMWIEAIDILFNDL-RENGWT 80
Cdd:PLN02669 10 FLGFDSSTQSLKATVLDSNLRIVASEIVHFDS--DLPHYGTKDGVYRDPKVngrIVSPTLMWVEALDLLLQKLaKEKFPF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 81 DKLRGISGCAQQHGTVYWKNGAENSLKGLDESRSLAEQLEMCFSVQKSPIWMDSSTEKQCQELETFVGGDQEMAKLTGSR 160
Cdd:PLN02669 88 HKVVAISGSGQQHGSVYWRKGASAVLKSLDPSKSLVAQLQDAFSTKDSPIWMDSSTTKQCREIEEAVGGAAELSKLTGSR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 161 AHHRFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYALIELTDGSGMNLMNIKTENWHKPLFDFISSDLESKLG 240
Cdd:PLN02669 168 AYERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYASIDETDGAGMNLMDIEKRCWSKAALEATAPGLEEKLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 241 TLVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSL-LPTDIGISLGTSDTVFFFTPTFEPNIDAHVFSHFA 319
Cdd:PLN02669 248 KLAPAHAVAGKIHPYFVQRFGFSSNCLVVQWSGDNPNSLAGLTLsTPGDLAISLGTSDTVFGITREPQPSLEGHVFPNPV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 320 PNSGYMAMVCFKNGSLTRERARN-LNNSSWDKWDKIMKKTPAGNDNYIGFFFDEDEIVPRKPKGDYTF-----------E 387
Cdd:PLN02669 328 DPESYMVMLCYKNGSLTREDIRNrCADGSWDVFNKLLEQTPPLNGGKLGFYYKEHEILPPLPVGFHRYilenfsgealdG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 388 CSEEELKNKHPEKFARAVFESQCLFKLLYTQKMGFkKSDCSRILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALGG 467
Cdd:PLN02669 408 LVEEEVGEFDPPSEVRAIIEGQFLSMRAHAERFGM-PVPPKRIIATGGASANQSILKLIASIFGCDVYTVQRPDSASLGA 486
|
....
gi 392895951 468 AMRS 471
Cdd:PLN02669 487 ALRA 490
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
5-476 |
3.40e-53 |
|
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: 186.22 E-value: 3.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIID-QNGKVVHTTAINfstheklkkfgtengvHKNGSVI----TSPVIMWIEAIDILFNDLRENGW 79
Cdd:cd07809 2 VLGIDLGTQSIKAVLIDaETGRVVASGSAP----------------HENILIDpgwaEQDPEDWWDALQAAFAQLLKDAG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 80 TDKLR----GISGcaQQHGTVYwkngaenslkgLDESRSLaeqlemcfsVQKSPIWMDSSTEKQCQELETFVGGDQEMAK 155
Cdd:cd07809 66 AELRDvaaiGISG--QMHGLVA-----------LDADGKV---------LRPAKLWCDTRTAPEAEELTEALGGKKCLLV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 156 LTGSRAhhRFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYALiELTDGSGMNLMNIKTENWHKPLFDFI--SS 233
Cdd:cd07809 124 GLNIPA--RFTASKLLWLKENEPEHYARIAKILLPHDYLNWKLTGEKVT-GLGDASGTFPIDPRTRDYDAELLAAIdpSR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 234 DLESKLGTLVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGL-SLLPTDIGISLGTSDTVFFFTPTfePNIDA 312
Cdd:cd07809 201 DLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTgVVNPGTVAVSLGTSGTAYGVSDK--PVSDP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 313 H----VFSHfaPNSGYMAMVCFKNgSLTR--ERARNLNNSSWDKWDKIMKKTPAGNDNYIGFFFDEDEIVPRKPKGDYTF 386
Cdd:cd07809 279 HgrvaTFCD--STGGMLPLINTTN-CLTAwtELFRELLGVSYEELDELAAQAPPGAGGLLLLPFLNGERTPNLPHGRASL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 387 ECSEEElkNKHPEKFARAVFESqclfkLLYTQKMGFKK-----SDCSRILVTGGASRNTVLLQILSDVFEMPVCTIDVDG 461
Cdd:cd07809 356 VGLTLS--NFTRANLARAALEG-----ATFGLRYGLDIlrelgVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGE 428
|
490
....*....|....*
gi 392895951 462 SAALGGAMRSRYVHS 476
Cdd:cd07809 429 GGALGAALQAAWGAG 443
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-513 |
4.24e-53 |
|
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: 187.35 E-value: 4.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHeklkkfgtengVHKNGSVITSPVIMW---IEAIDILFNDLRENGwtD 81
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYPLS-----------SPHPGWAEQDPEDWWeavVEAIRELLAKAGVDP--E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 82 KLRGISGCAQQHGTVywkngaenslkGLDESRSLaeqlemcfsVQKSPIWMDSSTEKQCQELETFVGGDqEMAKLTGSRA 161
Cdd:COG1070 70 EIAAIGVSGQMHGLV-----------LLDADGEP---------LRPAILWNDTRAAAEAAELREELGEE-ALYEITGNPL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 162 HHRFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDFISSDlESKLGT 241
Cdd:COG1070 129 HPGFTAPKLLWLKENEPEIFARIAKVLLPKDYLRYRLTGEFV-TDYSDASGTGLLDVRTRDWSDELLEALGID-RELLPE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 242 LVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSLL-PTDIGISLGTSDTVFFFT--PTFEPNIDAHVFSHF 318
