|
Name |
Accession |
Description |
Interval |
E-value |
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-496 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 1099.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 1 MEKYILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITN 80
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 81 QRETTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKGELL 160
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 161 FGTIDTWLVWKLSGGRAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYHFFGQEVPIAG 240
Cdd:PRK00047 163 FGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGEVPIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 241 IAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAWGIDGKVEYALEGSIFVAGSAIQWLRDGLR 320
Cdd:PRK00047 243 IAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSAIQWLRDGLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 321 MIKEAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEADSGI 400
Cdd:PRK00047 323 IISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 401 TLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWNIDRSFTPAMTKEVQEK 480
Cdd:PRK00047 403 RLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDEEEREK 482
|
490
....*....|....*.
gi 1593221718 481 LYEGWKKAVQAARAFK 496
Cdd:PRK00047 483 LYAGWKKAVKRTLAWA 498
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-496 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 1062.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 1 MEKYILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITN 80
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 81 QRETTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKGELL 160
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 161 FGTIDTWLVWKLSGGRAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPyHFFGQEVPIAG 240
Cdd:COG0554 161 FGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDP-DLFGAEIPIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 241 IAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAWGIDGKVEYALEGSIFVAGSAIQWLRDGLR 320
Cdd:COG0554 240 IAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQWLRDGLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 321 MIKEAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEADSGI 400
Cdd:COG0554 320 LIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 401 TLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWNIDRSFTPAMTKEVQEK 480
Cdd:COG0554 400 PLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDEEERER 479
|
490
....*....|....*.
gi 1593221718 481 LYEGWKKAVQAARAFK 496
Cdd:COG0554 480 LYAGWKKAVERTLGWA 495
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
4-490 |
0e+00 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 1009.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKGELLFGT 163
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELAFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDTWLVWKLSGGRAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYhFFGQEVPIAGIAG 243
Cdd:cd07786 161 IDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPD-LLGAEIPIAGIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 244 DQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAWGIDGKVEYALEGSIFVAGSAIQWLRDGLRMIK 323
Cdd:cd07786 240 DQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTYALEGSIFIAGAAVQWLRDGLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 324 EAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEADSGITLK 403
Cdd:cd07786 320 SAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 404 TLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWNIDRSFTPAMTKEVQEKLYE 483
Cdd:cd07786 400 ELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSEEEREALYA 479
|
....*..
gi 1593221718 484 GWKKAVQ 490
Cdd:cd07786 480 GWKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
4-490 |
0e+00 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 991.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKGELLFGT 163
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDTWLVWKLSGGRAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYHFfGQEVPIAGIAG 243
Cdd:cd07769 161 IDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGL-GAGIPIAGILG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 244 DQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAWGIDGKVEYALEGSIFVAGSAIQWLRDGLRMIK 323
Cdd:cd07769 240 DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAIQWLRDNLGLIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 324 EAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEADSGITLK 403
Cdd:cd07769 320 DAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 404 TLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWNIDRSFTPAMTKEVQEKLYE 483
Cdd:cd07769 400 ELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYR 479
|
....*..
gi 1593221718 484 GWKKAVQ 490
Cdd:cd07769 480 GWKKAVE 486
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
3-495 |
0e+00 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 877.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 3 KYILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQR 82
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIKPDDIAAIGITNQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 83 ETTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKGELLFG 162
Cdd:TIGR01311 81 ETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGEFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 163 TIDTWLVWKLSGGRAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYhFFGQEVPIAGIA 242
Cdd:TIGR01311 161 TIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPG-LLGAEIPITGVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 243 GDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAWGIDGKV-EYALEGSIFVAGSAIQWLRDGLRM 321
Cdd:TIGR01311 240 GDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKpVYALEGSVFVAGAAVQWLRDNLKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 322 IKEAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEADSGIT 401
Cdd:TIGR01311 320 IKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 402 LKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWNIDRSFTPAMTKEVQEKL 481
Cdd:TIGR01311 400 ITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVEKTFEPEMDEEEREAR 479
|
490
....*....|....
gi 1593221718 482 YEGWKKAVQAARAF 495
Cdd:TIGR01311 480 YAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
3-490 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 737.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 3 KYILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAA---VSPEQIAAIGIT 79
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKalgISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 80 NQRETTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKEQ---GYDElFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEK 156
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKtpgGKDH-FRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 157 GELLFGTIDTWLVWKLSGGR---AHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYHFFG 233
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTGGKnggVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 234 qeVPIAGIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAW--GIDGKVEYALEGSIFVAGSA 311
Cdd:cd07792 240 --VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYklGPDAPPVYALEGSIAIAGAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 312 IQWLRDGLRMIKEAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVL 391
Cdd:cd07792 318 VQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 392 MAMEADSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEI-AQQWNIDRSFT 470
Cdd:cd07792 398 DAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELkSLNEGGRTVFE 477
|
490 500
....*....|....*....|
gi 1593221718 471 PAMTKEVQEKLYEGWKKAVQ 490
Cdd:cd07792 478 PQISEEERERRYKRWKKAVE 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-496 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 674.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 3 KYILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVL--SEAAVSPEQIAAIGITN 80
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIkkLREKGPSFKIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 81 QRETTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKEQGY-DELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKGEL 159
Cdd:PTZ00294 82 QRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGgSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 160 LFGTIDTWLVWKLSGGRAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAH-TIPYHFFGQEVPI 238
Cdd:PTZ00294 162 LFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTiSGEAVPLLEGVPI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 239 AGIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAW--GIDGKVEYALEGSIFVAGSAIQWLR 316
Cdd:PTZ00294 242 TGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYqlGPNGPTVYALEGSIAVAGAGVEWLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 317 DGLRMIKEAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEA 396
Cdd:PTZ00294 322 DNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 397 DSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQ-QWNIDRSFTPAMTK 475
Cdd:PTZ00294 402 DAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKlIRRSNSTFSPQMSA 481
|
490 500
....*....|....*....|.
gi 1593221718 476 EVQEKLYEGWKKAVQAARAFK 496
Cdd:PTZ00294 482 EERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
4-495 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 649.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVS----PEQIAAIGIT 79
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKghnvDSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 80 NQRETTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKEQ--GYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKG 157
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKElsGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 158 ELLFGTIDTWLVWKLSGGRA---HVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIY---AHTIPyhf 231
Cdd:PLN02295 161 DALFGTIDSWLIWNLTGGASggvHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIgtiAKGWP--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 232 fGQEVPIAGIAGDQQAALFGQACfEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAW--GIDGKVEYALEGSIFVAG 309
Cdd:PLN02295 238 -LAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYklGPDAPTNYALEGSVAIAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 310 SAIQWLRDGLRMIKEAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKD 389
Cdd:PLN02295 316 AAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 390 VLMAMEAD-----SGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQ-W 463
Cdd:PLN02295 396 VLDAMRKDageekSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEkW 475
|
490 500 510
....*....|....*....|....*....|..
