|
Name |
Accession |
Description |
Interval |
E-value |
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
5-507 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 850.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:COG0554 4 YILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAASGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEAEPLklssarasslRDR 164
Cdd:COG0554 84 TTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGA----------RER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ARDGELLMGTIDSWLIYNLTG--EHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSdeAVYGHTDPDGF 242
Cdd:COG0554 154 AEAGELLFGTIDSWLIWKLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSS--EVFGETDPDLF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 243 lGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLSGEPVqYALEGSIFVTGA 322
Cdd:COG0554 232 -GAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVT-YALEGSIFVAGA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 323 AIEWLED-VDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAYQTRDI 401
Cdd:COG0554 310 AVQWLRDgLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 402 AAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLRENWRVDRSFE 481
Cdd:COG0554 390 LDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFE 469
|
490 500
....*....|....*....|....*.
gi 300659648 482 PEMDPSEADSKYGRWEDAVDRSLAWA 507
Cdd:COG0554 470 PQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
5-500 |
0e+00 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. 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: 466789 [Multi-domain] Cd Length: 486 Bit Score: 849.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAASGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEAEPLklssarasslRDR 164
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGA----------RER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ARDGELLMGTIDSWLIYNLTG--EHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDPDGF 242
Cdd:cd07769 151 AERGELLFGTIDTWLIWKLTGgkVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSE--VFGYTDPEGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 243 lGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLsGEPVQYALEGSIFVTGA 322
Cdd:cd07769 229 -GAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQI-GGKVTYALEGSIFIAGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 323 AIEWLEDVD-LINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAYQTRDI 401
Cdd:cd07769 307 AIQWLRDNLgLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 402 AAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLRENWRVDRSFE 481
Cdd:cd07769 387 LEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFE 466
|
490
....*....|....*....
gi 300659648 482 PEMDPSEADSKYGRWEDAV 500
Cdd:cd07769 467 PSMDEEERERLYRGWKKAV 485
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
5-501 |
0e+00 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains 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. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 801.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAASGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEAEplklssarasSLRDR 164
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVP----------GARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ARDGELLMGTIDSWLIYNLTG--EHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDPDgF 242
Cdd:cd07786 151 AERGELAFGTIDSWLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSE--VFGYTDPD-L 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 243 LGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLSGEpVQYALEGSIFVTGA 322
Cdd:cd07786 228 LGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGK-VTYALEGSIFIAGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 323 AIEWLED-VDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAYQTRDI 401
Cdd:cd07786 307 AVQWLRDgLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 402 AAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLRENWRVDRSFE 481
Cdd:cd07786 387 LEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFE 466
|
490 500
....*....|....*....|
gi 300659648 482 PEMDPSEADSKYGRWEDAVD 501
Cdd:cd07786 467 PSMSEEEREALYAGWKKAVK 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
4-506 |
0e+00 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 798.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 4 AYVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQR 83
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 84 ETTVVWDAASGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEAEplklssarasSLRD 163
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVP----------GVRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 164 RARDGELLMGTIDSWLIYNLTG--EHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDPdG 241
Cdd:TIGR01311 151 AAERGELLFGTIDTWLIWNLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSE--VYGYTDP-G 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 242 FLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLSGEPVQYALEGSIFVTG 321
Cdd:TIGR01311 228 LLGAEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPVYALEGSVFVAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 322 AAIEWLED-VDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAYQTRD 400
Cdd:TIGR01311 308 AAVQWLRDnLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 401 IAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLRENWRVDRSF 480
Cdd:TIGR01311 388 VLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTF 467
|
490 500
....*....|....*....|....*.
gi 300659648 481 EPEMDPSEADSKYGRWEDAVDRSLAW 506
Cdd:TIGR01311 468 EPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-507 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 797.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 1 MTDAYVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGIT 80
Cdd:PRK00047 2 MMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 81 NQRETTVVWDAASGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEAEplklssarasS 160
Cdd:PRK00047 82 NQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVE----------G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 161 LRDRARDGELLMGTIDSWLIYNLTGE--HITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTD 238
Cdd:PRK00047 152 ARERAEKGELLFGTIDTWLVWKLTGGkvHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSE--VYGKTN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 239 PDGFLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLSGEPVqYALEGSIF 318
Cdd:PRK00047 230 PYGFFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVV-YALEGSIF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 319 VTGAAIEWLED-VDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAYQ 397
Cdd:PRK00047 309 VAGSAIQWLRDgLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 398 TRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLRENWRVD 477
Cdd:PRK00047 389 TRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKID 468
|
490 500 510
....*....|....*....|....*....|
gi 300659648 478 RSFEPEMDPSEADSKYGRWEDAVDRSLAWA 507
Cdd:PRK00047 469 RRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-503 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. 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: 466802 [Multi-domain] Cd Length: 499 Bit Score: 673.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAG---LSAAGLDADDLAAIGITN 81
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAvekLKALGISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 82 QRETTVVWDAASGRPIHNALVWQDRRTTSRVESLEE--NGKIERIREKTGLEADAYFSATKTEWLLDEAEPLKlssaras 159
Cdd:cd07792 82 QRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAktPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVK------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 160 slrDRARDGELLMGTIDSWLIYNLTGE-----HITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVY 234
Cdd:cd07792 155 ---KAVDDGRLLFGTVDSWLIWNLTGGknggvHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSE--VY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 235 GHTDPDGFLGaaVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQL-SGEPVQYAL 313
Cdd:cd07792 230 GKIASGPLAG--VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLgPDAPPVYAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 314 EGSIFVTGAAIEWLED-VDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLE 392
Cdd:cd07792 308 EGSIAIAGAAVQWLRDnLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 393 SIAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLR- 471
Cdd:cd07792 388 AVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKs 467
|
490 500 510
....*....|....*....|....*....|..