Cdd:COG1070 207 LVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGAVePGDAAVSLGTSGVVFVVSdkPLPDPEGRVHTFCHA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 319 APNsGYMAMVCFKNGSLTRERARNL----NNSSWDKWDKIMKKTPAGNDN--YIGFFFDEdeivpRKPKGDYTFECSEEE 392
Cdd:COG1070 287 VPG-RWLPMGATNNGGSALRWFRDLfadgELDDYEELNALAAEVPPGADGllFLPYLSGE-----RTPHWDPNARGAFFG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 393 LKNKH-PEKFARAVFESqclfkLLYTQKMGFK-----KSDCSRILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALG 466
Cdd:COG1070 361 LTLSHtRAHLARAVLEG-----VAFALRDGLEaleeaGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALG 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 392895951 467 GAMRSRYVhsktTKTYSQY--YPCDNVSLA--CQPISANVEVYSNLFKTFK 513
Cdd:COG1070 436 AALLAAVG----LGLYDDLeeAAAAMVRVGetIEPDPENVAAYDELYERYR 482
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
5-469 |
1.35e-37 |
|
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: 144.22 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHeklkkfgtengVHKNGSVITSPvIMWIEAIDILFNDLREN--GWTDK 82
Cdd:cd07808 2 LLGIDLGTSSVKAVLVDEDGRVLASASAEYPTS-----------SPKPGWAEQDP-EDWWQATKEALRELLAKagISPSD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 83 LRGISGCAQQHGTVYwkngaenslkgLDESRSlaeqlemcfSVQKSPIWMDSSTEKQCQELETFVGgdQEMAKLTGSRAH 162
Cdd:cd07808 70 IAAIGLTGQMHGLVL-----------LDKNGR---------PLRPAILWNDQRSAAECEELEARLG--DEILIITGNPPL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 163 HRFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDFISSDlESKLGTL 242
Cdd:cd07808 128 PGFTLPKLLWLKENEPEIFARIRKILLPKDYLRYRLTGELA-TDPSDASGTLLFDVEKREWSEELLEALGLD-PSILPPI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 243 VHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSLL-PTDIGISLGTSDTVFFFT--PTFEPNIDAHVFSHFA 319
Cdd:cd07808 206 VESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGAGVVePGDALISLGTSGVVFAPTdkPVPDPKGRLHTFPHAV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 320 PNSgYMAMVCFKNGSLTRERARNL---NNSSWDKWDKIMKKTPAGNDNYIgFF----------FDEDeivprkPKGDY-- 384
Cdd:cd07808 286 PGK-WYAMGVTLSAGLSLRWLRDLfgpDRESFDELDAEAAKVPPGSEGLL-FLpylsgertpyWDPN------ARGSFfg 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 385 -TFECSEEElknkhpekFARAVFE------SQClFKLLytQKMGFKksdCSRILVTGGASRNTVLLQILSDVFEMPVCTI 457
Cdd:cd07808 358 lSLSHTRAH--------LARAVLEgvafslRDS-LEVL--KELGIK---VKEIRLIGGGAKSPLWRQILADVLGVPVVVP 423
|
490
....*....|..
gi 392895951 458 DVDGSAALGGAM 469
Cdd:cd07808 424 AEEEGSAYGAAL 435
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
5-469 |
4.08e-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: 142.34 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTtainfstheklKKFGTENGVHKNGSVITSPVIMWiEAIDILFNDLRENGWTDKLR 84
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILAS-----------ASRETPLIHPGPGWAELDPEELW-EAVKEAIREAAAQAGPDPIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 85 GISGCAQqhgtvywkngAEnSLKGLDES-RSLAeqlemcfsvqKSPIWMDSSTEKQCQELETFVGgDQEMAKLTGSRAHH 163
Cdd:cd07773 70 AISVSSQ----------GE-SGVPVDRDgEPLG----------PAIVWFDPRGKEEAEELAERIG-AEELYRITGLPPSP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 164 RFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDFISSDlESKLGTLV 243
Cdd:cd07773 128 MYSLAKLLWLREHEPEIFAKAAKWLSVADYIAYRLTGEPV-TDYSLASRTMLFDIRKRTWSEELLEAAGID-ASLLPELV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 244 HPMTSTGHVHSYWTRRFGIPSDCTVlpFLG--DNPSSLAGLSLL-PTDIGISLGTSDTVFFFTPTFEPNIDAH----VFS 316
Cdd:cd07773 206 PSGTVIGTVTPEAAEELGLPAGTPV--VVGghDHLCAALGAGVIePGDVLDSTGTAEALLAVVDEPPLDEMLAegglSYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 317 HFAPNSGYMAMVCFKNGSLTrERARNL---NNSSWDKWDKIMKKTPAGNDNYIgFF--FDEDEIVPRKPKGDYTFecseE 391
Cdd:cd07773 284 HHVPGGYYYLAGSLPGGALL-EWFRDLfggDESDLAAADELAEAAPPGPTGLL-FLphLSGSGTPDFDPDARGAF----L 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 392 ELKNKH-PEKFARAVFES-QCLFKLL--YTQKMGFKKsdcSRILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALGG 467
Cdd:cd07773 358 GLTLGTtRADLLRAILEGlAFELRLNleALEKAGIPI---DEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGA 434
|
..
