|
Name |
Accession |
Description |
Interval |
E-value |
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-492 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 939.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 1 MTRYLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITN 80
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 81 QRETTVIWDRATGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGALA 160
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 161 FGTVDSWLLWNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQWLGAPVMIAGI 240
Cdd:COG0554 161 FGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGAEIPIAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 241 AGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRLNGKPCYAVEGSIFVAGAAMQWLRDGLKL 320
Cdd:COG0554 241 AGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 321 IAHANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQND-GAR 399
Cdd:COG0554 321 IDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADsGIP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 400 LESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWECERQFHPEMRPALRESL 479
Cdd:COG0554 401 LKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERL 480
|
490
....*....|...
gi 2527343889 480 YAGWLDAVERVCN 492
Cdd:COG0554 481 YAGWKKAVERTLG 493
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
4-488 |
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: 903.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRATGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGALAFGT 163
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQWLGAPVMIAGIAGD 243
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLGAEIPIAGIAGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 244 QHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRLNGKPCYAVEGSIFVAGAAMQWLRDGLKLIAH 323
Cdd:cd07786 241 QQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 324 ANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQND-GARLES 402
Cdd:cd07786 321 AAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADsGIPLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 403 LRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWECERQFHPEMRPALRESLYAG 482
Cdd:cd07786 401 LRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYAG 480
|
....*.
gi 2527343889 483 WLDAVE 488
Cdd:cd07786 481 WKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
4-488 |
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: 867.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRATGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGALAFGT 163
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQWLGAPVMIAGIAGD 243
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLGAGIPIAGILGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 244 QHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRLNGKPCYAVEGSIFVAGAAMQWLRDGLKLIAH 323
Cdd:cd07769 241 QQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 324 ANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQND-GARLES 402
Cdd:cd07769 321 AAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDsGIKLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 403 LRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWECERQFHPEMRPALRESLYAG 482
Cdd:cd07769 401 LRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYRG 480
|
....*.
gi 2527343889 483 WLDAVE 488
Cdd:cd07769 481 WKKAVE 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-489 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 841.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 1 MTRYLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITN 80
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 81 QRETTVIWDRATGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGALA 160
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 161 FGTVDSWLLWNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYG-TAEVQWLGAPVMIAG 239
Cdd:PRK00047 163 FGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGkTNPYGFFGGEVPIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 240 IAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRLNGKPCYAVEGSIFVAGAAMQWLRDGLK 319
Cdd:PRK00047 243 IAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 320 LIAHANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQND-GA 398
Cdd:PRK00047 323 IISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADsGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 399 RLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWECERQFHPEMRPALRES 478
Cdd:PRK00047 403 RLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREK 482
|
490
....*....|.
gi 2527343889 479 LYAGWLDAVER 489
Cdd:PRK00047 483 LYAGWKKAVKR 493
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
4-492 |
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: 790.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:TIGR01311 2 YILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRATGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGALAFGT 163
Cdd:TIGR01311 82 TTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQWLGAPVMIAGIAGD 243
Cdd:TIGR01311 162 IDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLGAEIPITGVLGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 244 QHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRLNGK-PCYAVEGSIFVAGAAMQWLRDGLKLIA 322
Cdd:TIGR01311 242 QQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKkPVYALEGSVFVAGAAVQWLRDNLKLIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 323 HANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQND-GARLE 401
Cdd:TIGR01311 322 HAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDaGVEIT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 402 SLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWECERQFHPEMRPALRESLYA 481
Cdd:TIGR01311 402 KLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREARYA 481
|
490
....*....|.
gi 2527343889 482 GWLDAVERVCN 492
Cdd:TIGR01311 482 GWKEAVKRSLG 492
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
4-489 |
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: 651.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKA---GIDASELASIGITN 80
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLkalGISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 81 QRETTVIWDRATGEPIYHAIVWQDRRTASWCTKL--KSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGA 158
Cdd:cd07792 82 QRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELsaKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 159 LAFGTVDSWLLWNLTNGKS---HCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQWLgAPV 235
Cdd:cd07792 162 LLFGTVDSWLIWNLTGGKNggvHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPL-AGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 236 MIAGIAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRL--NGKPCYAVEGSIFVAGAAMQW 313
Cdd:cd07792 241 PISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLgpDAPPVYALEGSIAIAGAAVQW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 314 LRDGLKLIAHANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAI 393
Cdd:cd07792 321 LRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 394 QND-GARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWECERQ-FHPEM 471
Cdd:cd07792 401 NKDsGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTvFEPQI 480
|
490
....*....|....*...
gi 2527343889 472 RPALRESLYAGWLDAVER 489
Cdd:cd07792 481 SEEERERRYKRWKKAVER 498
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
4-489 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 589.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDST---LAVCRGALDKAGIDAsELASIGITN 80
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVykcMNEAIKKLREKGPSF-KIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 81 QRETTVIWDRATGEPIYHAIVWQDRRTASWCTKLKSD-GHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGAL 159
Cdd:PTZ00294 82 QRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKyGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 160 AFGTVDSWLLWNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQW--LGAPVMI 237
Cdd:PTZ00294 162 LFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAvpLLEGVPI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 238 AGIAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRL--NGKPCYAVEGSIFVAGAAMQWLR 315
Cdd:PTZ00294 242 TGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLgpNGPTVYALEGSIAVAGAGVEWLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 316 DGLKLIAHANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQN 395
Cdd:PTZ00294 322 DNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 396 D-GARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWECE-RQFHPEMRP 473
Cdd:PTZ00294 402 DaGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSnSTFSPQMSA 481
|
490
....*....|....*.
gi 2527343889 474 ALRESLYAGWLDAVER 489
Cdd:PTZ00294 482 EERKAIYKEWNKAVER 497
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
4-489 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 583.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDA----SELASIGIT 79
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGhnvdSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 80 NQRETTVIWDRATGEPIYHAIVWQDRRTASWCTKLKSDGHEDT--VVERTGLLIDPYFSATKIAWILDNVEGARARAESG 157
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRkhFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 158 ALAFGTVDSWLLWNLTNGKS---HCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQWLGAP 234
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGASggvHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 235 VMIAGIAGDQHAALVGQACfYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRLNGK--PCYAVEGSIFVAGAAMQ 312
Cdd:PLN02295 241 VPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDapTNYALEGSVAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 313 WLRDGLKLIAHANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRA 392
Cdd:PLN02295 320 WLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 393 IQNDGARLES------LRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQI-SALWECER 465
Cdd:PLN02295 400 MRKDAGEEKShkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFaSEKWKNTT 479
|
490 500
....*....|....*....|....
