|
Name |
Accession |
Description |
Interval |
E-value |
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-498 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 1072.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 1 MTEKKYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGI 80
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 81 ANQRETAIVWERETGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRGE 160
Cdd:PRK00047 81 TNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 161 LLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNIGGKGGTRIPI 240
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGEVPI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 241 AGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPSGEVNYALEGAVFMAGASIQWLRDE 320
Cdd:PRK00047 241 AGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 321 MKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADS 400
Cdd:PRK00047 321 LKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 401 GIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIEREFRPGIETTER 480
Cdd:PRK00047 401 GIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEER 480
|
490
....*....|....*...
gi 2207588688 481 NYRYSGWKKAVKRAMAWE 498
Cdd:PRK00047 481 EKLYAGWKKAVKRTLAWA 498
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
4-499 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 1021.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 4 KKYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQ 83
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 84 RETAIVWERETGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLF 163
Cdd:COG0554 82 RETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 164 GTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNIGGKGGtRIPIAGI 243
Cdd:COG0554 162 GTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGA-EIPIAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 244 AGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPSGEVNYALEGAVFMAGASIQWLRDEMKL 323
Cdd:COG0554 241 AGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 324 ISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIR 403
Cdd:COG0554 321 IDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 404 LHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIEREFRPGIETTERNYR 483
Cdd:COG0554 401 LKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERL 480
|
490
....*....|....*.
gi 2207588688 484 YSGWKKAVKRAMAWED 499
Cdd:COG0554 481 YAGWKKAVERTLGWAE 496
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
6-492 |
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: 971.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWERETGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLFGT 165
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 166 VDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNIGGkGGTRIPIAGIAG 245
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDL-LGAEIPIAGIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 246 DQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPSGEVNYALEGAVFMAGASIQWLRDEMKLIS 325
Cdd:cd07786 240 DQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 326 DAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIRLH 405
Cdd:cd07786 320 SAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 406 ALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIEREFRPGIETTERNYRYS 485
Cdd:cd07786 400 ELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYA 479
|
....*..
gi 2207588688 486 GWKKAVK 492
Cdd:cd07786 480 GWKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
6-492 |
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: 966.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWERETGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLFGT 165
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 166 VDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNIGGkGGTRIPIAGIAG 245
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEG-LGAGIPIAGILG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 246 DQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPSGEVNYALEGAVFMAGASIQWLRDEMKLIS 325
Cdd:cd07769 240 DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 326 DAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIRLH 405
Cdd:cd07769 320 DAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 406 ALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIEREFRPGIETTERNYRYS 485
Cdd:cd07769 400 ELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYR 479
|
....*..
gi 2207588688 486 GWKKAVK 492
Cdd:cd07769 480 GWKKAVE 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
5-497 |
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: 876.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 5 KYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQR 84
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 85 ETAIVWERETGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLFG 164
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 165 TVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNiGGKGGTRIPIAGIA 244
Cdd:TIGR01311 161 TIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTD-PGLLGAEIPITGVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 245 GDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPSGEVN-YALEGAVFMAGASIQWLRDEMKL 323
Cdd:TIGR01311 240 GDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPvYALEGSVFVAGAAVQWLRDNLKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 324 ISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIR 403
Cdd:TIGR01311 320 IKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 404 LHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIEREFRPGIETTERNYR 483
Cdd:TIGR01311 400 ITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREAR 479
|
490
....*....|....
gi 2207588688 484 YSGWKKAVKRAMAW 497
Cdd:TIGR01311 480 YAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-494 |
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: 752.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 5 KYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTL---VEVLAKADISSDQIAAIGIA 81
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIeeaVEKLKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 82 NQRETAIVWERETGKPIYNAIVWQCRRTADICEQL--KRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRG 159
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELsaKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 160 ELLFGTVDTWLIWKMT---QGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNIGGKGGt 236
Cdd:cd07792 161 RLLFGTVDSWLIWNLTggkNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 237 rIPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIA--CGPSGEVNYALEGAVFMAGASI 314
Cdd:cd07792 240 -VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAykLGPDAPPVYALEGSIAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 315 QWLRDEMKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLE 394
Cdd:cd07792 319 QWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 395 AMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIERE-FRP 473
Cdd:cd07792 399 AMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTvFEP 478
|
490 500
....*....|....*....|.
gi 2207588688 474 GIETTERNYRYSGWKKAVKRA 494
Cdd:cd07792 479 QISEEERERRYKRWKKAVERS 499
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
4-499 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 680.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 4 KKYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADI--SSDQIAAIGIA 81
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREkgPSFKIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 82 NQRETAIVWERETGKPIYNAIVWQCRRTADICEQLKRD-GLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRGE 160
Cdd:PTZ00294 81 NQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKyGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 161 LLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYG----QTNIGGKGgt 236
Cdd:PTZ00294 161 LLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGtisgEAVPLLEG-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 237 rIPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIA--CGPSGEVNYALEGAVFMAGASI 314
Cdd:PTZ00294 239 -VPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCyqLGPNGPTVYALEGSIAVAGAGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 315 QWLRDEMKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLE 394
Cdd:PTZ00294 318 EWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 395 AMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIE-REFRP 473
Cdd:PTZ00294 398 SMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSnSTFSP 477
|
490 500
....*....|....*....|....*.
gi 2207588688 474 GIETTERNYRYSGWKKAVKRAMAWED 499
Cdd:PTZ00294 478 QMSAEERKAIYKEWNKAVERSLKWAK 503
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
6-501 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 657.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISS----DQIAAIGIA 81
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGhnvdSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 82 NQRETAIVWERETGKPIYNAIVWQCRRTADICEQLKRD--GLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRG 159
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 160 ELLFGTVDTWLIWKMT---QGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNIGGKGGt 236
Cdd:PLN02295 161 DALFGTIDSWLIWNLTggaSGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 237 RIPIAGIAGDQQAALFGQLCvKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIA--CGPSGEVNYALEGAVFMAGASI 314
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAykLGPDAPTNYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 315 QWLRDEMKLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLE 394
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 395 AMQAD-----SGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDEL-QEKAVIE 468
Cdd:PLN02295 399 AMRKDageekSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFaSEKWKNT 478
|
490 500 510
....*....|....*....|....*....|...