gi 392895951 468 AM 469
Cdd:cd07773 435 AL 436
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
5-514 |
1.07e-35 |
|
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: 138.84 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHeklkkfgtengVHKNGSVITSPVIMWIEAIDILFNDLRENGwTDKLR 84
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLI-----------RPEPGWAEQDPEEILEAVLEALKEVLAKLG-GGEVD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 85 GISGCAQQHgtvywkngaenSLKGLDEsrslaeqlemcfsvQKSP-----IWMDSSTEKQCQELETfVGGDQEMAKLTGS 159
Cdd:cd07770 70 AIGFSSAMH-----------SLLGVDE--------------DGEPltpviTWADTRAAEEAERLRK-EGDGSELYRRTGC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 160 RAHHRFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDFISSDlESKL 239
Cdd:cd07770 124 PIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYLLYRLTGELV-TDYSTASGTGLLNIHTLDWDEEALELLGID-EEQL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 240 GTLVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNP-SSLAGLSLLPTDIGISLGTSDTVFFFTPTFEPNIDAHVFSHF 318
Cdd:cd07770 202 PELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGAlANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 319 APNSGY---MAMvcfKNGSLTRERARN---LNNSSWDKWDKIMKKTPAGNDN--YIGFFFDEdeivpRKPKGDYTFECSE 390
Cdd:cd07770 282 LDENRWlvgGAI---NNGGNVLDWLRDtllLSGDDYEELDKLAEAVPPGSHGliFLPYLAGE-----RAPGWNPDARGAF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 391 EELKNKH-PEKFARAVFESQCL-FKLLYtQKMGFKKSDCSRILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALGGA 468
Cdd:cd07770 354 FGLTLNHtRADILRAVLEGVAFnLKSIY-EALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAA 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 392895951 469 M--------RSRYVHSKTTKTYSQYypcdnvslacQPISANVEVYSNLFKTFKS 514
Cdd:cd07770 433 LlalealglISSLEADELVKIGKVV----------EPDPENHAIYAELYERFKK 476
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
5-469 |
3.78e-35 |
|
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: 135.77 E-value: 3.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHeklkkfgtengVHKNGSVITSPVIMW---IEAIDILFNDLRENGwtD 81
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLI-----------YPQPGWAEQDPEDWWqavVEAIREVLAKAGIDP--S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 82 KLRGISGCAQQHGTVYW-KNGaenslkgldesRSLAEqlemcfsvqkSPIWMDSstekqcqeletfvggdqemakltgsR 160
Cdd:cd00366 69 DIAAIGISGQMPGVVLVdADG-----------NPLRP----------AIIWLDR-------------------------R 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 161 AhhrfsaaqikkivdekqdvwkdteKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDFISSDLEsKLG 240
Cdd:cd00366 103 A------------------------KFLQPNDYIVFRLTGEFA-IDYSNASGTGLYDIKTGDWSEELLDALGIPRE-KLP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 241 TLVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSLL-PTDIGISLGTSDTVFFFTPT---FEPNIdaHVFS 316
Cdd:cd00366 157 PIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVVePGDAVDSTGTSSVLSVCTDEpvpPDPRL--LNRC 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 317 HFAPNsGYMAMVCFKNGSLTRERARNL------NNSSWDKWDKIMKKTPAGNDNYIGFFFDEDEIVPRKP---KGDY--- 384
Cdd:cd00366 235 HVVPG-LWLLEGAINTGGASLRWFRDEfgeeedSDAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDpaaRGVFfgl 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 385 TFECSEEElknkhpekFARAVFESQCL-----FKLLytQKMGFKksdCSRILVTGGASRNTVLLQILSDVFEMPVCTIDV 459
Cdd:cd00366 314 TLSHTRAH--------LIRAVLEGVAYalrdnLEIL--EELGVK---IKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEV 380
|
490
....*....|
gi 392895951 460 DGSAALGGAM 469
Cdd:cd00366 381 AEGAALGAAI 390
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-469 |
8.30e-26 |
|
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: 109.62 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIID-QNGKVVHTTAINFSTHEKlkkfGTENGVHkngsvITSPVIMW---IEAIDILFNDLREngwt 80
Cdd:cd07777 2 VLGIDIGTTSIKAALLDlESGRILESVSRPTPAPIS----SDDPGRS-----EQDPEKILeavRNLIDELPREYLS---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 81 dKLRGISGCAQQHGTVYWKngaenslkgldesrslaEQLEMCfsvqkSPI--WMDSSTEKQCQELETFVGgdQEMAKLTG 158
Cdd:cd07777 69 -DVTGIGITGQMHGIVLWD-----------------EDGNPV-----SPLitWQDQRCSEEFLGGLSTYG--EELLPKSG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 159 SRAHHRFSAAQIKKIVdEKQDVWKDTEKVSLISSFFASLLIGKYA-LIELTDGSGMNLMNIKTENWHKPLFDFISSDlES 237
Cdd:cd07777 124 MRLKPGYGLATLFWLL-RNGPLPSKADRAGTIGDYIVARLTGLPKpVMHPTNAASWGLFDLETGTWNKDLLEALGLP-VI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 238 KLGTLVHPMTSTGHVHSywtrrfGIPSDCTVLPFLGDNPSSLAGLSL-LPTDIGISLGTSDTVFFFTPTFEPNIDAHVFS 316
Cdd:cd07777 202 LLPEIVPSGEIVGTLSS------ALPKGIPVYVALGDNQASVLGSGLnEENDAVLNIGTGAQLSFLTPKFELSGSVEIRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 317 HFapNSGYMAMVCFKNG--------SLTRERARNLNN--SSWDKWDKIMKktPAGNDNYIG-----FFFDEdeivPRKPK 381
Cdd:cd07777 276 FF--DGRYLLVAASLPGgralavlvDFLREWLRELGGslSDDEIWEKLDE--LAESEESSDlsvdpTFFGE----RHDPE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 382 GDYTFECSEEElkNKHPEKFARAVFES--QCLFKLLytQKMGFKKSDCSRILVTGGASR-NTVLLQILSDVFEMPVCTID 458
Cdd:cd07777 348 GRGSITNIGES--NFTLGNLFRALCRGiaENLHEML--PRLDLDLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSE 423
|
490
....*....|.
