|
Name |
Accession |
Description |
Interval |
E-value |
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-496 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 1092.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 1 MKKYILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITN 80
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 81 QRETAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGDLL 160
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 161 FGTIDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETIDYHFFGQNVPIAG 240
Cdd:PRK00047 163 FGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGEVPIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 241 VAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGIDGKVNYALEGSIFVAGSAIQWLRDGMR 320
Cdd:PRK00047 243 IAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 321 MFKDASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAMEADSGI 400
Cdd:PRK00047 323 IISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 401 ELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQWHMDKRFEPTMEAETSEE 480
Cdd:PRK00047 403 RLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREK 482
|
490
....*....|....*.
gi 1214520716 481 LYAGWKKAIEATKAFK 496
Cdd:PRK00047 483 LYAGWKKAVKRTLAWA 498
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-496 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 1053.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 1 MKKYILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITN 80
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 81 QRETAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGDLL 160
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 161 FGTIDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETiDYHFFGQNVPIAG 240
Cdd:COG0554 161 FGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGET-DPDLFGAEIPIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 241 VAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGIDGKVNYALEGSIFVAGSAIQWLRDGMR 320
Cdd:COG0554 240 IAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 321 MFKDASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAMEADSGI 400
Cdd:COG0554 320 LIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 401 ELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQWHMDKRFEPTMEAETSEE 480
Cdd:COG0554 400 PLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERER 479
|
490
....*....|....*.
gi 1214520716 481 LYAGWKKAIEATKAFK 496
Cdd:COG0554 480 LYAGWKKAVERTLGWA 495
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
4-490 |
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: 1004.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGDLLFGT 163
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETiDYHFFGQNVPIAGVAG 243
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYT-DPDLLGAEIPIAGIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 244 DQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGIDGKVNYALEGSIFVAGSAIQWLRDGMRMFK 323
Cdd:cd07786 240 DQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 324 DASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAMEADSGIELK 403
Cdd:cd07786 320 SAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 404 TLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQWHMDKRFEPTMEAETSEELYA 483
Cdd:cd07786 400 ELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYA 479
|
....*..
gi 1214520716 484 GWKKAIE 490
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), ... |
4-490 |
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: 985.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGDLLFGT 163
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETiDYHFFGQNVPIAGVAG 243
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYT-DPEGLGAGIPIAGILG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 244 DQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGIDGKVNYALEGSIFVAGSAIQWLRDGMRMFK 323
Cdd:cd07769 240 DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 324 DASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAMEADSGIELK 403
Cdd:cd07769 320 DAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 404 TLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQWHMDKRFEPTMEAETSEELYA 483
Cdd:cd07769 400 ELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYR 479
|
....*..
gi 1214520716 484 GWKKAIE 490
Cdd:cd07769 480 GWKKAVE 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
3-495 |
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 1214520716 3 KYILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQR 82
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 83 ETAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGDLLFG 162
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 163 TIDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETiDYHFFGQNVPIAGVA 242
Cdd:TIGR01311 161 TIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYT-DPGLLGAEIPITGVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 243 GDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGIDGKVN-YALEGSIFVAGSAIQWLRDGMRM 321
Cdd:TIGR01311 240 GDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPvYALEGSVFVAGAAVQWLRDNLKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 322 FKDASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAMEADSGIE 401
Cdd:TIGR01311 320 IKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 402 LKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQWHMDKRFEPTMEAETSEEL 481
Cdd:TIGR01311 400 ITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREAR 479
|
490
....*....|....
gi 1214520716 482 YAGWKKAIEATKAF 495
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; ... |
3-490 |
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: 743.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 3 KYILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIA-TC--LSEADVKPEQIAGIGIT 79
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEeAVekLKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 80 NQRETAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYG--EMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENG 157
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGgkDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 158 DLLFGTIDTWLVWKLSGGK---AHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETIDYHFfgQ 234
Cdd:cd07792 161 RLLFGTVDSWLIWNLTGGKnggVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPL--A 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 235 NVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAW--GIDGKVNYALEGSIFVAGSAI 312
Cdd:cd07792 239 GVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYklGPDAPPVYALEGSIAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 313 QWLRDGMRMFKDASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLC 392
Cdd:cd07792 319 QWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 393 AMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQ-WHMDKRFEP 471
Cdd:cd07792 399 AMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLnEGGRTVFEP 478
|
490
....*....|....*....
gi 1214520716 472 TMEAETSEELYAGWKKAIE 490
Cdd:cd07792 479 QISEEERERRYKRWKKAVE 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
2-496 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 686.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 2 KKYILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCL--SEADVKPEQIAGIGIT 79
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIkkLREKGPSFKIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 80 NQRETAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYGEM-VREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGD 158
Cdd:PTZ00294 81 NQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNfFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 159 LLFGTIDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGE-TIDYHFFGQNVP 237
Cdd:PTZ00294 161 LLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTiSGEAVPLLEGVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 238 IAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAW--GIDGKVNYALEGSIFVAGSAIQWL 315
Cdd:PTZ00294 241 ITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYqlGPNGPTVYALEGSIAVAGAGVEWL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 316 RDGMRMFKDASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAME 395
Cdd:PTZ00294 321 RDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESME 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 396 ADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKE-QWHMDKRFEPTME 474
Cdd:PTZ00294 401 KDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKlIRRSNSTFSPQMS 480
|
490 500
....*....|....*....|..
gi 1214520716 475 AETSEELYAGWKKAIEATKAFK 496
Cdd:PTZ00294 481 AEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
4-492 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 641.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVK----PEQIAGIGIT 79
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKghnvDSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 80 NQRETAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEK--GYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENG 157
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 158 DLLFGTIDTWLVWKLSGGKA---HVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGeTIDYHFFGQ 234
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGASggvHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG-TIAKGWPLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 235 NVPIAGVAGDQQAALFGQACfGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAW--GIDGKVNYALEGSIFVAGSAI 312
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYklGPDAPTNYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 313 QWLRDGMRMFKDASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLC 392
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 393 AMEADSGIE-----LKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIK-EQWHMD 466
Cdd:PLN02295 399 AMRKDAGEEkshkgLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFAsEKWKNT 478
|
490 500
....*....|....*....|....*.
