|
Name |
Accession |
Description |
Interval |
E-value |
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-491 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 875.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 1 MSKYILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIAN 80
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 81 QRETTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAGELA 160
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 161 FGTVDSYLLWQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGGEIPICGI 240
Cdd:COG0554 161 FGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGAEIPIAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 241 AGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRLNGKPTYAIEGSIFMAGATMQWIVEGLKL 320
Cdd:COG0554 241 AGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 321 LENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGD-GLR 399
Cdd:COG0554 321 IDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADsGIP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 400 PSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASMWKSDRRFEPTMSSEERNDL 479
Cdd:COG0554 401 LKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERL 480
|
490
....*....|..
gi 1222443642 480 YAKWLHCIAQVR 491
Cdd:COG0554 481 YAGWKKAVERTL 492
|
|
| 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: 862.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAGELAFGT 163
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 164 VDSYLLWQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGGEIPICGIAGD 243
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLGAEIPIAGIAGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 244 QQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRLNGKPTYAIEGSIFMAGATMQWIVEGLKLLEN 323
Cdd:cd07786 241 QQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 324 AGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGD-GLRPSI 402
Cdd:cd07786 321 AAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADsGIPLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 403 LRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASMWKSDRRFEPTMSSEERNDLYAK 482
Cdd:cd07786 401 LRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYAG 480
|
....*.
gi 1222443642 483 WLHCIA 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), ... |
4-483 |
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: 799.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAGELAFGT 163
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 164 VDSYLLWQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGGEIPICGIAGD 243
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLGAGIPIAGILGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 244 QQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRLNGKPTYAIEGSIFMAGATMQWIVEGLKLLEN 323
Cdd:cd07769 241 QQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 324 AGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGD-GLRPSI 402
Cdd:cd07769 321 AAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDsGIKLKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 403 LRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASMWKSDRRFEPTMSSEERNDLYAK 482
Cdd:cd07769 401 LRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYRG 480
|
.
gi 1222443642 483 W 483
Cdd:cd07769 481 W 481
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-483 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 782.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 1 MSKYILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIAN 80
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 81 QRETTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAGELA 160
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 161 FGTVDSYLLWQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVT-ASELFGGEIPICG 239
Cdd:PRK00047 163 FGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTnPYGFFGGEVPIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 240 IAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRLNGKPTYAIEGSIFMAGATMQWIVEGLK 319
Cdd:PRK00047 243 IAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 320 LLENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGD-GL 398
Cdd:PRK00047 323 IISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADsGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 399 RPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASMWKSDRRFEPTMSSEERND 478
Cdd:PRK00047 403 RLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREK 482
|
....*
gi 1222443642 479 LYAKW 483
Cdd:PRK00047 483 LYAGW 487
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
3-483 |
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: 733.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 3 KYILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQR 82
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 83 ETTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAGELAFG 162
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 163 TVDSYLLWQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGGEIPICGIAG 242
Cdd:TIGR01311 161 TIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLGAEIPITGVLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 243 DQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRLNGK-PTYAIEGSIFMAGATMQWIVEGLKLL 321
Cdd:TIGR01311 241 DQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKkPVYALEGSVFVAGAAVQWLRDNLKLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 322 ENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGD-GLRP 400
Cdd:TIGR01311 321 KHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDaGVEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 401 SILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASMWKSDRRFEPTMSSEERNDLY 480
Cdd:TIGR01311 401 TKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREARY 480
|
...
gi 1222443642 481 AKW 483
Cdd:TIGR01311 481 AGW 483
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
3-483 |
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: 584.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 3 KYILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGI---A 79
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAigiT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 80 NQRETTLVWNKKTGQPIYNAIVWQDRRTSDYCDNL--RHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAG 157
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELsaKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 158 ELAFGTVDSYLLWQLTDGK---VHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGGe 234
Cdd:cd07792 161 RLLFGTVDSWLIWNLTGGKnggVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 235 IPICGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRL--NGKPTYAIEGSIFMAGATMQ 312
Cdd:cd07792 240 VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLgpDAPPVYALEGSIAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 313 WIVEGLKLLENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKA 392
Cdd:cd07792 320 WLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 393 MEGD-GLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASM-WKSDRRFEPT 470
Cdd:cd07792 400 MNKDsGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLnEGGRTVFEPQ 479
|
490
....*....|...
gi 1222443642 471 MSSEERNDLYAKW 483
Cdd:cd07792 480 ISEEERERRYKRW 492
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-483 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 550.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 3 KYILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVL--SQQQVTAADIIAIGIAN 80
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIkkLREKGPSFKIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 81 QRETTLVWNKKTGQPIYNAIVWQDRRTSDYCDNL-RHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAGEL 159
Cdd:PTZ00294 82 QRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELtKKYGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 160 AFGTVDSYLLWQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGG--EIPI 237
Cdd:PTZ00294 162 LFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPLleGVPI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 238 CGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRL--NGKPTYAIEGSIFMAGATMQWIV 315
Cdd:PTZ00294 242 TGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLgpNGPTVYALEGSIAVAGAGVEWLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 316 EGLKLLENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEG 395
Cdd:PTZ00294 322 DNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 396 D-GLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASMWK-SDRRFEPTMSS 473
Cdd:PTZ00294 402 DaGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRrSNSTFSPQMSA 481
|
490
....*....|
gi 1222443642 474 EERNDLYAKW 483
Cdd:PTZ00294 482 EERKAIYKEW 491
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
4-483 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 520.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGI----A 79
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDSGLKaigiT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 80 NQRETTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRH---AGHTQMVnDKTGLVLDPYFSATKIRWILDNVKGAKEQAHA 156
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKelsGGRKHFV-ETCGLPISTYFSATKLLWLLENVDAVKEAVKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 157 GELAFGTVDSYLLWQLTDGK---VHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGG 233
Cdd:PLN02295 160 GDALFGTIDSWLIWNLTGGAsggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 234 EIPICGIAGDQQAALIGQACfEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRLNGKPT--YAIEGSIFMAGATM 311
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPtnYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 312 QWIVEGLKLLENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQK 391
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 392 AMEGD------GLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLAS-MWKSD 464
Cdd:PLN02295 399 AMRKDageeksHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASeKWKNT 478
|
490
....*....|....*....