gi 392895951 459 VDGSAALGGAM 469
Cdd:cd07777 424 GSEEAAVGAAL 434
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-513 |
8.50e-23 |
|
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: 101.44 E-value: 8.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 6 LGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHeklkkFGTENGVHKNGSVitspvimWIEAIDILFNDLRENG--WTDKL 83
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTY-----YPKPGWAEQDPED-------WWDAVCRATRALLEKSgiDPSDI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 84 RGISGCAQQHGTVywkngaenslkGLDESRSLaeqlemcfsVQKSPIWMDSSTEKQCQELETFVGGDQEMAKLTGSRAHH 163
Cdd:cd07805 71 AAIAFSGQMQGVV-----------PVDKDGNP---------LRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 164 RFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDFISSDLEsKLGTLV 243
Cdd:cd07805 131 KDPLAKILWLKENEPEIYAKTHKFLDAKDYLNFRLTGRAA-TDPSTASTTGLMDLRKRRWSEELLRAAGIDPD-KLPELV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 244 HPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGL-SLLPTDIGISLGTSDTVFFFTPTFEPNIDAHVFSHFAPNS 322
Cdd:cd07805 209 PSTEVVGELTPEAAAELGLPAGTPVVGGGGDAAAAALGAgAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASADP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 323 G-YMAMVCFKNGSLTRERARNL-------NNSSWDKWDKIMKKTPAGNDNYI------GfffdedEIVPR---KPKGDYT 385
Cdd:cd07805 289 GrYLLAAEQETAGGALEWARDNlggdedlGADDYELLDELAAEAPPGSNGLLflpwlnG------ERSPVedpNARGAFI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 386 fecseeELKNKH-PEKFARAVFESQC-----LFKLLytQKMGFKksdCSRILVTGGASRNTVLLQILSDVFEMPVCTIDV 459
Cdd:cd07805 363 ------GLSLEHtRADLARAVLEGVAfnlrwLLEAL--EKLTRK---IDELRLVGGGARSDLWCQILADVLGRPVEVPEN 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 392895951 460 DGSAALGGAMRSRYVHSKTTKTYSQYYPCDNVSLACQPISANVEVYSNLFKTFK 513
Cdd:cd07805 432 PQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
5-469 |
5.85e-22 |
|
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: 98.36 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHeklkkfgtengvhkngsvitSPvimwieaidilfndlrENGWtdklr 84
Cdd:cd07779 2 ILGIDVGTTSTRAIIFDLDGNIVASGYREYPPY--------------------YP----------------EPGW----- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 85 gisgcAQQHGTVYWkNGAENSLKGL-DESRSLAEQLE-MCFSVQKSpiwmdsstekqcqeleTFVGGDQEmakltGSRAH 162
Cdd:cd07779 41 -----VEQDPDDWW-DALCEALKEAvAKAGVDPEDIAaIGLTSQRS----------------TFVPVDED-----GRPLR 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 163 HRFSaaqikkivdekqdvWKD--TEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDFISSDlESKLG 240
Cdd:cd07779 94 PAIS--------------WQDkrTAKFLTVQDYLLYRLTGEFV-TDTTSASRTGLPDIRTRDWSDDLLDAFGID-RDKLP 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 241 TLVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSLL-PTDIGISLGTSDTVFFFT--PTFEPNIDAHVFSH 317
Cdd:cd07779 158 ELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQCAALGAGVLePGTASLSLGTAAVVIAVSdkPVEDPERRIPCNPS 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 318 FAP---------NSGYMAMVCFKNGSLTRERARNLNN-SSWDKWDKIMKKTPAGNDnyiGFFFdedeiVPrkpkgdyTFE 387
Cdd:cd07779 238 AVPgkwvlegsiNTGGSAVRWFRDEFGQDEVAEKELGvSPYELLNEEAAKSPPGSD---GLLF-----LP-------YLA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 388 CSEEELKNKH-------------PEKFARAVFESqclfkLLYTQKMGF-----KKSDCSRILVTGGASRNTVLLQILSDV 449
Cdd:cd07779 303 GAGTPYWNPEargafigltlshtRAHLARAILEG-----IAFELRDNLeamekAGVPIEEIRVSGGGSKSDLWNQIIADV 377
|
490 500
....*....|....*....|
gi 392895951 450 FEMPVCTIDVDGSAALGGAM 469