gi 1214520716 467 KRFEPTMEAETSEELYAGWKKAIEAT 492
Cdd:PLN02295 479 TTFRPKLDEEERAKRYASWCKAVERS 504
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-490 |
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: 608.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVR----------EKTGLLIDAYFSGT------KVKWILDNV 147
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRggskflhfltRNKRFLAASVLKFStahvsiRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 148 EGAREKAENGDLLFGTIDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETi 227
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGST- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 228 DYHFFGQNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGIDGKVNYALEGSIFV 307
Cdd:cd07793 240 DPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 308 AGSAIQWLRDGMrMFKDASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQT 387
Cdd:cd07793 320 TGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 388 KDVLCAMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQWHMDK 467
Cdd:cd07793 399 KQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEK 478
|
490 500
....*....|....*....|...
gi 1214520716 468 RFEPTMEAETSEELYAGWKKAIE 490
Cdd:cd07793 479 IFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-495 |
2.33e-125 |
|
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: 374.55 E-value: 2.33e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 3 KYILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQR 82
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 83 ETAVVWDKtTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAEngdlLFG 162
Cdd:COG1070 81 HGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA----KVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 163 TIDTWLVWKLSGgkAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYG--------ETidyhffG- 233
Cdd:COG1070 156 LPKDYLRYRLTG--EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGtltaeaaaET------Gl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 234 -QNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTgEKAVASEHGLLTTIAWGIDGKvnYALEGSIFVAGSAI 312
Cdd:COG1070 228 pAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR--WLPMGATNNGGSAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 313 QWLRD--GMRMFKDASESEVYASRVE-STDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKD 389
Cdd:COG1070 305 RWFRDlfADGELDDYEELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 390 VLCAMEAdSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQW-HMDKR 468
Cdd:COG1070 385 GLEALEE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGET 463
|
490 500
....*....|....*....|....*...
gi 1214520716 469 FEPTME-AETSEELYAGWKKAIEATKAF 495
Cdd:COG1070 464 IEPDPEnVAAYDELYERYRELYPALKPL 491
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-475 |
3.62e-115 |
|
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: 346.43 E-value: 3.62e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKTtGKPIYNAIVWQSRQTAEICdelkekgygemvrektgllidayfsgtkvkwildnvegarekaengdllfgT 163
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQDKRTAKFL---------------------------------------------------T 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDTWLVWKLSGGkaHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYG--------ETidyhffG-- 233
Cdd:cd07779 109 VQDYLLYRLTGE--FVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGtltkeaaeET------Glp 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 234 QNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAwGIDGKvnYALEGSIFVAGSAIQ 313
Cdd:cd07779 181 EGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPS-AVPGK--WVLEGSINTGGSAVR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 314 WLRD---GMRMFKDASESEVYA---SRVEST----DGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESL 383
Cdd:cd07779 258 WFRDefgQDEVAEKELGVSPYEllnEEAAKSppgsDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGI 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 384 AYQTKDVLCAMEaDSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQW 463
Cdd:cd07779 338 AFELRDNLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAM 416
|
490
....*....|...
gi 1214520716 464 -HMDKRFEPTMEA 475
Cdd:cd07779 417 vRVTDTFEPDPEN 429
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-251 |
3.92e-112 |
|
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: 331.61 E-value: 3.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKTTgKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAEngdlLFGT 163
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH----KFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDTWLVWKLSGgkAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETIDYHFFG----QNVPIA 239
Cdd:pfam00370 156 IHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMwgldEGVPVV 233
|
250
....*....|..
gi 1214520716 240 GVAGDQQAALFG 251
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-446 |
1.79e-110 |
|
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: 332.99 E-value: 1.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKTtGKPIYNAIVWqsrqtaeicdelkekgygemvrektgllidayfsgtkvkwiLDNvegaREKaengdllFGT 163
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIW-----------------------------------------LDR----RAK-------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDTWLVWKLSGgkAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETIDYHF----FGQNVPIA 239
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAeetgLPAGTPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 240 GVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVasEHGLLTTIAWGIDGKvnYALEGSIFVAGSAIQWLRDgm 319
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVP--PDPRLLNRCHVVPGL--WLLEGAINTGGASLRWFRD-- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 320 rMFKDASESEVY-------ASRVE-STDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVL 391
Cdd:cd00366 260 -EFGEEEDSDAEyegldelAAEVPpGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNL 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1214520716 392 CAMEADsGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLA 446
Cdd:cd00366 339 EILEEL-GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
4-451 |
1.26e-104 |
|
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: 319.53 E-value: 1.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLseADVKPEQIAGIGITNQRE 83
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAA--AQAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKTtGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENgdllFGT 163
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDTWLVWKLSGgkAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYG----ETIDYHFFGQNVPIA 239
Cdd:cd07773 154 VADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGtvtpEAAEELGLPAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 240 gVAG-DQQAALFGQACFGEGMAKNTYGTG-CFMLMNTGEKAVASEHGLLTTIAWGIDGKVnYALEGSIfVAGSAIQWLRD 317
Cdd:cd07773 232 -VGGhDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPGGY-YYLAGSL-PGGALLEWFRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 318 --GMRMFKDASESEVYASRVESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAME 395
Cdd:cd07773 309 lfGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALE 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1214520716 396 AdSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVG 451
Cdd:cd07773 389 K-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-488 |
5.18e-99 |
|
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: 306.39 E-value: 5.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKtTGKPIYNAIVWQSRQTAEICDELKEKgYGEMVREKTGLLIDAYFSGTKVKWIldnvegAREKAENgdllFGT 163
Cdd:cd07808 81 GLVLLDK-NGRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWL------KENEPEI----FAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDT------WLVWKLSGgkAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGET---------ID 228
Cdd:cd07808 149 IRKillpkdYLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLtpeaaeelgLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 229 yhffgQNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTgEKAVASEHGLLTTIAWGIDGKvNYALeGSIFVA 308
Cdd:cd07808 227 -----EGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGK-WYAM-GVTLSA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 309 GSAIQWLRDgmrMFKDASES-EVYASRVEST----DGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESL 383
Cdd:cd07808 299 GLSLRWLRD---LFGPDRESfDELDAEAAKVppgsEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 384 AYQTKDVLCAMEaDSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQW 463
Cdd:cd07808 376 AFSLRDSLEVLK-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAAC 454
|
490 500
....*....|....*....|....*..
