|
Name |
Accession |
Description |
Interval |
E-value |
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-498 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 1025.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 1 MVEDKYIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGI 80
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 81 TNQRETTIIWEKETGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKGE 160
Cdd:PRK00047 81 TNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 161 LLFGTIDSWLVWKLTDGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYHFFGSKVPI 240
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGEVPI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 241 SGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGYGINGKIYYALEGSIFVAGSSIQWLRDG 320
Cdd:PRK00047 241 AGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 321 LHMIENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEADT 400
Cdd:PRK00047 321 LKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 401 GINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIREFYALGDMFEADMDAGRR 480
Cdd:PRK00047 401 GIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEER 480
|
490
....*....|....*...
gi 2467962001 481 EDLYKGWKRAVKATRLFA 498
Cdd:PRK00047 481 EKLYAGWKKAVKRTLAWA 498
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
5-498 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 961.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 5 KYIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQR 84
Cdd:COG0554 3 KYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 85 ETTIIWEKETGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKGELLFG 164
Cdd:COG0554 83 ETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELLFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 165 TIDSWLVWKLTDGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAyHFFGSKVPISGMA 244
Cdd:COG0554 163 TIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDP-DLFGAEIPIAGIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 245 GDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGYGINGKIYYALEGSIFVAGSSIQWLRDGLHMI 324
Cdd:COG0554 242 GDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLGLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 325 ENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEADTGINI 404
Cdd:COG0554 322 DSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 405 PVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIREFYALGDMFEADMDAGRREDLY 484
Cdd:COG0554 402 KELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERERLY 481
|
490
....*....|....
gi 2467962001 485 KGWKRAVKATRLFA 498
Cdd:COG0554 482 AGWKKAVERTLGWA 495
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
6-492 |
0e+00 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 918.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKETGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKGELLFGT 165
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDSWLVWKLTDGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYhFFGSKVPISGMAG 245
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPD-LLGAEIPIAGIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 246 DQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGYGINGKIYYALEGSIFVAGSSIQWLRDGLHMIE 325
Cdd:cd07786 240 DQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 326 NSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEADTGINIP 405
Cdd:cd07786 320 SAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 406 VLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIREFYALGDMFEADMDAGRREDLYK 485
Cdd:cd07786 400 ELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYA 479
|
....*..
gi 2467962001 486 GWKRAVK 492
Cdd:cd07786 480 GWKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
6-492 |
0e+00 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 898.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKETGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKGELLFGT 165
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDSWLVWKLTDGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYHFfGSKVPISGMAG 245
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGL-GAGIPIAGILG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 246 DQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGYGINGKIYYALEGSIFVAGSSIQWLRDGLHMIE 325
Cdd:cd07769 240 DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 326 NSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEADTGINIP 405
Cdd:cd07769 320 DAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 406 VLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIREFYALGDMFEADMDAGRREDLYK 485
Cdd:cd07769 400 ELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYR 479
|
....*..
gi 2467962001 486 GWKRAVK 492
Cdd:cd07769 480 GWKKAVE 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
5-495 |
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: 829.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 5 KYIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQR 84
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 85 ETTIIWEKETGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKGELLFG 164
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 165 TIDSWLVWKLTDGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYhFFGSKVPISGMA 244
Cdd:TIGR01311 161 TIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPG-LLGAEIPITGVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 245 GDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGYGINGKIY-YALEGSIFVAGSSIQWLRDGLHM 323
Cdd:TIGR01311 240 GDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPvYALEGSVFVAGAAVQWLRDNLKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 324 IENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEADTGIN 403
Cdd:TIGR01311 320 IKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 404 IPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIREFYALGDMFEADMDAGRREDL 483
Cdd:TIGR01311 400 ITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREAR 479
|
490
....*....|..
gi 2467962001 484 YKGWKRAVKATR 495
Cdd:TIGR01311 480 YAGWKEAVKRSL 491
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-492 |
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: 687.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 5 KYIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAG---SFIESGIKPDQIAGIGIT 81
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEaveKLKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 82 NQRETTIIWEKETGRPIYNAIVWQSRQSAGIANQL--KKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKG 159
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELsaKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 160 ELLFGTIDSWLVWKLT---DGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYHFFGs 236
Cdd:cd07792 161 RLLFGTVDSWLIWNLTggkNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 237 kVPISGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGY--GINGKIYYALEGSIFVAGSSI 314
Cdd:cd07792 240 -VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYklGPDAPPVYALEGSIAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 315 QWLRDGLHMIENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIE 394
Cdd:cd07792 319 QWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 395 TMEADTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIREFYALG-DMFEA 473
Cdd:cd07792 399 AMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGrTVFEP 478
|
490
....*....|....*....
gi 2467962001 474 DMDAGRREDLYKGWKRAVK 492
Cdd:cd07792 479 QISEEERERRYKRWKKAVE 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
5-498 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 632.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 5 KYIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSF--IESGIKPDQIAGIGITN 82
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIkkLREKGPSFKIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 83 QRETTIIWEKETGRPIYNAIVWQSRQSAGIANQLKKDGY-EDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKGEL 161
Cdd:PTZ00294 82 QRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGgSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 162 LFGTIDSWLVWKLTDGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYHFFGSK-VPI 240
Cdd:PTZ00294 162 LFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPLLEgVPI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 241 SGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGY--GINGKIYYALEGSIFVAGSSIQWLR 318
Cdd:PTZ00294 242 TGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYqlGPNGPTVYALEGSIAVAGAGVEWLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 319 DGLHMIENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEA 398
Cdd:PTZ00294 322 DNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 399 DTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIREF-YALGDMFEADMDA 477
Cdd:PTZ00294 402 DAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLiRRSNSTFSPQMSA 481
|
490 500
....*....|....*....|.
gi 2467962001 478 GRREDLYKGWKRAVKATRLFA 498
Cdd:PTZ00294 482 EERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
6-494 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 574.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIK----PDQIAGIGIT 81
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKghnvDSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 82 NQRETTIIWEKETGRPIYNAIVWQSRQSAGIANQLKKD--GYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKG 159
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 160 ELLFGTIDSWLVWKLT---DGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETqAYHFFGS 236
Cdd:PLN02295 161 DALFGTIDSWLIWNLTggaSGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTI-AKGWPLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 237 KVPISGMAGDQQAALFGQMAfEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGY--GINGKIYYALEGSIFVAGSSI 314
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYklGPDAPTNYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 315 QWLRDGLHMIENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIE 394
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 395 TMEADTGINIP-----VLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEI-REFYALG 468
Cdd:PLN02295 399 AMRKDAGEEKShkglfLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFaSEKWKNT 478
|
490 500
....*....|....*....|....*.