Cdd:cd07779 378 FGRPVERPETSEATALGAAI 397
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
5-469 |
1.90e-21 |
|
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: 96.83 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVhttAINFSTHEklkkfgtengvhkngsvITSPvimwieaidilfndlrENGWtdklr 84
Cdd:cd07804 2 LLGIDIGTTGTKGVLVDEDGKVL---ASASIEHD-----------------LLTP----------------KPGW----- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 85 gisgcAQQHGTVYWKNGAENSLKGLDESRSLAEQLE-MCFS---------------VQKSPIWMDSSTEKQCQELETFVG 148
Cdd:cd07804 41 -----AEHDPEVWWGAVCEIIRELLAKAGISPKEIAaIGVSglvpalvpvdengkpLRPAILYGDRRATEEIEWLNENIG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 149 GDQEMaKLTGSRAHHRFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMN-LMNIKTENWHKPL 227
Cdd:cd07804 116 EDRIF-EITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYIVYKLTGEYV-IDYSSAGNEGgLFDIRKRTWDEEL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 228 FDFISSDLEsKLGTLVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSLL-PTDIGISLGTSdtVFFFTPTF 306
Cdd:cd07804 194 LEALGIDPD-LLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDAAASALSAGVVePGDLLLMLGTA--GDIGVVTD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 307 EPNIDAHVFS--HFAPNSgYMAMVC-FKNGSLTR-----------ERARNLNNSSWDKWDKIMKKTPAGNDNYIgfffde 372
Cdd:cd07804 271 KLPTDPRLWLdyHDIPGT-YVLNGGmATSGSLLRwfrdefageevEAEKSGGDSAYDLLDEEAEKIPPGSDGLI------ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 373 deIVP-----RKPKGDYT-----FECSeeeLKNKHPEKFaRAVFESQCL-FK--LLYTQKMGFKKsdcSRILVTGGASRN 439
Cdd:cd07804 344 --VLPyfmgeRTPIWDPDargviFGLT---LSHTRAHLY-RALLEGVAYgLRhhLEVIREAGLPI---KRLVAVGGGAKS 414
|
490 500 510
....*....|....*....|....*....|
gi 392895951 440 TVLLQILSDVFEMPVCTIDVDGSAALGGAM 469
Cdd:cd07804 415 PLWRQIVADVTGVPQEYVKDTVGASLGDAF 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-469 |
7.57e-20 |
|
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: 91.90 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 6 LGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHEklkkfgteNGVHKNGSVItSPVIMWiEAIDILFND-LRENGWTDK-L 83
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWEYYT--------DDDYPDAKEF-DPEELW-EKICEAIREaLKKAGISPEdI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 84 RGISGCAQQHGTVyWKNGAENSLKGL---DeSRSLAEQLEMcfsvqkspiwmdsstekqcqeletfvgGDQEMAKLTGSR 160
Cdd:cd07798 73 SAVSSTSQREGIV-FLDKDGRELYAGpniD-ARGVEEAAEI---------------------------DDEFGEEIYTTT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 161 AHHR---FSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDFISSDLES 237
Cdd:cd07798 124 GHWPtelFPAARLLWFKENRPEIFERIATVLSISDWIGYRLTGELV-SEPSQASETQLFDIKKREWSQELLEALGLPPEI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 238 kLGTLVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSLL-PTDIGISLGTSdtvfffTP----TFEPNID- 311
Cdd:cd07798 203 -LPEIVPSGTVLGTVSEEAARELGLPEGTPVVVGGADTQCALLGSGAIePGDIGIVAGTT------TPvqmvTDEPIIDp 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 312 ---AHVFSHFAPNsGYM----AMVCfknGsLTRERARNL----NNSSWDKWDKIMKKTPAGNDNYIGFF----FDEDEIV 376
Cdd:cd07798 276 errLWTGCHLVPG-KWVlesnAGVT---G-LNYQWLKELlygdPEDSYEVLEEEASEIPPGANGVLAFLgpqiFDARLSG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 377 PrkPKGDYTFE--CSEEELKNKHpekFARAVFES-QCLFKLLYTQKMGFKKSDCSRILVTGGASRNTVLLQILSDVFEMP 453
Cdd:cd07798 351 L--KNGGFLFPtpLSASELTRGD---FARAILENiAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKP 425
|
490
....*....|....*.