gi 1222443642 465 RRFEPTMSSEERNDLYAKW 483
Cdd:PLN02295 479 TTFRPKLDEEERAKRYASW 497
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-483 |
8.83e-170 |
|
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: 488.22 E-value: 8.83e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVND--------------KTGLVL--DPYFSATKIRWILDNV 147
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRGgskflhfltrnkrfLAASVLkfSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 148 KGAKEQAHAGELAFGTVDSYLLWQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTA 227
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 228 SELFGGEIPICGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTLAYRLNGKPTYAIEGSIFMA 307
Cdd:cd07793 241 PSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASDT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 308 GATMQWIVEGLkLLENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTK 387
Cdd:cd07793 321 GTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 388 DLQKAMEGD-GLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASMWKSDRR 466
Cdd:cd07793 400 QLLETMEKEtSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKI 479
|
490
....*....|....*..
gi 1222443642 467 FEPTMSSEERNDLYAKW 483
Cdd:cd07793 480 FEPKMDNEKREELYKNW 496
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-491 |
1.39e-99 |
|
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: 308.30 E-value: 1.39e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 3 KYILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQR 82
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 83 ETTLVWNKKtGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAgelaFG 162
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK----VL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 163 TVDSYLLWQLTDGKVhkTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVT---ASELFG--GEIPI 237
Cdd:COG1070 156 LPKDYLRYRLTGEFV--TDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLtaeAAAETGlpAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 238 CGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTgDKALKSNNRLLTTLAYRLNGkpTYAIEGSIFMAGATMQWIVE- 316
Cdd:COG1070 234 VAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPG--RWLPMGATNNGGSALRWFRDl 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 317 -GLKLLENAGESEALVKDVPLD-HGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAME 394
Cdd:COG1070 311 fADGELDDYEELNALAAEVPPGaDGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 395 GDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQ-LASMWKSDRRFEPTMSS 473
Cdd:COG1070 391 EAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEaAAAMVRVGETIEPDPEN 470
|
490
....*....|....*....
gi 1222443642 474 EER-NDLYAKWLHCIAQVR 491
Cdd:COG1070 471 VAAyDELYERYRELYPALK 489
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-480 |
1.23e-91 |
|
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: 285.95 E-value: 1.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TT-LVwnKKTGQPIYNAIVWQDRRTSDYCdnlrhaghtqmvndktglvldpyfsatkirwildnvkgakeqahagelafg 162
Cdd:cd07779 81 TFvPV--DEDGRPLRPAISWQDKRTAKFL--------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 163 TVDSYLLWQLTDGKVhkTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFG-VT--ASELFG--GEIPI 237
Cdd:cd07779 108 TVQDYLLYRLTGEFV--TDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGtLTkeAAEETGlpEGTPV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 238 CGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTgDKALKSNNRLLTTLAYRLNGKptYAIEGSIFMAGATMQWIVEG 317
Cdd:cd07779 186 VAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAVPGK--WVLEGSINTGGSAVRWFRDE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 318 LKLLENAGES---------EALVKDVPLD-HGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTK 387
Cdd:cd07779 263 FGQDEVAEKElgvspyellNEEAAKSPPGsDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 388 DLQKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLA-SMWKSDRR 466
Cdd:cd07779 343 DNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVkAMVRVTDT 422
|
490
....*....|....
gi 1222443642 467 FEPtmsSEERNDLY 480
Cdd:cd07779 423 FEP---DPENVAIY 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-444 |
1.80e-83 |
|
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: 263.66 E-value: 1.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKtGQPIYNAIVWQDRRtsdycdnlrhaghtqmvndktglvldpyfsatkirwildnvkgAKeqahagelaFGT 163
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIWLDRR-------------------------------------------AK---------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 164 VDSYLLWQLTDgkVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFG-VT--ASELFGGE--IPIC 238
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGrVTpeAAEETGLPagTPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 239 GIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKalKSNNRLLTTLAYRLNGKptYAIEGSIFMAGATMQWIV--- 315
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEP--VPPDPRLLNRCHVVPGL--WLLEGAINTGGASLRWFRdef 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 316 --EGLKLLENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAM 393
Cdd:cd00366 262 geEEDSDAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1222443642 394 EGDGLRPSILRVDGGMANNN-WaMAFLANILGASVERPTLTETTSLGVAYLA 444
Cdd:cd00366 342 EELGVKIKEIRVTGGGAKSRlW-NQIKADVLGVPVVVPEVAEGAALGAAILA 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 |
2.54e-81 |
|
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: 259.44 E-value: 2.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQ--------VTAadiia 75
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGpdpiaaisVSS----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 76 igianQRET-TLVwnKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQA 154
Cdd:cd07773 76 -----QGESgVPV--DRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 155 HAgelaFGTVDSYLLWQLTDGKVhkTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASEL---- 230
Cdd:cd07773 149 AK----WLSVADYIAYRLTGEPV--TDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAaeel 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 231 -FGGEIPICgIAG-DQQAALIGQACFEEGMAksTYGTG---CFLML-NTGDKALKSNNRLLTTLAYRLNGKptYAIEGSI 304
Cdd:cd07773 223 gLPAGTPVV-VGGhDHLCAALGAGVIEPGDV--LDSTGtaeALLAVvDEPPLDEMLAEGGLSYGHHVPGGY--YYLAGSL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 305 FmAGATMQWIVE--GLKLLENAGESEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSV 382
Cdd:cd07773 298 P-GGALLEWFRDlfGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGL 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443642 383 GYQTKDLQKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTG 449
Cdd:cd07773 377 AFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-250 |
4.66e-79 |
|
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: 246.87 E-value: 4.66e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKTgQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHagelAFGT 163
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 164 VDSYLLWQLTDgkVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGG-----EIPIC 238
Cdd:pfam00370 156 IHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMwgldeGVPVV 233
|
250
....*....|..