gi 2467962001 469 DMFEADMDAGRREDLYKGWKRAVKAT 494
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 ... |
6-492 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 563.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKETGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFH-----------KKTGLVIDAY-----FSATKIRWILDNV 149
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRggskflhfltrNKRFLAASVLkfstaHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 150 EGAQERAEKGELLFGTIDSWLVWKLTDGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQ 229
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 230 AyHFFGSKVPISGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESPQYSDNKLLTTIGYGINGKIYYALEGSIFV 309
Cdd:cd07793 241 P-SIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 310 AGSSIQWLRDGLhMIENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQV 389
Cdd:cd07793 320 TGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 390 RDVIETMEADTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIREFYALGD 469
Cdd:cd07793 399 KQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEK 478
|
490 500
....*....|....*....|...
gi 2467962001 470 MFEADMDAGRREDLYKGWKRAVK 492
Cdd:cd07793 479 IFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-495 |
9.73e-110 |
|
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: 334.88 E-value: 9.73e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 5 KYIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQR 84
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 85 ETTIIWEKEtGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKgellFG 164
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK----VL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 165 TIDSWLVWKLTdgDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGET--QAYHFFG--SKVPI 240
Cdd:COG1070 156 LPKDYLRYRLT--GEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLtaEAAAETGlpAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 241 SGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTgESPQYSDNKLLTTIGYGINGKiyYALEGSIFVAGSSIQWLRDG 320
Cdd:COG1070 234 VAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR--WLPMGATNNGGSALRWFRDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 321 LHMIENSSDSE---AAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETME 397
Cdd:COG1070 311 FADGELDDYEElnaLAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 398 AdTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDE-IREFYALGDMFEADMD 476
Cdd:COG1070 391 E-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEaAAAMVRVGETIEPDPE 469
|
490 500
....*....|....*....|
gi 2467962001 477 AGRR-EDLYKGWKRAVKATR 495
Cdd:COG1070 470 NVAAyDELYERYRELYPALK 489
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
6-477 |
1.04e-106 |
|
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: 324.86 E-value: 1.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWQsrqsagianqlkkdgyedffhkktglvidayfsatkirwilDNvegaqeRAEKgellFGT 165
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQ-----------------------------------------DK------RTAK----FLT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDSWLVWKLTDgdVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGE--TQAYHFFG--SKVPIS 241
Cdd:cd07779 109 VQDYLLYRLTG--EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTltKEAAEETGlpEGTPVV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 242 GMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTgESPQYSDNKLLTTIGYGINGKiyYALEGSIFVAGSSIQWLRD-- 319
Cdd:cd07779 187 AGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAVPGK--WVLEGSINTGGSAVRWFRDef 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 320 -GLHMIENSSD-------SEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRD 391
Cdd:cd07779 264 gQDEVAEKELGvspyellNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 392 VIETMEaDTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDE-IREFYALGDM 470
Cdd:cd07779 344 NLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEaVKAMVRVTDT 422
|
....*..
gi 2467962001 471 FEADMDA 477
Cdd:cd07779 423 FEPDPEN 429
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
6-253 |
9.66e-104 |
|
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: 310.42 E-value: 9.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKETgRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKgellFGT 165
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHK----FLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDSWLVWKLTdgDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYHFFGS----KVPIS 241
Cdd:pfam00370 156 IHDYLRWRLT--GVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWgldeGVPVV 233
|
250
....*....|..
gi 2467962001 242 GMAGDQQAALFG 253
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-448 |
3.06e-103 |
|
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: 314.50 E-value: 3.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWqsrqsagianqlkkdgyedffhkktglvidayfsatkirwiLDNvegaqeRAekgelLFGT 165
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIW-----------------------------------------LDR------RA-----KFLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDSWLVWKLTDgdVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGET--QAYHFFG--SKVPIS 241
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVtpEAAEETGlpAGTPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 242 GMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGEsPQYSDnKLLTTIGYGINGKiyYALEGSIFVAGSSIQWLRDGL 321
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDE-PVPPD-PRLLNRCHVVPGL--WLLEGAINTGGASLRWFRDEF 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 322 H-----MIENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETM 396
Cdd:cd00366 262 GeeedsDAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2467962001 397 EADtGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLA 448
Cdd:cd00366 342 EEL-GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
6-453 |
2.12e-97 |
|
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: 301.43 E-value: 2.12e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGsfIESGIKPDQIAGIGITNQRE 85
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIRE--AAAQAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKgellFGT 165
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDSWLVWKLTDgdVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGET--QAYHFFG--SKVPIS 241
Cdd:cd07773 154 VADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVtpEAAEELGlpAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 242 gMAG-DQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGE-SPQYSDNKLLTTIGYGINGKiYYALEGSIfVAGSSIQWLRD 319
Cdd:cd07773 232 -VGGhDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEpPLDEMLAEGGLSYGHHVPGG-YYYLAGSL-PGGALLEWFRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 320 --GLHMIENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETME 397
Cdd:cd07773 309 lfGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALE 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2467962001 398 AdTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVG 453
Cdd:cd07773 389 K-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
6-490 |
8.90e-86 |
|
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: 272.49 E-value: 8.90e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWQSRQSAGIANQLKKDgYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKgeLLFGT 165
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRK--ILLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 iDsWLVWKLTdgDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGET--QAYHFFG--SKVPIS 241
Cdd:cd07808 157 -D-YLRYRLT--GELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLtpEAAEELGlpEGTPVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 242 GMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTgESPQYSDNKLLTTIGYGINGKiYYALeGSIFVAGSSIQWLRDgl 321
Cdd:cd07808 233 AGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGK-WYAM-GVTLSAGLSLRWLRD-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 322 hMIENSSDS-----EAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETM 396
Cdd:cd07808 308 -LFGPDRESfdeldAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 397 EaDTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEI-REFYALGDMFEADM 475
Cdd:cd07808 387 K-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAaAACIKIEKTIEPDP 465
|
490
....*....|....*.