gi 1593221718 464 NIDRSFTPAMTKEVQEKLYEGWKKAVQaaRAF 495
Cdd:PLN02295 476 KNTTTFRPKLDEEERAKRYASWCKAVE--RSF 505
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-490 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 598.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQTGQPIYNAIVWQSRQTVPICEQLKE-----------QGYDELFRAKTGLLIDAY-FSGT----KVKWILDHV 147
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRslllkalrggsKFLHFLTRNKRFLAASVLkFSTAhvsiRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 148 DGAREKAEKGELLFGTIDTWLVWKLSGGRAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTI 227
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 228 PyHFFGQEVPIAGIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAWGIDGKVEYALEGSIFV 307
Cdd:cd07793 241 P-SIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 308 AGSAIQWLRDGLrMIKEAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQT 387
Cdd:cd07793 320 TGTVIDWAKSIG-LFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 388 KDVLMAMEADSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWNIDR 467
Cdd:cd07793 399 KQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEK 478
|
490 500
....*....|....*....|...
gi 1593221718 468 SFTPAMTKEVQEKLYEGWKKAVQ 490
Cdd:cd07793 479 IFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-495 |
1.06e-125 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 375.32 E-value: 1.06e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 3 KYILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQR 82
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 83 ETTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKgellFG 162
Cdd:COG1070 81 HGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK----VL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 163 TIDTWLVWKLSGgrAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHT---------IPyhffg 233
Cdd:COG1070 156 LPKDYLRYRLTG--EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLtaeaaaetgLP----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 234 QEVPIAGIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTgEKAVQSKHGLLTTIAWGIDGKveYALEGSIFVAGSAIQ 313
Cdd:COG1070 229 AGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR--WLPMGATNNGGSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 314 WLRDGLRMIKEAKDSELYAtRVEST----DGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKD 389
Cdd:COG1070 306 WFRDLFADGELDDYEELNA-LAAEVppgaDGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 390 VLMAMEAdSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQW-NIDRS 468
Cdd:COG1070 385 GLEALEE-AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGET 463
|
490 500
....*....|....*....|....*...
gi 1593221718 469 FTPAMT-KEVQEKLYEGWKKAVQAARAF 495
Cdd:COG1070 464 IEPDPEnVAAYDELYERYRELYPALKPL 491
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-471 |
4.82e-117 |
|
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: 351.05 E-value: 4.82e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQsrqtvpiceqlkeqgyDElfRAKTgllidayfsgtkvkwildhvdgarekaekgellFGT 163
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQ----------------DK--RTAK---------------------------------FLT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDTWLVWKLSGGraHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRP--------SSEIYAHT-IPyhffgQ 234
Cdd:cd07779 109 VQDYLLYRLTGE--FVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPpgtvigtlTKEAAEETgLP-----E 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 235 EVP-IAGiAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTIAwGIDGKveYALEGSIFVAGSAIQ 313
Cdd:cd07779 182 GTPvVAG-GGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPS-AVPGK--WVLEGSINTGGSAVR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 314 WLRD---GLRMIKEAKDSELYA---TRVEST----DGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESL 383
Cdd:cd07779 258 WFRDefgQDEVAEKELGVSPYEllnEEAAKSppgsDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGI 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 384 AYQTKDVLMAMEaDSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQW 463
Cdd:cd07779 338 AFELRDNLEAME-KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAM 416
|
....*....
gi 1593221718 464 -NIDRSFTP 471
Cdd:cd07779 417 vRVTDTFEP 425
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-446 |
9.31e-115 |
|
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: 343.78 E-value: 9.31e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRqtvpiceqlkeqgydelfRAKtgllidayfsgtkvkwildhvdgarekaekgellFGT 163
Cdd:cd00366 81 GVVLVDAD-GNPLRPAIIWLDR------------------RAK----------------------------------FLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDTWLVWKLSGgrAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYHF----FGQEVPIA 239
Cdd:cd00366 108 PNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAeetgLPAGTPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 240 GIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKavQSKHGLLTTIAWGIDGKveYALEGSIFVAGSAIQWLRD-- 317
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEP--VPPDPRLLNRCHVVPGL--WLLEGAINTGGASLRWFRDef 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 318 GLRMIKEAKDSELYATRVES---TDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAM 394
Cdd:cd00366 262 GEEEDSDAEYEGLDELAAEVppgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1593221718 395 EADsGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLA 446
Cdd:cd00366 342 EEL-GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-251 |
2.60e-112 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 331.99 E-value: 2.60e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQTgQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKgellFGT 163
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHK----FLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDTWLVWKLSGgrAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYHFFG----QEVPIA 239
Cdd:pfam00370 156 IHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMwgldEGVPVV 233
|
250
....*....|..
gi 1593221718 240 GIAGDQQAALFG 251
Cdd:pfam00370 234 GGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
4-451 |
5.68e-110 |
|
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: 333.40 E-value: 5.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAvsPEQIAAIGITNQRE 83
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKgellFGT 163
Cdd:cd07773 79 SGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAK----WLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDTWLVWKLSGgrAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYHF----FGQEVPIA 239
Cdd:cd07773 154 VADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAeelgLPAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 240 gIAG-DQQAALFGQACFEEGMAKNTYGTG-CFMLMNTGEKAVQSKHGLLTTIAWGIDGKVeYALEGSIfVAGSAIQWLRD 317
Cdd:cd07773 232 -VGGhDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPGGY-YYLAGSL-PGGALLEWFRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 318 --GLRMIKEAKDSELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAME 395
Cdd:cd07773 309 lfGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALE 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1593221718 396 AdSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07773 389 K-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-488 |
8.18e-103 |
|
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: 316.40 E-value: 8.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQgYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKgeLLFGT 163
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRK--ILLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 iDtWLVWKLSGgrAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHT---------IPyhffgQ 234
Cdd:cd07808 157 -D-YLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLtpeaaeelgLP-----E 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 235 EVPIAGIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTgEKAVQSKHGLLTTIAWGIDGKvEYALeGSIFVAGSAIQW 314
Cdd:cd07808 228 GTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGK-WYAM-GVTLSAGLSLRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 315 LRDGL--------RMIKEAKDSELYAtrvestDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQ 386
Cdd:cd07808 305 LRDLFgpdresfdELDAEAAKVPPGS------EGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 387 TKDVLMAMEaDSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWN-I 465
Cdd:cd07808 379 LRDSLEVLK-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIkI 457
|
490 500
....*....|....*....|....