gi 1214520716 464 H-MDKRFEPTME-AETSEELYAGWKKA 488
Cdd:cd07808 455 IkIEKTIEPDPErHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
4-486 |
7.86e-91 |
|
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: 285.57 E-value: 7.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKtTGKPIYNAIVWQ-SRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNvegAREKAENGDLLFG 162
Cdd:cd07805 81 GVVPVDK-DGNPLRNAIIWSdTRAAEEAEEIAGGLGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 163 TIDtWLVWKLSGgkAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYG--------ETidyhffG- 233
Cdd:cd07805 157 AKD-YLNFRLTG--RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGeltpeaaaEL------Gl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 234 -QNVPIAGVAGDQQAALFGQACFGEGMAkNTY-GTGCFMLMNTGEKAVASEHGlLTTIAWGIDGKVNYAleGSIFVAGSA 311
Cdd:cd07805 228 pAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASADPGRYLLA--AEQETAGGA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 312 IQWLRDGMRMFKDASEsEVY------ASRVE-STDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLA 384
Cdd:cd07805 304 LEWARDNLGGDEDLGA-DDYelldelAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 385 YQTKDVLCAMEADSGiELKTLRVDGGAVKNNFLMKFQSDILDVPVERP-VINETTALGAAYLAGLAVGYWKNQDEIKEQW 463
Cdd:cd07805 383 FNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPeNPQEAGALGAALLAAVGLGLLKSFDEAKALV 461
|
490 500
....*....|....*....|....
gi 1214520716 464 HMDKRFEPTME-AETSEELYAGWK 486
Cdd:cd07805 462 KVEKVFEPDPEnRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-451 |
9.28e-84 |
|
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: 265.93 E-value: 9.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKtTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDN----VEGARekaengdl 159
Cdd:cd07804 81 ALVPVDE-NGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNepevFKKTR-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 160 LFGTIDTWLVWKLSGgkAHVTDYSNASRT-LMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYG--------ETidyh 230
Cdd:cd07804 152 KFLGAYDYIVYKLTG--EYVIDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGevtkeaaeET---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 231 ffG--QNVPIAGVAGDQQAALFGQACFGEG--MAKntYGTGCFMLMNTGEKAVASEHGLLTTIAWGIdgkvnYALEGSIF 306
Cdd:cd07804 226 --GlaEGTPVVAGTVDAAASALSAGVVEPGdlLLM--LGTAGDIGVVTDKLPTDPRLWLDYHDIPGT-----YVLNGGMA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 307 VAGSAIQWLRDGM-RMFKDASES---EVY------ASRVEST-DGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHF 375
Cdd:cd07804 297 TSGSLLRWFRDEFaGEEVEAEKSggdSAYdlldeeAEKIPPGsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1214520716 376 IRATLESLAYQTKDVLCAMEaDSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVG 451
Cdd:cd07804 377 YRALLEGVAYGLRHHLEVIR-EAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-487 |
3.83e-82 |
|
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: 262.49 E-value: 3.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLseADVKPEQIAGIGITNQRE 83
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVL--AKLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKtTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAEngdlLFGT 163
Cdd:cd07770 79 SLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAA----KFVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDTWLVWKLSGgkAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGEtIDYHFFGQ-----NVPI 238
Cdd:cd07770 154 IKEYLLYRLTG--ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPG-LKPEFAERlgllaGTPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 239 AGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLlttiaWgidgkvNYALEGSIFVAGSAI------ 312
Cdd:cd07770 231 VLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRL-----W------CYRLDENRWLVGGAInnggnv 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 313 -QWLRDGMRMFKDA-SESEVYASRVEST-DGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKD 389
Cdd:cd07770 300 lDWLRDTLLLSGDDyEELDKLAEAVPPGsHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 390 VLCAMEaDSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNqDEIKEQWHMDKRF 469
Cdd:cd07770 380 IYEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISS-LEADELVKIGKVV 457
|
490
....*....|....*....
gi 1214520716 470 EPTME-AETSEELYAGWKK 487
Cdd:cd07770 458 EPDPEnHAIYAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
4-450 |
1.17e-63 |
|
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: 212.85 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLseADVKPEQIAGIGITNQRE 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELP--AELRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKtTGKPIYNAIVWQSRQTAEICDELKEKgyGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAEngdlLFGT 163
Cdd:cd07783 79 TLVLVDR-EGEPLRPAIMYNDARAVAEAEELAEA--AGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTA----KFLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDTWLVWKLSGGKAhVTDYSNASRTLmFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGeTIDYHF-----FGQNVPI 238
Cdd:cd07783 152 QADWLAGRLTGDRG-VTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIG-TLTAEAaeelgLPAGTPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 239 agVAG--DQQAALFGQACFGEGMAKNTYGTG-CFMLMnTGEKAVASEHGLLttiawgidgkvNYALEGSIFVAGSAIQ-- 313
Cdd:cd07783 229 --VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLKLL-SDKRVPDPGGGVY-----------SHRHGDGYWLVGGASNtg 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 314 --WLRDgmrmFKDASESEVYASRVEST--DGVYVVPaFVGLG--TPYWDSEVRGAIfgVTRGTTKEHFIRATLESLAYQT 387
Cdd:cd07783 295 gaVLRW----FFSDDELAELSAQADPPgpSGLIYYP-LPLRGerFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIE 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1214520716 388 KDVLCAMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPViNETTALGAAYLAGLAV 450
Cdd:cd07783 368 RLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-451 |
6.74e-62 |
|
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: 208.56 E-value: 6.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKtTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIdayFSGTKV---KWILDNvegAREKAENGDLL 160