gi 2467962001 476 DAGRR-EDLYKGWKRA 490
Cdd:cd07808 466 ERHEAyDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
6-459 |
1.04e-80 |
|
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: 259.03 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFieSGIKPDQIAGIGITnqre 85
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVL--AKLGGGEVDAIGFS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 T---TIIWEKETGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKgell 162
Cdd:cd07770 75 SamhSLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 163 FGTIDSWLVWKLTdGDvHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYG----ETQAYHFFGSKV 238
Cdd:cd07770 151 FVSIKEYLLYRLT-GE-LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPglkpEFAERLGLLAGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 239 P-ISGmAGDQQAALFGQMAFEPGMVKNTYGT-GSFIVMntGESPQYSDNKLLTTigygingkiYYALEGSIFV------A 310
Cdd:cd07770 229 PvVLG-ASDGALANLGSGALDPGRAALTVGTsGAIRVV--SDRPVLDPPGRLWC---------YRLDENRWLVggainnG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 311 GSSIQWLRDGLHMIENSSD--SEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQ 388
Cdd:cd07770 297 GNVLDWLRDTLLLSGDDYEelDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFN 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2467962001 389 VRDVIETMEaDTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDID 459
Cdd:cd07770 377 LKSIYEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLE 446
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-488 |
7.04e-80 |
|
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: 257.06 E-value: 7.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWQSRQSAGIANQL-KKDGYEDFFHKKTGLVIDAYFSATKIRWILDNvegAQERAEKGELLFG 164
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIaGGLGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 165 TIDsWLVWKLTdgDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGE--TQAYHFFG--SKVPI 240
Cdd:cd07805 157 AKD-YLNFRLT--GRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGEltPEAAAELGlpAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 241 SGMAGDQQAALFGQMAFEPGMVkNTY-GTGSFIVMNTgESPQYSDNKLLTTIGYGINGKIYYAleGSIFVAGSSIQWLRD 319
Cdd:cd07805 234 VGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHV-PKPKTDPDHGIFTLASADPGRYLLA--AEQETAGGALEWARD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 320 GLHMIENSSDS------EAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVI 393
Cdd:cd07805 310 NLGGDEDLGADdyelldELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 394 ETMEADTGiNIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNL-ETTALGAAFLAGLAVGYWKDIDEIREFYALGDMFE 472
Cdd:cd07805 390 EALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFE 468
|
490
....*....|....*..
gi 2467962001 473 ADMD-AGRREDLYKGWK 488
Cdd:cd07805 469 PDPEnRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-453 |
9.04e-77 |
|
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: 248.21 E-value: 9.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKgellFGT 165
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRK----FLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDSWLVWKLTdgDVHVTDYSNASRTM-LFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGET--QAYHFFGSK--VPI 240
Cdd:cd07804 156 AYDYIVYKLT--GEYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVtkEAAEETGLAegTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 241 SGMAGDQQAALFGQMAFEPG--MVKntYGT-GSFIVMNtgESPQYSDNKLLTTigYGINGKiyYALEGSIFVAGSSIQWL 317
Cdd:cd07804 234 VAGTVDAAASALSAGVVEPGdlLLM--LGTaGDIGVVT--DKLPTDPRLWLDY--HDIPGT--YVLNGGMATSGSLLRWF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 318 RDGL-----HMIENSSDS------EAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIA 386
Cdd:cd07804 306 RDEFageevEAEKSGGDSaydlldEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467962001 387 YQVRDVIETMEADtGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVG 453
Cdd:cd07804 386 YGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
6-452 |
2.55e-59 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 201.68 E-value: 2.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFieSGIKPDQIAGIGITNQRE 85
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELP--AELRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWQSRQSAGIANQLKKDGyeDFFHKKTGLVIDAYFSATKIRWILDNVEGAQERAEKgeLLFGT 165
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAA--GAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAK--FLHQA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 iDsWLVWKLTdGDVHVTDYSNASRTmLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQ---AYHF-FGSKVPI- 240
Cdd:cd07783 154 -D-WLAGRLT-GDRGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTaeaAEELgLPAGTPVv 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 241 SGMAgDQQAALFGQMAFEPGmvkntygtGSFIVMNTGESPqysdnKLLTT-----IGYGIN----GKIYYALEGSIFVAG 311
Cdd:cd07783 230 AGTT-DSIAAFLASGAVRPG--------DAVTSLGTTLVL-----KLLSDkrvpdPGGGVYshrhGDGYWLVGGASNTGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 312 SSIQWLRDGLhmIENSSDSEAAAKKSTnddEVYVVPaFVGLG--APYWDQEARGsmFGLTRGTSDNDIVKATLQSIAYQV 389
Cdd:cd07783 296 AVLRWFFSDD--ELAELSAQADPPGPS---GLIYYP-LPLRGerFPFWDPDARG--FLLPRPHDRAEFLRALLEGIAFIE 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467962001 390 RDVIETMEADTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNlETTALGAAFLAGLAV 452
Cdd:cd07783 368 RLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
6-453 |
3.92e-59 |
|
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: 201.63 E-value: 3.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNvegAQERAEKGELLFGT 165
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKEN---EPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDsWLVWKLTdgDVHVTDYSNASrTMLFNINDLKWDQEILDLLNIPVAM--LPRVASNSEIYGETQAyhffgsKV----- 238