gi 1593221718 466 DRSFTP-AMTKEVQEKLYEGWKKA 488
Cdd:cd07808 458 EKTIEPdPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
4-486 |
2.62e-95 |
|
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: 297.12 E-value: 2.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQ-GYDELFRAKTGLLIDAYFSGTKVKWILDHvdgAREKAEKGELLFG 162
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGlGGIEGYRLGGGNPPSGKDPLAKILWLKEN---EPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 163 TIDtWLVWKLSGgrAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAH-T--------IPyhffg 233
Cdd:cd07805 157 AKD-YLNFRLTG--RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGElTpeaaaelgLP----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 234 QEVPIAGIAGDQQAALFGQACFEEGMAkNTY-GTGCFMLMNTGEKAVQSKHGLlTTIAWGIDGKveYALEGSIFVAGSAI 312
Cdd:cd07805 229 AGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHGI-FTLASADPGR--YLLAAEQETAGGAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 313 QWLRDGLRMiKEAKDSELYAT---RVEST----DGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAY 385
Cdd:cd07805 305 EWARDNLGG-DEDLGADDYELldeLAAEAppgsNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 386 QTKDVLMAMEADSGiTLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVV-NETTALGAAYLAGLAVGYWNSKEEIAQQWN 464
Cdd:cd07805 384 NLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVK 462
|
490 500
....*....|....*....|...
gi 1593221718 465 IDRSFTP-AMTKEVQEKLYEGWK 486
Cdd:cd07805 463 VEKVFEPdPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-451 |
3.01e-87 |
|
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: 275.17 E-value: 3.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKgellFGT 163
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRK----FLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDTWLVWKLSGgrAHVTDYSNASRT-LMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHT---------IPyhffg 233
Cdd:cd07804 156 AYDYIVYKLTG--EYVIDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVtkeaaeetgLA----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 234 QEVPIAGIAGDQQAALFGQACFEEG--MAKntYGT-GCFMLMNtgEKAVQSKHGLLTtiAWGIDGKveYALEGSIFVAGS 310
Cdd:cd07804 229 EGTPVVAGTVDAAASALSAGVVEPGdlLLM--LGTaGDIGVVT--DKLPTDPRLWLD--YHDIPGT--YVLNGGMATSGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 311 AIQWLRDGL----RMIKEAKDSELY------ATRVEST-DGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRAT 379
Cdd:cd07804 301 LLRWFRDEFageeVEAEKSGGDSAYdlldeeAEKIPPGsDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRAL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593221718 380 LESLAYQTKDVLMAMEaDSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07804 381 LEGVAYGLRHHLEVIR-EAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-487 |
1.32e-85 |
|
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: 271.74 E-value: 1.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAvsPEQIAAIGITNQRE 83
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG--GGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKgellFGT 163
Cdd:cd07770 79 SLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK----FVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDTWLVWKLSGgrAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEI-------YAHTIPyhfFGQEV 236
Cdd:cd07770 154 IKEYLLYRLTG--ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVlpglkpeFAERLG---LLAGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 237 P-IAGiAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTtiawgidgkveYALEGSIFVAGSAI--- 312
Cdd:cd07770 229 PvVLG-ASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWC-----------YRLDENRWLVGGAInng 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 313 ----QWLRD---GLRMIKEAKDSELYATRVEStDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAY 385
Cdd:cd07770 297 gnvlDWLRDtllLSGDDYEELDKLAEAVPPGS-HGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 386 QTKDVLMAMEaDSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKeEIAQQWNI 465
Cdd:cd07770 376 NLKSIYEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL-EADELVKI 453
|
490 500
....*....|....*....|...
gi 1593221718 466 DRSFTPAMTK-EVQEKLYEGWKK 487
Cdd:cd07770 454 GKVVEPDPENhAIYAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
4-450 |
9.89e-67 |
|
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: 220.94 E-value: 9.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAvsPEQIAAIGITNQRE 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELR--PRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRakTGLLIDAYFSGTKVKWILDHVDGAREKAEKgeLLFGT 163
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAGAVAPR--TGLAVSPSSSLAKLLWLKRHEPEVLAKTAK--FLHQA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 idTWLVWKLSGGRAhVTDYSNASRTLmFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHT---IPYHF-FGQEVPIa 239
Cdd:cd07783 154 --DWLAGRLTGDRG-VTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLtaeAAEELgLPAGTPV- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 240 gIAG--DQQAALFGQACFEEGMAKNTYGTG-CFMLmnTGEKAVQSKHGLLTTIAWGIDGkveYALEGSIFVAGSAIQWLR 316
Cdd:cd07783 229 -VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLKL--LSDKRVPDPGGGVYSHRHGDGY---WLVGGASNTGGAVLRWFF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 317 DGlrmiKEAKDSELYATRvESTDGVYVVPaFVGLG--TPYWDSDVRGAIfgLTRGTTKEHFIRATLESLAYQTKDVLMAM 394
Cdd:cd07783 303 SD----DELAELSAQADP-PGPSGLIYYP-LPLRGerFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1593221718 395 EADSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPvVNETTALGAAYLAGLAV 450
Cdd:cd07783 375 EELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIA-EEEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-451 |
1.85e-63 |
|
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: 212.80 E-value: 1.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGLLIdayFSGTKV---KWILDHvdgAREKAEKgell 160
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPL---WPGQPVallRWLKEN---EPERYDR---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 161 fgtIDT------WLVWKLSGgrAHVTDYSNASrTLMFNIHELKWDEELLSILNVP--KSMLPEVRPSSEIYAHTIPyhff 232
Cdd:cd07802 150 ---IRTvlfckdWIRYRLTG--EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTA---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 233 gqEV----------PIAGIAGDQQAALFGQACFEEGMAKNTYGTGCfmlMNTG--EKAVQSKHGLLtTIAWGIDGKVeYA 300
Cdd:cd07802 220 --EAaaltglpegtPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGS-NSLHADPGLY-LI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 301 LEGSIfVAGSAIQWLRD---GLRMIKEAKDSELYATRVES----TDGVYVVPaFVgLGTPYwDSDVRGAIFGLTRGTTKE 373