gi 300659648 472 ENWRVDRSFEPEMDPSEADSKYGRWEDAVDRS 503
Cdd:cd07792 468 LNEGGRTVFEPQISEEERERRYKRWKKAVERS 499
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
5-507 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 609.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLD--ADDLAAIGITNQ 82
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKgpSFKIKAIGITNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 83 RETTVVWDAASGRPIHNALVWQDRRTTSRVESL-EENGKIERIREKTGLEADAYFSATKTEWLLDEAEplklssarasSL 161
Cdd:PTZ00294 83 RETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELtKKYGGSNFFQKITGLPISTYFSAFKIRWMLENVP----------AV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 162 RDRARDGELLMGTIDSWLIYNLTGE--HITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDEavYGH--- 236
Cdd:PTZ00294 153 KDAVKEGTLLFGTIDTWLIWNLTGGksHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSEN--FGTisg 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 237 -TDPDgFLGaaVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLS-GEPVQYALE 314
Cdd:PTZ00294 231 eAVPL-LEG--VPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGpNGPTVYALE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 315 GSIFVTGAAIEWLED-VDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLES 393
Cdd:PTZ00294 308 GSIAVAGAGVEWLRDnMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 394 IAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLREN 473
Cdd:PTZ00294 388 IALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKL 467
|
490 500 510
....*....|....*....|....*....|....*
gi 300659648 474 WRV-DRSFEPEMDPSEADSKYGRWEDAVDRSLAWA 507
Cdd:PTZ00294 468 IRRsNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
5-510 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 592.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDA----DDLAAIGIT 80
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGhnvdSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 81 NQRETTVVWDAASGRPIHNALVWQDRRTTSRVESLEEN--GKIERIREKTGLEADAYFSATKTEWLLDEAEplklssara 158
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVD--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 159 sSLRDRARDGELLMGTIDSWLIYNLTG-----EHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaV 233
Cdd:PLN02295 152 -AVKEAVKSGDALFGTIDSWLIWNLTGgasggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSE--V 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 234 YGHTDPdGFLGAAVPVTAALGDQQAALFGQTCfDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLSGE-PVQYA 312
Cdd:PLN02295 229 IGTIAK-GWPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDaPTNYA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 313 LEGSIFVTGAAIEWLED-VDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATL 391
Cdd:PLN02295 307 LEGSVAIAGAAVQWLRDnLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 392 ESIAYQTRDIAAAMEAD-----SGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDS 466
Cdd:PLN02295 387 ESMCFQVKDVLDAMRKDageekSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTE 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 300659648 467 LDDL-RENWRVDRSFEPEMDPSEADSKYGRWEDAVDRSLAWATED 510
Cdd:PLN02295 467 EEIFaSEKWKNTTTFRPKLDEEERAKRYASWCKAVERSFDLADLS 511
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
5-500 |
0e+00 |
|
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: 539.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAASGRPIHNALVWQDRRTTSRVESLEENGKIERIRektGLEADAYFsATKTEWLLdEAEPLKLSSARAS----- 159
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALR---GGSKFLHF-LTRNKRFL-AASVLKFSTAHVSirllw 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 160 ------SLRDRARDGELLMGTIDSWLIYNLTG--EHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDE 231
Cdd:cd07793 156 ilqnnpELKEAAEKGELLFGTIDTWLLWKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 232 avYGHTDPDGFlGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLSGEPVqY 311
Cdd:cd07793 236 --FGSTDPSIF-GAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEIT-Y 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 312 ALEGSIFVTGAAIEWLEDVDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATL 391
Cdd:cd07793 312 LAEGNASDTGTVIDWAKSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAIL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 392 ESIAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLR 471
Cdd:cd07793 392 ESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELK 471
|
490 500
....*....|....*....|....*....
gi 300659648 472 ENWRVDRSFEPEMDPSEADSKYGRWEDAV 500
Cdd:cd07793 472 KLRKIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-502 |
1.45e-105 |
|
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: 324.09 E-value: 1.45e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAAsGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEaEPLKLSSARAsslrdr 164
Cdd:COG1070 82 GLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKEN-EPEIFARIAK------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ardgellMGTIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDEAvyGHTDPDGF-- 242
Cdd:COG1070 154 -------VLLPKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVA--GTLTAEAAae 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 243 --LGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTgEDAVSSEHGLLTTIGFQLSGepvQYALEGSIFVT 320
Cdd:COG1070 225 tgLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPG---RWLPMGATNNG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 321 GAAIEWL---------EDVDLINNAAQTAELASsvdttDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATL 391
Cdd:COG1070 301 GSALRWFrdlfadgelDDYEELNALAAEVPPGA-----DGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 392 ESIAYQTRDIAAAMEAdSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLR 471
Cdd:COG1070 376 EGVAFALRDGLEALEE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAA 454
|
490 500 510
....*....|....*....|....*....|...
gi 300659648 472 ENW-RVDRSFEPEMDPSEA-DSKYGRWEDAVDR 502
Cdd:COG1070 455 AAMvRVGETIEPDPENVAAyDELYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
5-485 |
5.48e-102 |
|
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: 312.92 E-value: 5.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAAsGRPIHNALVWQDRRTtsrvesleengkierirektgleadAYFSatktewlldeaeplklssarasslrdr 164
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQDKRT-------------------------AKFL--------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ardgellmgTIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDEAvyGHTDPD---- 240
Cdd:cd07779 108 ---------TVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVI--GTLTKEaaee 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 241 -GfLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTTIgfqlSGEPVQYALEGSIFV 319
Cdd:cd07779 177 tG-LPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNP----SAVPGKWVLEGSINT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 320 TGAAIEWLEDV---DLINNAAQ--------TAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVR 388
Cdd:cd07779 252 GGSAVRWFRDEfgqDEVAEKELgvspyellNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLAR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 389 ATLESIAYQTRDIAAAMEaDSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLD 468
Cdd:cd07779 332 AILEGIAFELRDNLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFE 410
|
490
....*....|....*...