gi 2527343889 466 QFHPEMRPALRESLYAGWLDAVER 489
Cdd:PLN02295 480 TFRPKLDEEERAKRYASWCKAVER 503
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-488 |
3.61e-171 |
|
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: 491.69 E-value: 3.61e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRATGEPIYHAIVWQDRRTA----SW--CTKLKS------DGHEDTVVER--TG--LLIDPYFSATKIAWILDNV 147
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAelceSWnrSLLLKAlrggskFLHFLTRNKRflAAsvLKFSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 148 EGARARAESGALAFGTVDSWLLWNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAE 227
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 228 VQWLGAPVMIAGIAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTMAYRLNGKPCYAVEGSIFVA 307
Cdd:cd07793 241 PSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASDT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 308 GAAMQWLRDGLkLIAHANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTK 387
Cdd:cd07793 321 GTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 388 DLVRAIQND-GARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWECERQ 466
Cdd:cd07793 400 QLLETMEKEtSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKI 479
|
490 500
....*....|....*....|..
gi 2527343889 467 FHPEMRPALRESLYAGWLDAVE 488
Cdd:cd07793 480 FEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-489 |
2.24e-109 |
|
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: 333.34 E-value: 2.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 3 RYLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQR 82
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 83 ETTVIWDRAtGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAEsgalAFG 162
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA----KVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 163 TVDSWLLWNLTnGKsHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYG--TAEVQWL-----GAPV 235
Cdd:COG1070 156 LPKDYLRYRLT-GE-FVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGtlTAEAAAEtglpaGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 236 mIAGiAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTgDKAVRSENRLLTTMAYRLNGKpcYAVEGSIFVAGAAMQWLR 315
Cdd:COG1070 234 -VAG-AGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR--WLPMGATNNGGSALRWFR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 316 DglkLIAHANESS-----AHAEAVGVD-NPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDL 389
Cdd:COG1070 309 D---LFADGELDDyeelnALAAEVPPGaDGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 390 VRAIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWEC-ERQFH 468
Cdd:COG1070 386 LEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRvGETIE 465
|
490 500
....*....|....*....|....
gi 2527343889 469 PemRPALRE---SLYAGWLDAVER 489
Cdd:COG1070 466 P--DPENVAaydELYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-471 |
8.77e-108 |
|
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: 327.17 E-value: 8.77e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRAtGEPIYHAIVWQDRRTAswctklksdghedtvvertgllidpyfsatkiawildnvegararaesgalAFGT 163
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQDKRTA---------------------------------------------------KFLT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTNGksHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYG--TAEVQWL-----GAPVm 236
Cdd:cd07779 109 VQDYLLYRLTGE--FVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGtlTKEAAEEtglpeGTPV- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 237 IAGiAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTgDKAVRSENRLLTTMAYRLNGKpcYAVEGSIFVAGAAMQWLRD 316
Cdd:cd07779 186 VAG-GGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAVPGK--WVLEGSINTGGSAVRWFRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 317 ----GLKLIAHANESS-----AHAEAVGVD-NPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQT 386
Cdd:cd07779 262 efgqDEVAEKELGVSPyellnEEAAKSPPGsDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFEL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 387 KDLVRAIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQ-ISALWECER 465
Cdd:cd07779 342 RDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEaVKAMVRVTD 421
|
....*.
gi 2527343889 466 QFHPEM 471
Cdd:cd07779 422 TFEPDP 427
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-444 |
1.77e-92 |
|
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: 286.38 E-value: 1.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRAtGEPIYHAIVWQDRRTAswctklksdghedtvvertgllidpyfsatkiawildnvegararaesgalaFGT 163
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIWLDRRAK----------------------------------------------------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTnGKsHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGT-----AEVQWL--GAPVm 236
Cdd:cd00366 108 PNDYIVFRLT-GE-FAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRvtpeaAEETGLpaGTPV- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 237 IAGiAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKavRSENRLLTTMAYRLNGKpcYAVEGSIFVAGAAMQWLRD 316
Cdd:cd00366 185 VAG-GGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEP--VPPDPRLLNRCHVVPGL--WLLEGAINTGGASLRWFRD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 317 --GLKLIAHANESSAHAEAVGV---DNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVR 391
Cdd:cd00366 260 efGEEEDSDAEYEGLDELAAEVppgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLE 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2527343889 392 AIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLA 444
Cdd:cd00366 340 ILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
4-449 |
1.49e-89 |
|
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: 280.63 E-value: 1.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGidASELASIGITNQRE 83
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRAtGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAEsgalAFGT 163
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAA----KWLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTnGKsHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQWL-------GAPVM 236
Cdd:cd07773 154 VADYIAYRLT-GE-PVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAeelglpaGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 237 IAGIagDQHAALVGQACFYPGMAksTYGTGCFLMLntgdkAVRSENRLLTTMAYRlnGKPCY--AVEG------SIFVAG 308
Cdd:cd07773 232 VGGH--DHLCAALGAGVIEPGDV--LDSTGTAEAL-----LAVVDEPPLDEMLAE--GGLSYghHVPGgyyylaGSLPGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 309 AAMQWLRD--GLKLIAHANESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQT 386
Cdd:cd07773 301 ALLEWFRDlfGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFEL 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527343889 387 KDLVRAIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTG 449
Cdd:cd07773 381 RLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-250 |
1.37e-88 |
|
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: 271.13 E-value: 1.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRATgEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAEsgalAFGT 163
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTnGKsHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGT-----AEVQWLGAPVMIA 238
Cdd:pfam00370 156 IHDYLRWRLT-GV-FVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGElnpelAAMWGLDEGVPVV 233
|
250
....*....|..