Cdd:cd07802 293 VEASP-TSASNLDWFLDtllGEEKEAGGSDYDELDELIAAvppgSSGVIFLP-YL-YGSGA-NPNARGGFFGLTAWHTRA 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1593221718 374 HFIRATLESLAYQTKDVLMAMeaDSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07802 369 HLLRAVYEGIAFSHRDHLERL--LVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-451 |
2.99e-63 |
|
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: 212.47 E-value: 2.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFP--QPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQ 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 82 RETTVVWDKQtGQPIY---N----AIVWQSrqtvpiceQLKEQGYDELFrAKTGLLIDAYFSGTKVKWILDHVDGAREKA 154
Cdd:cd07798 81 REGIVFLDKD-GRELYagpNidarGVEEAA--------EIDDEFGEEIY-TTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 155 EKgellFGTIDTWLVWKLSGGRahVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIY--------AHT 226
Cdd:cd07798 151 AT----VLSISDWIGYRLTGEL--VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLgtvseeaaREL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 227 IpyhfFGQEVPIAGIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTiAWGIDGKveYALEGSIF 306
Cdd:cd07798 225 G----LPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTG-CHLVPGK--WVLESNAG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 307 VAGSAIQWLRDGL---------RMIKEAKDSELYATRVESTDGVYVVPA---FVGLGTPYWDSDVRGAifgltrGTTKEH 374
Cdd:cd07798 298 VTGLNYQWLKELLygdpedsyeVLEEEASEIPPGANGVLAFLGPQIFDArlsGLKNGGFLFPTPLSAS------ELTRGD 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593221718 375 FIRATLESLAYQTKDVLMAMEADSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07798 372 FARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-451 |
1.87e-54 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 188.91 E-value: 1.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFN-RKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQR 82
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 83 ETTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQ-GYDElfRAKTGLLIDAYFSGTKVKWILDHVDGAREKAEKGELLF 161
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEAlGGKK--CLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 162 GtidtWLVWKLSGGRahVTDYSNASRTLMFNIHELKWDEELLSILNV---PKSMLPEVRPSSEIYAHTIPYH--FFG--Q 234
Cdd:cd07809 158 D----YLNWKLTGEK--VTGLGDASGTFPIDPRTRDYDAELLAAIDPsrdLRDLLPEVLPAGEVAGRLTPEGaeELGlpA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 235 EVPIAGIAGDQQAALFGQACFEEGMAKNTYGT-GCfmLMNTGEKAVQSKHGLLTTIAwGIDGKVEYALEGSIFVAgSAIQ 313
Cdd:cd07809 232 GIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFC-DSTGGMLPLINTTNCLT-AWTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 314 WLRDGLRMIKEAKDSELYATRVEStDGVYVVPAFVGLGTPYWdSDVRGAIFGLTRG-TTKEHFIRATLESLAYqtkDVLM 392
Cdd:cd07809 308 LFRELLGVSYEELDELAAQAPPGA-GGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATF---GLRY 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1593221718 393 AMEA--DSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd07809 383 GLDIlrELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
260-449 |
8.54e-53 |
|
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: 176.75 E-value: 8.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 260 AKNTYGTGCFMLMnTGEKAVQSKHGLLTTIAwGIDGKVEYALEGSIFVAGSAIQWLRDGLRMIKEAKDS---ELYATRVE 336
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYT-NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAgnvESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 337 S-----TDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEADSGITLKTLRVDGGA 411
Cdd:pfam02782 79 LaavapAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1593221718 412 VKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLA 449
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-493 |
4.79e-50 |
|
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: 178.50 E-value: 4.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFN-RKGEIVHIAQKEFTQYF--PQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGI-- 78
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVdt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 79 TnqrETTVVWDKQTGQPIYNAIVWQ----SRQTVPICEQLKEqgYDELFRAKTGLLIDA--YFSgtKVKWILDHvdgARE 152
Cdd:cd07781 81 T---SSTVVPVDEDGNPLAPAILWMdhraQEEAAEINETAHP--ALEYYLAYYGGVYSSewMWP--KALWLKRN---APE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 153 KAEKGELLFGTIDtWLVWKLSG----GRahvtdySNASRTLMFNIHELKWDEELLS-----ILNVPKSMLPEVRPSSEIY 223
Cdd:cd07781 151 VYDAAYTIVEACD-WINARLTGrwvrSR------CAAGHKWMYNEWGGGPPREFLAaldpgLLKLREKLPGEVVPVGEPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 224 AHTIPYH--FFG--QEVPIAGIAGDQQAALFGQACFEEG-MAKNTyGT-GCFMLMntGEKAVQSKhGLlttiaWGI--DG 295
Cdd:cd07781 224 GTLTAEAaeRLGlpAGIPVAQGGIDAHMGAIGAGVVEPGtLALIM-GTsTCHLMV--SPKPVDIP-GI-----CGPvpDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 296 KVE--YALEGSIFVAGSAIQWLRDGLRMIKEAKDSELY------ATRVE-STDGVYVVPAFVGLGTPYWDSDVRGAIFGL 366
Cdd:cd07781 295 VVPglYGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIYallseeAAKLPpGESGLVALDWFNGNRTPLVDPRLRGAIVGL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 367 TRGTTKEHFIRATLESLAYQTKDVLMAMEaDSGITLKTLRVDGG-AVKNNFLMQFQSDILGVPVERPVVNETTALGAAYL 445
Cdd:cd07781 375 TLGTTPAHIYRALLEATAFGTRAIIERFE-EAGVPVNRVVACGGiAEKNPLWMQIYADVLGRPIKVPKSDQAPALGAAIL 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1593221718 446 AGLAVGYWNSKEEIAQQW-NIDRSFTPAM-TKEVQEKLYEGWKKAVQAAR 493
Cdd:cd07781 454 AAVAAGVYADIEEAADAMvRVDRVYEPDPeNHAVYEELYALYKELYDALG 503
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
4-451 |
9.21e-49 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 173.96 E-value: 9.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQRE 83
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQGYDE-LFRAkTGLLIDAYFSGTKVKWILDHvdgAREKAEKGELLFG 162
Cdd:cd24121 81 GTWLVDED-GRPVRDAILWLDGRAADIVERWQADGIAEaVFEI-TGTGLFPGSQAAQLAWLKEN---EPERLERARTALH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 163 TIDtWLVWKLSGGRAhvTDYSNASRTlMFNIHELKWDEELLSILNVP--KSMLPEVRPSSEIyAHTI----------Pyh 230
Cdd:cd24121 156 CKD-WLFYKLTGEIA--TDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEV-IGPLtpeaaaatglP-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 231 ffgQEVPIAGIAGDQQAALFGQACFEEGMAKNTYGTGCF--MLMNtgeKAVQSKHGLLTTIAWGIDGKVEYALegSIFVA 308
Cdd:cd24121 229 ---AGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVheVVVD---EPDLEPEGVGYTICLGVPGRWLRAM--ANMAG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 309 GSAIQWLRD----GLRMIKEAKDSELYaTRVES--------TDGV----YVVPAfvGLGTPYWDSDVRGAIFGLTRGTTK 372
Cdd:cd24121 301 TPNLDWFLRelgeVLKEGAEPAGSDLF-QDLEElaassppgAEGVlyhpYLSPA--GERAPFVNPNARAQFTGLSLEHTR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1593221718 373 EHFIRATLESLAYQTKDVLMAMeadsGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVG 451