gi 1222443642 239 GIAGDQQAALIG 250
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-483 |
2.75e-74 |
|
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: 242.44 E-value: 2.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKtGQPIYNAIVWQDRRTSDYCDNLRhAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHagelafgT 163
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELE-ARLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIR-------K 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 164 V----DsYLLWQLTdGKVHkTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVT---ASELFG--GE 234
Cdd:cd07808 152 IllpkD-YLRYRLT-GELA-TDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLtpeAAEELGlpEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 235 IPICGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRlLTTLAYRLNGKpTYAIeGSIFMAGATMQWI 314
Cdd:cd07808 229 TPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGR-LHTFPHAVPGK-WYAM-GVTLSAGLSLRWL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 315 VEGLKLLENAGES-EALVKDVPLDHG--VFLvPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQK 391
Cdd:cd07808 306 RDLFGPDRESFDElDAEAAKVPPGSEglLFL-PYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 392 AMEGDGLRPSILRVDGGMANNN-WaMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYESTAQLASMW-KSDRRFEP 469
Cdd:cd07808 385 VLKELGIKVKEIRLIGGGAKSPlW-RQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACiKIEKTIEP 463
|
490
....*....|....*
gi 1222443642 470 TMSSEER-NDLYAKW 483
Cdd:cd07808 464 DPERHEAyDELYARY 478
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
4-484 |
2.53e-70 |
|
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: 232.03 E-value: 2.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKtGQPIYNAIVWQDRRTSDYCDNL-RHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAgelAFG 162
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIaGGLGGIEGYRLGGGNPPSGKDPLAKILWLKENEPEIYAKTHK---FLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 163 TVDsYLLWQLTDGKVhkTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFG-VT--ASELFG--GEIPI 237
Cdd:cd07805 157 AKD-YLNFRLTGRAA--TDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGeLTpeAAAELGlpAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 238 CGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRlLTTLAYRLNGKptYAIEGSIFMAGATMQWIVEG 317
Cdd:cd07805 234 VGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHG-IFTLASADPGR--YLLAAEQETAGGALEWARDN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 318 LKLLENAGES-----EALVKDV-PLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQK 391
Cdd:cd07805 311 LGGDEDLGADdyellDELAAEApPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 392 AMEGDGLRPSILRVDGGMANNN-WaMAFLANILGASVERPT-LTETTSLGVAYLAGLQTGVYESTAQLASMWKSDRRFEP 469
Cdd:cd07805 391 ALEKLTRKIDELRLVGGGARSDlW-CQILADVLGRPVEVPEnPQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEP 469
|
490
....*....|....*.
gi 1222443642 470 TMSSEER-NDLYAKWL 484
Cdd:cd07805 470 DPENRARyDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-485 |
2.09e-68 |
|
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: 227.05 E-value: 2.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQqqvtaadiiaigIANQRE 83
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAK------------LGGGEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVW----------NKKtGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQ 153
Cdd:cd07770 69 DAIGFssamhsllgvDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 154 AHAgelaFGTVDSYLLWQLTdGKvHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGV---TASEL 230
Cdd:cd07770 148 AAK----FVSIKEYLLYRLT-GE-LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGlkpEFAER 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 231 FGGEIPICGI--AGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTtlaYRLNGKpTYAIEGSIFMAG 308
Cdd:cd07770 222 LGLLAGTPVVlgASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWC---YRLDEN-RWLVGGAINNGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 309 ATMQWIVEGLKLLENAGES-EALVKDVPLD-HGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQT 386
Cdd:cd07770 298 NVLDWLRDTLLLSGDDYEElDKLAEAVPPGsHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 387 KDLQKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYEStAQLASMWKSDRR 466
Cdd:cd07770 378 KSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISS-LEADELVKIGKV 456
|
490
....*....|....*....