Cdd:cd07802 157 KD-WIRYRLT--GEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEELKdkLPPLVPSTEIAGRVTA------EAaaltg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 239 -----PISGMAGDQQAALFGQMAFEPGMVKNTYGTGSfivMNTGESPQYSDNKLLTTIGYGINGKIYYALEGSifVAGSS 313
Cdd:cd07802 227 lpegtPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVVTDEPVVPDSVGSNSLHADPGLYLIVEAS--PTSAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 314 -IQWLRD--GLHMIENSSDS-----EAAAKKSTNDDEVYVVPaFVgLGAPYwDQEARGSMFGLTRGTSDNDIVKATLQSI 385
Cdd:cd07802 302 nLDWFLDtlLGEEKEAGGSDydeldELIAAVPPGSSGVIFLP-YL-YGSGA-NPNARGGFFGLTAWHTRAHLLRAVYEGI 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2467962001 386 AYQVRDVIETMeaDTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVG 453
Cdd:cd07802 379 AFSHRDHLERL--LVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-453 |
7.74e-54 |
|
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: 187.43 E-value: 7.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFP--QEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQ 83
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 84 RETTIIWEKEtGRPIY---N----AIVWQSrqsagianQLKKDGYEDFfHKKTGLVIDAYFSATKIRWILDNVEGAQERA 156
Cdd:cd07798 81 REGIVFLDKD-GRELYagpNidarGVEEAA--------EIDDEFGEEI-YTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 157 EKgellFGTIDSWLVWKLTdGdVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGE--TQAYHFF 234
Cdd:cd07798 151 AT----VLSISDWIGYRLT-G-ELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTvsEEAAREL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 235 G--SKVP-ISGMAgDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGEsPQYSDNKLLTTIGYGINGKiyYALEGSIFVAG 311
Cdd:cd07798 225 GlpEGTPvVVGGA-DTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDE-PIIDPERRLWTGCHLVPGK--WVLESNAGVTG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 312 SSIQWLRDGLHmiENSSDS-----EAAAKKSTNDDEVYvvpAFVGLGAPYWDQEA--RGSMFGLTRGTSDN----DIVKA 380
Cdd:cd07798 301 LNYQWLKELLY--GDPEDSyevleEEASEIPPGANGVL---AFLGPQIFDARLSGlkNGGFLFPTPLSASEltrgDFARA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467962001 381 TLQSIAYQVRDVIETMEADTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVG 453
Cdd:cd07798 376 ILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
6-453 |
1.19e-45 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 165.49 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQRE 85
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKEtGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNvegAQERAEKGELLFGT 165
Cdd:cd24121 81 GTWLVDED-GRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKEN---EPERLERARTALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDsWLVWKLTdGDVhVTDYSNASRTMlFNINDLKWDQEILDLLNIPV--AMLPRVASNSEIYGE--TQAYHFFG--SKVP 239
Cdd:cd24121 157 KD-WLFYKLT-GEI-ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEElrHLLPPIRPGTEVIGPltPEAAAATGlpAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 240 ISGMAGDQQAALFGQMAFEPGMVKNTYGTGSF--IVMNTGESPQYsdnKLLTTIGYGINGKIYYALegSIFVAGSSIQWL 317
Cdd:cd24121 233 VVLGPFDVVATALGSGAIEPGDACSILGTTGVheVVVDEPDLEPE---GVGYTICLGVPGRWLRAM--ANMAGTPNLDWF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 318 RDGLhmiensSDSEAAAKKSTNDDEV---------------------YVVPAfvGLGAPYWDQEARGSMFGLTRGTSDND 376
Cdd:cd24121 308 LREL------GEVLKEGAEPAGSDLFqdleelaassppgaegvlyhpYLSPA--GERAPFVNPNARAQFTGLSLEHTRAD 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467962001 377 IVKATLQSIAYQVRDVIETMeadtGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVG 453
Cdd:cd24121 380 LLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
262-451 |
3.19e-43 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 151.71 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 262 VKNTYGTGSFiVMNTGESPQYSDNKLLTTIGYGInGKIYYALEGSIFVAGSSIQWLRDGLHMIE--------NSSDSEAA 333
Cdd:pfam02782 1 LAISAGTSSF-VLVETPEPVLSVHGVWGPYTNEM-LPGYWGLEGGQSAAGSLLAWLLQFHGLREelrdagnvESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 334 AKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEADTGINIPVLKVDGGA 413
Cdd:pfam02782 79 LAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2467962001 414 ANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLA 451
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
6-448 |
8.06e-39 |
|
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: 146.60 E-value: 8.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFP---QEGWVEHNANEIWNSVQSVIAGSFIESGIKpdqIAGIGITN 82
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVSRPTPAPIssdDPGRSEQDPEKILEAVRNLIDELPREYLSD---VTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 83 QrettIIWEKETGRPIYNAIVWQ-SRQSAGIANQLKKDGYEDFfhKKTGLVIDAYFSATKIRWILDNvegaqERAEKGEL 161
Cdd:cd07777 78 Qmh-gIVLWDEDGNPVSPLITWQdQRCSEEFLGGLSTYGEELL--PKSGMRLKPGYGLATLFWLLRN-----GPLPSKAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 162 LFGTIDSWLVWKLTDGDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQayHFFGSKVPIS 241
Cdd:cd07777 150 RAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLS--SALPKGIPVY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 242 GMAGDQQAALFGQMAFEPGMVKNTYGTGSFI--VMNTGESPQ------YSDNKLLTTIGyGINGkiyyalegsifvaGSS 313
Cdd:cd07777 228 VALGDNQASVLGSGLNEENDAVLNIGTGAQLsfLTPKFELSGsveirpFFDGRYLLVAA-SLPG-------------GRA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 314 IQWL----RDGLHMIENSSDSEAAAKK------STNDDEVYVVPAFvgLGAPyWDQEARGSMFGLtrgTSDN----DIVK 379
Cdd:cd07777 294 LAVLvdflREWLRELGGSLSDDEIWEKldelaeSEESSDLSVDPTF--FGER-HDPEGRGSITNI---GESNftlgNLFR 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 380 ATLQSIAYQVRDVIETMEADtGINIPVLKVDGGAAN-NSYLMQFQSDILDVPVQKAGNLETTALGAAFLA 448
Cdd:cd07777 368 ALCRGIAENLHEMLPRLDLD-LSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
6-460 |
4.56e-38 |
|
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: 145.76 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYD-KKGNHISSSQKEFTQYF--PQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGI-- 80