Cdd:cd07802 81 GLYLVDK-DGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPL---WPGQPVallRWLKEN---EPERYDRIRTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 161 FGTIDtWLVWKLSGgkAHVTDYSNASrTLMFNIHDLQWDDELLDMLTVP--KSMLPEVRPSSEVYG--------ETidyh 230
Cdd:cd07802 154 LFCKD-WIRYRLTG--EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGrvtaeaaaLT---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 231 ffG--QNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCfmlMNTGE-KAVASEHGLLTTIAWGIDGKVnYALEGSIfV 307
Cdd:cd07802 226 --GlpEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVVtDEPVVPDSVGSNSLHADPGLY-LIVEASP-T 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 308 AGSAIQWLRDgmRMFKDASES-----EVYASRVES----TDGVYVVPaFVgLGTPYwDSEVRGAIFGVTRGTTKEHFIRA 378
Cdd:cd07802 299 SASNLDWFLD--TLLGEEKEAggsdyDELDELIAAvppgSSGVIFLP-YL-YGSGA-NPNARGGFFGLTAWHTRAHLLRA 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1214520716 379 TLESLAYQTKDvlCAMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVG 451
Cdd:cd07802 374 VYEGIAFSHRD--HLERLLVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-451 |
4.87e-61 |
|
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: 206.69 E-value: 4.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPK--PGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQ 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDdyPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 82 RETAVVWDKTtGKPIY---N----AIVWQsrqtAEICDELKEKGYgemvrEKTGLLIDAYFSGTKVKWILDNVEGAREKA 154
Cdd:cd07798 81 REGIVFLDKD-GRELYagpNidarGVEEA----AEIDDEFGEEIY-----TTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 155 ENgdllFGTIDTWLVWKLSGGKahVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGeTIDYHF--- 231
Cdd:cd07798 151 AT----VLSISDWIGYRLTGEL--VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLG-TVSEEAare 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 232 FGQN--VPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTiAWGIDGKvnYALEGSIFVAG 309
Cdd:cd07798 224 LGLPegTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTG-CHLVPGK--WVLESNAGVTG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 310 SAIQWLRDgmRMFKDASES-----EVYASRVESTDGVYvvpAFVGLGTPYWDSEV--RGAIF----GVTRGTTKEHFIRA 378
Cdd:cd07798 301 LNYQWLKE--LLYGDPEDSyevleEEASEIPPGANGVL---AFLGPQIFDARLSGlkNGGFLfptpLSASELTRGDFARA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1214520716 379 TLESLAYQTKDVLCAMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVG 451
Cdd:cd07798 376 ILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-451 |
6.24e-54 |
|
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: 187.37 E-value: 6.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFN-KKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQR 82
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 83 ETAVVWDKtTGKPIYNAIVWQSRQTAEICDELKEKgYGEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGDLLFG 162
Cdd:cd07809 81 HGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEA-LGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 163 tidtWLVWKLSGGKahVTDYSNASRTLMFNIHDLQWDDELL---DMLTVPKSMLPEVRPSSEVYGETIDYH--FFG--QN 235
Cdd:cd07809 159 ----YLNWKLTGEK--VTGLGDASGTFPIDPRTRDYDAELLaaiDPSRDLRDLLPEVLPAGEVAGRLTPEGaeELGlpAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 236 VPIAGVAGDQQAALFGQACFGEGMAKNTYGT-GCfmLMNTGEKAVASEHGLLTTIAwgidgKVNYALEGSIFVAG---SA 311
Cdd:cd07809 233 IPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFC-----DSTGGMLPLINTTNcltAW 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 312 IQWLRDGMRMFKDASESEVYASRVEStDGVYVVPAFVGLGTPYWdSEVRGAIFGVTRG-TTKEHFIRATLESLAYQTKDV 390
Cdd:cd07809 306 TELFRELLGVSYEELDELAAQAPPGA-GGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLRYG 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1214520716 391 LCAMEADsGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVG 451
Cdd:cd07809 384 LDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
260-449 |
8.00e-52 |
|
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: 174.44 E-value: 8.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 260 AKNTYGTGCFMLMnTGEKAVASEHGLLTTIAwGIDGKVNYALEGSIFVAGSAIQWLRD---GMRMFKDASESEVYASRVE 336
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYT-NEMLPGYWGLEGGQSAAGSLLAWLLQfhgLREELRDAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 337 S-----TDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAMEADSGIELKTLRVDGGA 411
Cdd:pfam02782 79 LaavapAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1214520716 412 VKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLA 449
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-493 |
3.51e-51 |
|
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: 181.58 E-value: 3.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFN-KKGEIVHSAQKEFTQHF--PKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITN 80
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 81 QRETAVVWDKTtGKPIYNAIVW-------QSRQTAEICDELKE---KGYGEMVRektgllIDAYFSgtKVKWILDNVEGA 150
Cdd:cd07781 81 TSSTVVPVDED-GNPLAPAILWmdhraqeEAAEINETAHPALEyylAYYGGVYS------SEWMWP--KALWLKRNAPEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 151 REKA----ENGDllfgtidtWLVWKLSGG-KAHVtdySNASRTLMFNIHDLQWDDELL-----DMLTVPKSMLPEVRPSS 220
Cdd:cd07781 152 YDAAytivEACD--------WINARLTGRwVRSR---CAAGHKWMYNEWGGGPPREFLaaldpGLLKLREKLPGEVVPVG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 221 EVYG-------ETIDYHffgQNVPIAGVAGDQQAALFGQACFGEG-MAKNTyGT-GCFMLMNTGEKAVaseHGLlttiaW 291
Cdd:cd07781 221 EPAGtltaeaaERLGLP---AGIPVAQGGIDAHMGAIGAGVVEPGtLALIM-GTsTCHLMVSPKPVDI---PGI-----C 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 292 GI-DGKVN---YALEGSIFVAGSAIQWLRDGMRMFKDASESEVY------ASRVE-STDGVYVVPAFVGLGTPYWDSEVR 360
Cdd:cd07781 289 GPvPDAVVpglYGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIYallseeAAKLPpGESGLVALDWFNGNRTPLVDPRLR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 361 GAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAMEaDSGIELKTLRVDGG-AVKNNFLMKFQSDILDVPVERPVINETTA 439
Cdd:cd07781 369 GAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGiAEKNPLWMQIYADVLGRPIKVPKSDQAPA 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1214520716 440 LGAAYLAGLAVGYWKNQDEIKEQW-HMDKRFEPTMEA-ETSEELYAGWKKAIEATK 493