gi 2527343889 239 GIAGDQHAALVG 250
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-481 |
3.92e-83 |
|
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: 265.17 E-value: 3.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDrATGEPIYHAIVWQDRRTASWCTKLKSDgHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGALAfgt 163
Cdd:cd07808 81 GLVLLD-KNGRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLP--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDsWLLWNLTNgkSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYG--TAEV-QWLG----APVm 236
Cdd:cd07808 156 KD-YLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGtlTPEAaEELGlpegTPV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 237 IAGiAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLLTTmayrlngkpCYAVE------GSIFVAGAA 310
Cdd:cd07808 232 VAG-AGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTF---------PHAVPgkwyamGVTLSAGLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 311 MQWLRDglkLIAHANES----SAHAEAV--GVDNPVYLvPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCY 384
Cdd:cd07808 302 LRWLRD---LFGPDRESfdelDAEAAKVppGSEGLLFL-PYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 385 QTKDLVRAIQNDGARLESLRVDGGMVVND-WvMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALW-E 462
Cdd:cd07808 378 SLRDSLEVLKELGIKVKEIRLIGGGAKSPlW-RQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACiK 456
|
490 500
....*....|....*....|
gi 2527343889 463 CERQFHPEMRPALR-ESLYA 481
Cdd:cd07808 457 IEKTIEPDPERHEAyDELYA 476
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
4-477 |
5.53e-74 |
|
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: 241.66 E-value: 5.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRAtGEPIYHAIVWQDRRTASWCTKL-KSDGHEDTVVERTGLLIDPYFSATKIAWILDNvegARARAESGALAFG 162
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIaGGLGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 163 TVDsWLLWNLTnGKsHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYG--TAEV-QWLG----APV 235
Cdd:cd07805 157 AKD-YLNFRLT-GR-AATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGelTPEAaAELGlpagTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 236 mIAGiAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRlLTTMAYRLNGKpcYAVEGSIFVAGAAMQWLR 315
Cdd:cd07805 234 -VGG-GGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHG-IFTLASADPGR--YLLAAEQETAGGALEWAR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 316 DGLkLIAHANESSAHAE--------AVGVDNPVYLvPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTK 387
Cdd:cd07805 309 DNL-GGDEDLGADDYELldelaaeaPPGSNGLLFL-PWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 388 DLVRAIQNDGARLESLRVDGGMVVND-WvMKFLADILNVTVDRPRV-TETTALGAAYLAGLQTGIFDNLEQISALWECER 465
Cdd:cd07805 387 WLLEALEKLTRKIDELRLVGGGARSDlW-CQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVKVEK 465
|
490
....*....|..
gi 2527343889 466 QFHPemRPALRE 477
Cdd:cd07805 466 VFEP--DPENRA 475
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-469 |
6.97e-74 |
|
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: 240.92 E-value: 6.97e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDasELASIGITNQRE 83
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDrATGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESgalaFGT 163
Cdd:cd07770 79 SLLGVD-EDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK----FVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTnGKsHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGTAEVQWL-------GAPVM 236
Cdd:cd07770 154 IKEYLLYRLT-GE-LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAerlgllaGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 237 IAgiAGDQHAALVGQACFYPGMAKSTYGTgcflmlnTGdkAVRsenrlLTTMAYRLNGKP---CYAVEGSIFVAGAAM-- 311
Cdd:cd07770 232 LG--ASDGALANLGSGALDPGRAALTVGT-------SG--AIR-----VVSDRPVLDPPGrlwCYRLDENRWLVGGAInn 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 312 -----QWLRDGLKLIAHANE---SSAHAEAVGVDNPVYLvPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVC 383
Cdd:cd07770 296 ggnvlDWLRDTLLLSGDDYEeldKLAEAVPPGSHGLIFL-PYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 384 YQTKDLVRAIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEqISALWEC 463
Cdd:cd07770 375 FNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLE-ADELVKI 453
|
....*.
gi 2527343889 464 ERQFHP 469
Cdd:cd07770 454 GKVVEP 459
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-449 |
3.56e-73 |
|
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: 238.19 E-value: 3.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRAtGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESgalaFGT 163
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRK----FLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTNgkSHCTDATNASRTA-LFNIHKQDWDDDLLALFRVPRALLPEVLDS-----------AADYGTAEvqwl 231
Cdd:cd07804 156 AYDYIVYKLTG--EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSteivgevtkeaAEETGLAE---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 232 GAPVmIAGiAGDQHAALVGQACFYPGMAKSTYGT-GCFLMLNtgDKAVRSENrllttMAYRLNGKPC-YAVEGSIFVAGA 309
Cdd:cd07804 230 GTPV-VAG-TVDAAASALSAGVVEPGDLLLMLGTaGDIGVVT--DKLPTDPR-----LWLDYHDIPGtYVLNGGMATSGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 310 AMQWLRDGL----KLIAHANESSAH------AEAV--GVDNPVYLvPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTA 377
Cdd:cd07804 301 LLRWFRDEFageeVEAEKSGGDSAYdlldeeAEKIppGSDGLIVL-PYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527343889 378 GLQSVCYQTKDLVRAIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTG 449
Cdd:cd07804 380 LLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-449 |
4.08e-56 |
|
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: 193.15 E-value: 4.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRAtGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNvEGARARAESGALafgT 163
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN-EPERYDRIRTVL---F 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTnGKsHCTDATNASrTALFNIHKQDWDDDLLALFRVP--RALLPEVLDSAADYG--TAEVQWL-----GAP 234
Cdd:cd07802 156 CKDWIRYRLT-GE-ISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGrvTAEAAALtglpeGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 235 VmiAGIAGDQHAALVGQACFYPGMAKSTYGTGCflmLNTG--DKAVRSENRLLtTMAYRLNGKpCYAVEGSifVAGAA-M 311