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVdt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 81 TnqrETTIIWEKETGRPIYNAIVWQ----SRQSAGIaNQLKKDGYEDFFHKKTGLV-IDAYFSatKIRWILDNvegAQER 155
Cdd:cd07781 81 T---SSTVVPVDEDGNPLAPAILWMdhraQEEAAEI-NETAHPALEYYLAYYGGVYsSEWMWP--KALWLKRN---APEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 156 AEKGELLFGTIDsWLVWKLTdGDVhVTDYSNASRTMLFNINDLKWDQEIL-----DLLNIPVAMLPRVASNSEIYGE--T 228
Cdd:cd07781 152 YDAAYTIVEACD-WINARLT-GRW-VRSRCAAGHKWMYNEWGGGPPREFLaaldpGLLKLREKLPGEVVPVGEPAGTltA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 229 QAYHFFG--SKVPISGMAGDQQAALFGQMAFEPG-MVKNTyGTgSFIVMNTGESPQYSDnkllttigyGINGKI------ 299
Cdd:cd07781 229 EAAERLGlpAGIPVAQGGIDAHMGAIGAGVVEPGtLALIM-GT-STCHLMVSPKPVDIP---------GICGPVpdavvp 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 300 -YYALEGSIFVAGSSIQWLRD--GLHMIENSSD-----SEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRG 371
Cdd:cd07781 298 gLYGLEAGQSAVGDIFAWFVRlfVPPAEERGDSiyallSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 372 TSDNDIVKATLQSIAYQVRDVIETMEaDTGINIPVLKVDGGAA-NNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGL 450
Cdd:cd07781 378 TTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAV 456
|
490
....*....|
gi 2467962001 451 AVGYWKDIDE 460
Cdd:cd07781 457 AAGVYADIEE 466
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-453 |
1.47e-37 |
|
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: 143.07 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYD-KKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQR 84
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 85 ETTIIWEKEtGRPIYNAIVWQSRQSAGIANQLKKD-GYEDFFhkKTGLVIDAYFSATKIRWILDNVEGAQERAEKGELLF 163
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEAlGGKKCL--LVGLNIPARFTASKLLWLKENEPEHYARIAKILLPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 164 GtidsWLVWKLTDGdvHVTDYSNASRTMLFNINDLKWDQEIL---DLLNIPVAMLPRVASNSEIYGE--TQAYHFFG--S 236
Cdd:cd07809 158 D----YLNWKLTGE--KVTGLGDASGTFPIDPRTRDYDAELLaaiDPSRDLRDLLPEVLPAGEVAGRltPEGAEELGlpA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 237 KVPISGMAGDQQAALFGQMAFEPGMVKNTYGTgSFIVMNTGESPQYSDNKLLTT-----IGY-----GINgkIYYAlegs 306
Cdd:cd07809 232 GIPVAPGEGDNMTGALGTGVVNPGTVAVSLGT-SGTAYGVSDKPVSDPHGRVATfcdstGGMlplinTTN--CLTA---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 307 ifvagssiqWLRDGLHMIENSSDS--EAAAKKSTNDDEVYVVPAFVGLGAPYWdQEARGSMFGLT--RGTSDNdIVKATL 382
Cdd:cd07809 305 ---------WTELFRELLGVSYEEldELAAQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTlsNFTRAN-LARAAL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2467962001 383 QSIAYQVRDVIETMEaDTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVG 453
Cdd:cd07809 374 EGATFGLRYGLDILR-ELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-460 |
9.06e-35 |
|
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: 136.31 E-value: 9.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQ-YFPQ-EGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITNQ 83
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHkEVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 84 RETTIIWEKEtGRPIYNAIVWQSRqSAGIANQLKK--DGYEDFFHKKTG--LVIDAyfsATKIRWILDNVEGAQERAEKg 159
Cdd:cd07775 81 REGIVLYDNE-GEEIWACANVDAR-AAEEVSELKElyNTLEEEVYRISGqtFALGA---IPRLLWLKNNRPEIYRKAAK- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 160 ellFGTIDSWLVWKLTdGDVhVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYHFF----- 234
Cdd:cd07775 155 ---ITMLSDWIAYKLS-GEL-AVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEetglk 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 235 -GSKVPISGmaGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESpqYSDNKLLTTIG-YGINGKIYYalEGSIFVAGS 312
Cdd:cd07775 230 eGTPVVVGG--GDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAP--VTDPAMNIRVNcHVIPDMWQA--EGISFFPGL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 313 SIQWLRDGLhmieNSSDSEAAAKKSTND-----DEVYVVPA-FVGLGAPYWD-------QEARGSMFGLT---RGTSDND 376
Cdd:cd07775 304 VMRWFRDAF----CAEEKEIAERLGIDAydlleEMAKDVPPgSYGIMPIFSDvmnyknwRHAAPSFLNLDidpEKCNKAT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 377 IVKATLQSIAYQVRDVIETMEADTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWK 456
Cdd:cd07775 380 FFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYS 459
|
....
gi 2467962001 457 DIDE 460
Cdd:cd07775 460 SLEE 463
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
6-463 |
1.17e-22 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 101.16 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYD-KKGNHISSSQKEFTQY-FPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITN- 82
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDsSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 83 ------QRETTIIWEKETGRPIYNAIVWQSRQSAGIA---NQLKKDGYEDFFhkktGLVIDAYFSATKIRWILDNVEGAQ 153
Cdd:cd07768 81 cslaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAqwiNMQCPQQLLDYL----GGKISPEMGVPKLKYFLDEYSHLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 154 ERAEKgelLFGTIDsWLVWKLTdgdvhvTDYSNASRTMLFNINDLK----WDQEILDLLNipvamlPRVASNSeiygetq 229
Cdd:cd07768 157 DKHFH---IFDLHD-YIAYELT------RLYEWNICGLLGKENLDGeesgWSSSFFKNID------PRLEHLT------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 230 AYHFFGSKVPISGMAGDQQAALFGQMAFEPGMV---------KNTYGTGSF-----IVMNTGESPQYsdnKLLTTIGY-- 293
Cdd:cd07768 214 TTKNLPSNVPIGTTSGVALPEMAEKMGLHPGTAvvvscidahASWFAVASPhletsLFMIAGTSSCH---MYGTTISDri 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 294 -GINGKIYYALEG--SIFVAGSS-----IQWL-------RDGLHMIENSSDSEAAAKKSTNDDE--------VYVVPAFV 350
Cdd:cd07768 291 pGVWGPFDTIIDPdySVYEAGQSatgklIEHLfeshpcaRKFDEALKKGADIYQVLEQTIRQIEknnglsihILTLDMFF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 351 GLGAPYWDQEARGSMFGLTRGTSDND---IVKATLQSIAYQVRDVIETMEADtGINIPVLKVDGGAANNSYLMQFQSDIL 427
Cdd:cd07768 371 GNRSEFADPRLKGSFIGESLDTSMLNltyKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVT 449
|
490 500 510
....*....|....*....|....*....|....*.