Cdd:cd24121 378 ADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-485 |
1.45e-47 |
|
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: 171.36 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQ-YFPQ-PGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITNQ 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHkEVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 82 RETTVVWDKQtGQPIY---NAIVWQSRQTvpicEQLKEQGY---DELFRaKTG--LLIDAyfsGTKVKWILDHVDGAREK 153
Cdd:cd07775 81 REGIVLYDNE-GEEIWacaNVDARAAEEV----SELKELYNtleEEVYR-ISGqtFALGA---IPRLLWLKNNRPEIYRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 154 AEKgellFGTIDTWLVWKLSGgrAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIPYHFF- 232
Cdd:cd07775 152 AAK----ITMLSDWIAYKLSG--ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEe 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 233 ---GQEVPIAGIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKhGLLTTIAWGIDGKVEYalEGSIFVAG 309
Cdd:cd07775 226 tglKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPA-MNIRVNCHVIPDMWQA--EGISFFPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 310 SAIQWLRDG----LRMIKEAKDSELY------ATRVEStdGVY-VVPAFvglgtpywdSDVRG---------AIFGLT-- 367
Cdd:cd07775 303 LVMRWFRDAfcaeEKEIAERLGIDAYdlleemAKDVPP--GSYgIMPIF---------SDVMNyknwrhaapSFLNLDid 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 368 -RGTTKEHFIRATLESLAYQTKDVLMAMEADSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLA 446
Cdd:cd07775 372 pEKCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAA 451
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1593221718 447 GLAVGYWNSKEEIAQQW-NIDRSFTPAM-TKEVQEKLYEGW 485
Cdd:cd07775 452 GVGAGIYSSLEEAVESLvKWEREYLPNPeNHEVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-446 |
1.75e-40 |
|
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: 150.84 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFN-RKGEIVHIAQKEFTQYFPQ--PGWVEHNPNEIWGSILAVIATVLSEAAvspEQIAAIGITN 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEAVRNLIDELPREYL---SDVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 81 QRETTVVWDKQtGQPIYNAIVWQ-SRQTVPICEQLKEqgYDELFRAKTGLLIDAYFSGTKVKWILDHvdgarEKAEKGEL 159
Cdd:cd07777 78 QMHGIVLWDED-GNPVSPLITWQdQRCSEEFLGGLST--YGEELLPKSGMRLKPGYGLATLFWLLRN-----GPLPSKAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 160 LFGTIDTWLVWKLSGGRAHVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIpyHFFGQEVPI- 238
Cdd:cd07777 150 RAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLS--SALPKGIPVy 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 239 AGIaGDQQAALFGQACFEEGMAKNTYGTGC--FMLMNTGEK--AVQS----KHGLLTTIAwgidgkveyALEGsifvaGS 310
Cdd:cd07777 228 VAL-GDNQASVLGSGLNEENDAVLNIGTGAqlSFLTPKFELsgSVEIrpffDGRYLLVAA---------SLPG-----GR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 311 AIQWLRDGLRMI-----KEAKDSELY-----ATRVESTDGVYVVPAFvgLGTPyWDSDVRGAIFGLTRGTTK-EHFIRAT 379
Cdd:cd07777 293 ALAVLVDFLREWlrelgGSLSDDEIWekldeLAESEESSDLSVDPTF--FGER-HDPEGRGSITNIGESNFTlGNLFRAL 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1593221718 380 LESLAYQTKDVLMAMEADSGiTLKTLRVDGGAV-KNNFLMQFQSDILGVPVERPVVNETTALGAAYLA 446
Cdd:cd07777 370 CRGIAENLHEMLPRLDLDLS-GIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
4-481 |
9.55e-34 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 132.84 E-value: 9.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVhiaQKEFTQYFPQPGwvEHNP-------NEIWGSiLAVIATVLSeAAVSPEQIAAI 76
Cdd:PRK10331 3 VILVLDCGATNVRAIAVDRQGKIV---ARASTPNASDIA--AENSdwhqwslDAILQR-FADCCRQIN-SELTECHIRGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 77 GITNQRETTVVWDKQtGQPIYNAIVWQSRQTVPICEQLKEQGYDELFRAKTGllIDAYFSGT--KVKWILDHVDGAREKA 154
Cdd:PRK10331 76 TVTTFGVDGALVDKQ-GNLLYPIISWKCPRTAAVMENIERYISAQQLQQISG--VGAFSFNTlyKLVWLKENHPQLLEQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 155 EKgeLLFgtIDTWLVWKLSGGRAhvTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIP--YHFF 232
Cdd:PRK10331 153 HA--WLF--ISSLINHRLTGEFT--TDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPsaAALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 233 GQEVPIAGI-AG-DQQAALFGQacfeeGMAKN----TYGTGCFMLMNTG--EKAVQSKHGLLTTiawGIDGKVEYALEGS 304
Cdd:PRK10331 227 GLPVGIPVIsAGhDTQFALFGS-----GAGQNqpvlSSGTWEILMVRSAqvDTSLLSQYAGSTC---ELDSQSGLYNPGM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 305 IFVAGSAIQWLRDGL--------RMIKEAKdselyaTRVESTDGVYVVPAFVGLGTpywdsdvrGAIFGLTRGTTKEHFI 376
Cdd:PRK10331 299 QWLASGVLEWVRKLFwtaetpyqTMIEEAR------AIPPGADGVKMQCDLLACQN--------AGWQGVTLNTTRGHFY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 377 RATLESLAYQTKDVLMAMEADSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSK 456
Cdd:PRK10331 365 RAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSP 444
|
490 500
....*....|....*....|....*.
gi 1593221718 457 EEIAQQWNID-RSFTPAMTKEVQEKL 481
Cdd:PRK10331 445 EQARAQMKYQyRYFYPQTEPEFIEEV 470
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
2-483 |
2.86e-33 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 132.16 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 2 EKYILALDQGTTSSRAILFN-RKGEIVHIAQKEFTQY------FPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIA 74
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWviglylPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 75 AIGItnqrETT----VVWDKQtGQPI-----------YNAIVWQ----SRQTVPICEQLKEQGYDELfraktgllidAYF 135
Cdd:COG1069 81 GIGV----DATgctpVPVDAD-GTPLallpefaenphAMVILWKdhtaQEEAERINELAKARGEDYL----------RYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 136 SGT--------KVKWILDHvdgAREKAEKGELLFGTIDtWLVWKLSGgrahvtdysNASRTL-------MFNIHELKW-D 199
Cdd:COG1069 146 GGIissewfwpKILHLLRE---DPEVYEAADSFVELCD-WITWQLTG---------SLKRSRctaghkaLWHAHEGGYpS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 200 EELLSILNVPKSMLPEvRPSSEIYAHTIPyhfFGQ-------------EVPIAGIAGDQQAALFGQACFEEG-MAKNtYG 265
Cdd:COG1069 213 EEFFAALDPLLDGLAD-RLGTEIYPLGEP---AGTltaewaarlglppGTAVAVGAIDAHAGAVGAGGVEPGtLVKV-MG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 266 T-GCFMLMNTGEKAVQskhgllttiawGIDGKVE-------YALEGSIFVAGSAIQWLRD----GLRMIKEAKD------ 327
Cdd:COG1069 288 TsTCHMLVSPEERFVP-----------GICGQVDgsivpgmWGYEAGQSAVGDIFAWFVRllvpPLEYEKEAEErgislh 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 328 ---SELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEAdSGITLKT 404
Cdd:COG1069 357 pllTEEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEE-EGVPIDE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 405 LRVDGG-AVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWN--IDRSFTP-AMTKEVQEK 480
Cdd:COG1069 436 IIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGsgFDKVYTPdPENVAVYDA 515
|
...