Cdd:cd07802 233 V--AAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGS-NSLHADPGL-YLIVEAS--PTSASnL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 312 QWLRD---------GLKLIAHANE--SSAHAEAVGVdnpVYLvPAFTGLGAphwDPHARGAIMGLTRDTGIGEIVTAGLQ 380
Cdd:cd07802 304 DWFLDtllgeekeaGGSDYDELDEliAAVPPGSSGV---IFL-PYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYE 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527343889 381 SVCYQTKDLVRAIQNDGaRLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTG 449
Cdd:cd07802 377 GIAFSHRDHLERLLVAR-KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
4-445 |
6.07e-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: 187.04 E-value: 6.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIdaSELASIGITNQRE 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRP--RRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRAtGEPIYHAIVWQDRRTASWCTKLKSdgHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESGALAfgt 163
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAEELAE--AAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQ--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 vDSWLLWNLTnGKSHCTDATNASRTaLFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYG--TAEV-QWLGAPVMIAGI 240
Cdd:cd07783 153 -ADWLAGRLT-GDRGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGtlTAEAaEELGLPAGTPVV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 241 AG--DQHAALVGQACFYPGMAKSTYGTG-CFlmlntgdKAVRSENRLLTTMA---YRLnGKPCYAVEGSIFVAGAAMQWL 314
Cdd:cd07783 230 AGttDSIAAFLASGAVRPGDAVTSLGTTlVL-------KLLSDKRVPDPGGGvysHRH-GDGYWLVGGASNTGGAVLRWF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 315 RDGLKLiahaNESSAHAEAVGVDNPVYLVPAFTGLGAPHWDPHARGAImgLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQ 394
Cdd:cd07783 302 FSDDEL----AELSAQADPPGPSGLIYYPLPLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLE 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2527343889 395 NDGAR-LESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTEtTALGAAYLAG 445
Cdd:cd07783 376 ELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE-AALGAALLAA 426
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-449 |
4.76e-47 |
|
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: 168.94 E-value: 4.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKD--GWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQ 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDypDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 82 RETTVIWDRAtGEPIYhAIVWQDRRTASWCTKLkSDGHEDTVVERTGLLIDPYFSATKIAWILDNVEGARARAESgalaF 161
Cdd:cd07798 81 REGIVFLDKD-GRELY-AGPNIDARGVEEAAEI-DDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIAT----V 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 162 GTVDSWLLWNLTnGKSHcTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDS-----------AADYGTAEvqw 230
Cdd:cd07798 154 LSISDWIGYRLT-GELV-SEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSgtvlgtvseeaARELGLPE--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 231 lGAPVMIAGiaGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTgDKAVRSENRLLTTMAYRLNGKpcYAVEGSIFVAGAA 310
Cdd:cd07798 229 -GTPVVVGG--ADTQCALLGSGAIEPGDIGIVAGTTTPVQMVT-DEPIIDPERRLWTGCHLVPGK--WVLESNAGVTGLN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 311 MQWLRDGL---------KLIAHANESSAHAEAVgvdnpvylvpaFTGLGAPHWDPHARGAIMGL--------TRDTGIGE 373
Cdd:cd07798 303 YQWLKELLygdpedsyeVLEEEASEIPPGANGV-----------LAFLGPQIFDARLSGLKNGGflfptplsASELTRGD 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527343889 374 IVTAGLQSVCYQTKDLVRAIQND-GARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTG 449
Cdd:cd07798 372 FARAILENIAFAIRANLEQLEEVsGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
4-449 |
6.95e-45 |
|
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: 163.18 E-value: 6.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQRE 83
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TTVIWDRAtGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAWILDNvEGARARAESGALafgT 163
Cdd:cd24121 81 GTWLVDED-GRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN-EPERLERARTAL---H 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 164 VDSWLLWNLTnGKShCTDATNASRTaLFNIHKQDWDDDLLALFRVP--RALLPEVLDS--AADYGTAEV-QWLGAPVMIA 238
Cdd:cd24121 156 CKDWLFYKLT-GEI-ATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGteVIGPLTPEAaAATGLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 239 GIAG--DQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSEN--------------RLLTTMAyrlnGKPC---YA 299
Cdd:cd24121 233 VVLGpfDVVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGvgyticlgvpgrwlRAMANMA----GTPNldwFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 300 VEGSIFVAGAAMQWLRDGLKLI-AHANESSAHAEAVgVDNPvYLVPAftGLGAPHWDPHARGAIMGLTRDTGIGEIVTAG 378
Cdd:cd24121 309 RELGEVLKEGAEPAGSDLFQDLeELAASSPPGAEGV-LYHP-YLSPA--GERAPFVNPNARAQFTGLSLEHTRADLLRAV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527343889 379 LQSVCYQTKDLVRAIqndGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTG 449
Cdd:cd24121 385 YEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-445 |
1.05e-44 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 162.72 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFD-QTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQR 82
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 83 ETTVIWDRAtGEPIYHAIVWQDRRTASWCTKLKSD-GHEDTVVerTGLLIDPYFSATKIAWILDNVEGARARAEsgalAF 161
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEAlGGKKCLL--VGLNIPARFTASKLLWLKENEPEHYARIA----KI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 162 GTVDSWLLWNLTNGKshCTDATNASRTALFNIHKQDWDDDLLALF---RVPRALLPEVLDSAADYGT-----AEVQWLGA 233
Cdd:cd07809 154 LLPHDYLNWKLTGEK--VTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVAGRltpegAEELGLPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 234 PVMIAGIAGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTgDKAVRSENRLLTTMAYRLNGK-PCyavegsIFVAGAAMQ 312
Cdd:cd07809 232 GIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVS-DKPVSDPHGRVATFCDSTGGMlPL------INTTNCLTA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 313 WLRDGLKLI-AHANESSAHAEAVGVDNP-VYLVPAFTGLGAPHWdPHARGAIMGLT-RDTGIGEIVTAGLQSVCYQTKDL 389
Cdd:cd07809 305 WTELFRELLgVSYEELDELAAQAPPGAGgLLLLPFLNGERTPNL-PHGRASLVGLTlSNFTRANLARAALEGATFGLRYG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2527343889 390 VRAIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAG 445