gi 2467962001 428 DVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEIRE 463
Cdd:cd07768 450 NVAIIKPKENMMGILGAAVLAKVAAGKKQLADSITE 485
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
6-460 |
2.24e-22 |
|
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: 100.30 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIAGIGITnqre 85
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TT---IIWEKE--------TGRPIYNAIVWQSRQSAGIANQLKKDGYE--DFFhkktGLVIDAYFSATKIRWILDNVEGA 152
Cdd:cd07782 77 ATcslVVLDAEgkpvsvspSGDDERNVILWMDHRAVEEAERINATGHEvlKYV----GGKISPEMEPPKLLWLKENLPET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 153 QERAEKgelLFGTIDsWLVWKLTDGDVHvtdySNASRT-----MLFNINDLKWDQEIL------DLLNIPVAMLPR-VAS 220
Cdd:cd07782 153 WAKAGH---FFDLPD-FLTWKATGSLTR----SLCSLVckwtyLAHEGSEGGWDDDFFkeigleDLVEDNFAKIGSvVLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 221 NSEIYGET---QAYHFFG--SKVPI-SGMAgDQQAALFGQMAFEPGMVKNTY-----------GTGSfIVMNTGESPQYS 283
Cdd:cd07782 225 PGEPVGGGltaEAAKELGlpEGTPVgVSLI-DAHAGGLGTLGADVGGLPCEAdpltrrlalicGTSS-CHMAVSPEPVFV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 284 DnkllttigyGINGKIYYAL-------EGSIFVAGSSIQwlrdglHMIEN---SSDSEAAAKKS---------------- 337
Cdd:cd07782 303 P---------GVWGPYYSAMlpglwlnEGGQSATGALLD------HIIEThpaYPELKEEAKAAgksiyeylnerleqla 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 338 ----------TNDdeVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVK---ATLQSIAYQVRDVIETMEADtGINI 404
Cdd:cd07782 368 eekglplaylTRD--LHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAA-GHKI 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2467962001 405 PVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDE 460
Cdd:cd07782 445 DTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWD 500
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
6-461 |
4.88e-22 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 98.89 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YImAIDQGTTSSRAIIYDKKGNHISSSQKEFTQYFPQEGWVEHNANEIWNSVQSVIAGSFIESGIKpdQIAGIGITNQRE 85
Cdd:PRK15027 2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 86 TTIIWEKETgRPIYNAIVWQSRQSAGIANQLKKDGYEDffHKKTGLVIDAYFSATKIRWIldnvegaqERAEKGelLFGT 165
Cdd:PRK15027 79 GATLLDAQQ-RVLRPAILWNDGRCAQECALLEARVPQS--RVITGNLMMPGFTAPKLLWV--------QRHEPE--IFRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 166 IDS------WLVWKLTdGDVhVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQ---AYHFFGS 236
Cdd:PRK15027 146 IDKvllpkdYLRLRMT-GEF-ASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLpevAKAWGMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 237 KVPISGMAGDQQAALFGQMAFEPGMVKNTYGT-GSFIVMNTG-----ESPQYSdnkllttIGYGINGKiyYALEGSIFVA 310
Cdd:PRK15027 224 TVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHS-------FCHALPQR--WHLMSVMLSA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 311 GSSIQWLRDGLHMIENSSDSEAAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVR 390
Cdd:PRK15027 295 ASCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALA 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467962001 391 DVIETMEAdTGINIPVLKVDGGAANNSYLMQFQSDI--LDVPVQKAGNLeTTALGAAFLAGLAVGYWKDIDEI 461
Cdd:PRK15027 375 DGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADIsgQQLDYRTGGDV-GPALGAARLAQIAANPEKSLIEL 445
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
4-460 |
2.41e-20 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 94.03 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 4 DKYIMAIDQGTTSSRAIIYD-KKGNHISSSQKEFTQY------FPQEGWVEHNANEIWNSVQSVIAGSFIESGIKPDQIA 76
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWviglylPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 77 GIGI--TNqreTTIIWEKETGRPI-----------YNAIVWQ----SRQSAGIaNQLKKDGYEDFFhKKTGLVIDA--YF 137
Cdd:COG1069 81 GIGVdaTG---CTPVPVDADGTPLallpefaenphAMVILWKdhtaQEEAERI-NELAKARGEDYL-RYVGGIISSewFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 138 SatKIRWILDNvegAQERAEKGELLFGTIDsWLVWKLTDGDVHvtdySNASRT--MLFNINDLKW-DQEILDLLNipvam 214
Cdd:COG1069 156 P--KILHLLRE---DPEVYEAADSFVELCD-WITWQLTGSLKR----SRCTAGhkALWHAHEGGYpSEEFFAALD----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 215 lPRVASNSE-IYGETQAyhfFGSK-----------------VPISGMAGDQQAALFGQMAFEPG-MVKNtYGTGSFIVMN 275
Cdd:COG1069 221 -PLLDGLADrLGTEIYP---LGEPagtltaewaarlglppgTAVAVGAIDAHAGAVGAGGVEPGtLVKV-MGTSTCHMLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 276 TGESP-------QYSDnkllttigyGIngkI--YYALEG--SIFvaGSSIQWLRDGL-------HMIENSSDS------E 331
Cdd:COG1069 296 SPEERfvpgicgQVDG---------SI---VpgMWGYEAgqSAV--GDIFAWFVRLLvppleyeKEAEERGISlhplltE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 332 AAAKKSTNDDEVYVVPAFVGLGAPYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEADtGINIPVLKVDG 411
Cdd:COG1069 362 EAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEEE-GVPIDEIIACG 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2467962001 412 GAA-NNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDE 460
Cdd:COG1069 441 GIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEE 490
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
4-463 |
3.38e-20 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 93.53 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 4 DKYIMAIDQGTTSSRAIIYDKKGNHISSSQKEFTqYFPQEGW-------VEHNaneiWNSVQSVIAGSFIESGIKPDQIA 76
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWR-HLAVPDVpgsmefdLEKN----WQLACQCIRQALQKAGIPASDIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 77 GIGITNQRETTIIWEKeTGRPIYNAIVWQSRQSAGIAnQLKKD--GYEDFFHKKTGLVIdAYFSATKIRWILDNVEGAQE 154
Cdd:PRK10939 77 AVSATSMREGIVLYDR-NGTEIWACANVDARASREVS-ELKELhnNFEEEVYRCSGQTL-ALGALPRLLWLAHHRPDIYR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 155 RAEKgellFGTIDSWLVWKLTdgDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYH-- 232
Cdd:PRK10939 154 QAHT----ITMISDWIAYMLS--GELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAaa 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 233 ----FFGSKVPISGmaGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGESpqYSDNKLLTTIG-YGINGKIYYalEGSI 307
Cdd:PRK10939 228 etglRAGTPVVMGG--GDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAP--VTDPNMNIRINpHVIPGMVQA--ESIS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 308 FVAGSSIQWLRDGLhmienSSDSEAAAKKSTNDdeVY----------------VVPAFVGL--------GAPYW-----D 358
Cdd:PRK10939 302 FFTGLTMRWFRDAF-----CAEEKLLAERLGID--AYslleemasrvpvgshgIIPIFSDVmrfkswyhAAPSFinlsiD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 359 QEA--RGSMFgltRGTSDND-IVKA-TLQSIayqvrdvietmEADTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKA 434
Cdd:PRK10939 375 PEKcnKATLF---RALEENAaIVSAcNLQQI-----------AAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVP 440
|
490 500
....*....|....*....|....*....