gi 300659648 469 DLRENW-RVDRSFEPEMD 485
Cdd:cd07779 411 EAVKAMvRVTDTFEPDPE 428
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
8-449 |
6.74e-99 |
|
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: 303.72 E-value: 6.74e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 8 AIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRETTV 87
Cdd:cd00366 4 GIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMPGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 88 VWDAAsGRPIHNALVWQDRRttsrvesleengkierirektgleadAYFsatktewlldeaeplklssarasslrdrard 167
Cdd:cd00366 84 LVDAD-GNPLRPAIIWLDRR--------------------------AKF------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 168 gellmGTIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDPDGF----L 243
Cdd:cd00366 106 -----LQPNDYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGE--VVGRVTPEAAeetgL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 244 GAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSseHGLLTTIGfqlSGEPVQYALEGSIFVTGAA 323
Cdd:cd00366 179 PAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPP--DPRLLNRC---HVVPGLWLLEGAINTGGAS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 324 IEWL------EDVDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAYQ 397
Cdd:cd00366 254 LRWFrdefgeEEDSDAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYA 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 300659648 398 TRDIAAAMEADsGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETT 449
Cdd:cd00366 334 LRDNLEILEEL-GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
5-262 |
5.68e-89 |
|
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: 272.67 E-value: 5.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDaASGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEaEPlklssarasSLRDR 164
Cdd:pfam00370 81 GTVLLD-KNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKEN-EP---------EVFEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ARdgelLMGTIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSdeAVYGHTDPDGF-- 242
Cdd:pfam00370 150 IH----KFLTIHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESS--EIYGELNPELAam 223
|
250 260
....*....|....*....|..
gi 300659648 243 --LGAAVPVTAALGDQQAALFG 262
Cdd:pfam00370 224 wgLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
5-499 |
1.75e-84 |
|
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: 269.41 E-value: 1.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAaSGRPIHNALVWQDRRTTSRVESLEENGKiERIREKTGLEADAYFSATKTEWLLdEAEPLKLSSARASSLrdr 164
Cdd:cd07808 81 GLVLLDK-NGRPLRPAILWNDQRSAAECEELEARLG-DEILIITGNPPLPGFTLPKLLWLK-ENEPEIFARIRKILL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ARDgellmgtidsWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDEAvyGHTDPDG--F 242
Cdd:cd07808 155 PKD----------YLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIV--GTLTPEAaeE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 243 LG--AAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTgEDAVSSEHGLLTTIGFqlsGEPVQYALEGSIFVT 320
Cdd:cd07808 223 LGlpEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPH---AVPGKWYAMGVTLSA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 321 GAAIEWL--------EDVDLINNAAQTAELASsvdttDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLE 392
Cdd:cd07808 299 GLSLRWLrdlfgpdrESFDELDAEAAKVPPGS-----EGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 393 SIAYQTRDIAAAMEaDSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYWDSLDDLRE 472
Cdd:cd07808 374 GVAFSLRDSLEVLK-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAA 452
|
490 500
....*....|....*....|....*....
gi 300659648 473 NW-RVDRSFEPEMDPSEA-DSKYGRWEDA 499
Cdd:cd07808 453 ACiKIEKTIEPDPERHEAyDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
5-449 |
1.16e-83 |
|
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: 265.99 E-value: 1.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGaIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAglSAAGLDADDLAAIGITNQRE 84
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIRE--AAAQAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAaSGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLdEAEPLKLSSARAsslrdr 164
Cdd:cd07773 79 SGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLR-EHEPEIFAKAAK------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ardgeLLmgTIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDEAvyGHTDPDGF-- 242
Cdd:cd07773 151 -----WL--SVADYIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVI--GTVTPEAAee 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 243 --LGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEH-GLLTTIGFqlSGEPVQYALEGSIfV 319
Cdd:cd07773 222 lgLPAGTPVVVGGHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLaEGGLSYGH--HVPGGYYYLAGSL-P 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 320 TGAAIEWLED---VDLINNAAQTAELASSVDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAY 396
Cdd:cd07773 299 GGALLEWFRDlfgGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAF 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 300659648 397 QTRDIAAAMEAdSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETT 449
Cdd:cd07773 379 ELRLNLEALEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
5-497 |
2.02e-75 |
|
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: 245.89 E-value: 2.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDaASGRPIHNALVWQDRRTTSRVESLEEN-GKIERIREKTGLEADAYFSATKTEWLLDEaEPLKLSSARAsslrd 163
Cdd:cd07805 81 GVVPVD-KDGNPLRNAIIWSDTRAAEEAEEIAGGlGGIEGYRLGGGNPPSGKDPLAKILWLKEN-EPEIYAKTHK----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 164 rardgelLMGTIDsWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDEAvyGHTDPD--- 240
Cdd:cd07805 154 -------FLDAKD-YLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVV--GELTPEaaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 241 --GfLGAAVPVTAALGDQQAALFGQTCFDAGDAkNTY-GTGSFYLMNTGEDAVSSEHGLLTTigfqLSGEPVQYALEGSI 317
Cdd:cd07805 224 elG-LPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHGIFTL----ASADPGRYLLAAEQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 318 FVTGAAIEWL------------EDVDLINNAAQTAELASsvdttDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAH 385
Cdd:cd07805 298 ETAGGALEWArdnlggdedlgaDDYELLDELAAEAPPGS-----NGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRAD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 386 IVRATLESIAYQTRDIAAAMEADsGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVD-ETTALGAAYAAGLAVGYW 464
Cdd:cd07805 373 LARAVLEGVAFNLRWLLEALEKL-TRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGLGLL 451
|
490 500 510
....*....|....*....|....*....|....*.