Cdd:cd07809 384 LDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAA 439
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-483 |
1.13e-42 |
|
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: 158.26 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEF-HQYFPKD-GWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITNQ 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWrHKEVPDVpGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 82 RETTVIWDRAtGEPIYhAIVWQDRRTASWCTKLK--SDGHEDTVVERTGllidPYFSATKIA---WILDNVEGARARAES 156
Cdd:cd07775 81 REGIVLYDNE-GEEIW-ACANVDARAAEEVSELKelYNTLEEEVYRISG----QTFALGAIPrllWLKNNRPEIYRKAAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 157 galaFGTVDSWLLWNLTnGKShCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYG--TAEVQWL--- 231
Cdd:cd07775 155 ----ITMLSDWIAYKLS-GEL-AVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGkvTKEAAEEtgl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 232 --GAPVMIAGiaGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSENRLlttmayRLNgkpCYAV------EGS 303
Cdd:cd07775 229 keGTPVVVGG--GDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNI------RVN---CHVIpdmwqaEGI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 304 IFVAGAAMQWLRDglkliAHANESSAHAEAVGVDnpVY----------------LVPAFTGL-GAPHWDpHARGAIMGLT 366
Cdd:cd07775 298 SFFPGLVMRWFRD-----AFCAEEKEIAERLGID--AYdlleemakdvppgsygIMPIFSDVmNYKNWR-HAAPSFLNLD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 367 RD---TGIGEIVTAGLQS---VCYQTKDLVRAIQndGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGA 440
Cdd:cd07775 370 IDpekCNKATFFRAIMENaaiVSAGNLERIAEFS--GIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGA 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2527343889 441 AYLAGLQTGIFDNLE---QISALWECERQFHPEMRpALRESLYAGW 483
Cdd:cd07775 448 AIAAGVGAGIYSSLEeavESLVKWEREYLPNPENH-EVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-455 |
6.67e-40 |
|
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: 150.76 E-value: 6.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFD-QTGNSVATDQQEFHQYF--PKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGI-- 78
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVdt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 79 TnqrETTVIWDRATGEPIYHAIVWQDRRTAswctklksdgHEDTVVERTGLLIDPYFSAT------------KIAWILDN 146
Cdd:cd07781 81 T---SSTVVPVDEDGNPLAPAILWMDHRAQ----------EEAAEINETAHPALEYYLAYyggvyssewmwpKALWLKRN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 147 VEGARARAesgALAFGTVDsWLLWNLTnGK---SHCtdatNASRTALFNIHKQDWDDDLLA-----LFRVPRALLPEVL- 217
Cdd:cd07781 148 APEVYDAA---YTIVEACD-WINARLT-GRwvrSRC----AAGHKWMYNEWGGGPPREFLAaldpgLLKLREKLPGEVVp 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 218 -DSAADYGTAEV-QWLG--APVMIAGIAGDQHAALVGQACFYPG-MAKSTyGT-GCFLMLNTGDKAVRS-----ENRLLT 286
Cdd:cd07781 219 vGEPAGTLTAEAaERLGlpAGIPVAQGGIDAHMGAIGAGVVEPGtLALIM-GTsTCHLMVSPKPVDIPGicgpvPDAVVP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 287 TMayrlngkpcYAVE------GSIFvagaamQWLRDGLKLIAHANESSAHAE--------AVGVDNPVYLvPAFTGLGAP 352
Cdd:cd07781 298 GL---------YGLEagqsavGDIF------AWFVRLFVPPAEERGDSIYALlseeaaklPPGESGLVAL-DWFNGNRTP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 353 HWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQNDGARLESLRVDGGMVV-NDWVMKFLADILNVTVDRPR 431
Cdd:cd07781 362 LVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAEkNPLWMQIYADVLGRPIKVPK 441
|
490 500
....*....|....*....|....
gi 2527343889 432 VTETTALGAAYLAGLQTGIFDNLE 455
Cdd:cd07781 442 SDQAPALGAAILAAVAAGVYADIE 465
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
259-445 |
2.10e-39 |
|
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: 141.31 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 259 AKSTYGTGCFLMLnTGDKAVRSENRLLTTMaYRLNGKPCYAVEGSIFVAGAAMQWLR------------DGLKLIAHANE 326
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPY-TNEMLPGYWGLEGGQSAAGSLLAWLLqfhglreelrdaGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 327 SSAHAEAVGVdnpvYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQND-GARLESLRV 405
Cdd:pfam02782 79 LAAVAPAGGL----LFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQeGHPIDTIHV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2527343889 406 DGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAG 445
Cdd:pfam02782 155 SGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAA 194
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-444 |
8.50e-33 |
|
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: 129.65 E-value: 8.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPK---DGWVEHDAREIWDSTlavcRGALDKAGIDA-SELASIGIT 79
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVSRPTPAPISsddPGRSEQDPEKILEAV----RNLIDELPREYlSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 80 NQRETTVIWDrATGEPIYHAIVWQDRRtaswCTKLKSDGHEDTVVE---RTGLLIDPYFSATKIAWILDNVEgararAES 156
Cdd:cd07777 77 GQMHGIVLWD-EDGNPVSPLITWQDQR----CSEEFLGGLSTYGEEllpKSGMRLKPGYGLATLFWLLRNGP-----LPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 157 GALAFGTVDSWLLWNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGT-AEVQWLGAPV 235
Cdd:cd07777 147 KADRAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTlSSALPKGIPV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 236 MIAgiAGDQhaalvgQACFYPGMAKS------TYGTG---CFLM---LNTGDKAVR--SENRLLTTMAyRLNGkpcyave 301
Cdd:cd07777 227 YVA--LGDN------QASVLGSGLNEendavlNIGTGaqlSFLTpkfELSGSVEIRpfFDGRYLLVAA-SLPG------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 302 gsifvaGAAMQWL----RDGLKLIAHANESS------AHAEAVGVDNPVYLVPAFTGlgaPHWDPHARGAIMGLT-RDTG 370
Cdd:cd07777 291 ------GRALAVLvdflREWLRELGGSLSDDeiweklDELAESEESSDLSVDPTFFG---ERHDPEGRGSITNIGeSNFT 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527343889 371 IGEIVTAGLQSVCYQTKDLVRAIQNDGARLESLRVDGGMVV-NDWVMKFLADILNVTVDRPRVTETTALGAAYLA 444
Cdd:cd07777 362 LGNLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-486 |
1.07e-32 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 130.51 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 1 MTRYLLAIDQGTTSSRAIVFDQTGNSVATDQQEF-HQYFPK-DGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGI 78