gi 2207588688 469 REFRPGIETTERNYRYSGWKKAVKRAMAWEDHD 501
Cdd:PLN02295 479 TTFRPKLDEEERAKRYASWCKAVERSFDLADLS 511
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
6-492 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 562.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWERETGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLV----------------VDPYFSGTKVKWILDHV 149
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRGGSKFLhfltrnkrflaasvlkFSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 150 EGSRERAKRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTN 229
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 230 IGGkGGTRIPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPSGEVNYALEGAVFM 309
Cdd:cd07793 241 PSI-FGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 310 AGASIQWLRDEMkLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQT 389
Cdd:cd07793 320 TGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 390 RDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAVIER 469
Cdd:cd07793 399 KQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEK 478
|
490 500
....*....|....*....|...
gi 2207588688 470 EFRPGIETTERNYRYSGWKKAVK 492
Cdd:cd07793 479 IFEPKMDNEKREELYKNWKKAVK 501
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
6-253 |
3.46e-115 |
|
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: 339.70 E-value: 3.46e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWERETgKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKrgelLFGT 165
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 166 VDTWLIWKMTQgrVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTNIGGKGGT----RIPIA 241
Cdd:pfam00370 156 IHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWgldeGVPVV 233
|
250
....*....|..
gi 2207588688 242 GIAGDQQAALFG 253
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-493 |
7.64e-115 |
|
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: 347.98 E-value: 7.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 5 KYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQR 84
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 85 ETAIVWEREtGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRgellFG 164
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK----VL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 165 TVDTWLIWKMTqGRvHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTN------IGGKGGTRI 238
Cdd:COG1070 156 LPKDYLRYRLT-GE-FVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTaeaaaeTGLPAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 239 pIAGiAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTgEKAVKSENGLLTTIACGPSGevNYALEGAVFMAGASIQWLR 318
Cdd:COG1070 234 -VAG-AGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPG--RWLPMGATNNGGSALRWFR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 319 DEmkLISDAFDS-EYFATKVKDT----NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVL 393
Cdd:COG1070 309 DL--FADGELDDyEELNALAAEVppgaDGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 394 EAMQAdSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAV-IEREFR 472
Cdd:COG1070 387 EALEE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVrVGETIE 465
|
490 500
....*....|....*....|...
gi 2207588688 473 PGIETTERnYR--YSGWKKAVKR 493
Cdd:COG1070 466 PDPENVAA-YDelYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
6-480 |
5.52e-113 |
|
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: 341.04 E-value: 5.52e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAI-VweRETGKPIYNAIVWQCRRTADICeqlkrdgledyirdntglvvdpyfsgtkvkwildhvegsrerakrgellfg 164
Cdd:cd07779 81 TFVpV--DEDGRPLRPAISWQDKRTAKFL--------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 165 TVDTWLIWKMTqGRvHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTN------IGGKGGTRI 238
Cdd:cd07779 108 TVQDYLLYRLT-GE-FVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTkeaaeeTGLPEGTPV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 239 pIAGiAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPSgevNYALEGAVFMAGASIQWLR 318
Cdd:cd07779 186 -VAG-GGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPG---KWVLEGSINTGGSAVRWFR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 319 DE------MKLISDAFDSEYFATKVKDT----NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQ 388
Cdd:cd07779 261 DEfgqdevAEKELGVSPYELLNEEAAKSppgsDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 389 TRDVLEAMQaDSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAV-I 467
Cdd:cd07779 341 LRDNLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVrV 419
|
490
....*....|...
gi 2207588688 468 EREFRPGIETTER 480
Cdd:cd07779 420 TDTFEPDPENVAI 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-448 |
1.21e-112 |
|
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: 338.77 E-value: 1.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWEREtGKPIYNAIVWQCRRtadiceqlkrdgledyirdntglvvdpyfsgtkvkwildhvegsrerAKrgellFGT 165
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIWLDRR-----------------------------------------------AK-----FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 166 VDTWLIWKMTQgrVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTN------IGGKGGTriP 239
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTpeaaeeTGLPAGT--P 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 240 IAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKavKSENGLLTTIACGPSGevNYALEGAVFMAGASIQWLRD 319
Cdd:cd00366 184 VVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEP--VPPDPRLLNRCHVVPG--LWLLEGAINTGGASLRWFRD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 320 EMKLISDAFDSEYF----ATKVKD-TNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLE 394
Cdd:cd00366 260 EFGEEEDSDAEYEGldelAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLE 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2207588688 395 AMQADsGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLA 448
Cdd:cd00366 340 ILEEL-GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
6-453 |
4.57e-101 |
|
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: 310.67 E-value: 4.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADIssDQIAAIGIANQRE 85
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP--DPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWEREtGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRgellFGT 165
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 166 VDTWLIWKMTqGRvHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTN------IGGKGGTRIP 239
Cdd:cd07773 154 VADYIAYRLT-GE-PVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTpeaaeeLGLPAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 240 IAGIagDQQAALFGQLCVKEGMAKNTYGTG-CFMLmnTGEKAVKSENGLLTTIACGPSGEVNYALEGAVFMAGASIQWLR 318
Cdd:cd07773 232 VGGH--DHLCAALGAGVIEPGDVLDSTGTAeALLA--VVDEPPLDEMLAEGGLSYGHHVPGGYYYLAGSLPGGALLEWFR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 319 DEM--KLISDAFDSEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAM 396
Cdd:cd07773 308 DLFggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2207588688 397 QAdSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07773 388 EK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
6-490 |
4.95e-98 |
|
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: 304.08 E-value: 4.95e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWErETGKPIYNAIVWQCRRTADICEQLkRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRgeLLFgT 165
Cdd:cd07808 81 GLVLLD-KNGRPLRPAILWNDQRSAAECEEL-EARLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRK--ILL-P 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 166 VDtWLIWKMTqGRvHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTN------IGGKGGTRIp 239
Cdd:cd07808 156 KD-YLRYRLT-GE-LATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTpeaaeeLGLPEGTPV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 240 IAGiAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTiaCGPSGEVNYALeGAVFMAGASIQWLRD 319
Cdd:cd07808 232 VAG-AGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTF--PHAVPGKWYAM-GVTLSAGLSLRWLRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 320 EMKLISDAFDSeyFATKVKDT----NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEA 395
Cdd:cd07808 308 LFGPDRESFDE--LDAEAAKVppgsEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 396 MQaDSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEKAV-IEREFRPG 474
Cdd:cd07808 386 LK-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIkIEKTIEPD 464
|
490
....*....|....*..