gi 1222443642 467 FEPtmsSEERNDLYAKWLH 485
Cdd:cd07770 457 VEP---DPENHAIYAELYE 472
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-449 |
7.02e-60 |
|
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: 203.53 E-value: 7.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVtaadiiaigiaNQRE 83
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGI-----------SPKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 ----------TTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQ 153
Cdd:cd07804 70 iaaigvsglvPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 154 AHagelAFGTVDSYLLWQLTdGKVHkTDATNASRT-LLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFG-VT--ASE 229
Cdd:cd07804 150 TR----KFLGAYDYIVYKLT-GEYV-IDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGeVTkeAAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 230 LFG---GeIPICGIAGDQQAALIGQACFEEGMAKSTYGT-GCFLMLNTGDKALKsnnrlltTLAYRLNGKP-TYAIEGSI 304
Cdd:cd07804 224 ETGlaeG-TPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVVTDKLPTDP-------RLWLDYHDIPgTYVLNGGM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 305 FMAGATMQWIVEGLKLLENAGES----------EALVKDVPL--DhGVFLVPSFTGLGAPYWDANARGAILGLTRDSGIS 372
Cdd:cd07804 296 ATSGSLLRWFRDEFAGEEVEAEKsggdsaydllDEEAEKIPPgsD-GLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRA 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443642 373 TIVAAALQSVGYQTKDLQKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTG 449
Cdd:cd07804 375 HLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
4-445 |
1.05e-43 |
|
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: 159.70 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQqqvtaadiiaiGIANQRE 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAE-----------LRPRRVV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 ---------TTLVWNKKtGQPIYNAIVWQDRRTSDYCDNLRHAGHTqmVNDKTGLVLDPYFSATKIRWILDNVKGAKEQA 154
Cdd:cd07783 70 aiavdgtsgTLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAGA--VAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 155 ----HAGElafgtvdsYLLWQLTDGKVHkTDATNASRTlLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVT---A 227
Cdd:cd07783 147 akflHQAD--------WLAGRLTGDRGV-TDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLtaeA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 228 SELFG--GEIPICGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTgDKALKSNNRLLTTlaYRLnGKPTYAIEGSIF 305
Cdd:cd07783 217 AEELGlpAGTPVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLS-DKRVPDPGGGVYS--HRH-GDGYWLVGGASN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 306 MAGATMQWIVEG--LKLLenagESEAlvkDVPLDHGVFLVP-SFTGLGAPYWDANARGAILGLTRDSGIstIVAAALQSV 382
Cdd:cd07783 293 TGGAVLRWFFSDdeLAEL----SAQA---DPPGPSGLIYYPlPLRGERFPFWDPDARGFLLPRPHDRAE--FLRALLEGI 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222443642 383 GYQTKDLQKAMEGDGLRP--SILRVDGGMANNNWaMAFLANILGASVERPtLTETTSLGVAYLAG 445
Cdd:cd07783 364 AFIERLGYERLEELGAPPveEVRTAGGGARNDLW-NQIRADVLGVPVVIA-EEEEAALGAALLAA 426
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-449 |
3.97e-43 |
|
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: 158.48 E-value: 3.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKtGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAgelAFGT 163
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRT---VLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 164 VDsYLLWQLTdGKVHkTDATNASrTLLFNIHQQCWDEELLALFNIPA--SMLPEVMDSAADFG-VT--ASELFG---GeI 235
Cdd:cd07802 157 KD-WIRYRLT-GEIS-TDYTDAG-SSLLDLDTGEYDDELLDLLGIEElkDKLPPLVPSTEIAGrVTaeAAALTGlpeG-T 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 236 PICGIAGDQQAALIGQACFEEGMAKSTYGTGCflmLNTG-DKALKSNNRLLTTLAYRLNGKpTYAIEGSifMAGA-TMQW 313
Cdd:cd07802 232 PVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvTDEPVVPDSVGSNSLHADPGL-YLIVEAS--PTSAsNLDW 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 314 IVEGLKLLENAGES------EALVKDVPLD-HGVFLVPSFTGLGApywDANARGAILGLTRDSGISTIVAAALQSVGYQT 386
Cdd:cd07802 306 FLDTLLGEEKEAGGsdydelDELIAAVPPGsSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSH 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222443642 387 KDLQKAMeGDGLRPSILRVDGGMANNN-WAMAFlANILGASVERPTLTETTSLGVAYLAGLQTG 449
Cdd:cd07802 383 RDHLERL-LVARKPETIRLTGGGARSPvWAQIF-ADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-445 |
1.79e-34 |
|
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: 134.60 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILY-TKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQR 82
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIdAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 83 ETtLVWNKKTGQPIYNAIVWQDRRTSDYCDNL-RHAGHTQMVndKTGLVLDPYFSATKIRWILDNvkgakEQAHAGELAF 161
Cdd:cd07809 81 HG-LVALDADGKVLRPAKLWCDTRTAPEAEELtEALGGKKCL--LVGLNIPARFTASKLLWLKEN-----EPEHYARIAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 162 GTVDS-YLLWQLTDGKVhkTDATNASRTLLFNIHQQCWDEELLALFN---IPASMLPEVMDSAADFGV---TASELFG-- 232
Cdd:cd07809 153 ILLPHdYLNWKLTGEKV--TGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVLPAGEVAGRltpEGAEELGlp 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 233 GEIPICGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTgDKALKSNNRLLTTLAyrlngKPTYAIEGSIFMAGATMQ 312
Cdd:cd07809 231 AGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVS-DKPVSDPHGRVATFC-----DSTGGMLPLINTTNCLTA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 313 WIVEGLKLLE-NAGESEALVKDVPLD-HGVFLVPSFTGLGAPYWdANARGAILGLT-RDSGISTIVAAALQSVGYQTKDL 389