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWrHLAVPDvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 79 TNQRETTVIWDRaTGEPIYhAIVWQDRRTASWCTKLKSD--GHEDTVVERTGLLIDpyFSAT-KIAWIldnvegARARAE 155
Cdd:PRK10939 81 TSMREGIVLYDR-NGTEIW-ACANVDARASREVSELKELhnNFEEEVYRCSGQTLA--LGALpRLLWL------AHHRPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 156 --SGALAFGTVDSWLLWNLTNGKShcTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVL-----------DSAAD 222
Cdd:PRK10939 151 iyRQAHTITMISDWIAYMLSGELA--VDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKetgtvlghvtaKAAAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 223 YGTAEvqwlGAPVMIAGiaGDQHAALVGQACFYPGMAKSTYGTGCFLMLNTGDKAVRSEnrllttMAYRLNgkpCYAVEG 302
Cdd:PRK10939 229 TGLRA----GTPVVMGG--GDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPN------MNIRIN---PHVIPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 303 -----SI-FVAGAAMQWLRD----GLKLIAHANESSAHA--EAVGVDNPV--Y-LVPAFTG-LGAPHWdPHARGAIMGLT 366
Cdd:PRK10939 294 mvqaeSIsFFTGLTMRWFRDafcaEEKLLAERLGIDAYSllEEMASRVPVgsHgIIPIFSDvMRFKSW-YHAAPSFINLS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 367 RD---TGIGEIVTAGLQSVCYQTKDLVRAIQN-DGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAY 442
Cdd:PRK10939 373 IDpekCNKATLFRALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAI 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2527343889 443 LAGLQTGIFDNLEQIS-ALWECERQFHPEMR-PALRESLYAGWLDA 486
Cdd:PRK10939 453 AAGVGAGIYSSLAETGeRLVRWERTFEPNPEnHELYQEAKEKWQAV 498
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-459 |
5.27e-32 |
|
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: 128.81 E-value: 5.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITnqre 83
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 84 TT---VIWDRA--------TGEPIYHAIVWQDRRTASWCTKLKSDGHEdtVVERTGLLIDPYFSATKIAWILDNVEGARA 152
Cdd:cd07782 77 ATcslVVLDAEgkpvsvspSGDDERNVILWMDHRAVEEAERINATGHE--VLKYVGGKISPEMEPPKLLWLKENLPETWA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 153 RAesgALAFGTVDsWLLWNLTNG--KSHCTdaTNASRTALFNIHKQD-WDDDLLAL-----------------FRVPRAL 212
Cdd:cd07782 155 KA---GHFFDLPD-FLTWKATGSltRSLCS--LVCKWTYLAHEGSEGgWDDDFFKEigledlvednfakigsvVLPPGEP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 213 LPEVL--DSAADYGTAEvqwlGAPVMIAGIagDQHAALVGqacfypgmakstygtgcflMLNTGDKAVRSEN-RLLTTMA 289
Cdd:cd07782 229 VGGGLtaEAAKELGLPE----GTPVGVSLI--DAHAGGLG-------------------TLGADVGGLPCEAdPLTRRLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 290 YRLNGKPCYAV--EGSIFVAG------AAM---QWLRDG-----LKLIAH-------ANESSAHAEAVGVDNPVYLV--- 343
Cdd:cd07782 284 LICGTSSCHMAvsPEPVFVPGvwgpyySAMlpgLWLNEGgqsatGALLDHiiethpaYPELKEEAKAAGKSIYEYLNerl 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 344 ---------------------PAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVT---AGLQSVCYQTKDLVRAIQNDGAR 399
Cdd:cd07782 364 eqlaeekglplayltrdlhvlPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAAGHK 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 400 LESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISA 459
Cdd:cd07782 444 IDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMA 503
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
6-490 |
1.18e-29 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 121.23 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 6 LAIDQGTTSSRAIVFDQTGNSVATDQQEFHQYFPKDGWVEHDAREIWDSTLAVCRGALDKAGIdaSELASIGITNQRETT 85
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 86 VIWDrATGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVerTGLLIDPYFSATKIAWIldnvegARARAEsgalAFGTVD 165
Cdd:PRK15027 81 TLLD-AQQRVLRPAILWNDGRCAQECALLEARVPQSRVI--TGNLMMPGFTAPKLLWV------QRHEPE----IFRQID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 166 SWLL----WNLTNGKSHCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAADYGT--AEV--QWLGAPVMI 237
Cdd:PRK15027 148 KVLLpkdyLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGAllPEVakAWGMATVPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 238 AGIAGDQHAALVGQACFYPGMAKSTYGT-GCFLMLNTG-----DKAVRSenrllttMAYRLNGKpcYAVEGSIFVAGAAM 311
Cdd:PRK15027 228 VAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHS-------FCHALPQR--WHLMSVMLSAASCL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 312 QW------LRDGLKLIAHANESSAHAEavgvdnPVYLVPAFTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQ 385
Cdd:PRK15027 299 DWaakltgLSNVPALIAAAQQADESAE------PVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 386 TKDLVRAIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVD-RPRVTETTALGAAYLAGLQTGIFDNLEQISALWECE 464
Cdd:PRK15027 373 LADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLE 452
|
490 500
....*....|....*....|....*.
gi 2527343889 465 RQFHPEmrpALRESLYAGWLDAVERV 490
Cdd:PRK15027 453 QSHLPD---AQRYAAYQPRRETFRRL 475
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-457 |
1.33e-22 |
|
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: 100.78 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFD-QTGNSVATDQQEFHQY-FPKDGWVEHDAREIWDSTLAVCRGALDKAGIDASELASIGITN- 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDsSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 81 ------QRETTVIWDRATGEPIYHAIVWQDRRTASWCTKLKSDGHEdTVVERTGLLIDPYFSATKIAWILDNVEGARARA 154
Cdd:cd07768 81 cslaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQ-QLLDYLGGKISPEMGVPKLKYFLDEYSHLRDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 155 ESgalaFGTVDSWLLWNLTNG--KSHCTdatnASRTALFNIHKQDWDD------DLLALFRVPRALLPEVLDSAADYGTA 226
Cdd:cd07768 160 FH----IFDLHDYIAYELTRLyeWNICG----LLGKENLDGEESGWSSsffkniDPRLEHLTTTKNLPSNVPIGTTSGVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 227 EVQWLGAPVMIAGIAG-----DQHAAlvgqacfYPGMAKSTYGTGCFLMLNTGdkavrSENRLLTTMAYRLNG------- 294
Cdd:cd07768 232 LPEMAEKMGLHPGTAVvvsciDAHAS-------WFAVASPHLETSLFMIAGTS-----SCHMYGTTISDRIPGvwgpfdt 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 295 --KPCYAV-EGSIFVAGAAMQWL--------------RDGLKLIAHANES-SAHAEAVGVDNPVYLVPAFTGLGAPHWDP 356
Cdd:cd07768 300 iiDPDYSVyEAGQSATGKLIEHLfeshpcarkfdealKKGADIYQVLEQTiRQIEKNNGLSIHILTLDMFFGNRSEFADP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 357 HARGAIMGLTRDTGI---GEIVTAGLQSVCYQTKDLVRAIQNDGARLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVT 433
Cdd:cd07768 380 RLKGSFIGESLDTSMlnlTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKEN 459
|
490 500
....*....|....*....|....