gi 2207588688 475 IETTER-NYRYSGWKKA 490
Cdd:cd07808 465 PERHEAyDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-480 |
2.75e-86 |
|
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: 273.63 E-value: 2.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAI-VweRETGKPIYNAIVWQCRRTADICEQL-KRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHvegSRERAKRGELLF 163
Cdd:cd07805 81 GVVpV--DKDGNPLRNAIIWSDTRAAEEAEEIaGGLGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 164 GTVDtWLIWKMTqGRVhVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYG--------QTNIggKGG 235
Cdd:cd07805 156 DAKD-YLNFRLT-GRA-ATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGeltpeaaaELGL--PAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 236 TRIpIAGiAGDQQAALFGQLCVKEGMAkNTY-GTGCFMLMNTGEKAVKSENGlLTTIACGPSGEVNYAleGAVFMAGASI 314
Cdd:cd07805 231 TPV-VGG-GGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASADPGRYLLA--AEQETAGGAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 315 QWLRDEMKLISDAFDSEY-FATK-VKDT----NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQ 388
Cdd:cd07805 305 EWARDNLGGDEDLGADDYeLLDElAAEAppgsNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 389 TRDVLEAMQADSGiRLHALRVDGGAVANNFLMQFQSDILGTRVERPEV-REVTALGAAYLAGLAVGYWQNLDELQEKAVI 467
Cdd:cd07805 385 LRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVKV 463
|
490
....*....|...
gi 2207588688 468 EREFRPGIETTER 480
Cdd:cd07805 464 EKVFEPDPENRAR 476
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-453 |
3.84e-83 |
|
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: 264.77 E-value: 3.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIanqre 85
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAI------VWERetGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRg 159
Cdd:cd07804 76 SGLvpalvpVDEN--GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRK- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 160 ellFGTVDTWLIWKMTqGRVhVTDYTNASRTM-LFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYG--------QTni 230
Cdd:cd07804 153 ---FLGAYDYIVYKLT-GEY-VIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGevtkeaaeET-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 231 GGKGGTRIpIAGiAGDQQAALFGQLCVKEG--MAKntYGT-GCFMLMNtgEKAVKSENgLLTTIACGPSGevnYALEGAV 307
Cdd:cd07804 226 GLAEGTPV-VAG-TVDAAASALSAGVVEPGdlLLM--LGTaGDIGVVT--DKLPTDPR-LWLDYHDIPGT---YVLNGGM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 308 FMAGASIQWLRDEM------------KLISDAFDSEyfATKVKDT-NGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNS 374
Cdd:cd07804 296 ATSGSLLRWFRDEFageeveaeksggDSAYDLLDEE--AEKIPPGsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTR 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2207588688 375 NHIIRATLESIAYQTRDVLEAMqADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07804 374 AHLYRALLEGVAYGLRHHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
6-480 |
6.05e-79 |
|
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: 254.40 E-value: 6.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADisSDQIAAIGIANQRE 85
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG--GGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWEREtGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRgellFGT 165
Cdd:cd07770 79 SLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK----FVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 166 VDTWLIWKMTqGRvHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQ------TNIGGKGGTRIp 239
Cdd:cd07770 154 IKEYLLYRLT-GE-LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGlkpefaERLGLLAGTPV- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 240 IAGiAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTgEKAVKSENGLLttiACGPSGEVNYALEGAVFMAGASIQWLRD 319
Cdd:cd07770 231 VLG-ASDGALANLGSGALDPGRAALTVGTSGAIRVVS-DRPVLDPPGRL---WCYRLDENRWLVGGAINNGGNVLDWLRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 320 EMKLISDAFD--SEYFATKVKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQ 397
Cdd:cd07770 306 TLLLSGDDYEelDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 398 aDSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLdELQEKAVIEREFRPGIET 477
Cdd:cd07770 386 -ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL-EADELVKIGKVVEPDPEN 463
|
...