Cdd:cd07809 305 WTELFRELLGvSYEELDELAAQAPPGaGGLLLLPFLNGERTPNL-PHGRASLVGLTlSNFTRANLARAALEGATFGLRYG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443642 390 QKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAG 445
Cdd:cd07809 384 LDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAA 439
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
259-445 |
1.42e-31 |
|
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: 120.12 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 259 AKSTYGTGCFLMLNTGDKalKSNNRLLTTLAYRLNGKPTYAIEGSIFMAGATMQWIVEGLKLLENAGES-------EALV 331
Cdd:pfam02782 1 LAISAGTSSFVLVETPEP--VLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAgnveslaELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 332 KDVPLDHG-VFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGD-GLRPSILRVDGGM 409
Cdd:pfam02782 79 LAAVAPAGgLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQeGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1222443642 410 ANNNWAMAFLANILGASVERPTLTETTSLGVAYLAG 445
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAA 194
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
4-449 |
1.66e-31 |
|
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: 126.20 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TT-LVwnKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAgelAFG 162
Cdd:cd24121 81 GTwLV--DEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERART---ALH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 163 TVDsYLLWQLTdGKVhKTDATNASRTlLFNIHQQCWDEELLALFNIPA--SMLPEVMDS---AADFGVTASELFG--GEI 235
Cdd:cd24121 156 CKD-WLFYKLT-GEI-ATDPSDASLT-FLDFRTRQYDDEVLDLLGLEElrHLLPPIRPGtevIGPLTPEAAAATGlpAGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 236 PICGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTgDKAlksnnrllttlayRLNGKPT-----YAIEGSIFMAGAT 310
Cdd:cd24121 232 PVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVV-DEP-------------DLEPEGVgyticLGVPGRWLRAMAN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 311 M------QWIVEGLKLLENAGES----------EALVKDVPL-DHGVFLVP--SFTGLGAPYWDANARGAILGLTRDSGI 371
Cdd:cd24121 298 MagtpnlDWFLRELGEVLKEGAEpagsdlfqdlEELAASSPPgAEGVLYHPylSPAGERAPFVNPNARAQFTGLSLEHTR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443642 372 STIVAAALQSVGYQTKDLQKAMegdGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTG 449
Cdd:cd24121 378 ADLLRAVYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-449 |
2.78e-31 |
|
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: 125.41 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKN--GWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQ 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDypDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 82 RETTlVWNKKTGQPIY---NaivwQDRRTSDYCDNLRHAgHTQMVNDKTGLVLDPYFSATKIRWILDNVKGAKEQAHAge 158
Cdd:cd07798 81 REGI-VFLDKDGRELYagpN----IDARGVEEAAEIDDE-FGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIAT-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 159 laFGTVDSYLLWQLTdGKVHkTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGV----TASEL-FGG 233
Cdd:cd07798 153 --VLSISDWIGYRLT-GELV-SEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTvseeAARELgLPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 234 EIP-ICGiAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLLTTlAYRLNGKptYAIEGSIFMAGATMQ 312
Cdd:cd07798 229 GTPvVVG-GADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTG-CHLVPGK--WVLESNAGVTGLNYQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 313 WIVEglKLLENAGES----EALVKDVPLdhGVFLVPSFTGLGAPYWDANA--RGAIL----GLTRDSGISTIVAAALQSV 382
Cdd:cd07798 305 WLKE--LLYGDPEDSyevlEEEASEIPP--GANGVLAFLGPQIFDARLSGlkNGGFLfptpLSASELTRGDFARAILENI 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443642 383 GYQTK-DLQKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTG 449
Cdd:cd07798 381 AFAIRaNLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-444 |
1.68e-26 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 111.54 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTS---------SRAILYTKDAEVFDTAQQTFPQHFvkngwvEHDPVDIWQTVLSSVKNVLSQqqvtaadii 74
Cdd:cd07777 1 NVLGIDIGTTSikaalldleSGRILESVSRPTPAPISSDDPGRS------EQDPEKILEAVRNLIDELPRE--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 75 aigiANQRETTL---------VWNKKTGQPIYNAIVWQDRRTS-DYCDNLRHAGHTQMvnDKTGLVLDPYFSATKIRWIL 144
Cdd:cd07777 66 ----YLSDVTGIgitgqmhgiVLWDEDGNPVSPLITWQDQRCSeEFLGGLSTYGEELL--PKSGMRLKPGYGLATLFWLL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 145 DNvkgakEQAHAGELAFGTVDSYLLWQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFG 224
Cdd:cd07777 140 RN-----GPLPSKADRAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 225 VTASELFGGeIPICGIAGDQQAALIGQACFEEGMAKSTYGTG---CFLMlntgDKALKS---------NNRLLTTLAyRL 292
Cdd:cd07777 215 TLSSALPKG-IPVYVALGDNQASVLGSGLNEENDAVLNIGTGaqlSFLT----PKFELSgsveirpffDGRYLLVAA-SL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 293 NGkptyaiegsifmaGATMQWIV----EGLKLLENAGESEALVKDV------PLDHGVFLVPSFTGlGApyWDANARGAI 362
Cdd:cd07777 289 PG-------------GRALAVLVdflrEWLRELGGSLSDDEIWEKLdelaesEESSDLSVDPTFFG-ER--HDPEGRGSI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 363 LGLTRDS-GISTIVAAALQSVGyqtKDLQKAMEGDGLRPSILR---VDGGMAN-NNWAMAFLANILGASVERPTLTETTS 437