gi 2527343889 434 ETTALGAAYLAGLQTGIFDNLEQI 457
Cdd:cd07768 460 MMGILGAAVLAKVAAGKKQLADSI 483
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
4-479 |
3.14e-21 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 96.25 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVA-------TDQQE----FHQyfpkdgWvehDAREIWDSTLAVCRGALdkAGIDASE 72
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVArastpnaSDIAAensdWHQ------W---SLDAILQRFADCCRQIN--SELTECH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 73 LASIGITNQRETTVIWDRAtGEPIYHAIVWQDRRTAswctklksdghedTVVERtgllIDPYFSATKIawildnvegaRA 152
Cdd:PRK10331 72 IRGITVTTFGVDGALVDKQ-GNLLYPIISWKCPRTA-------------AVMEN----IERYISAQQL----------QQ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 153 RAESGALAFGTVDSwLLWNLTN-----GKSHC-----------------TDATNASRTALFNIHKQDWDDDLLALFRVPR 210
Cdd:PRK10331 124 ISGVGAFSFNTLYK-LVWLKENhpqllEQAHAwlfisslinhrltgeftTDITMAGTSQMLDIQQRDFSPEILQATGLSR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 211 ALLPEVLDSAADYGT---AEVQWLGAPVMIAGI-AG-DQHAALVGQACFYPGMAKSTyGTGCFLMLNTG--DKAVRSENR 283
Cdd:PRK10331 203 RLFPRLVEAGEQIGTlqpSAAALLGLPVGIPVIsAGhDTQFALFGSGAGQNQPVLSS-GTWEILMVRSAqvDTSLLSQYA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 284 LLTTmayRLNGKPCYAVEGSIFVAGAAMQWLRdglKLIAHANE------SSAHAEAVGVDNpVYLVPAFTGLGaphwdph 357
Cdd:PRK10331 282 GSTC---ELDSQSGLYNPGMQWLASGVLEWVR---KLFWTAETpyqtmiEEARAIPPGADG-VKMQCDLLACQ------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 358 aRGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQNDGA-RLESLRVDGGMVVNDWVMKFLADILNVTVDRPRVTETT 436
Cdd:PRK10331 348 -NAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETT 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2527343889 437 ALGAAYLAGLQTGIFDNLEQISALWECE-RQFHPEMRPALRESL 479
Cdd:PRK10331 427 VAGAAMFGWYGVGEFSSPEQARAQMKYQyRYFYPQTEPEFIEEV 470
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
4-460 |
4.21e-17 |
|
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: 83.35 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIV--FDqtGNSVATdqQEFHQyFP-----KDG---WvehDAREIWDSTLAvcrgALDKAGIDASEL 73
Cdd:cd07771 1 NYLAVDLGASSGRVILgsLD--GGKLEL--EEIHR-FPnrpveINGhlyW---DIDRLFDEIKE----GLKKAAEQGGDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 74 ASIGITnqretT-----VIWDRAtGEPIYHAIVWQDRRTASWCTKLKSDGHEDTVVERTGLLIDPYFSATKIAwildnve 148
Cdd:cd07771 69 DSIGID-----TwgvdfGLLDKN-GELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLY------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 149 garARAESGALAFGTVDSWLL------WNLTNGKshCTDATNASRTALFNIHKQDWDDDLLALFRVPRALLPEVLDSAAD 222
Cdd:cd07771 136 ---ALKKEGPELLERADKLLMlpdllnYLLTGEK--VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 223 YGT------AEVQWLGAPVmiagIAGDQH---AALVGqacfYPGMAKSTY----GT----GCFLmlntgDKAVRSENrll 285
Cdd:cd07771 211 LGTlkpevaEELGLKGIPV----IAVASHdtaSAVAA----VPAEDEDAAfissGTwsliGVEL-----DEPVITEE--- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 286 ttmAYRLNgkpcYAVEGSIF--------VAGaaM--------QWLRDGLK-----LIAHANESSAHAEAVGVDNPVYLVP 344
Cdd:cd07771 275 ---AFEAG----FTNEGGADgtirllknITG--LwllqecrrEWEEEGKDysydeLVALAEEAPPFGAFIDPDDPRFLNP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 345 AftglgaphwdpHARGAIMGLTRDTG------IGEIVTAGLQSVCYQTKDLVRAIQN-DGARLESLRVDGGMVVNDWVMK 417
Cdd:cd07771 346 G-----------DMPEAIRAYCRETGqpvpesPGEIARCIYESLALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQ 414
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2527343889 418 FLADILNVTVdrprVT---ETTALG--AAYLAGLqtGIFDNLEQISAL 460
Cdd:cd07771 415 LTADATGLPV----IAgpvEATAIGnlLVQLIAL--GEIKSLEEGREL 456
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
4-444 |
2.35e-07 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 53.33 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 4 YLLAIDQGTTSSRAIVFDQTGNSVATDQ----QEFHQYFPKDGWVEH-DAREI------WDSTLAVCRGALDKAGIDASE 72
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESvnfdSDLPEYGTKGGVHRDgDGGEVtspvlmWVEALDLLLEKLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 73 LASIGITNQRETTVIW-------------DRATGEPIYHAI------VWQDRRTASWCTKL-KSDGHEDTVVERTGllID 132
Cdd:cd07776 81 VKAISGSGQQHGSVYWskgaesalanldpSKSLAEQLEGAFsvpdspIWMDSSTTKQCRELeKAVGGPEALAKLTG--SR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 133 PY--FSATKIAWILDNVEGARARAESGALA--FGTvdSWLLwnltnGKSHCTDATNASRTALFNIHKQDWDDDLLALFRV 208
Cdd:cd07776 159 AYerFTGPQIAKIAQTDPEAYENTERISLVssFLA--SLLL-----GRYAPIDESDGSGMNLMDIRSRKWSPELLDAATA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 209 P--RALLPEVLDSAADYGTAE----VQWLGAP-VMIAGIAGDQHAALVGQACFYPGMAKStygtgcflmLNTGDkavrse 281
Cdd:cd07776 232 PdlKEKLGELVPSSTVAGGISsyfvERYGFSPdCLVVAFTGDNPASLAGLGLEPGDVAVS---------LGTSD------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 282 nrllTTMAYRLNGKPcyAVEGSIFV----AGAAM------------QWLRDglkliAHANES------SAHAEAVGVDNP 339
Cdd:cd07776 297 ----TVFLVLDEPKP--GPEGHVFAnpvdPGSYMamlcykngslarERVRD-----RYAGGSwekfneLLESTPPGNNGN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 340 VYL-------VPafTGLGAPHWDPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQndgarLESLRVDGGMVVN 412
Cdd:cd07776 366 LGLyfdepeiTP--PVPGGGRRFFGDDGVDAFFDPAVEVRAVVESQFLSMRLHAERLGSDIP-----PTRILATGGASAN 438
|
490 500 510
....*....|....*....|....*....|..