gi 2207588688 478 TER 480
Cdd:cd07770 464 HAI 466
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
6-453 |
1.56e-69 |
|
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: 228.97 E-value: 1.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 TAIVWEREtGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHvegSRERAKRGELLFGT 165
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN---EPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 166 VDtWLIWKMTqGRVHvTDYTNASrTMLFNIHDLDWDDKMLDVLDIP--RAMLPQVRKSSEVYG--------QTNIggKGG 235
Cdd:cd07802 157 KD-WIRYRLT-GEIS-TDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGrvtaeaaaLTGL--PEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 236 TriPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCfmlMNTG--EKAVKSENGLLTTIACGPsgevNYALEGAVFMAGAS 313
Cdd:cd07802 231 T--PVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNSLHADP----GLYLIVEASPTSAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 314 -IQWLRDEM--------KLISDAFDsEYFATKVKDTNGVYVVPAFTGLGApywDPYARGAIFGLTRGVNSNHIIRATLES 384
Cdd:cd07802 302 nLDWFLDTLlgeekeagGSDYDELD-ELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEG 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2207588688 385 IAYQTRDVLEAMQADSGIRlhALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07802 378 IAFSHRDHLERLLVARKPE--TIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
6-452 |
5.79e-59 |
|
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: 200.53 E-value: 5.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWasqsSTLVEVLAK--ADISSDQIAAIGIANQ 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWW----EALRSLLRElpAELRPRRVVAIAVDGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 84 RETAIVWEREtGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRdnTGLVVDPYFSGTKVKWILDHVEGSRERAKRgeLLF 163
Cdd:cd07783 77 SGTLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAGAVAPR--TGLAVSPSSSLAKLLWLKRHEPEVLAKTAK--FLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 164 GTvdTWLIWKMTqGRVHVTDYTNASRTmLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQT------NIGGKGGTR 237
Cdd:cd07783 152 QA--DWLAGRLT-GDRGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLtaeaaeELGLPAGTP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 238 IpIAGIAgDQQAALFGQLCVKEGMAKNTYGTG-CFMLMNTGEKAVKSENgllttIACGPSGEVNYALEGAVFMAGASIQW 316
Cdd:cd07783 228 V-VAGTT-DSIAAFLASGAVRPGDAVTSLGTTlVLKLLSDKRVPDPGGG-----VYSHRHGDGYWLVGGASNTGGAVLRW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 317 L--RDEMKLISDAFDSEYfatkvkdTNGVYVVP-AFTGLGAPYWDPYARGAIfgLTRGVNSNHIIRATLESIAYQTRDVL 393
Cdd:cd07783 301 FfsDDELAELSAQADPPG-------PSGLIYYPlPLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGY 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2207588688 394 EAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREvTALGAAYLAGLAV 452
Cdd:cd07783 372 ERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE-AALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-453 |
9.85e-57 |
|
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: 195.13 E-value: 9.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPK--PGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQ 83
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDdyPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 84 RETaIVWERETGKPIY---N----AIVWqcrrtADICEqlkrDGLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERA 156
Cdd:cd07798 81 REG-IVFLDKDGRELYagpNidarGVEE-----AAEID----DEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 157 KRgellFGTVDTWLIWKMTqGRVhVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYG------QTNI 230
Cdd:cd07798 151 AT----VLSISDWIGYRLT-GEL-VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGtvseeaAREL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 231 GGKGGTRIPIAGiaGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPSGevnYALEGAVFMA 310
Cdd:cd07798 225 GLPEGTPVVVGG--ADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGK---WVLESNAGVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 311 GASIQWLRDEM-KLISDAFD--SEYFATKVKDTNGVYvvpAFTGLGAPYWD--PYARGAIF----GLTRGVNSNHIIRAT 381
Cdd:cd07798 300 GLNYQWLKELLyGDPEDSYEvlEEEASEIPPGANGVL---AFLGPQIFDARlsGLKNGGFLfptpLSASELTRGDFARAI 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2207588688 382 LESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07798 377 LENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
6-453 |
1.59e-49 |
|
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: 175.89 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQRE 85
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 86 -TAIVweRETGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSGTKVKWILDHvegSRERAKRGELLFG 164
Cdd:cd24121 81 gTWLV--DEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERARTALH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 165 TVDtWLIWKMTQGRvhVTDYTNASRTMlFNIHDLDWDDKMLDVLDIP--RAMLPQVRKSSEVYGQTN------IGGKGGT 236
Cdd:cd24121 156 CKD-WLFYKLTGEI--ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTpeaaaaTGLPAGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 237 riPIAGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSEN-GllTTIACGPSGEVNYALegAVFMAGASIQ 315
Cdd:cd24121 232 --PVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGvG--YTICLGVPGRWLRAM--ANMAGTPNLD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 316 WLRDEM-------KLISDAFDSEYFATKVKD----TNGVYVVP--AFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATL 382
Cdd:cd24121 306 WFLRELgevlkegAEPAGSDLFQDLEELAASsppgAEGVLYHPylSPAGERAPFVNPNARAQFTGLSLEHTRADLLRAVY 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2207588688 383 ESIAYQTRDVLEAMQADSGirlhALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd24121 386 EGVALAMRDCYEHMGEDPG----ELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-453 |
3.46e-48 |
|
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: 172.35 E-value: 3.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMD-HDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQR 84
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 85 ETAIVWEREtGKPIYNAIVWQCRRTADICEQLKRDgLEDYIRDNTGLVVDPYFSGTKVKWILDHVEGSRERAKRGELLFG 164
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEA-LGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 165 tvdtWLIWKMTqGRvHVTDYTNASRTMLFNIHDLDWDDKMLDVLD---IPRAMLPQVRKSSEVYGQ-TNIGGKGG---TR 237
Cdd:cd07809 159 ----YLNWKLT-GE-KVTGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVLPAGEVAGRlTPEGAEELglpAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 238 IPIAGIAGDQQAALFGQLCVKEGMAKNTYGT-GCfmLMNTGEKAVKSENGLLTTIAcgpsgEVNYALEGAVFMAGASIQW 316
Cdd:cd07809 233 IPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFC-----DSTGGMLPLINTTNCLTAW 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 317 LRDEMKLIS---DAFDSEYFATKVkDTNGVYVVPAFTGLGAPYWdPYARGAIFGLTrgvNSN----HIIRATLESIAYQT 389
Cdd:cd07809 306 TELFRELLGvsyEELDELAAQAPP-GAGGLLLLPFLNGERTPNL-PHGRASLVGLT---LSNftraNLARAALEGATFGL 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2207588688 390 RDVLEAMQADsGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG 453
Cdd:cd07809 381 RYGLDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
262-451 |
1.30e-46 |
|
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: 160.57 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 262 AKNTYGTGCFMLMnTGEKAVKSENGLLTTIAcGPSGEVNYALEGAVFMAGASIQWLRDEM----KLISDAFDSEYFATK- 336
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYT-NEMLPGYWGLEGGQSAAGSLLAWLLQFHglreELRDAGNVESLAELAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 337 ---VKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGA 413
Cdd:pfam02782 79 laaVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2207588688 414 VANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLA 451
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-476 |
2.52e-43 |
|
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: 160.19 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFeqIYPK----PGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIA 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREW--RHKEvpdvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 82 NQRETAIVWEREtGKPIynaivWQCR----RTADICEQLK--RDGLEDYIRDNTGlvvDPYFSGT--KVKWILDHVEGSR 153
Cdd:cd07775 79 SMREGIVLYDNE-GEEI-----WACAnvdaRAAEEVSELKelYNTLEEEVYRISG---QTFALGAipRLLWLKNNRPEIY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 154 ERAKRgellFGTVDTWLIWKMTQgrVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQTN---- 229
Cdd:cd07775 150 RKAAK----ITMLSDWIAYKLSG--ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTkeaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 230 --IGGKGGTRIpIAGIaGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPsGEVNYalEGAV 307
Cdd:cd07775 224 eeTGLKEGTPV-VVGG-GDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIP-DMWQA--EGIS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 308 FMAGASIQWLRD----EMKLIS-----DAFDseYFATKVKDT------------------NGVYVVPAFTGLGApywDP- 359
Cdd:cd07775 299 FFPGLVMRWFRDafcaEEKEIAerlgiDAYD--LLEEMAKDVppgsygimpifsdvmnykNWRHAAPSFLNLDI---DPe 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 360 -YARGAIFgltrgvnsnhiiRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVRE 438
Cdd:cd07775 374 kCNKATFF------------RAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKE 441
|
490 500 510
....*....|....*....|....*....|....*....