gi 300659648 465 DSLDDLRENWRVDRSFEPemDPSEA---DSKYGRWE 497
Cdd:cd07805 452 KSFDEAKALVKVEKVFEP--DPENRaryDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
5-446 |
6.57e-71 |
|
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: 232.80 E-value: 6.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDaASGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEaEPlklssarasslrDR 164
Cdd:cd07804 81 ALVPVD-ENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRN-EP------------EV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ARDGELLMgTIDSWLIYNLTGEHITDVSNASRTM-LYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDPD--- 240
Cdd:cd07804 147 FKKTRKFL-GAYDYIVYKLTGEYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTE--IVGEVTKEaae 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 241 --GfLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTgSFYLMNTGEDAVSSEHGLLTTigfqlSGEPVQYALEGSIF 318
Cdd:cd07804 224 etG-LAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGT-AGDIGVVTDKLPTDPRLWLDY-----HDIPGTYVLNGGMA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 319 VTGAAIEWLEDV---DLINNAAQT--------AELASSVDTT-DGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHI 386
Cdd:cd07804 297 TSGSLLRWFRDEfagEEVEAEKSGgdsaydllDEEAEKIPPGsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 387 VRATLESIAYQTRDIAAAMEaDSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVD 446
Cdd:cd07804 377 YRALLEGVAYGLRHHLEVIR-EAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDT 435
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
5-498 |
8.47e-67 |
|
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: 222.82 E-value: 8.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAglSAAGLDADDLAAIGITNQRE 84
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKE--VLAKLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAaSGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEAEPLKLSSARASSlrdr 164
Cdd:cd07770 79 SLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVS---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ardgellmgtIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSsdEAVYGHTDPDGF-- 242
Cdd:cd07770 154 ----------IKEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDP--TEVLPGLKPEFAer 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 243 --LGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGT-GSFYLMnTGEDAVSSEHGLLTtigfqlsgepvqYALEGSIFV 319
Cdd:cd07770 222 lgLLAGTPVVLGASDGALANLGSGALDPGRAALTVGTsGAIRVV-SDRPVLDPPGRLWC------------YRLDENRWL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 320 TGAAI-------EWL--------EDVDLINNAAQTAELASsvdttDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKA 384
Cdd:cd07770 289 VGGAInnggnvlDWLrdtlllsgDDYEELDKLAEAVPPGS-----HGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 385 HIVRATLESIAYQTRDIAAAMEaDSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGLAVGYW 464
Cdd:cd07770 364 DILRAVLEGVAFNLKSIYEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLI 442
|
490 500 510
....*....|....*....|....*....|....*..
gi 300659648 465 DSLdDLRENWRVDRSFEPemDPSEA---DSKYGRWED 498
Cdd:cd07770 443 SSL-EADELVKIGKVVEP--DPENHaiyAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
5-449 |
2.26e-55 |
|
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: 191.61 E-value: 2.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRE 84
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAAsGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEaEPLKLSSARAS-SLRD 163
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN-EPERYDRIRTVlFCKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 164 rardgellmgtidsWLIYNLTGEHITDVSNASrTMLYNITDLEWDDWLLEEFDIP--REMLPEVRPSSDEAvyGHTDPD- 240
Cdd:cd07802 159 --------------WIRYRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIA--GRVTAEa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 241 ----GfLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTgsfYLMNTGedAVSSEHGLLTTIGFQLSGEPVQY-ALEG 315
Cdd:cd07802 222 aaltG-LPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGT---WSINEV--VTDEPVVPDSVGSNSLHADPGLYlIVEA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 316 SifVTGAA-IEWL-------------EDVDLINNAAQTAELASsvdttDGVYMVPAFTGLGAphwDGRARGTLVGMTRGT 381
Cdd:cd07802 296 S--PTSASnLDWFldtllgeekeaggSDYDELDELIAAVPPGS-----SGVIFLPYLYGSGA---NPNARGGFFGLTAWH 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300659648 382 RKAHIVRATLESIAYQTRDIAAAMeaDSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETT 449
Cdd:cd07802 366 TRAHLLRAVYEGIAFSHRDHLERL--LVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELG 431
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
5-448 |
1.26e-54 |
|
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: 189.36 E-value: 1.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGaIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAglSAAGLDADDLAAIGITNQRE 84
Cdd:cd07783 2 FLG-IDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRE--LPAELRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDAAsGRPIHNALVWQDRRttSRVESLEENGKIERIREKTGLEADAYFSATKTEWLLDEaEPLKLSSARAssLRdR 164
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDAR--AVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRH-EPEVLAKTAK--FL-H 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ARDgellmgtidsWLIYNLTG-EHITDVSNASRTmLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDPD--- 240
Cdd:cd07783 152 QAD----------WLAGRLTGdRGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGT--VIGTLTAEaae 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 241 --GfLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTgsfylmntgedavssehgllTTIGFQLSGEPV--------- 309
Cdd:cd07783 219 elG-LPAGTPVVAGTTDSIAAFLASGAVRPGDAVTSLGT--------------------TLVLKLLSDKRVpdpgggvys 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 310 ------QYALEGSIFVTGAAIEWL-EDVDLinnaaqtAELASSVDTT--DGVYMVP-AFTGLGAPHWDGRARGTLVgmTR 379