gi 392895951 454 VCTIDVDGSAALGGAM 469
Cdd:cd07798 426 VLVPEGREASALGAAI 441
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
5-469 |
1.96e-19 |
|
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: 90.74 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHeklkkfgtengVHKNGSVITSPViMWIEAIDILFNDLRENGWTDKLR 84
Cdd:cd07783 2 FLGIDLGTSGVRAVVVDEDGTVLASASEPYPTS-----------RPGPGWVEQDPE-DWWEALRSLLRELPAELRPRRVV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 85 GISGCAQQhGTVYwkngaenslkGLD-ESRSLAEQLemcfsvqkspIWMDSSTEKQCQELetfvggdQEMAKLTGSRAHH 163
Cdd:cd07783 70 AIAVDGTS-GTLV----------LVDrEGEPLRPAI----------MYNDARAVAEAEEL-------AEAAGAVAPRTGL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 164 RFSA----AQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYALielTDGSgmNLM----NIKTENWHKPLFDFISSDl 235
Cdd:cd07783 122 AVSPssslAKLLWLKRHEPEVLAKTAKFLHQADWLAGRLTGDRGV---TDYN--NALklgyDPETGRWPSWLLALLGIP- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 236 ESKLGTLVHPMTSTGHVHSYWTRRFGIPSDCTVLpfLGDNPSSLAGLSLLPTDIG---ISLGTSDTVFFFTPTFEPNIDA 312
Cdd:cd07783 196 PDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVV--AGTTDSIAAFLASGAVRPGdavTSLGTTLVLKLLSDKRVPDPGG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 313 HVFSHFAPNSGYMAmvcfkNGSltrerarnlNNSS--WDKWdkimkktpagndnyigFFFDED------EIVPRKPKG-D 383
Cdd:cd07783 274 GVYSHRHGDGYWLV-----GGA---------SNTGgaVLRW----------------FFSDDElaelsaQADPPGPSGlI 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 384 YT----------FECSEEE---LKNKH-PEKFARAVFES------QCLFKLlytQKMGFKKSDcsRILVTGGASRNTVLL 443
Cdd:cd07783 324 YYplplrgerfpFWDPDARgflLPRPHdRAEFLRALLEGiafierLGYERL---EELGAPPVE--EVRTAGGGARNDLWN 398
|
490 500
....*....|....*....|....*.
gi 392895951 444 QILSDVFEMPVCTIDVDGsAALGGAM 469
Cdd:cd07783 399 QIRADVLGVPVVIAEEEE-AALGAAL 423
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
291-469 |
2.26e-18 |
|
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: 83.14 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 291 ISLGTSDtvFFFTPTFEPNIDAHVFSH-----FAPNSGYMAMVCFKNGSL----------TRERARNLNNSSWDKWDKIM 355
Cdd:pfam02782 3 ISAGTSS--FVLVETPEPVLSVHGVWGpytneMLPGYWGLEGGQSAAGSLlawllqfhglREELRDAGNVESLAELAALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 356 KKTPAGndnyiGFFFDEDEIVPRKPKGDYTFECSEEELKNKH-PEKFARAVFESQCL-FKLLYTQKMGFKKSDCSRILVT 433
Cdd:pfam02782 81 AVAPAG-----GLLFYPDFSGNRAPGADPGARGSITGLSSPTtLAHLYRAILESLALqLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 392895951 434 GGASRNTVLLQILSDVFEMPVCTIDVDGSAALGGAM 469
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALGAAL 191
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
6-281 |
2.21e-16 |
|
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: 78.92 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 6 LGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHEKlkkfgtengvhKNGSVITSPVIMWIEAIDILFNDLRENGWTDKL-R 84
Cdd:pfam00370 3 LGIDCGTTSTKAILFNEQGKIIAVAQLENPQITP-----------HPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQiK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 85 GISGCAQQHGTVYW-KNGaenslkgldesrslaEQLEMCFSvqkspiWMDSSTEKQCQELETfVGGDQEMAKLTGSRAHH 163
Cdd:pfam00370 72 GIGISNQGHGTVLLdKND---------------KPLYNAIL------WKDRRTAEIVENLKE-EGNNQKLYEITGLPIWP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 164 RFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDF--ISsdlESKLGT 241
Cdd:pfam00370 130 GFTLSKLRWIKENEPEVFEKIHKFLTIHDYLRWRLTGVFV-TDHTNASRSMMFNIHKLDWDPELLAAlgIP---RDHLPP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 392895951 242 LVHPMTSTGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAG 281
Cdd:pfam00370 206 LVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
5-469 |
6.93e-14 |
|
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: 73.74 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHEklkkfgtengvHKNGSVITSPVIMW---IEAIdilfNDLRENG--W 79
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVIS-----------PRPGWAERDMDELWqatAEAI----RELLEKSgvD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 80 TDKLRGISGCAQQHGtvywkngaensLKGLDEsrslAEQlemcfSVQKSPIWMDSSTEKQCQELETfVGGDQEMAKLTGS 159