gi 2467962001 435 GNLETTALGAAFLAGLAVGYWKDIDEIRE 463
Cdd:PRK10939 441 VVKEATALGCAIAAGVGAGIYSSLAETGE 469
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
6-463 |
1.11e-19 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 91.63 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISS-SQKEFTQYFPQEG-WVEHNANEIWNSVQSviAGSFIESGIKPDQIAGIGITNQ 83
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIVARaSTPNASDIAAENSdWHQWSLDAILQRFAD--CCRQINSELTECHIRGITVTTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 84 RETTIIWEKEtGRPIYNAIVWQSRQSAGIANQLkkdgyEDFFHKKTGLVID---AYFSAT--KIRWILDNVEGAQERAEK 158
Cdd:PRK10331 81 GVDGALVDKQ-GNLLYPIISWKCPRTAAVMENI-----ERYISAQQLQQISgvgAFSFNTlyKLVWLKENHPQLLEQAHA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 159 geLLFgtIDSWLVWKLTDgdVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYG--ETQAYHFFG- 235
Cdd:PRK10331 155 --WLF--ISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGtlQPSAAALLGl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 236 -SKVPISGMAGDQQAALFGQMAF--EPGMVKNTYGtgsfIVM------NTGESPQYSDnkllTTIGYGINGKIYYAleGS 306
Cdd:PRK10331 229 pVGIPVISAGHDTQFALFGSGAGqnQPVLSSGTWE----ILMvrsaqvDTSLLSQYAG----STCELDSQSGLYNP--GM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 307 IFVAGSSIQWLRDGLHMIENSSDseaaakksTNDDEVYVVPAfvglGA------PYWDQEARGSMFGLTRGTSDNDIVKA 380
Cdd:PRK10331 299 QWLASGVLEWVRKLFWTAETPYQ--------TMIEEARAIPP----GAdgvkmqCDLLACQNAGWQGVTLNTTRGHFYRA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 381 TLQSIAYQVRDVIETMEADTGINIPVLKVDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDE 460
Cdd:PRK10331 367 ALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQ 446
|
...
gi 2467962001 461 IRE 463
Cdd:PRK10331 447 ARA 449
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
6-463 |
1.01e-18 |
|
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: 88.74 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 6 YIMAIDQGTTSSRAIIYDKKGNHISssQKE---FTQYFPQEG----WvehNANEIWNSVQSVIAgSFIESGikpDQIAGI 78
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKLE--LEEihrFPNRPVEINghlyW---DIDRLFDEIKEGLK-KAAEQG---GDIDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 79 GITnqretTiiW-------EKEtGRPIYNAIVWQSRQSAGIANQLKKDGYEDFFHKKTGLVIDAYFSATKIRWILDNVEG 151
Cdd:cd07771 72 GID-----T--WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 152 AQERAEKgeLLFgtIDSWLVWKLTdGDVhVTDYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQ-- 229
Cdd:cd07771 144 LLERADK--LLM--LPDLLNYLLT-GEK-VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKpe 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 230 -AYHFFGSKVP-ISGMAGDQQAALfgqMAFePGMVKNTY----GTGSFIVMNTgESPQYSD---NKLLTTIGyGINGKIY 300
Cdd:cd07771 218 vAEELGLKGIPvIAVASHDTASAV---AAV-PAEDEDAAfissGTWSLIGVEL-DEPVITEeafEAGFTNEG-GADGTIR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 301 YalegsifvagssiqwLRD--GLHMIE-----------NSSDSE--AAAKKSTN-------DDEVYVVPafvglgapywd 358
Cdd:cd07771 292 L---------------LKNitGLWLLQecrreweeegkDYSYDElvALAEEAPPfgafidpDDPRFLNP----------- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 359 qearGSM----------FGLTRGTSDNDIVKATLQSIAYQVRDVIETMEADTGINIPVLKVDGGAANNSYLMQFQSDILD 428
Cdd:cd07771 346 ----GDMpeairaycreTGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATG 421
|
490 500 510
....*....|....*....|....*....|....*
gi 2467962001 429 VPVqKAGNLETTALGAAFLAGLAVGYWKDIDEIRE 463
Cdd:cd07771 422 LPV-IAGPVEATAIGNLLVQLIALGEIKSLEEGRE 455
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
355-460 |
1.30e-12 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 69.87 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 355 PYWDQEARGSMFGLTRGTSDNDIVKATLQSIAYQVRDVIETMEaDTGINIPVLKVDGG-AANNSYLMQFQSDILDVPVQK 433
Cdd:PRK04123 391 PLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQV 469
|
90 100
....*....|....*....|....*..
gi 2467962001 434 AGNLETTALGAAFLAGLAVGYWKDIDE 460
Cdd:PRK04123 470 VASDQCPALGAAIFAAVAAGAYPDIPE 496
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
177-464 |
9.61e-11 |
|
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: 64.12 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 177 GDVHVTDYSNASRTMLFNINDLKWDQEILDLLNIPV--AMLPRVASNSEIYGETQAYHF----FGSKVPISGMAGDQQAA 250
Cdd:cd07776 198 GRYAPIDESDGSGMNLMDIRSRKWSPELLDAATAPDlkEKLGELVPSSTVAGGISSYFVerygFSPDCLVVAFTGDNPAS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 251 LFGqMAFEPGMVKNTYGTgSFIVMntGESPQYSDNkllttigygingkiyyaLEGSIFVA---------------GS-SI 314
Cdd:cd07776 278 LAG-LGLEPGDVAVSLGT-SDTVF--LVLDEPKPG-----------------PEGHVFANpvdpgsymamlcyknGSlAR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 315 QWLRDGLhmieNSSD----SEAAAKKSTNDDEVyvvpafvgLGAPYWDQEARGSMFGLTRGTSDNDIVKATLqSIAYQVR 390
Cdd:cd07776 337 ERVRDRY----AGGSwekfNELLESTPPGNNGN--------LGLYFDEPEITPPVPGGGRRFFGDDGVDAFF-DPAVEVR 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 391 DVIE----TME---ADTGINIPVLK--VDGGAANNSYLMQFQSDILDVPVQKAGNLETTALGAAFLAGLAVGYWKDIDEI 461
Cdd:cd07776 404 AVVEsqflSMRlhaERLGSDIPPTRilATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFS 483
|
...