Cdd:cd07781 448 LGAAILAAVAAGVYADIEEAADAMvRVDRVYEPDPENhAVYEELYALYKELYDALG 503
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-485 |
2.24e-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: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFtQH--FPK-PGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITN 80
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREW-RHkeVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 81 QRETAVVWDKtTGKPIYNAIVWQSRQTAEIcDELKEKGYG--EMVREKTG--LLIDAyfsGTKVKWILDNVEGAREKAEN 156
Cdd:cd07775 80 MREGIVLYDN-EGEEIWACANVDARAAEEV-SELKELYNTleEEVYRISGqtFALGA---IPRLLWLKNNRPEIYRKAAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 157 gdllFGTIDTWLVWKLSGgkAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGE-TIDYHF---F 232
Cdd:cd07775 155 ----ITMLSDWIAYKLSG--ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKvTKEAAEetgL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 233 GQNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVaSEHGLLTTIAWGIDGKVNYalEGSIFVAGSAI 312
Cdd:cd07775 229 KEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVT-DPAMNIRVNCHVIPDMWQA--EGISFFPGLVM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 313 QWLRDGM---------RMFKDA-SESEVYASRVEStdGVYVV-----------------PAFVGLGTpywDSEvrgaifg 365
Cdd:cd07775 306 RWFRDAFcaeekeiaeRLGIDAyDLLEEMAKDVPP--GSYGImpifsdvmnyknwrhaaPSFLNLDI---DPE------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 366 vtrGTTKEHFIRATLESLAYQTKDVLCAMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYL 445
Cdd:cd07775 374 ---KCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIA 450
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1214520716 446 AGLAVGYWKNQDEIKEQW-HMDKRFEPTME-AETSEELYAGW 485
Cdd:cd07775 451 AGVGAGIYSSLEEAVESLvKWEREYLPNPEnHEVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
4-451 |
2.92e-43 |
|
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: 158.94 E-value: 2.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRE 83
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKtTGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWILDNvegAREKAENGDLLFGT 163
Cdd:cd24121 81 GTWLVDE-DGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERARTALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDtWLVWKLSGgkAHVTDYSNASRTlMFNIHDLQWDDELLDMLTVP--KSMLPEVRPSSEVYGETIDYHFFGQNVPiAG- 240
Cdd:cd24121 157 KD-WLFYKLTG--EIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLP-AGt 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 241 -VAgdqqAALFGQACFGEGMAKNTYGTGCFMLMNTG--EKAVASEH----GLLTTIAWGIDGKV-------------NYA 300
Cdd:cd24121 232 pVV----LGPFDVVATALGSGAIEPGDACSILGTTGvhEVVVDEPDlepeGVGYTICLGVPGRWlramanmagtpnlDWF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 301 LEgsIFVAGSAIQWLRDGMRMFKDAsESEVYASRVeSTDGV----YVVPAfvGLGTPYWDSEVRGAIFGVTRGTTKEHFI 376
Cdd:cd24121 308 LR--ELGEVLKEGAEPAGSDLFQDL-EELAASSPP-GAEGVlyhpYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1214520716 377 RATLESLAYQTKDVLCAMeadsGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVG 451
Cdd:cd24121 382 RAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-446 |
4.58e-41 |
|
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: 152.76 E-value: 4.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFN-KKGEIVHSAQKEFTQHFPK--PGWVEHNAQEIWGSILAVIATCLSEADvkpEQIAGIGITN 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEAVRNLIDELPREYL---SDVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 81 QRETAVVWDKTtGKPIYNAIVWQSRQTAEICDElKEKGYGEMVREKTGLLIDAYFSGTKVKWIldnvegarekAENGDLL 160
Cdd:cd07777 78 QMHGIVLWDED-GNPVSPLITWQDQRCSEEFLG-GLSTYGEELLPKSGMRLKPGYGLATLFWL----------LRNGPLP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 161 -----FGTIDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETIdyHFFGQN 235
Cdd:cd07777 146 skadrAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLS--SALPKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 236 VPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTgEKAVASEH---------GLLTTIAwGIDGKVNYAlegsIF 306
Cdd:cd07777 224 IPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLT-PKFELSGSveirpffdgRYLLVAA-SLPGGRALA----VL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 307 VagsaiQWLRDGMRMF-KDASESEVY-----ASRVESTDGVYVVPAFvgLGTPyWDSEVRGAIFGVTRGTTK-EHFIRAT 379
Cdd:cd07777 298 V-----DFLREWLRELgGSLSDDEIWekldeLAESEESSDLSVDPTF--FGER-HDPEGRGSITNIGESNFTlGNLFRAL 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1214520716 380 LESLAyqtkDVLCAM---EADSGIELKTLRVDGGAV-KNNFLMKFQSDILDVPVERPVINETTALGAAYLA 446
Cdd:cd07777 370 CRGIA----ENLHEMlprLDLDLSGIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
4-481 |
7.81e-31 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 124.37 E-value: 7.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAqkeFTQHFPKPGwVEHNAQEIWG--SILAVIATCLSE--ADVKPEQIAGIGIT 79
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVARA---STPNASDIA-AENSDWHQWSldAILQRFADCCRQinSELTECHIRGITVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 80 NQRETAVVWDKTtGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGllIDAYFSGT--KVKWILDNVEGAREKAENg 157
Cdd:PRK10331 79 TFGVDGALVDKQ-GNLLYPIISWKCPRTAAVMENIERYISAQQLQQISG--VGAFSFNTlyKLVWLKENHPQLLEQAHA- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 158 dLLFgtIDTWLVWKLSGGKAhvTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYG----ETIDYHFFG 233
Cdd:PRK10331 155 -WLF--ISSLINHRLTGEFT--TDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGtlqpSAAALLGLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 234 QNVPIAGVAGDQQAALFGQacfGEGMAKNTYGTGCF-MLMNTGEKAVAS----EHGLltTIAwgIDGKVNYALEGSIFVA 308
Cdd:PRK10331 230 VGIPVISAGHDTQFALFGS---GAGQNQPVLSSGTWeILMVRSAQVDTSllsqYAGS--TCE--LDSQSGLYNPGMQWLA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 309 GSAIQWLRDgmRMFkdaSESEVYASRVES-------TDGVYVVPAFVGLGTpywdsevrGAIFGVTRGTTKEHFIRATLE 381
Cdd:PRK10331 303 SGVLEWVRK--LFW---TAETPYQTMIEEaraippgADGVKMQCDLLACQN--------AGWQGVTLNTTRGHFYRAALE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 382 SLAYQTKDVLCAMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKE 461
Cdd:PRK10331 370 GLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARA 449
|
490 500
....*....|....*....|.