Cdd:cd07783 278 hrhgdgYWLVGGASNTGGAVLRWFfSDDEL-------AELSAQADPPgpSGLIYYPlPLRGERFPFWDPDARGFLL--PR 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300659648 380 GTRKAHIVRATLESIAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDET 448
Cdd:cd07783 349 PHDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
5-449 |
5.02e-53 |
|
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: 185.50 E-value: 5.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPE--PGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQ 82
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDdyPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 83 RETTVVWDAAsGRPIHnALVWQDRRTTSRVESLEENgKIERIREKTGLEADAYFSATKTEWLLDEAEplklssarasSLR 162
Cdd:cd07798 81 REGIVFLDKD-GRELY-AGPNIDARGVEEAAEIDDE-FGEEIYTTTGHWPTELFPAARLLWFKENRP----------EIF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 163 DRARdgELLMgtIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPS-------SDEAV-- 233
Cdd:cd07798 148 ERIA--TVLS--ISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSgtvlgtvSEEAAre 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 234 YGhtdpdgfLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTGEDAVSSEHGLLTtiGFQLSGEpvQYAL 313
Cdd:cd07798 224 LG-------LPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWT--GCHLVPG--KWVL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 314 EGSIFVTGAAIEWLEDVDLINNAAQ----TAELASSVDTTDGVYmvpAFTGLGAPHWDGRA--RGTLVGMTRGTR----K 383
Cdd:cd07798 293 ESNAGVTGLNYQWLKELLYGDPEDSyevlEEEASEIPPGANGVL---AFLGPQIFDARLSGlkNGGFLFPTPLSAseltR 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300659648 384 AHIVRATLESIAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETT 449
Cdd:cd07798 370 GDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREAS 435
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
8-448 |
8.54e-48 |
|
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: 171.65 E-value: 8.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 8 AIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQRETTV 87
Cdd:cd24121 4 GIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGDGTW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 88 VWDAAsGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWlLDEAEPLKLSSARASSlrdRARD 167
Cdd:cd24121 84 LVDED-GRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAW-LKENEPERLERARTAL---HCKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 168 gellmgtidsWLIYNLTGEHITDVSNASRTMLyNITDLEWDDWLLEEFDIP--REMLPEVRPSSDEAVYGHTDPDGFLG- 244
Cdd:cd24121 159 ----------WLFYKLTGEIATDPSDASLTFL-DFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 245 -AAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMntgedAVSSEHGLLTTIGFQLS-GEPVQYALEGSIFVTGA 322
Cdd:cd24121 228 pAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEV-----VVDEPDLEPEGVGYTIClGVPGRWLRAMANMAGTP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 323 AIEWLEDV--DLINNAAQTA----------ELASSVDTTDGV----YMVPAftGLGAPHWDGRARGTLVGMTRGTRKAHI 386
Cdd:cd24121 303 NLDWFLRElgEVLKEGAEPAgsdlfqdleeLAASSPPGAEGVlyhpYLSPA--GERAPFVNPNARAQFTGLSLEHTRADL 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300659648 387 VRATLESIAYQTRDIAAAMeadsGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDET 448
Cdd:cd24121 381 LRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEF 438
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
271-449 |
6.07e-43 |
|
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: 151.32 E-value: 6.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 271 AKNTYGTGSFYLMnTGEDAVSSEHGLLTTIGFqlSGEPVQYALEGSIFVTGAAIEWL----------EDVDLINNAAQTA 340
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYTN--EMLPGYWGLEGGQSAAGSLLAWLlqfhglreelRDAGNVESLAELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 341 ELASSVDTtDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAYQTRDIAAAMEADSGVSTTTLRVDG 420
Cdd:pfam02782 78 ALAAVAPA-GGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180
....*....|....*....|....*....
gi 300659648 421 GAVKNNFLCQLQSDIIQTDLARPEVDETT 449
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEAT 185
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
5-452 |
6.70e-41 |
|
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: 152.70 E-value: 6.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFD-QHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQR 83
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 84 ETTVVWDAAsGRPIHNALVWQDRRTTSRVESLEE--NGKIERIrekTGLEADAYFSATKTEWLLDEAEPLKlssARASSL 161
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEalGGKKCLL---VGLNIPARFTASKLLWLKENEPEHY---ARIAKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 162 rdrardgeLLMGTidsWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFD---IPREMLPEVRPSSDEAvyGHTD 238
Cdd:cd07809 154 --------LLPHD---YLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVLPAGEVA--GRLT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 239 PDG--FLG--AAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTgSFYLMNTGEDAVSSEHGLLTTigfqLSGEPVQYALe 314
Cdd:cd07809 221 PEGaeELGlpAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGT-SGTAYGVSDKPVSDPHGRVAT----FCDSTGGMLP- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 315 gSIFVTGAAIEWLE--------DVDLINNAAQTAELASsvdttDGVYMVPAFTG---LGAPHwdgrARGTLVGMTRG-TR 382
Cdd:cd07809 295 -LINTTNCLTAWTElfrellgvSYEELDELAAQAPPGA-----GGLLLLPFLNGertPNLPH----GRASLVGLTLSnFT 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300659648 383 KAHIVRATLESIAYQTRDiaaAMEA--DSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALG 452
Cdd:cd07809 365 RANLARAALEGATFGLRY---GLDIlrELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALG 433
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-435 |
1.18e-37 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 144.34 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGaIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLdaDDLAAIGITNQRE 84
Cdd:PRK15027 2 YIG-IDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TTVVWDaASGRPIHNALVWQDRRTTSRVESLEEngKIERIREKTGLEADAYFSATKTEWlLDEAEPLKLssarasslrdR 164