gi 2467962001 462 REF 464
Cdd:cd07776 484 PEF 486
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
10-463 |
2.70e-07 |
|
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: 53.18 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 10 IDQGTTSSRAIIYDKKGNHISSSQKEFT-QYFPQEGW-VEHNANEIWNSVQSVIAGSFIESGIKpdQIAGIGIT------ 81
Cdd:cd07778 5 IDVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDY--IVSGIGVSatcsmv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 82 -NQRETT--------IIWEKETgrPIYNAIVWQSRQSAGIA---NQLKKDGYEDFFhkkTGLVIdAYFSATKIRWILDNV 149
Cdd:cd07778 83 vMQRDSDtsylvpynVIHEKSN--PDQDIIFWMDHRASEETqwlNNILPDDILDYL---GGGFI-PEMAIPKLKYLIDLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 150 EgaQERAEKgeLLFGTIDSWLVWKLTDGDVHVTD-YSNASRTMLFNIN-DLK-WDQEILDLLNIPVAMLPRVASNSEIYG 226
Cdd:cd07778 157 K--EDTFKK--LEVFDLHDWISYMLATNLGHSNIvPVNAPPSIGIGIDgSLKgWSKDFYSKLKISTKVCNVGNTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 227 ETQAYHFFG-SKVPISGMAG------------DQQAALFGQMAfEPGMVKNTY----GTGSFIVMNTGESP--------- 280
Cdd:cd07778 233 LPYAGIPIGkVNVILASYLGidkstvvghgciDCYAGWFSTFA-AAKTLDTTLfmvaGTSTCFLYATSSSQvgpipgiwg 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 281 ---QYSDNKLLTTIGYGINGKIyyaLEGSIFVAGSSIQWLRDGLHMIENSSDSEAAAKKSTNDDEVYVVPAFVGLG---- 353
Cdd:cd07778 312 pfdQLLKNYSVYEGGQSATGKL---IEKLFNSHPAIIELLKSDANFFETVEEKIDKYERLLGQSIHYLTRHMFFYGdylg 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 354 --APYWDQEARGSMFGLTRGTSDNDIVK---ATLQSIAYQVRDVIETMEaDTGINIPVLKVDGGAANNSYLMQFQSDILD 428
Cdd:cd07778 389 nrTPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQ-KEKIIIQKVVISGSQAKNARLLQLLSTVLS 467
|
490 500 510
....*....|....*....|....*....|....*..
gi 2467962001 429 VPV--QKAGNLETTALGAAFLAGLAVGYWKDIDEIRE 463
Cdd:cd07778 468 KIHiiVPLSDSKYAVVKGAALLGKAAFLHNQSIEERL 504
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
183-462 |
1.29e-04 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 44.32 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 183 DYSNASRTMLFNINDLKWDQEILDLLNIPVAMLPRVASNSEIYGETQAYHffGSKVPISGMAG-DQQAALFGQMAFEPGM 261
Cdd:PRK10640 157 EYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQ--GNEIPVVAVAShDTASAVIASPLNDSDA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 262 VKNTYGTGSFIVMNTGEsPQYSDNKL---LTTIGyGINGKiYYALEGSIfvagssiqwlrdGLHMIENSSDSEAAAKKST 338
Cdd:PRK10640 235 AYLSSGTWSLMGFESQT-PFTNDTALaanITNEG-GAEGR-YRVLKNIM------------GLWLLQRVLQERQITDLPA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 339 NDDEVYVVPAFVGLGAPYWD---------QEARGSMF--GLTRGTSDNDIVKATLQSIAYQVRDVIETMEADTGINIPVL 407
Cdd:PRK10640 300 LIAATAALPACRFLINPNDDrfinppsmcSEIQAACRetAQPVPESDAELARCIFDSLALLYADVLHELAQLRGEPFSQL 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2467962001 408 KVDGGAANNSYLMQFQSDILDVPVQkAGNLETTALGAAFLAGLAVGYWKDIDEIR 462
Cdd:PRK10640 380 HIVGGGCQNALLNQLCADACGIRVI-AGPVEASTLGNIGIQLMTLDELNNVDDFR 433
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
170-448 |
2.40e-04 |
|
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: 43.40 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 170 LVWKLTdGdVHVTDYSNAS-RTMLFNINDLKW----DQEILDLLnipvaMLPRVASN---SEIYGETQAYHFFGSKVPIs 241
Cdd:cd07772 153 WAWRLT-G-KAASEITSLGcHTDLWDFEKNEYsslvKKEGWDKL-----FPPLRKAWevlGPLRPDLARRTGLPKDIPV- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 242 gMAG--DQQAALFG-QMAFEPGMVKNTYGTGsFIVMNTGESPQYSDNKLLTTIGYGIN--GKIYYAlegSIFVAGSSIQW 316
Cdd:cd07772 225 -GCGihDSNAALLPyLAAGKEPFTLLSTGTW-CIAMNPGNDLPLTELDLARDCLYNLDvfGRPVKT---ARFMGGREYER 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467962001 317 LRDGLHMIENSSDSEAAAKKsTNDDEVYVVPAFVGLGAPYWDQEARGsmfGLTRGTSDNDIVKATLQSIAYQVRDVIETM 396
Cdd:cd07772 300 LVERIAKSFPQLPSLADLAK-LLARGTFALPSFAPGGGPFPGSGGRG---VLSAFPSAEEAYALAILYLALMTDYALDLL 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2467962001 397 EADTGiniPVLkVDGGAANNSYLMQFQSDIL-DVPVQKAGNLETTALGAAFLA 448
Cdd:cd07772 376 GSGVG---RII-VEGGFAKNPVFLRLLAALRpDQPVYLSDDSEGTALGAALLA 424
|
|
| |