Cdd:cd07802 67 PSDIAGVGVTGHGNG-----------LYLVDK----DGK-----PVRNAILSNDSRAADIVDRWEE-DGTLEKVYPLTGQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 160 --------------RAHHRFSAAQIKKIVDEKqDV--WKdtekvslissffaslLIGKYALiELTDGSGmNLMNIKTENW 223
Cdd:cd07802 126 plwpgqpvallrwlKENEPERYDRIRTVLFCK-DWirYR---------------LTGEIST-DYTDAGS-SLLDLDTGEY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 224 HKPLFDFIS-SDLESKLGTLVHPMTSTGHVhsywTR--------RFGIPsdctVLPFLGDNPSSLAGLSLL-PTDIGISL 293
Cdd:cd07802 188 DDELLDLLGiEELKDKLPPLVPSTEIAGRV----TAeaaaltglPEGTP----VAAGAFDVVASALGAGAVdEGQLCVIL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 294 GTSDTVFFFTPTFEPNIDAHVFSHFAPNSGYMAMVCFKNGSLTRERARNL--------NNSSWDKWDKIMKKTPAGNDN- 364
Cdd:cd07802 260 GTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSASNLDWFLDTllgeekeaGGSDYDELDELIAAVPPGSSGv 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 365 ----YI----------GFFFDedeivprkpkgdytfecseeeLKNKH-PEKFARAVFESQCLFKLLYTQKMGFKKSDcSR 429
Cdd:cd07802 340 iflpYLygsganpnarGGFFG---------------------LTAWHtRAHLLRAVYEGIAFSHRDHLERLLVARKP-ET 397
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 392895951 430 ILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALGGAM 469
Cdd:cd07802 398 IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAI 437
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-469 |
4.06e-11 |
|
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: 65.05 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 6 LGIDLSTQQIKAVIIDQNGKVVHTTAINFsTHEKLKKF--GTENGVHKNGSVITSPVIMWIEAIDILFNDlrengwtdkL 83
Cdd:cd07775 3 LALDAGTGSGRAVIFDLEGNQIAVAQREW-RHKEVPDVpgSMDFDTEKNWKLICECIREALKKAGIAPKS---------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 84 RGISGCAQQHGTVywkngaenslkgldesrslaeqlemCFSVQKSPIW----MDSSTEKQCQEL-ETFVGGDQEMAKLTG 158
Cdd:cd07775 73 AAISTTSMREGIV-------------------------LYDNEGEEIWacanVDARAAEEVSELkELYNTLEEEVYRISG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 159 srahHRFSAAQIKKIV---DEKQDVWKDTEKVSLISSFFASLLIGKYAlIELTDGSGMNLMNIKTENWHKPLFDF--ISS 233
Cdd:cd07775 128 ----QTFALGAIPRLLwlkNNRPEIYRKAAKITMLSDWIAYKLSGELA-VEPSNGSTTGLFDLKTRDWDPEILEMagLKA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 234 DLESKL---GTLVhpmtstGHVHSYWTRRFGIPSDCTVLPFLGDNPSSLAGLSLLPTDIGISLGTSdtvfFF-------T 303
Cdd:cd07775 203 DILPPVvesGTVI------GKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGS----FWqqevntaA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 304 PTFEPNIDAHVFSHFAPNSGYMAMVCFKNGSLTR-----------ERARNLNNSSWDKWDKIMKKTPAGNDNYIGFFFDE 372
Cdd:cd07775 273 PVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRwfrdafcaeekEIAERLGIDAYDLLEEMAKDVPPGSYGIMPIFSDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 373 -DEIVPRKPKGDYTFECSEEELKNKhpEKFARAVFESQCLFKLLYTQKM-GFKKSDCSRILVTGGASRNTVLLQILSDVF 450
Cdd:cd07775 353 mNYKNWRHAAPSFLNLDIDPEKCNK--ATFFRAIMENAAIVSAGNLERIaEFSGIFPDSLVFAGGASKGKLWCQILADVL 430
|
490
....*....|....*....
gi 392895951 451 EMPVCTIDVDGSAALGGAM 469
Cdd:cd07775 431 GLPVKVPVVKEATALGAAI 449
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
133-463 |
1.23e-09 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 60.23 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 133 DSSTEKQCQELETFVGgDQEMAKLTGSrAHHRF-SAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKyALIELTDGS 211
Cdd:cd07771 98 DPRTEGMMEELFEKIS-KEELYERTGI-QFQPInTLYQLYALKKEGPELLERADKLLMLPDLLNYLLTGE-KVAEYTIAS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 212 GMNLMNIKTENWHKPLFDFISSDlESKLGTLVHPMTSTGHVHSYWTRRFGIPsDCTVLPFLG-DNPSSLAGLSLLPTD-I 289
Cdd:cd07771 175 TTQLLDPRTKDWSEELLEKLGLP-RDLFPPIVPPGTVLGTLKPEVAEELGLK-GIPVIAVAShDTASAVAAVPAEDEDaA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 290 GISLGTSDTVFFFTPtfEPNIDAHVFSHFAPNSG-----YMAmvcFKNGS-------LTRERARNLNNSSWDKWDKIMKK 357
Cdd:cd07771 253 FISSGTWSLIGVELD--EPVITEEAFEAGFTNEGgadgtIRL---LKNITglwllqeCRREWEEEGKDYSYDELVALAEE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 358 TPAgndnyIGFFFDEDEIVPRKPKG------DYtfeCSEEELKN-KHPEKFARAVFESQCL-FKLLYTQKMGFKKSDCSR 429
Cdd:cd07771 328 APP-----FGAFIDPDDPRFLNPGDmpeairAY---CRETGQPVpESPGEIARCIYESLALkYAKTIEELEELTGKRIDR 399
|
330 340 350
....*....|....*....|....*....|....