gi 1214520716 462 QWHMD-KRFEPTMEAETSEEL 481
Cdd:PRK10331 450 QMKYQyRYFYPQTEPEFIEEV 470
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-488 |
5.80e-27 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 113.95 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 1 MKKYILSLDQGTTSSRAILFNKKGEIVHSAQKEFTqHFPK---PGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIG 77
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWR-HLAVpdvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 78 ITNQRETAVVWDKtTGKPIYNAIVWQSRQTAEIcDELKE--KGYGEMVREKTG--LLIDAYfsgTKVKWILDNVEGAREK 153
Cdd:PRK10939 80 ATSMREGIVLYDR-NGTEIWACANVDARASREV-SELKElhNNFEEEVYRCSGqtLALGAL---PRLLWLAHHRPDIYRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 154 AENgdllFGTIDTWLVWKLSGGKAhvTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETIDYHF-- 231
Cdd:PRK10939 155 AHT----ITMISDWIAYMLSGELA--VDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAae 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 232 --FGQNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLlttiawgidgKVNYAL-------E 302
Cdd:PRK10939 229 tgLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNI----------RINPHVipgmvqaE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 303 GSIFVAGSAIQWLRDGM---------RMFKDASES-EVYASRVEStdGVYVV-----------------PAFVGLGTpyw 355
Cdd:PRK10939 299 SISFFTGLTMRWFRDAFcaeekllaeRLGIDAYSLlEEMASRVPV--GSHGIipifsdvmrfkswyhaaPSFINLSI--- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 356 DSEV--RGAIFgvtrgttkehfiRATLESLAYQTKDVLCAMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPV 433
Cdd:PRK10939 374 DPEKcnKATLF------------RALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1214520716 434 INETTALGAAYLAGLAVGYWKNQDEIKEQW-HMDKRFEPTME-AETSEELYAGWKKA 488
Cdd:PRK10939 442 VKEATALGCAIAAGVGAGIYSSLAETGERLvRWERTFEPNPEnHELYQEAKEKWQAV 498
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
4-471 |
1.71e-26 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 111.98 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YIlSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKpeQIAGIGITNQRE 83
Cdd:PRK15027 2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 TAVVWDKTTgKPIYNAIVWQSRQTAEICDELKEKgyGEMVREKTGLLIDAYFSGTKVKWIldnvegAREKAEngdlLFGT 163
Cdd:PRK15027 79 GATLLDAQQ-RVLRPAILWNDGRCAQECALLEAR--VPQSRVITGNLMMPGFTAPKLLWV------QRHEPE----IFRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 164 IDT------WLVWKLSGGKAhvTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETID--YHFFGQ- 234
Cdd:PRK15027 146 IDKvllpkdYLRLRMTGEFA--SDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPevAKAWGMa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 235 NVPIAGVAGDQQAALFGQACFGEGMAKNTYGT-GCFMLMNTG-----EKAVASE-HGLlttiawgiDGKvnYALEGSIFV 307
Cdd:PRK15027 224 TVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSFcHAL--------PQR--WHLMSVMLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 308 AGSAIQW------LRDGMRMFKDASESEvyasrvESTDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLE 381
Cdd:PRK15027 294 AASCLDWaakltgLSNVPALIAAAQQAD------ESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 382 SLAYQTKDVLCAMEAdSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVE-RPVINETTALGAAYLAGLAVGYWKNQDEIK 460
Cdd:PRK15027 368 GVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRTGGDVGPALGAARLAQIAANPEKSLIELL 446
|
490
....*....|.
gi 1214520716 461 EQWHMDKRFEP 471
Cdd:PRK15027 447 PQLPLEQSHLP 457
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-472 |
6.62e-26 |
|
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: 110.70 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITnqre 83
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 84 tA----VVWDKT--------TGKPIYNAIVWQ----SRQTAEIcdelkEKGYGEMVRektgllidaYFSGT--------K 139
Cdd:cd07782 77 -AtcslVVLDAEgkpvsvspSGDDERNVILWMdhraVEEAERI-----NATGHEVLK---------YVGGKispemeppK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 140 VKWILDNVEGAREKAENgdlLFGTIDtWLVWKLSGGKAHvtdySNASRT-----LMFNIHDLQWDDELL------DMLTV 208
Cdd:cd07782 142 LLWLKENLPETWAKAGH---FFDLPD-FLTWKATGSLTR----SLCSLVckwtyLAHEGSEGGWDDDFFkeigleDLVED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 209 PKSMLPE-VRPSSEVYGET---------------------IDYHffgqnvpiAGVAGDQQAALFGQACFGEGMAKN---T 263
Cdd:cd07782 214 NFAKIGSvVLPPGEPVGGGltaeaakelglpegtpvgvslIDAH--------AGGLGTLGADVGGLPCEADPLTRRlalI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 264 YGTG-CFMLMntgekavaSEHGLLTTIAWG------IDGKvnYALEGSIFVAGSAIQWLRDGMRMFKDASES-------- 328
Cdd:cd07782 286 CGTSsCHMAV--------SPEPVFVPGVWGpyysamLPGL--WLNEGGQSATGALLDHIIETHPAYPELKEEakaagksi 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 329 -EVYASRVES------------TDGVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIR---ATLESLAYQTKDVLC 392
Cdd:cd07782 356 yEYLNERLEQlaeekglplaylTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 393 AMEAdSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKN-QDEIKEQWHMDKRFEP 471
Cdd:cd07782 436 AMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSlWDAMAAMSGPGKVVEP 514
|
.