gi 1593221718 481 LYE 483
Cdd:COG1069 516 LYA 518
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-494 |
2.56e-32 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 129.36 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 1 MEKYILALDQGTTSSRAILFNRKGEIVHIAQKEFTqYFPQPGW-------VEHNpneiWGSILAVIATVLSEAAVSPEQI 73
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWR-HLAVPDVpgsmefdLEKN----WQLACQCIRQALQKAGIPASDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 74 AAIGITNQRETTVVWDKQtGQPIYNAIVWQSRQTVPICEqLKE--QGYDELFRAKTG--LLIDAYfsgTKVKWILDHVDG 149
Cdd:PRK10939 76 AAVSATSMREGIVLYDRN-GTEIWACANVDARASREVSE-LKElhNNFEEEVYRCSGqtLALGAL---PRLLWLAHHRPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 150 AREKAEKgellFGTIDTWLVWKLSGGRAhvTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTipy 229
Cdd:PRK10939 151 IYRQAHT----ITMISDWIAYMLSGELA--VDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHV--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 230 hffGQEV----------PIAGIAGDQQAALFGQACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTiAWGIDGKVEY 299
Cdd:PRK10939 222 ---TAKAaaetglragtPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNIRIN-PHVIPGMVQA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 300 alEGSIFVAGSAIQWLRD----GLRMIKEAKDSELYATRVESTDGVYV---------------------VPAFVGLGTpy 354
Cdd:PRK10939 298 --ESISFFTGLTMRWFRDafcaEEKLLAERLGIDAYSLLEEMASRVPVgshgiipifsdvmrfkswyhaAPSFINLSI-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 355 wDSDV--RGAIFgltrgttkehfiRATLESLAYQTKDVLMAMEADSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERP 432
Cdd:PRK10939 374 -DPEKcnKATLF------------RALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVP 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593221718 433 VVNETTALGAAYLAGLAVGYWNSKEEIAQQW-NIDRSFTPAMT-KEVQEKLYEGWKKAVQAARA 494
Cdd:PRK10939 441 VVKEATALGCAIAAGVGAGIYSSLAETGERLvRWERTFEPNPEnHELYQEAKEKWQAVYADQLG 504
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
4-483 |
1.33e-31 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 127.01 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YIlALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAavSPEQIAAIGITNQRE 83
Cdd:PRK15027 2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TTVVWDKQTgQPIYNAIVWQSRQTVPICEQLKEQGydELFRAKTGLLIDAYFSGTKVKWIldhvdgAREKAEkgelLFGT 163
Cdd:PRK15027 79 GATLLDAQQ-RVLRPAILWNDGRCAQECALLEARV--PQSRVITGNLMMPGFTAPKLLWV------QRHEPE----IFRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 164 IDT------WLVWKLSGGRAhvTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRPSSEIYAHTIP--YHFFGQ- 234
Cdd:PRK15027 146 IDKvllpkdYLRLRMTGEFA--SDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPevAKAWGMa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 235 EVPIAGIAGDQQAALFGQACFEEGMAKNTYGT-GCFMLMNTG-----EKAVQS-KHGLlttiawgidgKVEYALEGSIFV 307
Cdd:PRK15027 224 TVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSfCHAL----------PQRWHLMSVMLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 308 AGSAIQW------LRDGLRMIKEAKDSElyatrvESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLE 381
Cdd:PRK15027 294 AASCLDWaakltgLSNVPALIAAAQQAD------ESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 382 SLAYQTKDVLMAMEAdSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVE-RPVVNETTALGAAYLAGLAVGYWNSKEEIA 460
Cdd:PRK15027 368 GVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRTGGDVGPALGAARLAQIAANPEKSLIELL 446
|
490 500 510
....*....|....*....|....*....|.
gi 1593221718 461 QQWNIDRSFTP--------AMTKEVQEKLYE 483
Cdd:PRK15027 447 PQLPLEQSHLPdaqryaayQPRRETFRRLYQ 477
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-462 |
1.48e-29 |
|
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: 121.49 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGITnqre 83
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 84 TT---VVWDKQ--------TGQPIYNAIVWQSRQTVPICEQLKEQGYDELfraktgllidAYFSGT--------KVKWIL 144
Cdd:cd07782 77 ATcslVVLDAEgkpvsvspSGDDERNVILWMDHRAVEEAERINATGHEVL----------KYVGGKispemeppKLLWLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 145 DHVDGAREKAEKgelLFGTIDtWLVWKLSGGRAHvtdySNASRT-----LMFNIHELKWDEELL---------------- 203
Cdd:cd07782 147 ENLPETWAKAGH---FFDLPD-FLTWKATGSLTR----SLCSLVckwtyLAHEGSEGGWDDDFFkeigledlvednfaki 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 204 -SILNVPKSM--------------LPEVRP--SSEIYAHtipyhffgqevpiAGIAGDQQAALFGQAC----FEEGMAKn 262
Cdd:cd07782 219 gSVVLPPGEPvgggltaeaakelgLPEGTPvgVSLIDAH-------------AGGLGTLGADVGGLPCeadpLTRRLAL- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 263 TYGTG-CFMlmntgekaVQSKHGLLTTIAWG------IDGKveYALEGSIFVAGSAIQWLRDG-------LRMIKEAKDS 328
Cdd:cd07782 285 ICGTSsCHM--------AVSPEPVFVPGVWGpyysamLPGL--WLNEGGQSATGALLDHIIEThpaypelKEEAKAAGKS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 329 --ELYATRVES------------TDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIR---ATLESLAYQTKDVL 391
Cdd:cd07782 355 iyEYLNERLEQlaeekglplaylTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHII 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1593221718 392 MAMEAdSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQ 462
Cdd:cd07782 435 EAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAA 504