Cdd:PRK15027 79 GATLLD-AQQRVLRPAILWNDGRCAQECALLEA--RVPQSRVITGNLMMPGFTAPKLLW-VQRHEPEIF----------R 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 165 ARDGELLMgtiDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDPD---G 241
Cdd:PRK15027 145 QIDKVLLP---KDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSE--ITGALLPEvakA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 242 FLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYL------MNTGEDAVSSE-HGLlttigfqlsgePVQYALE 314
Cdd:PRK15027 220 WGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFavsegfLSKPESAVHSFcHAL-----------PQRWHLM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 315 GSIFVTGAAIEW------LEDVDLINNAAQTAElassvDTTDGVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVR 388
Cdd:PRK15027 289 SVMLSAASCLDWaakltgLSNVPALIAAAQQAD-----ESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELAR 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 300659648 389 ATLESIAYQtrdIAAAMEA--DSGVSTTTLRVDGGAVKNNFLCQLQSDI 435
Cdd:PRK15027 364 AVLEGVGYA---LADGMDVvhACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
5-496 |
1.40e-30 |
|
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: 124.37 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEK--HEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITNQ 82
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREwrHKEVPDVPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 83 RETTVVWDAAsGRPI---HNAlvwqDRRTTSRVESLEENgkierireKTGLEADAYFSATKTEWLLDEAEPLKLSSARAS 159
Cdd:cd07775 81 REGIVLYDNE-GEEIwacANV----DARAAEEVSELKEL--------YNTLEEEVYRISGQTFALGAIPRLLWLKNNRPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 160 SLRDRARdgellMGTIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDP 239
Cdd:cd07775 148 IYRKAAK-----ITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGT--VIGKVTK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 240 D-----GfLGAAVPVTAALGDQQAALFGQTCFDAGDAknTYGTGSFYLMNTGEDAVSSEHGLLTTIGFQLSGEPVQYalE 314
Cdd:cd07775 221 EaaeetG-LKEGTPVVVGGGDVQLGCLGLGVVRPGQT--AVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIPDMWQA--E 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 315 GSIFVTGAAIEWLEDV---DLINNAAQTA--------ELASSVDTtdGVY-MVPAFTGL-GAPHWDgRARGTLVGMT--- 378
Cdd:cd07775 296 GISFFPGLVMRWFRDAfcaEEKEIAERLGidaydlleEMAKDVPP--GSYgIMPIFSDVmNYKNWR-HAAPSFLNLDidp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 379 RGTRKAHIVRATLESIAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAG 458
Cdd:cd07775 373 EKCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAG 452
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 300659648 459 LAVGYWDSLDDLRENW-RVDRSFEPEMDPSEA-DSKYGRW 496
Cdd:cd07775 453 VGAGIYSSLEEAVESLvKWEREYLPNPENHEVyQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
5-449 |
1.52e-30 |
|
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: 124.19 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFD-QHGDVVAnTYE---KHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGI- 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELA-SAVvpyPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 80 -TnqrETTVVWDAASGRPIHNALVWQDRRttsrveSLEENGKIERIREKTGLEADAYFSAT--------KTEWLLDEAep 150
Cdd:cd07781 80 tT---SSTVVPVDEDGNPLAPAILWMDHR------AQEEAAEINETAHPALEYYLAYYGGVyssewmwpKALWLKRNA-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 151 lklssaraSSLRDRARdgeLLMGTIDsWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIP----REMLPEVR 226
Cdd:cd07781 149 --------PEVYDAAY---TIVEACD-WINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGllklREKLPGEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 227 PSSDEAVyGHTDPD-----GfLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSFYLMNTG------------EDA 289
Cdd:cd07781 217 VPVGEPA-GTLTAEaaerlG-LPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPkpvdipgicgpvPDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 290 VSsehgllttigfqlsgePVQYALEGSIFVTGAAIEWLedVDLINNAAQT---------AELASSVDTT-DGVYMVPAFT 359
Cdd:cd07781 295 VV----------------PGLYGLEAGQSAVGDIFAWF--VRLFVPPAEErgdsiyallSEEAAKLPPGeSGLVALDWFN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 360 GLGAPHWDGRARGTLVGMTRGTRKAHIVRATLESIAYQTRDIAAAMEaDSGVSTTTLRVDGG-AVKNNFLCQLQSDIIQT 438
Cdd:cd07781 357 GNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGiAEKNPLWMQIYADVLGR 435
|
490
....*....|.
gi 300659648 439 DLARPEVDETT 449
Cdd:cd07781 436 PIKVPKSDQAP 446
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-449 |
6.71e-28 |
|
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: 115.78 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVANTYEKHEQ---HYPEPGWVEHDPLEIWENTKSVVtAGLSAAGLDadDLAAIGITN 81
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVSRPTPapiSSDDPGRSEQDPEKILEAVRNLI-DELPREYLS--DVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 82 QRETTVVWDAaSGRPIHNALVWQDRRtTSRVESLEENGKIERIREKTGLeadayfsatktewlldeaePLKLSSArASSL 161
Cdd:cd07777 78 QMHGIVLWDE-DGNPVSPLITWQDQR-CSEEFLGGLSTYGEELLPKSGM-------------------RLKPGYG-LATL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 162 RDRARDGELL-----MGTIDSWLIYNLTG--EHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDEAVY 234
Cdd:cd07777 136 FWLLRNGPLPskadrAGTIGDYIVARLTGlpKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 235 GHTDpdgfLGAAVPVTAALGDQQAALFGQTCFDAGDAKNTYGTGSfylmntgedavssehgllttigfQLS--------G 306
Cdd:cd07777 216 LSSA----LPKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGA-----------------------QLSfltpkfelS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 307 EPVQYA--LEGSIFVTGAAI--------------EWLEDVDLINNAAQ----TAELASSvDTTDGVYMVPAFTGlgaPHW 366
Cdd:cd07777 269 GSVEIRpfFDGRYLLVAASLpggralavlvdflrEWLRELGGSLSDDEiwekLDELAES-EESSDLSVDPTFFG---ERH 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 367 DGRARGTLVGMTRGTRK-AHIVRATLESIAyqtRDIAAAMEADSGVST--TTLRVDGGAV-KNNFLCQLQSDIIQTDLAR 442
Cdd:cd07777 345 DPEGRGSITNIGESNFTlGNLFRALCRGIA---ENLHEMLPRLDLDLSgiERIVGSGGALrKNPVLRRIIEKRFGLPVVL 421
|
....*..