gi 2527343889 413 DWVMKFLADILNVTVDRPRVTETTALGAAYLA 444
Cdd:cd07776 439 KAILQVLADVFGAPVYTLDVANSAALGAALRA 470
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-481 |
2.50e-07 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 53.31 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 1 MTRYLLAIDQGTTSSRAIVFD-QTGNSVATDQQEF-H----QYFP-KDGWVEHDAREIWDSTLAVCRGALDKAGIDASEL 73
Cdd:PRK04123 1 MMAYVIGLDFGTDSVRALLVDcATGEELATAVVEYpHwvkgRYLDlPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 74 ASIGI--TNqreTTVIWDRATGEPIY---------HAIV--WQDRRT---ASWCTKLKSDGHEDTVVERTGLLIDPYFSA 137
Cdd:PRK04123 81 VGIGVdfTG---STPAPVDADGTPLAllpefaenpHAMVklWKDHTAqeeAEEINRLAHERGEADLSRYIGGIYSSEWFW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 138 TKIAWILDNVEGARARAESgalAFGTVDsWLLWNLTNGkshcTDATNASRTALFNIHKQDWD---------------DDL 202
Cdd:PRK04123 158 AKILHVLREDPAVYEAAAS---WVEACD-WVVALLTGT----TDPQDIVRSRCAAGHKALWHeswgglpsadffdalDPL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 203 LALF---RVPRALLPevLDSAADYGTAEV-QWLGAP--VMIAGIAGDQHAALVGQACfYPG-----MAKSTygtgCFLML 271
Cdd:PRK04123 230 LARGlrdKLFTETWT--AGEPAGTLTAEWaQRLGLPegVAVSVGAFDAHMGAVGAGA-EPGtlvkvMGTST----CDILL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 272 NTGDKAVRSenrllttMayrlngkpCYAVEGSI---FVAGAAMQ--------WLRDglkliaHANESSAHAEAVGVDNPV 340
Cdd:PRK04123 303 ADKQRAVPG-------I--------CGQVDGSIvpgLIGYEAGQsavgdifaWFAR------LLVPPEYKDEAEARGKQL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 341 Y---------LVPAFTGLGAPHW---------DPHARGAIMGLTRDTGIGEIVTAGLQSVCYQTKDLVRAIQNDGARLES 402
Cdd:PRK04123 362 LellteaaakQPPGEHGLVALDWfngrrtplaDQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQGVPVEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 403 LRVDGGMVV-NDWVMKFLADILNVTVDRPRVTETTALGAAYLAGLQTGIFDNLEQISALWEC--ERQFHPE-MRPALRES 478
Cdd:PRK04123 442 VIAAGGIARkNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASpvEKTYQPDpENVARYEQ 521
|
...
gi 2527343889 479 LYA 481
Cdd:PRK04123 522 LYQ 524
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
32-247 |
1.01e-04 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 44.71 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 32 QEFHQYfpKDGWVEHDAREIWD--STLAVCRGALDKAGIDASELASIGITNQRETTVIWDRaTGEPIYHAIVWQDRRTAS 109
Cdd:PRK10640 15 REIHRF--NNGLHSQDGFDTWDvdSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDYVLLDK-QGQRVGLPVSYRDSRTDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 110 WCTKLKSDGHEDTVVERTGLLIDPYFSATKIawildnvegaRARAESGALAFGTVDSWLL------WNLTnGKSHCtDAT 183
Cdd:PRK10640 92 VMAQAQQQLGKRDIYRRSGIQFLPFNTLYQL----------RALTEQQPELIAQVAHALLipdyfsYRLT-GKMNW-EYT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527343889 184 NASRTALFNIHKQDWDDDLLALFRVPRAllpevldsaadygtaevqWLGAPVMIAGIAGDQHAA 247
Cdd:PRK10640 160 NATTTQLVNINSDDWDESLLAWSGAPKA------------------WFGRPTHPGNVIGHWICP 205
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-54 |
1.32e-03 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. 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: 466797 [Multi-domain] Cd Length: 544 Bit Score: 41.24 E-value: 1.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2527343889 5 LLAIDQGTTSSRAIVFDQTGNSVATDQQEFH-QYFPKDGW-VEHDAREIWDS 54
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWfVTQSSTEIWKA 53
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
352-444 |
3.66e-03 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. 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: 466797 [Multi-domain] Cd Length: 544 Bit Score: 39.69 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527343889 352 PHWDPHARGAIMGLTRDTGIGEIVT---AGLQSVCYQTKDLVRAIQNDGARLESLRVDGGMVVNDWVMKFLADILN---V 425
Cdd:cd07778 392 PYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSkihI 471
|
90
....*....|....*....
gi 2527343889 426 TVDRPRVTETTALGAAYLA 444
Cdd:cd07778 472 IVPLSDSKYAVVKGAALLG 490
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-78 |
7.07e-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: 38.34 E-value: 7.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527343889 1 MTRYLLAIDQGTTSSRAIVFDQTGNSVATDQQEFHQyfpkdgwvEHDAREIWDSTLAVCRGALDKAGIDASELASIGI 78
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPA--------GAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| |