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-483 |
8.91e-26 |
|
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: 110.41 E-value: 8.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFN-RKGEIVHIAQKEFTQY-FPQPGWVEHNPNEIWGSILAVIATVLSEAAVSPEQIAAIGItNQ 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDsSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGV-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 82 RETTVVWDKQ----TGQPIY----NAIVWQSRQTVPICEQLKEQGYDELfRAKTGLLIDAYFSGTKVKWILDHVDGAREK 153
Cdd:cd07768 80 TCSLAIFDREgtplMALIPYpnedNVIFWMDHSAVNEAQWINMQCPQQL-LDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 154 AEKgelLFGTIDtWLVWKLSGgrahvtDYSNASRTLM----FNIHELKWDEELLSIL------NVPKSMLPEVRPSSEIY 223
Cdd:cd07768 159 HFH---IFDLHD-YIAYELTR------LYEWNICGLLgkenLDGEESGWSSSFFKNIdprlehLTTTKNLPSNVPIGTTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 224 AHTIPYHF--FGQEVPIAGIAG--DQQAALFG--QACFEEGMAKNTYGTGCFMLMNTGEKAVQSKHGLLTTiawGIDGkv 297
Cdd:cd07768 229 GVALPEMAekMGLHPGTAVVVSciDAHASWFAvaSPHLETSLFMIAGTSSCHMYGTTISDRIPGVWGPFDT---IIDP-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 298 EYAL-EGSIFVAGSAIQWLRDG------LRMIKEaKDSELYATRVES----------TDGVYVVPAFVGLGTPYWDSDVR 360
Cdd:cd07768 304 DYSVyEAGQSATGKLIEHLFEShpcarkFDEALK-KGADIYQVLEQTirqieknnglSIHILTLDMFFGNRSEFADPRLK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 361 GAIFGLTRGTTKEHF---IRATLESLAYQTKDVLMAMEADsGITLKTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNET 437
Cdd:cd07768 383 GSFIGESLDTSMLNLtykYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1593221718 438 TALGAAYLAGLA----VGYWNSKEEIAQQWNIDRSFTPAMTKEVQ--EKLYE 483
Cdd:cd07768 462 GILGAAVLAKVAagkkQLADSITEADISNDRKSETFEPLAYRLGAdyILLYK 513
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
4-461 |
5.12e-22 |
|
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: 98.37 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAIL--FNRKG---EIVHiaqkeftqYFPqpgwveHNPNEI-------WGSILAVIATVLSEAAVSPE 71
Cdd:cd07771 1 NYLAVDLGASSGRVILgsLDGGKlelEEIH--------RFP------NRPVEInghlywdIDRLFDEIKEGLKKAAEQGG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 72 QIAAIGITnqretTvvW-------DKQtGQPIYNAIVWQSRQTVPICEQLKEQ-GYDELFRaKTGLLIDAYFSGTKVKWI 143
Cdd:cd07771 67 DIDSIGID-----T--WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKiSKEELYE-RTGIQFQPINTLYQLYAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 144 LDHVDGAREKAEKgeLLFgtIDTWLVWKLSGGRahVTDYSNASRTLMFNIHELKWDEELLSILNVPKSMLPEVRP----- 218
Cdd:cd07771 138 KKEGPELLERADK--LLM--LPDLLNYLLTGEK--VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPpgtvl 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 219 ---SSEIYAHTIpyhffGQEVPIAGIAG-DQQAALFGQACFEEGMAkntY---GTGCFMlmntGekaVQSKHGLLTTIAW 291
Cdd:cd07771 212 gtlKPEVAEELG-----LKGIPVIAVAShDTASAVAAVPAEDEDAA---FissGTWSLI----G---VELDEPVITEEAF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 292 GIDGKVEYALEGSIF----VAGSAI------QWLRDGLR-----MIKEAKDSELYATRVESTDgvyvvPAFvglGTPywd 356
Cdd:cd07771 277 EAGFTNEGGADGTIRllknITGLWLlqecrrEWEEEGKDysydeLVALAEEAPPFGAFIDPDD-----PRF---LNP--- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 357 SDVRGAI------FGLTRGTTKEHFIRATLESLAYQTKDVLMAMEADSGITLKTLRVDGGAVKNNFLMQFQSDILGVPVE 430
Cdd:cd07771 346 GDMPEAIraycreTGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVI 425
|
490 500 510
....*....|....*....|....*....|..
gi 1593221718 431 R-PVvnETTALGAAYLAGLAVGYWNSKEEIAQ 461
Cdd:cd07771 426 AgPV--EATAIGNLLVQLIALGEIKSLEEGRE 455
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-487 |
2.00e-17 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 84.90 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 1 MEKYILALDQGTTSSRAILFN-RKGEIVHIAQKEFT-----QYFPQPG-WVEHNPNEIWGSILAVIATVLSEAAVSPEQI 73
Cdd:PRK04123 1 MMAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPhwvkgRYLDLPPnQALQHPLDYIESLEAAIPAVLKEAGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 74 AAIGITNQRETTVVWDKQtGQPIY---------NAIV--W-------QSRQTVPICEQLKEQGYD---------ELFRAK 126
Cdd:PRK04123 81 VGIGVDFTGSTPAPVDAD-GTPLAllpefaenpHAMVklWkdhtaqeEAEEINRLAHERGEADLSryiggiyssEWFWAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 127 tgllidayfsgtkVKWILDHvdgAREKAEKGELLFGTIDtWLVWKLSGgrahVTDYSNASRT-------LMFniHElKWD 199
Cdd:PRK04123 160 -------------ILHVLRE---DPAVYEAAASWVEACD-WVVALLTG----TTDPQDIVRSrcaaghkALW--HE-SWG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 200 ----EELLSILN------VPKSMLPEVRPSSEIYAHTIPY--HFFG--QEVPIAGIAGDQQAALFGQACfEEGMAKNTYG 265
Cdd:PRK04123 216 glpsADFFDALDpllargLRDKLFTETWTAGEPAGTLTAEwaQRLGlpEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 266 TG-CFMLMNTGEKAVQskhgllttiawGIDGKVE-------YALE------GSIFvagsaiQWLRDGL---RMIKEAKD- 327
Cdd:PRK04123 295 TStCDILLADKQRAVP-----------GICGQVDgsivpglIGYEagqsavGDIF------AWFARLLvppEYKDEAEAr 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 328 --------SELYATRVESTDGVYVVPAFVGLGTPYWDSDVRGAIFGLTRGTTKEHFIRATLESLAYQTKDVLMAMEaDSG 399
Cdd:PRK04123 358 gkqllellTEAAAKQPPGEHGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQG 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 400 ITLKTLRVDGG-AVKNNFLMQFQSDILGVPVErpVV--NETTALGAAYLAGLAVGYWNSKEEIAQQW--NIDRSFTP-AM 473
Cdd:PRK04123 437 VPVEEVIAAGGiARKNPVLMQIYADVLNRPIQ--VVasDQCPALGAAIFAAVAAGAYPDIPEAQQAMasPVEKTYQPdPE 514
|
570
....*....|....