gi 300659648 443 PEVDETT 449
Cdd:cd07777 422 SEGSEEA 428
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
10-486 |
2.30e-20 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 93.55 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 10 DQGTTGTRFIVFDQHGDVVANTYEK-HEQHYPE-PGWVEHDPLEIWenTKSVVTAGLSAAGLDADDLAAIGITnqretTV 87
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnASDIAAEnSDWHQWSLDAIL--QRFADCCRQINSELTECHIRGITVT-----TF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 88 VWDAA----SGRPIHNALVWQDRRTTSRVESLEENGKIERIREKTGLEADAYFSATKTEWLlDEAEPLKLSSARASSLrd 163
Cdd:PRK10331 81 GVDGAlvdkQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWL-KENHPQLLEQAHAWLF-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 164 rardgellmgtIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDPDGF- 242
Cdd:PRK10331 158 -----------ISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGE--QIGTLQPSAAa 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 243 ---LGAAVPVTAALGDQQAALFGqtcfdAGDAKN----TYGTGSFYLMNTGE---DAVSSEHGLltTIGF-QLSG--EP- 308
Cdd:PRK10331 225 llgLPVGIPVISAGHDTQFALFG-----SGAGQNqpvlSSGTWEILMVRSAQvdtSLLSQYAGS--TCELdSQSGlyNPg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 309 VQYalegsifVTGAAIEWLEDV---------DLINNAAQTAELAssvdttDGVYMVPAFTGLGAPHWDGRARGTlvgmTR 379
Cdd:PRK10331 298 MQW-------LASGVLEWVRKLfwtaetpyqTMIEEARAIPPGA------DGVKMQCDLLACQNAGWQGVTLNT----TR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 380 GtrkaHIVRATLESIAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDETTALGAAYAAGL 459
Cdd:PRK10331 361 G----HFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWY 436
|
490 500
....*....|....*....|....*...
gi 300659648 460 AVGYWDSLDDLRENWRVD-RSFEPEMDP 486
Cdd:PRK10331 437 GVGEFSSPEQARAQMKYQyRYFYPQTEP 464
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
48-437 |
9.86e-20 |
|
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: 91.82 E-value: 9.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 48 DPLEIWENTKsvvtAGLSAAGLDADDLAAIGITnqretTvvW-------DAaSGRPIHNALVWQDRRTTSRVESLEENGK 120
Cdd:cd07771 46 DIDRLFDEIK----EGLKKAAEQGGDIDSIGID-----T--WgvdfgllDK-NGELLGNPVHYRDPRTEGMMEELFEKIS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 121 IERIREKTGLEADAYFSATKtewLLDEAEPLKLSSARASSLrdrardgeLLMGTIdswLIYNLTGEHITDVSNASRTMLY 200
Cdd:cd07771 114 KEELYERTGIQFQPINTLYQ---LYALKKEGPELLERADKL--------LMLPDL---LNYLLTGEKVAEYTIASTTQLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 201 NITDLEWDDWLLEEFDIPREMLPEVRPSSDeaVYGHTDP---DGFLGAAVPVTAALG-DQQAALFGQTCFDAGDAkntY- 275
Cdd:cd07771 180 DPRTKDWSEELLEKLGLPRDLFPPIVPPGT--VLGTLKPevaEELGLKGIPVIAVAShDTASAVAAVPAEDEDAA---Fi 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 276 GTGSFYLM-------NTGEDAVssEHGLLTTIGFqlsgepvqyalEGSIF----VTG------AAIEWLE-----DVDLI 333
Cdd:cd07771 255 SSGTWSLIgveldepVITEEAF--EAGFTNEGGA-----------DGTIRllknITGlwllqeCRREWEEegkdySYDEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 334 NNAAQTAE-LASSVDTTDGVYMVP-----------AFTGLGAPHwdgrargtlvgmTRGtrkaHIVRATLESIAYQTRDI 401
Cdd:cd07771 322 VALAEEAPpFGAFIDPDDPRFLNPgdmpeairaycRETGQPVPE------------SPG----EIARCIYESLALKYAKT 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 300659648 402 AAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQ 437
Cdd:cd07771 386 IEELEELTGKRIDRIHIVGGGSRNALLCQLTADATG 421
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
5-505 |
2.33e-19 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 90.84 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFDQHGDVVAnTYEKHEQHYPE---PGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITN 81
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIA-VGQAEWRHLAVpdvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSATS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 82 QRETTVVWDAaSGRPIhnalvWQ----DRRTTSRVESLEENgkierireKTGLEADAYFSATKTEWL--------LDEAE 149
Cdd:PRK10939 83 MREGIVLYDR-NGTEI-----WAcanvDARASREVSELKEL--------HNNFEEEVYRCSGQTLALgalprllwLAHHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 150 PLKLSSARASSLrdrardgellmgtIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPEVRPSS 229
Cdd:PRK10939 149 PDIYRQAHTITM-------------ISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 230 deAVYGHTDPDGF----LGAAVPVTAALGDQQAALFGQTCFDAGDAKnTYGtGSFY--LMNTGEDAVSSEHGLltTIGFQ 303
Cdd:PRK10939 216 --TVLGHVTAKAAaetgLRAGTPVVMGGGDVQLGCLGLGVVRPGQTA-VLG-GTFWqqVVNLPAPVTDPNMNI--RINPH 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 304 LSGEPVQYalEGSIFVTGAAIEWLEDV---DLINNAAQTA--------ELASSVDTtdGVY-MVPAFTGL--------GA 363
Cdd:PRK10939 290 VIPGMVQA--ESISFFTGLTMRWFRDAfcaEEKLLAERLGidayslleEMASRVPV--GSHgIIPIFSDVmrfkswyhAA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 364 PHW-----DGRARGtlvgmtrgtrKAHIVRATLESIAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQT 438
Cdd:PRK10939 366 PSFinlsiDPEKCN----------KATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGL 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300659648 439 DLARPEVDETTALGAAYAAGLAVGYWDSLDDLRENW-RVDRSFEPEMDPSEA-DSKYGRWEDAVDRSLA 505
Cdd:PRK10939 436 PVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLvRWERTFEPNPENHELyQEAKEKWQAVYADQLG 504
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
5-491 |