gi 2207588688 439 VTALGAAYLAGLAVGYWQNLDELQEKAV-IEREFRPGIE 476
Cdd:cd07775 442 ATALGAAIAAGVGAGIYSSLEEAVESLVkWEREYLPNPE 480
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
6-480 |
2.00e-39 |
|
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: 149.61 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMD-HDANIVSVSQREFEQIY--PKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIAN 82
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 83 qreTA--IVWERETGKPIYNAIVWQ-CR--RTADICEQLKRDGLEDYIRDNTGLV-VDPYFSgtKVKWILDHVEGSRERA 156
Cdd:cd07781 81 ---TSstVVPVDEDGNPLAPAILWMdHRaqEEAAEINETAHPALEYYLAYYGGVYsSEWMWP--KALWLKRNAPEVYDAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 157 KR-GELlfgtVDtWLIWKMTqGRVhVTDYTNASRTMLFNIHDLDWDDKMLDVLDIP----RAMLPQ-VRKSSEVYGQTN- 229
Cdd:cd07781 156 YTiVEA----CD-WINARLT-GRW-VRSRCAAGHKWMYNEWGGGPPREFLAALDPGllklREKLPGeVVPVGEPAGTLTa 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 230 -----IGGKGGTRIPIAGIagDQQAALFGQLCVKEG-MAKNTyGT-GCFMLMNTGEKAVKsenGLlttiaCGP-SGEVN- 300
Cdd:cd07781 229 eaaerLGLPAGIPVAQGGI--DAHMGAIGAGVVEPGtLALIM-GTsTCHLMVSPKPVDIP---GI-----CGPvPDAVVp 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 301 --YALEGAVFMAGASIQWLRDEMKLISDAFDSEYF------ATKVK-DTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRG 371
Cdd:cd07781 298 glYGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIYallseeAAKLPpGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 372 VNSNHIIRATLESIAYQTRDVLEAMQaDSGIRLHALRVDGGAVANN-FLMQFQSDILGTRVERPEVREVTALGAAYLAGL 450
Cdd:cd07781 378 TTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGIAEKNpLWMQIYADVLGRPIKVPKSDQAPALGAAILAAV 456
|
490 500 510
....*....|....*....|....*....|.
gi 2207588688 451 AVGYWQNLDELQEKAV-IEREFRPGIETTER 480
Cdd:cd07781 457 AAGVYADIEEAADAMVrVDRVYEPDPENHAV 487
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-493 |
1.12e-34 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 135.87 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 8 VALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPmEIWASQSSTLVEVLAkADISSDQIAAIGIANQRETA 87
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDP-EQWWQATDRAMKALG-DQHSLQDVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 88 IVWERETgKPIYNAIVWQCRRTADICEQLKRDGLEDyiRDNTGLVVDPYFSGTKVKWILDH-VEGSRERAKrgELLfgtV 166
Cdd:PRK15027 81 TLLDAQQ-RVLRPAILWNDGRCAQECALLEARVPQS--RVITGNLMMPGFTAPKLLWVQRHePEIFRQIDK--VLL---P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 167 DTWLIWKMTQgrVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYG--QTNIGGKGGT-RIPIAGI 243
Cdd:PRK15027 153 KDYLRLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGalLPEVAKAWGMaTVPVVAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 244 AGDQQAALFGQLCVKEGMAKNTYGT-GCFMLMNTG-----EKAVKSengllttiACgpsgevnYALEG-----AVFMAGA 312
Cdd:PRK15027 231 GGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHS--------FC-------HALPQrwhlmSVMLSAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 313 S-IQW------LRDEMKLISDAFDSEyfatkvKDTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESI 385
Cdd:PRK15027 296 ScLDWaakltgLSNVPALIAAAQQAD------ESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 386 AYQTRDVLEAMQAdSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREV-TALGAAYLAGLAVGYWQNLDELQEK 464
Cdd:PRK15027 370 GYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVgPALGAARLAQIAANPEKSLIELLPQ 448
|
490 500
....*....|....*....|....*....