Cdd:cd07777 353 TNIGESNfTLGNLFRALCRGIA---ENLHEMLPRLDLDLSGIErivGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAA 429
|
....*..
gi 1222443642 438 LGVAYLA 444
Cdd:cd07777 430 VGAALLA 436
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-485 |
7.88e-23 |
|
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: 101.46 E-value: 7.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILY-TKDAEVFDTAQQTFPQHFV--KNGWVEHDPVDIWQTVLSSVKNVLSQQQVtaadiiaigian 80
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVdLADGEELASAVVPYPTGYIppRPGWAEQNPADYWEALEEAVRGALAEAGV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 81 QRET-----------TLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHtqmvnDKTGLVLDPY---FSA----TKIRW 142
Cdd:cd07781 69 DPEDvvgigvdttssTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAH-----PALEYYLAYYggvYSSewmwPKALW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 143 ILDNVKGAKEQAH-AGELAfgtvdSYLLWQLTdGKVhKTDATNASRTLLFNIHQQCWDEELLA-----LFNIPASMLPEV 216
Cdd:cd07781 144 LKRNAPEVYDAAYtIVEAC-----DWINARLT-GRW-VRSRCAAGHKWMYNEWGGGPPREFLAaldpgLLKLREKLPGEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 217 --MDSAADfGVT--ASELFG--GEIPICGIAGDQQAALIGQACFEEG-MAKSTyGT-GCFLMLNTGDKALKSnnrllttl 288
Cdd:cd07781 217 vpVGEPAG-TLTaeAAERLGlpAGIPVAQGGIDAHMGAIGAGVVEPGtLALIM-GTsTCHLMVSPKPVDIPG-------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 289 ayrLNG-------KPTYAIE------GSIFmagatmQWIVE--GLKLLENAGE-----SEALVKDVPLDHGVFLVPSFTG 348
Cdd:cd07781 287 ---ICGpvpdavvPGLYGLEagqsavGDIF------AWFVRlfVPPAEERGDSiyallSEEAAKLPPGESGLVALDWFNG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 349 LGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGDGLRPSILRVDGGMANNN-WAMAFLANILGASV 427
Cdd:cd07781 358 NRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAEKNpLWMQIYADVLGRPI 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222443642 428 ERPTLTETTSLGVAYLAGLQTGVYES--TAQlASMWKSDRRFEPTMSSEER-NDLYAKWLH 485
Cdd:cd07781 438 KVPKSDQAPALGAAILAAVAAGVYADieEAA-DAMVRVDRVYEPDPENHAVyEELYALYKE 497
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
4-457 |
5.75e-22 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 98.50 E-value: 5.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YIlSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQRE 83
Cdd:PRK15027 2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 84 TTLVWNKKTGQPiynAIVWQDRRTSDYCDNLRHagHTQMVNDKTGLVLDPYFSATKIRWIldnvkgakeQAHAGELaFGT 163
Cdd:PRK15027 81 TLLDAQQRVLRP---AILWNDGRCAQECALLEA--RVPQSRVITGNLMMPGFTAPKLLWV---------QRHEPEI-FRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 164 VDSYLL----WQLTDGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVTASELFGG----EI 235
Cdd:PRK15027 146 IDKVLLpkdyLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAwgmaTV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 236 PICGIAGDQQAALIGQACFEEGMAKSTYGT-GCFLMLNTGdkALKSNNRLLTTLAYRLNGKptYAIEGSIFMAGATMQWI 314
Cdd:PRK15027 226 PVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEG--FLSKPESAVHSFCHALPQR--WHLMSVMLSAASCLDWA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 315 VEgLKLLEN-----AGESEALVKDVPldhgVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDL 389
Cdd:PRK15027 302 AK-LTGLSNvpaliAAAQQADESAEP----VWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADG 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222443642 390 QKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTET-TSLGVAYLAGLQTGVYESTAQL 457
Cdd:PRK15027 377 MDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVgPALGAARLAQIAANPEKSLIEL 445
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-483 |
2.32e-21 |
|
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: 97.02 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKN--GWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIANQ 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHKEVPDvpGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 82 RETTLVWNKKtGQPIYnAIVWQDRRTSDYCDNLRHAGHT--QMVNDKTGlvldPYFS---ATKIRWILDNVKGAKEQAHA 156
Cdd:cd07775 81 REGIVLYDNE-GEEIW-ACANVDARAAEEVSELKELYNTleEEVYRISG----QTFAlgaIPRLLWLKNNRPEIYRKAAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 157 gelaFGTVDSYLLWQLTdGKVhKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFG-VT--ASELFG- 232
Cdd:cd07775 155 ----ITMLSDWIAYKLS-GEL-AVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGkVTkeAAEETGl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 233 -GEIPICGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLlttlayRLNGKPTYAI---EGSIFMAG 308
Cdd:cd07775 229 kEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNI------RVNCHVIPDMwqaEGISFFPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 309 ATMQWIVEGL--KLLENAGES--------EALVKDVPL-DHGVflVPSFTGL--------GAPywdanargAILGLTRD- 368
Cdd:cd07775 303 LVMRWFRDAFcaEEKEIAERLgidaydllEEMAKDVPPgSYGI--MPIFSDVmnyknwrhAAP--------SFLNLDIDp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 369 --SGISTIVAAALQSVGYQTK-DLQKAMEGDGLRPSILRVDGGMANNN-WAMaFLANILGASVERPTLTETTSLGVAYLA 444
Cdd:cd07775 373 ekCNKATFFRAIMENAAIVSAgNLERIAEFSGIFPDSLVFAGGASKGKlWCQ-ILADVLGLPVKVPVVKEATALGAAIAA 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1222443642 445 GLQTGVYESTAQLA-SMWKSDRRFEPtmsSEERN----DLYAKW 483
Cdd:cd07775 452 GVGAGIYSSLEEAVeSLVKWEREYLP---NPENHevyqDLYEKW 492
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-469 |