3.50e-17 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. 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. 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. 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: 466788 [Multi-domain] Cd Length: 522 Bit Score: 84.21 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGAIDQGTTGTRFIVFD--QHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITN- 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlyAGLEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 82 ------QRETTVVWDAASGRPIHNALVWQDRRTTSRVESLEENgKIERIREKTGLEADAYFSATKTEWLLDEAEPLklss 155
Cdd:cd07768 81 cslaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQ-CPQQLLDYLGGKISPEMGVPKLKYFLDEYSHL---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 156 arasslrdRARDGELLMGTidSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPRE------MLPEVRPSS 229
Cdd:cd07768 156 --------RDKHFHIFDLH--DYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLEhltttkNLPSNVPIG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 230 DEAVYGHTDPDGFLGAAVPVTAALG--DQQAALFGQtcfdagdAKNTYGTGSFYLMNTgedavSSEHGLLTTIGFQLSG- 306
Cdd:cd07768 226 TTSGVALPEMAEKMGLHPGTAVVVSciDAHASWFAV-------ASPHLETSLFMIAGT-----SSCHMYGTTISDRIPGv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 307 -EPVQYALEGSIFV-------TGAAIEWL---------------EDVDLINNAAQTA-ELASSVDTTDGVYMVPAFTGLG 362
Cdd:cd07768 294 wGPFDTIIDPDYSVyeagqsaTGKLIEHLfeshpcarkfdealkKGADIYQVLEQTIrQIEKNNGLSIHILTLDMFFGNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 363 APHWDGRARGTLVGMTRGTRK---AHIVRATLESIAYQTRDIAAAMEADsGVSTTTLRVDGGAVKNNFLCQLQSDIIQTD 439
Cdd:cd07768 374 SEFADPRLKGSFIGESLDTSMlnlTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVA 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 300659648 440 LARPEVDETTALGAAYAAGLAVGYWDSLDDLRE----NWRVDRSFEPEMDPSEADS 491
Cdd:cd07768 453 IIKPKENMMGILGAAVLAKVAAGKKQLADSITEadisNDRKSETFEPLAYRLGADY 508
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
5-448 |
1.89e-14 |
|
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: 75.65 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 5 YVGaIDQGTTGTRFIVFDQHGDVVANTYEKHEQHYPEPGWVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGITnqre 84
Cdd:cd07782 2 YIG-VDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 85 TT---VVWDAA--------SGRPIHNALVWQDRRTTSRVEsleengkieRIrEKTGLEADAYFSAT--------KTEWLL 145
Cdd:cd07782 77 ATcslVVLDAEgkpvsvspSGDDERNVILWMDHRAVEEAE---------RI-NATGHEVLKYVGGKispemeppKLLWLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 146 deaEPLKLSSARASSLRDRArdgellmgtiDsWLIYNLTGEHITdvSNASRT--MLYNITDLE---WDDWLLEEfdIPRE 220
Cdd:cd07782 147 ---ENLPETWAKAGHFFDLP----------D-FLTWKATGSLTR--SLCSLVckWTYLAHEGSeggWDDDFFKE--IGLE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 221 MLPEVRPS---SDEAVYGHTDPDGF---------LGAAVPVTAALGDQQAALFGqtCFDAGDAKNTYGTGSF-----YLM 283
Cdd:cd07782 209 DLVEDNFAkigSVVLPPGEPVGGGLtaeaakelgLPEGTPVGVSLIDAHAGGLG--TLGADVGGLPCEADPLtrrlaLIC 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 284 NTgedavSSEHgllttigFQLSGEPVQ----------------YALEGSIFVTGAAIEWLED------------------ 329
Cdd:cd07782 287 GT-----SSCH-------MAVSPEPVFvpgvwgpyysamlpglWLNEGGQSATGALLDHIIEthpaypelkeeakaagks 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 330 -----VDLINNAAQTAELASSVDTTDgVYMVPAFTGLGAPHWDGRARGTLVGMTRGTRKAHIVR---ATLESIAYQTRDI 401
Cdd:cd07782 355 iyeylNERLEQLAEEKGLPLAYLTRD-LHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHI 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 300659648 402 AAAMEAdSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTDLARPEVDET 448
Cdd:cd07782 434 IEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
367-435 |
3.74e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 49.46 E-value: 3.74e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 367 DGRARGTLVGMTRGTRKAHIVRATLESIAYQTRDIAAAMEaDSGVSTTTLRVDGG-AVKNNFLCQLQSDI 435
Cdd:PRK04123 394 DQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGiARKNPVLMQIYADV 462
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
170-443 |
8.11e-05 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 45.10 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 170 LLMgtIDSWLIYNLTGEHITDVSNASRTMLYNITDLEWDDWLLEEFDIPREMLPevRPSSDEAVYGH-TDPdgfLGAAVP 248
Cdd:PRK10640 139 ALL--IPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFG--RPTHPGNVIGHwICP---QGNEIP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 249 VTA-ALGDQQAALFGQTCFDAGDAKNTYGTGSfyLMntgedavssehgllttiGFQlSGEPV--QYALEGSIFVTGAAIE 325
Cdd:PRK10640 212 VVAvASHDTASAVIASPLNDSDAAYLSSGTWS--LM-----------------GFE-SQTPFtnDTALAANITNEGGAEG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300659648 326 -----------WL-------EDVD----LINNAAQTAELASSVDTTDGVYMVPAftglgAPHWDGRARGTLVGMTRGTRK 383
Cdd:PRK10640 272 ryrvlknimglWLlqrvlqeRQITdlpaLIAATAALPACRFLINPNDDRFINPP-----SMCSEIQAACRETAQPVPESD 346
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300659648 384 AHIVRATLESIAYQTRDIAAAMEADSGVSTTTLRVDGGAVKNNFLCQLQSDIIQTD-LARP 443
Cdd:PRK10640 347 AELARCIFDSLALLYADVLHELAQLRGEPFSQLHIVGGGCQNALLNQLCADACGIRvIAGP 407
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
4-79 |
3.09e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 39.49 E-value: 3.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300659648 4 AYVGAIDQGTTGTRFIVFDQHGDVVAntyeKHEQHYPepgwVEHDPLEIWENTKSVVTAGLSAAGLDADDLAAIGI 79
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLA----RERIPTP----AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| |