gi 2207588688 465 AVIEREFRPgieTTERNYRYSGWKKAVKR 493
Cdd:PRK15027 449 LPLEQSHLP---DAQRYAAYQPRRETFRR 474
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
6-448 |
7.48e-33 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 129.65 E-value: 7.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMD-HDANIVSVSQREFEQI--YPKPGWVEHDPMEIWASQSSTLVEVLAKADIssdQIAAIGIAN 82
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPisSDDPGRSEQDPEKILEAVRNLIDELPREYLS---DVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 83 QRETAIVWeRETGKPIYNAIVWQCRRtadiCEQLKRDGLEDYIRDntglvvDPYFSGTKVK---------WIldhvegsr 153
Cdd:cd07777 78 QMHGIVLW-DEDGNPVSPLITWQDQR----CSEEFLGGLSTYGEE------LLPKSGMRLKpgyglatlfWL-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 154 erAKRGELL-----FGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGQT 228
Cdd:cd07777 139 --LRNGPLPskadrAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 229 NIGGKGGtrIPI-AGIaGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTgEKAVKS---------ENGLLTTIACGPSGE 298
Cdd:cd07777 217 SSALPKG--IPVyVAL-GDNQASVLGSGLNEENDAVLNIGTGAQLSFLT-PKFELSgsveirpffDGRYLLVAASLPGGR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 299 vnyALegAVFmagasIQWLRDEMKLISDAFDSEYF------ATKVKDTNGVYVVPAFTGlGApyWDPYARGAIFGLTrgv 372
Cdd:cd07777 293 ---AL--AVL-----VDFLREWLRELGGSLSDDEIwekldeLAESEESSDLSVDPTFFG-ER--HDPEGRGSITNIG--- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 373 NSN----HIIRATLESIAYQTRDVLEAMQAD-SGIRlhALRVDGGAVA-NNFLMQFQSDILGTRVERPEVREVTALGAAY 446
Cdd:cd07777 357 ESNftlgNLFRALCRGIAENLHEMLPRLDLDlSGIE--RIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAAL 434
|
..
gi 2207588688 447 LA 448
Cdd:cd07777 435 LA 436
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
5-500 |
8.66e-30 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 122.42 E-value: 8.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 5 KYIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPK--PGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIAN 82
Cdd:PRK10939 3 SYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPdvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSATS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 83 QREtAIVWERETGKPIynaivWQC-----RRTADICEqLK--RDGLEDYIRDNTG----LVVDPyfsgtKVKWILDHVEG 151
Cdd:PRK10939 83 MRE-GIVLYDRNGTEI-----WACanvdaRASREVSE-LKelHNNFEEEVYRCSGqtlaLGALP-----RLLWLAHHRPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 152 SRERAKRgellFGTVDTWLIWKMTQgrVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYG----- 226
Cdd:PRK10939 151 IYRQAHT----ITMISDWIAYMLSG--ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGhvtak 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 227 ---QTniGGKGGTRIPIAGiaGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLltTIACGPSGEVNYAl 303
Cdd:PRK10939 225 aaaET--GLRAGTPVVMGG--GDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNI--RINPHVIPGMVQA- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 304 EGAVFMAGASIQWLRD----EMKLIS-----DAFDS-EYFATKVKdtNGVY-VVPAFTGL--------GAPYW-----DP 359
Cdd:PRK10939 298 ESISFFTGLTMRWFRDafcaEEKLLAerlgiDAYSLlEEMASRVP--VGSHgIIPIFSDVmrfkswyhAAPSFinlsiDP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 360 YA--RGAIFgltrgvnsnhiiRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVR 437
Cdd:PRK10939 376 EKcnKATLF------------RALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVK 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2207588688 438 EVTALGAAYLAGLAVGYWQNLDELQEKAV-IEREFRPGIETTERnYR--YSGWKKAVKRAMAWEDH 500
Cdd:PRK10939 444 EATALGCAIAAGVGAGIYSSLAETGERLVrWERTFEPNPENHEL-YQeaKEKWQAVYADQLGLVDH 508
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
6-482 |
1.44e-28 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 118.21 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIV-SVSQREFEQIYP-KPGWVEHDPMEIWASQSSTLVEVLAKadISSDQIAAIGIAN- 82
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVaRASTPNASDIAAeNSDWHQWSLDAILQRFADCCRQINSE--LTECHIRGITVTTf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 83 QRETAIVWERetGKPIYNAIVWQCRRTADICEQLKR--DGLEDYIRDNTGlvvdpYFS-GT--KVKWILDHvegsrerak 157
Cdd:PRK10331 81 GVDGALVDKQ--GNLLYPIISWKCPRTAAVMENIERyiSAQQLQQISGVG-----AFSfNTlyKLVWLKEN--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 158 rGELLFGTVDTWL-IWKMTQGR---VHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYG--QTNIG 231
Cdd:PRK10331 145 -HPQLLEQAHAWLfISSLINHRltgEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGtlQPSAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 232 GKGG--TRIPIAGIAGDQQAALFGQlcvkeGMAKN----TYGTGCFMLMNTG--EKAVKSENGLLTTIACGPSGEVNYAL 303
Cdd:PRK10331 224 ALLGlpVGIPVISAGHDTQFALFGS-----GAGQNqpvlSSGTWEILMVRSAqvDTSLLSQYAGSTCELDSQSGLYNPGM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 304 EgavFMAGASIQWLRdemKLISDAfdSEYFATKVKD-------TNGVYVVPAFTGLGapywdpyaRGAIFGLTRGVNSNH 376
Cdd:PRK10331 299 Q---WLASGVLEWVR---KLFWTA--ETPYQTMIEEaraippgADGVKMQCDLLACQ--------NAGWQGVTLNTTRGH 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 377 IIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQ 456
Cdd:PRK10331 363 FYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFS 442
|
490 500
....*....|....*....|....*..