4.90e-17 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 83.83 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAeVFDTAQQTFP-QHFV--KNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGIan 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYA-GLEMAQEPVPyYQDSskKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 81 QRETTLVWNKKTGQPIY---------NAIVWQDRRTSDYCDNLRHAGHTQMVnDKTGLVLDPYFSATKIRWILDnvkgak 151
Cdd:cd07768 78 DATCSLAIFDREGTPLMalipypnedNVIFWMDHSAVNEAQWINMQCPQQLL-DYLGGKISPEMGVPKLKYFLD------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 152 EQAHAGELAFGTVD--SYLLWQLTdGKVHKTDATNASRTLLFNiHQQCWDEE------LLALFNIPASMLPEVMDSAADF 223
Cdd:cd07768 151 EYSHLRDKHFHIFDlhDYIAYELT-RLYEWNICGLLGKENLDG-EESGWSSSffknidPRLEHLTTTKNLPSNVPIGTTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 224 GVTASELFGGEIPICGIAG-----DQQAALIGqacfeegMAKSTYGTGCFLMLNTgdkalKSNNRLLTTLAYRLNG--KP 296
Cdd:cd07768 229 GVALPEMAEKMGLHPGTAVvvsciDAHASWFA-------VASPHLETSLFMIAGT-----SSCHMYGTTISDRIPGvwGP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 297 TYAI--------EGSIFMAGATMQWIVEG------LKLLENAGES---------EALVKDVPLDHGVFLVPSFTGLGAPY 353
Cdd:cd07768 297 FDTIidpdysvyEAGQSATGKLIEHLFEShpcarkFDEALKKGADiyqvleqtiRQIEKNNGLSIHILTLDMFFGNRSEF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 354 WDANARGAILGLTRDSGI---STIVAAALQSVGYQTKDLQKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERP 430
Cdd:cd07768 377 ADPRLKGSFIGESLDTSMlnlTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKP 456
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1222443642 431 TLTETTSLGVAYLAGLQTGV---YES-TAQLASMWKSDRRFEP 469
Cdd:cd07768 457 KENMMGILGAAVLAKVAAGKkqlADSiTEADISNDRKSETFEP 499
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
4-469 |
2.00e-13 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 72.37 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAIlytkdaeVFDTAQQTFPQHFVKNG---------WVEHDPVDIWQTVLS---SVKNVLSQQQVTAA 71
Cdd:PRK10331 3 VILVLDCGATNVRAI-------AVDRQGKIVARASTPNAsdiaaensdWHQWSLDAILQRFADccrQINSELTECHIRGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 72 DIiaigianqreTT------LVwnKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHTQMVNDKTGLVLDPYFSATKIRWILD 145
Cdd:PRK10331 76 TV----------TTfgvdgaLV--DKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 146 NVKGAKEQAHAgelaFGTVDSYLLWQLTDgkVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGV 225
Cdd:PRK10331 144 NHPQLLEQAHA----WLFISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 226 ---TASELFG--GEIPICGIAGDQQAALIGQ-ACFEEGMAKStyGTGCFLMLNTG--DKALKSNNRLLTTlayRLNGKPT 297
Cdd:PRK10331 218 lqpSAAALLGlpVGIPVISAGHDTQFALFGSgAGQNQPVLSS--GTWEILMVRSAqvDTSLLSQYAGSTC---ELDSQSG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 298 YAIEGSIFMAGATMQWIVeglKLLENAGE------SEAlvKDVPLD-HGVFLVPSFtglgapywDANARGAILGLTRDSG 370
Cdd:PRK10331 293 LYNPGMQWLASGVLEWVR---KLFWTAETpyqtmiEEA--RAIPPGaDGVKMQCDL--------LACQNAGWQGVTLNTT 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 371 ISTIVAAALQSVGYQTK-DLQKAMEGDGLRP-SILRVDGGMANNNWAMaFLANILGASVERPTLTETTSLGVAYLAGLQT 448
Cdd:PRK10331 360 RGHFYRAALEGLTAQLKrNLQVLEKIGHFKAsELLLVGGGSRNALWNQ-IKANMLDIPIKVLDDAETTVAGAAMFGWYGV 438
|
490 500
....*....|....*....|...
gi 1222443642 449 GVYES--TAQlASMWKSDRRFEP 469
Cdd:PRK10331 439 GEFSSpeQAR-AQMKYQYRYFYP 460
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-484 |
6.24e-13 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 70.81 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 1 MSKYILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKN--GWVEHDPVDIWQTVLSSVKNVLSQQQVTAADIIAIGI 78
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvpGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 79 ANQRETTLVWNKkTGQPIYnAIVWQDRRTSDYCDNLR--HAGHTQMVNDKTGLVLDpyFSAT-KIRWILDNVKGAKEQAH 155
Cdd:PRK10939 81 TSMREGIVLYDR-NGTEIW-ACANVDARASREVSELKelHNNFEEEVYRCSGQTLA--LGALpRLLWLAHHRPDIYRQAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 156 AgelaFGTVDSYLLWQLTDgkVHKTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFG-VT--ASELFG 232
Cdd:PRK10939 157 T----ITMISDWIAYMLSG--ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGhVTakAAAETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 233 --GEIPICGIAGDQQAALIGQACFEEGMAKSTYGTGCFLMLNTGDKALKSNNRLlttlayRLNgkpTYAIEG-----SI- 304
Cdd:PRK10939 231 lrAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNI------RIN---PHVIPGmvqaeSIs 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 305 FMAGATMQWIV----EGLKLL-ENAGES-----EALVKDVPL-DHGVflVPSFTG---LGAPYwdaNARGAILGLTRDSG 370
Cdd:PRK10939 302 FFTGLTMRWFRdafcAEEKLLaERLGIDaysllEEMASRVPVgSHGI--IPIFSDvmrFKSWY---HAAPSFINLSIDPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 371 IST-------------IVAAAlqsvgyqtkDLQKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTS 437
Cdd:PRK10939 377 KCNkatlfraleenaaIVSAC---------NLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATA 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1222443642 438 LGVAYLAGLQTGVYESTAQLASMW-KSDRRFEPTMSSEE-RNDLYAKWL 484
Cdd:PRK10939 448 LGCAIAAGVGAGIYSSLAETGERLvRWERTFEPNPENHElYQEAKEKWQ 496
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-482 |
1.74e-10 |
|
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: 63.32 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 4 YILSIDQGTTSSRAILYTKDAEVFDTAQQTFPQHFVKNGWVEHDPVDIWQTVLSSVKNVLSQQQVTAadiiaigiaNQ-- 81
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDP---------EQvk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 82 --------------RETTLVWNKKTGQPIYNAIVWQDRRTSDYCDNLRHAGHtqMVNDKTGLVLDPYFSATKIRWILDNV 147