gi 1593221718 474 TKEVQEKLYEGWKK 487
Cdd:PRK04123 515 NVARYEQLYQEYKQ 528
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
4-464 |
1.20e-14 |
|
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: 76.06 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 4 YILALDQGTTSSRAILFNRKGEIVHIAQKEFTQYFPQ---PGWVEHNPNE--------IWGSILAVIATVLSEAAVSPEQ 72
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEygtKGGVHRDGDGgevtspvlMWVEALDLLLEKLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 73 IAAIGITNQRETTVVWDKQTGQPIYN-------------------AIVWQSRQTVPICEQLKEQ--GYDELfrAK-TGll 130
Cdd:cd07776 81 VKAISGSGQQHGSVYWSKGAESALANldpskslaeqlegafsvpdSPIWMDSSTTKQCRELEKAvgGPEAL--AKlTG-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 131 IDAY--FSGTKV-KWILDHVDgAREKAEKGELL--FGTidTWLVwklsgGRAHVTDYSNASRTLMFNIHELKWDEELLSI 205
Cdd:cd07776 157 SRAYerFTGPQIaKIAQTDPE-AYENTERISLVssFLA--SLLL-----GRYAPIDESDGSGMNLMDIRSRKWSPELLDA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 206 LNVP--KSMLPEVRPSSEIYAHTIPYHF----FGQEVPIAGIAGDQQAALFGQACfEEGMAKNTYGTG--CFMLMNTGEK 277
Cdd:cd07776 229 ATAPdlKEKLGELVPSSTVAGGISSYFVerygFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTSdtVFLVLDEPKP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 278 avqskhgllttiawgidgkveyALEGSIFVA---------------GS-AIQWLRDGLRmikeAKDSELYATRVEST--- 338
Cdd:cd07776 308 ----------------------GPEGHVFANpvdpgsymamlcyknGSlARERVRDRYA----GGSWEKFNELLESTppg 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 339 -DGVyvvpafvgLGTPYWDSD----------VRGAIFGLTRGTTKEHFIRATLESlayQtkdvLMAMEADS-----GITL 402
Cdd:cd07776 362 nNGN--------LGLYFDEPEitppvpgggrRFFGDDGVDAFFDPAVEVRAVVES---Q----FLSMRLHAerlgsDIPP 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593221718 403 KTLRVDGGAVKNNFLMQFQSDILGVPVERPVVNETTALGAAYLAGLAVGYWNSKEEIAQQWN 464
Cdd:cd07776 427 TRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVV 488
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
6-458 |
5.70e-13 |
|
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: 70.90 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 6 LALDQGTTSSRAILFNRKGEIVHIAQKE--FTQYFPQPGWVEHNPNEIWGSILAVIATVLSEAAVSpeQIAAIGIT---- 79
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLATSERPisYKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDY--IVSGIGVSatcs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 80 ---NQRETT--------VVWDKQtgQPIYNAIVWQSRQTVPICEQLKEQGYDElfraktgllIDAYFSGT--------KV 140
Cdd:cd07778 81 mvvMQRDSDtsylvpynVIHEKS--NPDQDIIFWMDHRASEETQWLNNILPDD---------ILDYLGGGfipemaipKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 141 KWILDHVDGAREKaekgELLFGTIDTWLVWKLSGGRAHVTD-YSNAS-RTLMFNIHELK-WDEELLSilNVPKSMLPEVR 217
Cdd:cd07778 150 KYLIDLIKEDTFK----KLEVFDLHDWISYMLATNLGHSNIvPVNAPpSIGIGIDGSLKgWSKDFYS--KLKISTKVCNV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 218 PSSEIYAHTIPY-------------HFFGQEVPIAGIAG--DQQAALFGQACfEEGMAKNTY----GTGCFMLMNTGEKA 278
Cdd:cd07778 224 GNTFKEAPPLPYagipigkvnvilaSYLGIDKSTVVGHGciDCYAGWFSTFA-AAKTLDTTLfmvaGTSTCFLYATSSSQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 279 VQSKHGLlttiaWG-----IDGKVEY-------------------ALEGSIFVAGSAIQWLRDGLRMI-KEAKDSELYAT 333
Cdd:cd07778 303 VGPIPGI-----WGpfdqlLKNYSVYeggqsatgklieklfnshpAIIELLKSDANFFETVEEKIDKYeRLLGQSIHYLT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 334 RVESTDGVYVvpafvGLGTPYWDSDVRGAIFGLTRGTTKE----HFIrATLESLAYQTKDVLMAMEaDSGITLKTLRVDG 409
Cdd:cd07778 378 RHMFFYGDYL-----GNRTPYNDPNMSGSFIGESTDSSLTdlvlKYI-LILEFLAFQTKLIIDNFQ-KEKIIIQKVVISG 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1593221718 410 GAVKNNFLMQFQSDILGVP---VERPVVNETTALGAAYLAGLAVGYWNSKEE 458
Cdd:cd07778 451 SQAKNARLLQLLSTVLSKIhiiVPLSDSKYAVVKGAALLGKAAFLHNQSIEE 502
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
181-441 |
2.23e-07 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 53.18 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 181 DYSNASRTLMFNIHELKWDEELLSILNVPKSMLPevRPSSEiyAHTIPYHFF--GQEVPIAGIAG-DQQAALFGQACFEE 257
Cdd:PRK10640 157 EYTNATTTQLVNINSDDWDESLLAWSGAPKAWFG--RPTHP--GNVIGHWICpqGNEIPVVAVAShDTASAVIASPLNDS 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 258 GMAKNTYGTGCFMLMN-----TGEKAVQSKhgllTTIAWGIDGKveYALEGSIFVAgsaiqWLRDglRMIKEAKDSELYA 332
Cdd:PRK10640 233 DAAYLSSGTWSLMGFEsqtpfTNDTALAAN----ITNEGGAEGR--YRVLKNIMGL-----WLLQ--RVLQERQITDLPA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593221718 333 TrVESTDGvyvVPAFVGLGTPYWD-----SDVRGAIFGLTRGT------TKEHFIRATLESLAYQTKDVLMAMEADSGIT 401
Cdd:PRK10640 300 L-IAATAA---LPACRFLINPNDDrfinpPSMCSEIQAACRETaqpvpeSDAELARCIFDSLALLYADVLHELAQLRGEP 375
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1593221718 402 LKTLRVDGGAVKNNFLMQFQSDILGVPV-ERPVvnETTALG 441
Cdd:PRK10640 376 FSQLHIVGGGCQNALLNQLCADACGIRViAGPV--EASTLG 414
|
|
| |