gi 2207588688 457 NLDELQEKAVIE-REFRPGieTTERNY 482
Cdd:PRK10331 443 SPEQARAQMKYQyRYFYPQ--TEPEFI 467
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
6-473 |
4.99e-27 |
|
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: 114.26 E-value: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANI-VSVSQREFEQ-IYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIGIANQ 83
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYAGLeMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 84 RETAIVwERE--------TGKPIYNAIVWQCRRTADICEQL---KRDGLEDYIrdntGLVVDPYFSGTKVKWILDHVEGS 152
Cdd:cd07768 81 CSLAIF-DREgtplmaliPYPNEDNVIFWMDHSAVNEAQWInmqCPQQLLDYL----GGKISPEMGVPKLKYFLDEYSHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 153 RERAKRgelLFGTVDtWLIWKMTQgrvhvtDYTNASRTML----FNIHDLDWDDKMLDVLDIPRAML--PQVRKSSEVYG 226
Cdd:cd07768 156 RDKHFH---IFDLHD-YIAYELTR------LYEWNICGLLgkenLDGEESGWSSSFFKNIDPRLEHLttTKNLPSNVPIG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 227 QTNIGG------KGGTRIPIAGIAG--DQQAALFG----QLCVKEGMAKNTygTGCFMLMNTGEKAVKSENGLLTTIACg 294
Cdd:cd07768 226 TTSGVAlpemaeKMGLHPGTAVVVSciDAHASWFAvaspHLETSLFMIAGT--SSCHMYGTTISDRIPGVWGPFDTIID- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 295 PSGEVNYALEGAVfmaGASIQWL-------RDEMKLISDAFDS----EYFATKVKD----TNGVYVVPAFTGLGAPYWDP 359
Cdd:cd07768 303 PDYSVYEAGQSAT---GKLIEHLfeshpcaRKFDEALKKGADIyqvlEQTIRQIEKnnglSIHILTLDMFFGNRSEFADP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 360 YARGAIFGL---TRGVNSNHIIRATLESIAYQTRDVLEAMQADsGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEV 436
Cdd:cd07768 380 RLKGSFIGEsldTSMLNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2207588688 437 REVTALGAAYLAGLAVGYWQNLDELQEKAV----IEREFRP 473
Cdd:cd07768 459 NMMGILGAAVLAKVAAGKKQLADSITEADIsndrKSETFEP 499
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
4-480 |
5.58e-25 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 107.89 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 4 KKYIVALDQGTTSSRAVVMD-HDANIVSVSQREF------EQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIA 76
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYprwvigLYLPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 77 AIGIANQRETAIVWEREtGKPI-----------YNAIVW-------QCRRTADICEQLKrdglEDYIRdntglvvdpYFS 138
Cdd:COG1069 81 GIGVDATGCTPVPVDAD-GTPLallpefaenphAMVILWkdhtaqeEAERINELAKARG----EDYLR---------YVG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 139 GT--------KVKWILDHVEGSRERAKRgelLFGTVDtWLIWKMTqGRVHvtdytnASRT-----MLFNIHDLDWDD--- 202
Cdd:COG1069 147 GIissewfwpKILHLLREDPEVYEAADS---FVELCD-WITWQLT-GSLK------RSRCtaghkALWHAHEGGYPSeef 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 203 -KMLD-VLDIPRAMLPQvrkssEVYgqtNIGGKGGT-------------RIPIAGIAGDQQAALFGQLCVKEG-MAKNtY 266
Cdd:COG1069 216 fAALDpLLDGLADRLGT-----EIY---PLGEPAGTltaewaarlglppGTAVAVGAIDAHAGAVGAGGVEPGtLVKV-M 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 267 GT-GCFMLMNTGEKAVKsenGLlttiaCGPsgeVN-------YALEG---AVfmaGASIQWLRDE-------MKLISDAF 328
Cdd:COG1069 287 GTsTCHMLVSPEERFVP---GI-----CGQ---VDgsivpgmWGYEAgqsAV---GDIFAWFVRLlvppleyEKEAEERG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 329 DS--EYFATKVK----DTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQAdSGI 402
Cdd:COG1069 353 ISlhPLLTEEAAklppGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEE-EGV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 403 RLHALRVDGG-AVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQEK--AVIEREFRPGIETTE 479
Cdd:COG1069 432 PIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAmgSGFDKVYTPDPENVA 511
|
.
gi 2207588688 480 R 480
Cdd:COG1069 512 V 512
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
6-460 |
1.38e-21 |
|
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: 97.99 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVSVSQREFEQIYPKPGWVEHDPMEIWASQSSTLVEVLAKADISSDQIAAIG------ 79
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGfdatcs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 80 -IANQRETAIVWERETGKPIYNAIVWQCRRTADICEQLKRdgledyirdnTGLVVDPYFSGT--------KVKWILDHVE 150
Cdd:cd07782 81 lVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINA----------TGHEVLKYVGGKispemeppKLLWLKENLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 151 GSRERAKRgelLFGTVDtWLIWKMTQGRVHVTDYTNASRTMLFNIHDLD-WDDKML------DVLDIPRAMLPQVRKSse 223
Cdd:cd07782 151 ETWAKAGH---FFDLPD-FLTWKATGSLTRSLCSLVCKWTYLAHEGSEGgWDDDFFkeigleDLVEDNFAKIGSVVLP-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 224 vyGQTNIGG------------KGGTRIPIAGIagDQQAALFGQLCVKEGMAKNTY-----------GTG-CFMLMNTGEK 279
Cdd:cd07782 225 --PGEPVGGgltaeaakelglPEGTPVGVSLI--DAHAGGLGTLGADVGGLPCEAdpltrrlalicGTSsCHMAVSPEPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 280 AVK----------------SENG----------LLTTIACGPsgevnyALEGAVFMAGASI-QWLRDEMKLISDA--FDS 330
Cdd:cd07782 301 FVPgvwgpyysamlpglwlNEGGqsatgalldhIIETHPAYP------ELKEEAKAAGKSIyEYLNERLEQLAEEkgLPL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 331 EYFatkvkdTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIR---ATLESIAYQTRDVLEAMQAdSGIRLHAL 407
Cdd:cd07782 375 AYL------TRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNA-AGHKIDTI 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2207588688 408 RVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDE 460
Cdd:cd07782 448 FMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWD 500
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
6-463 |
2.68e-15 |
|
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: 77.95 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 6 YIVALDQGTTSSRAVVMDHDANIVsvsqrEFEQIYPkpgwVEHDPMEI-------WASQSSTLVEVLAKADISSDQIAAI 78