gi 392895951 430 ILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSA 463
Cdd:cd07771 400 IHIVGGGSRNALLCQLTADATGLPVIAGPVEATA 433
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
5-227 |
3.08e-06 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 49.59 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 5 FLGIDLSTQQIKAVIIDQNGKVVHTTAINFSTHeklkkFGTENGVHKNGSVITSPVImwiEAIDILFNDLRENGWTDKLR 84
Cdd:PTZ00294 4 IGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQI-----TPHPGWLEHDPEEILRNVY---KCMNEAIKKLREKGPSFKIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 85 GISGCAQQHGTVYWkngaenslkgldeSRSLAEQLemcfsvQKSPIWMDSSTEKQCQELETFVGGDQEMAKLTGSRAHHR 164
Cdd:PTZ00294 76 AIGITNQRETVVAW-------------DKVTGKPL------YNAIVWLDTRTYDIVNELTKKYGGSNFFQKITGLPISTY 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392895951 165 FSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLI-----GKYALIELTDGSGMNLMNIKTENWHKPL 227
Cdd:PTZ00294 137 FSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIwnltgGKSHVTDVTNASRTFLMNIKTLKWDEEL 204
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
429-519 |
1.71e-05 |
|
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: 47.53 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 429 RILVTGG-ASRNTVLLQILSDVFEMPVCTIDVDGSAALGGAM-------RSRYVHSKTTK---TYSQYypcdnvslacQP 497
Cdd:cd07781 411 RVVACGGiAEKNPLWMQIYADVLGRPIKVPKSDQAPALGAAIlaavaagVYADIEEAADAmvrVDRVY----------EP 480
|
90 100
....*....|....*....|..
gi 392895951 498 ISANVEVYSNLFKTFKSRFDEF 519
Cdd:cd07781 481 DPENHAVYEELYALYKELYDAL 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
130-229 |
3.57e-05 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 46.23 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 130 IWMDSSTEKQCQELE-TFVGGDQEMAKLTGSRAHHRFSAAQIKKIVDEKQDVWKDTEKVSLISSFFASLLI-----GKYA 203
Cdd:PLN02295 102 VWMDSRTSSICRRLEkELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSGDALFGTIDSWLIwnltgGASG 181
|
90 100
....*....|....*....|....*....
gi 392895951 204 LIELTD---GSGMNLMNIKTENWHKPLFD 229
Cdd:PLN02295 182 GVHVTDvtnASRTMLMNLKTLDWDKPTLE 210
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
169-257 |
4.45e-04 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 42.78 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 169 QIKKIVDEKQDVWKDTEKVSLISSFFASLLIGKYALiELTDGSGMNLMNIKTENWHKPLFDFISSDLeSKLGTLVHPmts 248
Cdd:PRK10640 121 QLRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNW-EYTNATTTQLVNINSDDWDESLLAWSGAPK-AWFGRPTHP--- 195
|
....*....
gi 392895951 249 tGHVHSYWT 257
Cdd:PRK10640 196 -GNVIGHWI 203
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
401-469 |
7.11e-04 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 42.32 E-value: 7.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392895951 401 FARAVFES---QCLFKLLYTQKMGFKKSDcsRILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALGGAM 469
Cdd:PRK10331 363 FYRAALEGltaQLKRNLQVLEKIGHFKAS--ELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAM 432
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
429-522 |
7.50e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 42.14 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 429 RILVTGG-ASRNTVLLQILSDVFEMPVCTIDVDGSAALGGAM--------------RSRYVHSKTTKTYsqyypcdnvsl 493
Cdd:PRK04123 441 EVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIfaavaagaypdipeAQQAMASPVEKTY----------- 509
|
90 100
....*....|....*....|....*....
gi 392895951 494 acQPISANVEVYSNLFKTFKSRFDEFIKQ 522
Cdd:PRK04123 510 --QPDPENVARYEQLYQEYKQLHDYFGRG 536
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
402-469 |
6.42e-03 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It 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: 466971 [Multi-domain] Cd Length: 452 Bit Score: 39.14 E-value: 6.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392895951 402 ARAVFESqclfkllytqkMGFKKSDC--------SRILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALGGAM 469
Cdd:cd24121 381 LRAVYEG-----------VALAMRDCyehmgedpGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAM 445
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
428-469 |
7.14e-03 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 39.06 E-value: 7.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 392895951 428 SRILVTGGASRNTVLLQILSDVFEMPVCTIDVDGSAALGGAM 469
Cdd:cd07782 445 DTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAI 486
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
348-469 |
8.31e-03 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 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: 466811 [Multi-domain] Cd Length: 329 Bit Score: 38.62 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895951 348 WDKWDKIMKKTPAGNDNYIGFFFDEDEIVPRKPKGDYTFECSEEELKnkhpEKFARAVfesQCLFKLLYTQKMGFKKSDC 427
Cdd:cd10170 210 LREFEEAKKRFSGGEEDERLVPSLLGGGLPELGLEKGTLLLTEEEIR----DLFDPVI---DKILELIEEQLEAKSGTPP 282
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 392895951 428 SRILVTGGASRNTVLLQILSDVFEMPVCTIDVDG-----SAALGGAM 469
Cdd:cd10170 283 DAVVLVGGFSRSPYLRERLRERFGSAGIIIVLRSddpdtAVARGAAL 329
|
|
| |