gi 1214520716 472 T 472
Cdd:cd07782 515 N 515
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-479 |
6.65e-24 |
|
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: 104.63 E-value: 6.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFN-KKGEIVHSAQKEFTQ-HFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQ 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 82 RETAVVWDKTT-------GKPIYNAIVWQSRQTAEICDELKEKGYgEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKA 154
Cdd:cd07768 81 CSLAIFDREGTplmalipYPNEDNVIFWMDHSAVNEAQWINMQCP-QQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 155 engDLLFGTIDtWLVWKLSGgkahvtDYSNASRTLM----FNIHDLQWDDE------LLDMLTVPKSMLPEVRPSSEVYG 224
Cdd:cd07768 160 ---FHIFDLHD-YIAYELTR------LYEWNICGLLgkenLDGEESGWSSSffknidPRLEHLTTTKNLPSNVPIGTTSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 225 ETIDYHF--FGQNVPIAGVAG--DQQAALFGqacfgegMAKNTYGTGCFMLMNTgekavASEHGLLTTIAW---GIDGKV 297
Cdd:cd07768 230 VALPEMAekMGLHPGTAVVVSciDAHASWFA-------VASPHLETSLFMIAGT-----SSCHMYGTTISDripGVWGPF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 298 NYALEGSIFV-------AGSAIQWLRDG---MRMFKDASE--SEVYASRVES----------TDGVYVVPAFVGLGTPYW 355
Cdd:cd07768 298 DTIIDPDYSVyeagqsaTGKLIEHLFEShpcARKFDEALKkgADIYQVLEQTirqieknnglSIHILTLDMFFGNRSEFA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 356 DSEVRGAIFGVTRGTTKEHF---IRATLESLAYQTKDVLCAMEADsGIELKTLRVDGGAVKNNFLMKFQSDILDVPVERP 432
Cdd:cd07768 378 DPRLKGSFIGESLDTSMLNLtykYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAIIKP 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1214520716 433 VINETTALGAAYLAGLAVGYWKNQDEIKEQWHMDKRFEPTMEAETSE 479
Cdd:cd07768 457 KENMMGILGAAVLAKVAAGKKQLADSITEADISNDRKSETFEPLAYR 503
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
4-461 |
2.68e-21 |
|
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: 96.44 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAIL--FNKKG---EIVHSaqkeftqhFPKPG--------WvehNAQEIWGSILAVIATCLSEADvkp 70
Cdd:cd07771 1 NYLAVDLGASSGRVILgsLDGGKlelEEIHR--------FPNRPveinghlyW---DIDRLFDEIKEGLKKAAEQGG--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 71 eQIAGIGITnqreTavvW-------DKTtGKPIYNAIVWQSRQTAEICDELKEKGYGEMVREKTGLLIDAYFSGTKVKWI 143
Cdd:cd07771 67 -DIDSIGID----T---WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 144 ldnvegarekAENGDLLFGTIDTWL------VWKLSGGKahVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVR 217
Cdd:cd07771 138 ----------KKEGPELLERADKLLmlpdllNYLLTGEK--VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 218 PSSEVYG---ETIDYHFFGQNVPIAGVAG-DQQAALFGQACFGEGMAkntY---GTGCFMLMNTgEKAVASEHGLLTTIA 290
Cdd:cd07771 206 PPGTVLGtlkPEVAEELGLKGIPVIAVAShDTASAVAAVPAEDEDAA---FissGTWSLIGVEL-DEPVITEEAFEAGFT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 291 --WGIDGKVNYA--LEGSIFVAGSAIQWLRDGMR-----MFKDASESEVYASRVESTDGVYVVPAFVglgtpywDSEVRG 361
Cdd:cd07771 282 neGGADGTIRLLknITGLWLLQECRREWEEEGKDysydeLVALAEEAPPFGAFIDPDDPRFLNPGDM-------PEAIRA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 362 AI--FGVTRGTTKEHFIRATLESLAYQTKDVLCAMEADSGIELKTLRVDGGAVKNNFLMKFQSDILDVPVER-PVinETT 438
Cdd:cd07771 355 YCreTGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAgPV--EAT 432
|
490 500
....*....|....*....|...
gi 1214520716 439 ALGAAYLAGLAVGYWKNQDEIKE 461
Cdd:cd07771 433 AIGNLLVQLIALGEIKSLEEGRE 455
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
4-484 |
1.96e-16 |
|
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: 81.84 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFP----KPGWVEHNAQEI-------WGSILAVIATCLSEADVKPEQ 72
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPeygtKGGVHRDGDGGEvtspvlmWVEALDLLLEKLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 73 IAGIGITNQRETAVVWDKTTGKPIYN-------------------AIVWQSRQTAEICDELKEK--GYGEMVReKTGllI 131
Cdd:cd07776 81 VKAISGSGQQHGSVYWSKGAESALANldpskslaeqlegafsvpdSPIWMDSSTTKQCRELEKAvgGPEALAK-LTG--S 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 132 DAY--FSGTKVKWILDNVEGAREKAENGDLL--FGTidTWLVWKLSGgkahvTDYSNASRTLMFNIHDLQWDDELLDMLT 207
Cdd:cd07776 158 RAYerFTGPQIAKIAQTDPEAYENTERISLVssFLA--SLLLGRYAP-----IDESDGSGMNLMDIRSRKWSPELLDAAT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 208 VP--KSMLPEVRPSSEVYGETIDYHF----FGQNVPIAGVAGDQQAALFGQACfGEGMAKNTYGTG--CFMLMNTGEKav 279
Cdd:cd07776 231 APdlKEKLGELVPSSTVAGGISSYFVerygFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTSdtVFLVLDEPKP-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 280 asehgllttiawGIDGKV--NYALEGSIFVA-----GS-AIQWLRDgmrmfKDASES-EVYASRVEST----DGVyvvpa 346
Cdd:cd07776 308 ------------GPEGHVfaNPVDPGSYMAMlcyknGSlARERVRD-----RYAGGSwEKFNELLESTppgnNGN----- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 347 fvgLGTPYWDSE----------VRGAIFGVTRGTTKEHFIRATLE----SLAYQTKDVLcameadSGIELKTLRVDGGAV 412
Cdd:cd07776 366 ---LGLYFDEPEitppvpgggrRFFGDDGVDAFFDPAVEVRAVVEsqflSMRLHAERLG------SDIPPTRILATGGAS 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1214520716 413 KNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNQDEIKEQWHMDKRF-----EPTMEAetsEELYAG 484
Cdd:cd07776 437 ANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAEEpklvaEPDPEA---AEVYDK 510
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-487 |
2.06e-14 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 75.65 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 1 MKKYILSLDQGTTSSRAILFN-KKGEIVHSAQKEFTQHF------PKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQI 73
Cdd:PRK04123 1 MMAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWVkgryldLPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 74 AGIGITNQRETAVVWDKTtGKPIY---------NAIV--W-------QSRQTAEICDELKEKGYGEmvrektgllidaYF 135