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKL-----ELEEIHR----FPNRPVEInghlywdIDRLFDEIKEGLKKAAEQGGDIDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 79 GI-----------ANqretaivweretGKPIYNAIVWQCRRTADICEQLKRDGLEDYIRDNTGLVVDPYFSgtkvkwiLD 147
Cdd:cd07771 72 GIdtwgvdfglldKN------------GELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINT-------LY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 148 HVegsRERAKRGELLFGTVDTWLI------WKMTqGRVhVTDYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKS 221
Cdd:cd07771 133 QL---YALKKEGPELLERADKLLMlpdllnYLLT-GEK-VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 222 SEVYGQTN---IGGKGGTRIPIAGIAG-DQQAALFGQLCVKEGMAkntY---GTGCFMlmntGekaVKSENGLLTTIACg 294
Cdd:cd07771 208 GTVLGTLKpevAEELGLKGIPVIAVAShDTASAVAAVPAEDEDAA---FissGTWSLI----G---VELDEPVITEEAF- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 295 psgEVNYALEGAVF--------MAGASI------QWLRDEMK-----LISDAFDSEYFATKVkDTNGvyvvPAF------ 349
Cdd:cd07771 277 ---EAGFTNEGGADgtirllknITGLWLlqecrrEWEEEGKDysydeLVALAEEAPPFGAFI-DPDD----PRFlnpgdm 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 350 ----------TGLGAPYwdpyargaifglTRGvnsnHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFL 419
Cdd:cd07771 349 peairaycreTGQPVPE------------SPG----EIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALL 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2207588688 420 MQFQSDILGTRVER-PEvrEVTALGAAYLAGLAVGYWQNLDELQE 463
Cdd:cd07771 413 CQLTADATGLPVIAgPV--EATAIGNLLVQLIALGEIKSLEEGRE 455
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
355-480 |
3.83e-12 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 68.33 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 355 PYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLEAMQaDSGIRLHALRVDGG-AVANNFLMQFQSDILGTRVER 433
Cdd:PRK04123 391 PLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQV 469
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2207588688 434 PEVREVTALGAAYLAGLAVGYWQNLDELQEK--AVIEREFRPGIETTER 480
Cdd:PRK04123 470 VASDQCPALGAAIFAAVAAGAYPDIPEAQQAmaSPVEKTYQPDPENVAR 518
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
177-471 |
1.05e-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: 51.02 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 177 GRVHVTDYTNASRTMLFNIHDLDWDDKMLDVLDIP--RAMLPQVRKSSEVYGQT------NIGGKGGTRIpIAGiAGDQQ 248
Cdd:cd07776 198 GRYAPIDESDGSGMNLMDIRSRKWSPELLDAATAPdlKEKLGELVPSSTVAGGIssyfveRYGFSPDCLV-VAF-TGDNP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 249 AALFGqLCVKEGMAKNTYGTG--CFMLMNTGekavksengllttiACGPSGEV--NYALEGAvFMA------GA-SIQWL 317
Cdd:cd07776 276 ASLAG-LGLEPGDVAVSLGTSdtVFLVLDEP--------------KPGPEGHVfaNPVDPGS-YMAmlcyknGSlARERV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 318 RDEMKLIS-DAFDsEYFATKVKDTNGVyvvpaftgLGAPYWDP--YARGAIFGLTRGVNSNHIIRATLESIAyqtRDVLE 394
Cdd:cd07776 340 RDRYAGGSwEKFN-ELLESTPPGNNGN--------LGLYFDEPeiTPPVPGGGRRFFGDDGVDAFFDPAVEV---RAVVE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 395 AmQADSgIRLHA-----------LRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGYWQNLDELQE 463
Cdd:cd07776 408 S-QFLS-MRLHAerlgsdipptrILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPE 485
|
....*...
gi 2207588688 464 KAVIEREF 471
Cdd:cd07776 486 FVVFSAEE 493
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
11-448 |
1.11e-06 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 51.25 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 11 DQGTTSSRAVVMDHDANIVSVSQREFE-QIYPKPGW-VEHDPMEIWASqsstLVEVLAKADISSDQ--IAAIGIAnqrET 86
Cdd:cd07778 6 DVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWfVTQSSTEIWKA----IKTALKELIEELSDyiVSGIGVS---AT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 87 A--IVWERETGK--------------PIYNAIVW---QCRRTADICEQLKRDGLEDYIRdntGLVVdPYFSGTKVKWILD 147
Cdd:cd07778 79 CsmVVMQRDSDTsylvpynviheksnPDQDIIFWmdhRASEETQWLNNILPDDILDYLG---GGFI-PEMAIPKLKYLID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 148 HVegSRERAKrgELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHD---LDWDDKMLDVLDIPRAMLPQVRKSSEV 224
Cdd:cd07778 155 LI--KEDTFK--KLEVFDLHDWISYMLATNLGHSNIVPVNAPPSIGIGIDgslKGWSKDFYSKLKISTKVCNVGNTFKEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 225 YGQTNIGGKGGTRIPIA----GIAG---------DQQAALFGQLC---VKEGMAKNTYGTG-CFMLMNTGEKAVK----- 282
Cdd:cd07778 231 PPLPYAGIPIGKVNVILasylGIDKstvvghgciDCYAGWFSTFAaakTLDTTLFMVAGTStCFLYATSSSQVGPipgiw 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 283 -----------------SENG-----LLTTIACGPSGEVNYALEGAVFMagasiQWLRDEMKLISdafDSEYFATKVKDT 340
Cdd:cd07778 311 gpfdqllknysvyeggqSATGkliekLFNSHPAIIELLKSDANFFETVE-----EKIDKYERLLG---QSIHYLTRHMFF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207588688 341 NGVYvvpafTGLGAPYWDPYARGAIFGltrGVNSNHIIR------ATLESIAYQTRDVLEAMQaDSGIRLHALRVDGGAV 414
Cdd:cd07778 383 YGDY-----LGNRTPYNDPNMSGSFIG---ESTDSSLTDlvlkyiLILEFLAFQTKLIIDNFQ-KEKIIIQKVVISGSQA 453
|
490 500 510
....*....|....*....|....*....|....*..
gi 2207588688 415 ANNFLMQFQS---DILGTRVERPEVREVTALGAAYLA 448
Cdd:cd07778 454 KNARLLQLLStvlSKIHIIVPLSDSKYAVVKGAALLG 490
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
183-244 |
5.01e-06 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 48.95 E-value: 5.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2207588688 183 DYTNASRTMLFNIHDLDWDDKMLDVLDIPRAMLPQVRKSSEVYGqtNIGGKGGTRIPIAGIA 244
Cdd:PRK10640 157 EYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIG--HWICPQGNEIPVVAVA 216
|
|
| |