Cdd:cd07782 72 gigfdatcslvvldAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGH--EVLKYVGGKISPEMEPPKLLWLKENL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 148 KGA-KEQAHAGELAfgtvDsYLLWQLTDGKVHKTDATNASRTLLFNIHQQC-WDEELLALFNipasmLPE-VMDSAADFG 224
Cdd:cd07782 150 PETwAKAGHFFDLP----D-FLTWKATGSLTRSLCSLVCKWTYLAHEGSEGgWDDDFFKEIG-----LEDlVEDNFAKIG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 225 VTAseLFGGEIPICGIAgdQQAALigqacfEEGMAKST-YGT-------GCFLMLNTGDKALKSNN-RLLTTLA------ 289
Cdd:cd07782 220 SVV--LPPGEPVGGGLT--AEAAK------ELGLPEGTpVGVslidahaGGLGTLGADVGGLPCEAdPLTRRLAlicgts 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 290 -------------------YR--------LNgkptyaiEGSIFMAGATMQWIVEG------LK------------LLENA 324
Cdd:cd07782 290 schmavspepvfvpgvwgpYYsamlpglwLN-------EGGQSATGALLDHIIEThpaypeLKeeakaagksiyeYLNER 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 325 GESEALVKDVPLDH---GVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVA---AALQSVGYQTKDLQKAMEGDGL 398
Cdd:cd07782 363 LEQLAEEKGLPLAYltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAAGH 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 399 RPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYES-TAQLASMWKSDRRFEPtmsSEERN 477
Cdd:cd07782 443 KIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSlWDAMAAMSGPGKVVEP---NEELK 519
|
....*
gi 1222443642 478 DLYAK 482
Cdd:cd07782 520 KYHDR 524
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
167-439 |
5.06e-10 |
|
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: 61.39 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 167 YLLWQLTdGKVHkTDATNASRTLLFNIHQQCWDEELLALFNIPASMLPEVMDSAADFGVT----ASELFGGEIPICGIAG 242
Cdd:cd07771 157 LLNYLLT-GEKV-AEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLkpevAEELGLKGIPVIAVAS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 243 -DQQAALIGQACFEEGmakstygtgcFLMLNTGDKAL---KSNNRLLTTLAYRLNGKPTYAIEGSIF----MAGatMqWI 314
Cdd:cd07771 235 hDTASAVAAVPAEDED----------AAFISSGTWSLigvELDEPVITEEAFEAGFTNEGGADGTIRllknITG--L-WL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 315 VEGLK--------------LLENAGESEALVKDVPLDHGVFLVPSftglgapywdaNARGAILGLTRDSG------ISTI 374
Cdd:cd07771 302 LQECRreweeegkdysydeLVALAEEAPPFGAFIDPDDPRFLNPG-----------DMPEAIRAYCRETGqpvpesPGEI 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443642 375 VAAALQSVGYQTKD-LQKAMEGDGLRPSILRVDGGMANNNWAMAFLANILGASVER-PtlTETTSLG 439
Cdd:cd07771 371 ARCIYESLALKYAKtIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAgP--VEATAIG 435
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
261-444 |
2.95e-06 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. 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: 466792 [Multi-domain] Cd Length: 424 Bit Score: 49.57 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 261 STyGTGCFLMlNTGDKALKSNNRLLTTLAYRLN--GKPtyaIEGSIFMAGATMQWIVEGLKLLENAGESEALVKDVpLDH 338
Cdd:cd07772 250 ST-GTWCIAM-NPGNDLPLTELDLARDCLYNLDvfGRP---VKTARFMGGREYERLVERIAKSFPQLPSLADLAKL-LAR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 339 GVFLVPSFTGLGAPYwdaNARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGDGLRpsiLRVDGGMANNNWAMAF 418
Cdd:cd07772 324 GTFALPSFAPGGGPF---PGSGGRGVLSAFPSAEEAYALAILYLALMTDYALDLLGSGVGR---IIVEGGFAKNPVFLRL 397
|
170 180
....*....|....*....|....*..
gi 1222443642 419 LANIL-GASVERPTLTETTSLGVAYLA 444
Cdd:cd07772 398 LAALRpDQPVYLSDDSEGTALGAALLA 424
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
101-444 |
4.23e-06 |
|
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: 49.09 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 101 VWQDRRTSDYCDNLRHA-GHTQMVNDKTGLVLDPYFSATKIRwildnvKGAKEQAHAGE------LA--FGTvdSYLLwq 171
Cdd:cd07776 128 IWMDSSTTKQCRELEKAvGGPEALAKLTGSRAYERFTGPQIA------KIAQTDPEAYEnterisLVssFLA--SLLL-- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 172 ltdGKVHKTDATNASRTLLFNIHQQCWDEELLALFNIP--ASMLPEVMDSAADFGVTASELF---GG--EIPICGIAGDQ 244
Cdd:cd07776 198 ---GRYAPIDESDGSGMNLMDIRSRKWSPELLDAATAPdlKEKLGELVPSSTVAGGISSYFVeryGFspDCLVVAFTGDN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 245 QAALIGQACFEEGMAKStygtgcflmLNTGDKALKSNNRLLTTLAYRLNGKPTYAIEgsiFMA------GA-TMQWIVEg 317
Cdd:cd07776 275 PASLAGLGLEPGDVAVS---------LGTSDTVFLVLDEPKPGPEGHVFANPVDPGS---YMAmlcyknGSlARERVRD- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 318 lkllENAGES-----EALVKDVPLDHGV----FLVPSFT--GLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQT 386
Cdd:cd07776 342 ----RYAGGSwekfnELLESTPPGNNGNlglyFDEPEITppVPGGGRRFFGDDGVDAFFDPAVEVRAVVESQFLSMRLHA 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443642 387 KDLqkameGDGLRPSILRVDGGMANNNWAMAFLANILGASVERPTLTETTSLGVAYLA 444
Cdd:cd07776 418 ERL-----GSDIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRA 470
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
327-485 |
1.79e-03 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 40.98 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 327 SEALVKDVPLDHGVFLVPSFTGLGAPYWDANARGAILGLTRDSGISTIVAAALQSVGYQTKDLQKAMEGDGLRPSILRVD 406
Cdd:PRK04123 366 TEAAAKQPPGEHGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443642 407 GGMANNN-WAMAFLANILGASVERPTLTETTSLGVAYLAGLQTGVYES--TAQLASMWKSDRRFEPTMSSEER-NDLYAK 482
Cdd:PRK04123 446 GGIARKNpVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDipEAQQAMASPVEKTYQPDPENVARyEQLYQE 525
|
...
gi 1222443642 483 WLH 485
Cdd:PRK04123 526 YKQ 528
|
|
| |