Cdd:PRK04123 81 VGIGVDFTGSTPAPVDAD-GTPLAllpefaenpHAMVklWkdhtaqeEAEEINRLAHERGEADLSR------------YI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 136 SGT--------KVKWILDNVEGAREKA----ENGDllfgtidtWLVWKLSGGkahvtdysNASRTLMFNI----HDLQWD 199
Cdd:PRK04123 148 GGIyssewfwaKILHVLREDPAVYEAAaswvEACD--------WVVALLTGT--------TDPQDIVRSRcaagHKALWH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 200 D--------ELLDML------TVPKSMLPEVRPSSEVYGE-TIDY-HFFG--QNVPIAGVAGDQQAALFGQACfGEGMAK 261
Cdd:PRK04123 212 EswgglpsaDFFDALdpllarGLRDKLFTETWTAGEPAGTlTAEWaQRLGlpEGVAVSVGAFDAHMGAVGAGA-EPGTLV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 262 NTYGTG-CFMLMNTGEKAVAsehgllttiawGIDGKVnyalEGSI------FVAG-SAI----QWLRD------------ 317
Cdd:PRK04123 291 KVMGTStCDILLADKQRAVP-----------GICGQV----DGSIvpgligYEAGqSAVgdifAWFARllvppeykdeae 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 318 --GMRMFKDASESevyASRVESTD-GVYVVPAFVGLGTPYWDSEVRGAIFGVTRGTTKEHFIRATLESLAYQTKDVLCAM 394
Cdd:PRK04123 356 arGKQLLELLTEA---AAKQPPGEhGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 395 EaDSGIELKTLRVDGG-AVKNNFLMKFQSDILDVPVERPVINETTALGAAYLAGLAVGYWKNqdeIKE-QWHM----DKR 468
Cdd:PRK04123 433 E-DQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPD---IPEaQQAMaspvEKT 508
|
570 580
....*....|....*....|
gi 1214520716 469 FEPTME-AETSEELYAGWKK 487
Cdd:PRK04123 509 YQPDPEnVARYEQLYQEYKQ 528
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
6-446 |
4.44e-09 |
|
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: 58.57 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 6 LSLDQGTTSSRAILFNKKGEIVHSAQKE--FTQHFPKPGWVEHNAQEIWGSILaviaTCLSEADVKPEQ--IAGIGIT-- 79
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLATSERPisYKQDPKDLWFVTQSSTEIWKAIK----TALKELIEELSDyiVSGIGVSat 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 80 -----NQRETA--------VVWDKTTgkPIYNAIVWQSRQTAEICDELkekgygEMVREKTGLLidaYFSGT-------- 138
Cdd:cd07778 79 csmvvMQRDSDtsylvpynVIHEKSN--PDQDIIFWMDHRASEETQWL------NNILPDDILD---YLGGGfipemaip 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 139 KVKWILDNVEGAREKaengDLLFGTIDTWLVWKLSGGKAHVTD-YSNAS-RTLMFNIHDLQ-WDDELLDmlTVPKSMLPE 215
Cdd:cd07778 148 KLKYLIDLIKEDTFK----KLEVFDLHDWISYMLATNLGHSNIvPVNAPpSIGIGIDGSLKgWSKDFYS--KLKISTKVC 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 216 VRPSSEVYGETIDYhfFGQ-----NVPIAGVAG------------DQQAALFGQACfGEGMAKNTY----GTG-CFMLMN 273
Cdd:cd07778 222 NVGNTFKEAPPLPY--AGIpigkvNVILASYLGidkstvvghgciDCYAGWFSTFA-AAKTLDTTLfmvaGTStCFLYAT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 274 TgekavASEHGLLTTIaWG-----IDGKVNYalEGSIFVAG-----------SAIQWLRDGMRMFKDASESEVYASRVES 337
Cdd:cd07778 299 S-----SSQVGPIPGI-WGpfdqlLKNYSVY--EGGQSATGklieklfnshpAIIELLKSDANFFETVEEKIDKYERLLG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 338 TDGVYVVPAFVGLG------TPYWDSEVRGAIFGVTRGTTKE----HFIrATLESLAYQTKDVLCAMEaDSGIELKTLRV 407
Cdd:cd07778 371 QSIHYLTRHMFFYGdylgnrTPYNDPNMSGSFIGESTDSSLTdlvlKYI-LILEFLAFQTKLIIDNFQ-KEKIIIQKVVI 448
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1214520716 408 DGGAVKNNFLMKFQSDILDVP---VERPVINETTALGAAYLA 446
Cdd:cd07778 449 SGSQAKNARLLQLLSTVLSKIhiiVPLSDSKYAVVKGAALLG 490
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
5-446 |
3.05e-07 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 52.65 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 5 ILSLDQGTTSSRAILFNKKGEIVHSAQKEFTqHFPKPGWVEHNAQEIWGSILAVIATCLSEAdvkpeQIAGIGITNQRET 84
Cdd:cd07772 2 IAVFDIGKTNKKLLLFDENGEVLAERSTPNP-EIEEDGYPCEDVEAIWEWLLDSLAELAKRH-----RIDAINFTTHGAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 85 AVVWDKTtGK---PIYNaivwqsrQTAEICDELKEKGYGEM-VREKTG--LLIDAYFSGTKVKWIldnvegAREKAEngd 158
Cdd:cd07772 76 FALLDEN-GElalPVYD-------YEKPIPDEINEAYYAERgPFEETGspPLPGGLNLGKQLYWL------KREKPE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 159 lLFGTIDTWL------VWKLSGGKahVTDYSNAS-RTLMFNIHDLQWDDELLDMLTvpKSMLPEVRPSSEVYG----ETI 227
Cdd:cd07772 139 -LFARAKTILplpqywAWRLTGKA--ASEITSLGcHTDLWDFEKNEYSSLVKKEGW--DKLFPPLRKAWEVLGplrpDLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 228 DYHFFGQNVPI-AGVAgDQQAALFG-QACFGEGMAKNTYGTGCfMLMNTGEKAVASEHGLLTTIAWGID--GKVnyaLEG 303
Cdd:cd07772 214 RRTGLPKDIPVgCGIH-DSNAALLPyLAAGKEPFTLLSTGTWC-IAMNPGNDLPLTELDLARDCLYNLDvfGRP---VKT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 304 SIFVAGSAIQWLRDGMRMFKDASESEVYASRVEStDGVYVVPAFVGLGTPYwdSEVRGAIFGVTRGTTKEHFIRATLeSL 383
Cdd:cd07772 289 ARFMGGREYERLVERIAKSFPQLPSLADLAKLLA-RGTFALPSFAPGGGPF--PGSGGRGVLSAFPSAEEAYALAIL-YL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1214520716 384 AYQTKDVLCAMEADSGielkTLRVDGGAVKNNFLMKFQSDIL-DVPVERPVINETTALGAAYLA 446
Cdd:cd07772 365 ALMTDYALDLLGSGVG----RIIVEGGFAKNPVFLRLLAALRpDQPVYLSDDSEGTALGAALLA 424
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
181-242 |
3.95e-05 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 45.87 E-value: 3.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1214520716 181 DYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETIDYHffGQNVPIAGVA 242
Cdd:PRK10640 157 EYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQ--GNEIPVVAVA 216
|
|
| ASKHA_NBD_GspK-like |
cd24082 |
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
4-83 |
5.73e-03 |
|
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar.
Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 38.67 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214520716 4 YILSLDQGTTSSRAILFNKKGEIVHSAQKeftqhfpKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQ---------IA 74
Cdd:cd24082 1 YFIGIDGGGTKCRARLADADGTVLGEATG-------GPANLSSDLDQAWASILAAIKQALAQAGLDAAAlsdlhaglgLA 73
|
....*....
gi 1214520716 75 GIGITNQRE 83
Cdd:cd24082 74 GANVPEARA 82
|
|
| |
