|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
8-445 |
1.12e-143 |
|
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: 419.30 E-value: 1.12e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYSChDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASV-PFPVKNISIASFGESGV 86
Cdd:cd07773 3 LGIDIGTTNVKAVLFDE-DGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAgPDPIAAISVSSQGESGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 87 FVDKEGVILTPMLAWYDRRGESYLSSL-SKAEAEELYSITGLPPHSNYSAFKMRWLLDNYSLHERKDICWLHAPEVLLWR 165
Cdd:cd07773 82 PVDRDGEPLGPAIVWFDPRGKEEAEELaERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 166 MTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDHMVGA 245
Cdd:cd07773 162 LTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHLCAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 246 RALQL-QPGDVLNSTGTTEGILLLNTQPTLDVQARRDKLANGCYSDGEFFTLFASLPvGGYALEWVKKTFRLTDKEISTG 324
Cdd:cd07773 242 LGAGViEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSYGHHVPGGYYYLAGSLP-GGALLEWFRDLFGGDESDLAAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 325 LEKAMEQYLKPSwsvehVPVFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFAHCHGCF---NIPAG 401
Cdd:cd07773 321 DELAEAAPPGPT-----GLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALekaGIPID 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 447036295 402 RtVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07773 396 E-IRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLA 438
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
8-482 |
3.27e-104 |
|
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: 320.24 E-value: 3.27e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYSChDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFP---VKNISIASFGES 84
Cdd:COG1070 4 LGIDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDpeeIAAIGVSGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 85 GVFVDKEGVILTPMLAWYDRRGESYLSSLSKA-EAEELYSITGLPPHSNYSAFKMRWLLDNYSLHERKDICWLHAPEVLL 163
Cdd:COG1070 83 LVLLDADGEPLRPAILWNDTRAAAEAAELREElGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 164 WRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDHMV 243
Cdd:COG1070 163 YRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 244 GARALQ-LQPGDVLNSTGTTEGILLLNTQPTLDVQARrdkLANGCYSDGEFFTLFASLPVGGYALEWVKKTFRLTDKEIS 322
Cdd:COG1070 243 AALGAGaVEPGDAAVSLGTSGVVFVVSDKPLPDPEGR---VHTFCHAVPGRWLPMGATNNGGSALRWFRDLFADGELDDY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 323 TGLEKAMEQYLKPSwsveHVPVFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFAHCHGCF---NIP 399
Cdd:COG1070 320 EELNALAAEVPPGA----DGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALeeaGVK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 400 AGRtVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIAC---------PNVVPPTVPVAERYFPDAVRSAKL 470
Cdd:COG1070 396 IDR-IRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAvglglyddlEEAAAAMVRVGETIEPDPENVAAY 474
|
490
....*....|..
gi 447036295 471 KIYQQQWLSFYQ 482
Cdd:COG1070 475 DELYERYRELYP 486
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
8-445 |
8.90e-66 |
|
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: 217.43 E-value: 8.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYScHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFP---VKNISIASFGES 84
Cdd:cd00366 3 LGIDIGTTSVKAALFD-EDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDpsdIAAIGISGQMPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 85 GVFVDKEGVILTPMLAWYDRRGesylsslskaeaeelysitglpphsnysafkmrwlldnyslherkdiCWLHAPEVLLW 164
Cdd:cd00366 82 VVLVDADGNPLRPAIIWLDRRA-----------------------------------------------KFLQPNDYIVF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 165 RMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDHM-- 242
Cdd:cd00366 115 RLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAaa 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 243 -VGARAlqLQPGDVLNSTGTTEGILLLNTQPtldvQARRDKLANGCYSDGEFFTLFASLPVGGYALEWVKKTF--RLTDK 319
Cdd:cd00366 195 aLGAGV--VEPGDAVDSTGTSSVLSVCTDEP----VPPDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFgeEEDSD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 320 EISTGLEKAMEQYLKPSWSVehvpVFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFAHCHGCF--- 396
Cdd:cd00366 269 AEYEGLDELAAEVPPGSDGL----IFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILeel 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 447036295 397 NIPAGRtVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd00366 345 GVKIKE-IRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
8-481 |
1.47e-63 |
|
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: 213.96 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYSCHDVSVLEVRKfPTPIISSDKGEVDFDIEALWQALRLVMAELVASV-PFPVKNISIASFGESGV 86
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVASSSA-EYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLgGGEVDAIGFSSAMHSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 87 FVDKEGVILTPMLAWYDRRGESYLSSLSKAE-AEELYSITGLPPHSNYSAFKMRWLLDNYSLHERKDICWLHAPEVLLWR 165
Cdd:cd07770 82 GVDEDGEPLTPVITWADTRAAEEAERLRKEGdGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYLLYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 166 MTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHD---HM 242
Cdd:cd07770 162 LTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDgalAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 243 VGARAlqLQPGDVLNSTGTTEGILLLNTQPTLDVQARrdklaNGCY-SDGEFFTLFASLPVGGYALEWVKKTFRLTDKEI 321
Cdd:cd07770 242 LGSGA--LDPGRAALTVGTSGAIRVVSDRPVLDPPGR-----LWCYrLDENRWLVGGAINNGGNVLDWLRDTLLLSGDDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 322 STgLEKAMEQYLKPSwsveHVPVFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFAHCH---GCFNI 398
Cdd:cd07770 315 EE-LDKLAEAVPPGS----HGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYealEELAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 399 PAgRTVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIAC-------PNVVPPTVPVAERYFPDAVRSAKLK 471
Cdd:cd07770 390 PV-KEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALealglisSLEADELVKIGKVVEPDPENHAIYA 468
|
490
....*....|
gi 447036295 472 IYQQQWLSFY 481
Cdd:cd07770 469 ELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
8-445 |
3.12e-58 |
|
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: 200.05 E-value: 3.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYSChDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFPVKNISIASFgeSG-- 85
Cdd:cd07805 3 LAIDLGTSGVKAALVDL-DGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAF--SGqm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 86 ---VFVDKEGVILTPMLAWYDRRGESYLSSLSKAE-AEELYSITGLPPHS-NYSAFKMRWLLDNyslheRKDI-----CW 155
Cdd:cd07805 80 qgvVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLgGIEGYRLGGGNPPSgKDPLAKILWLKEN-----EPEIyakthKF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 156 LHAPEVLLWRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVT 235
Cdd:cd07805 155 LDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 236 LAGHDHM---VGARAlqLQPGDVLNSTGTTEGILLLNTQPTLDVQARrdkLANGCYSDGEFFTLFASLPVGGYALEWVKK 312
Cdd:cd07805 235 GGGGDAAaaaLGAGA--VEEGDAHIYLGTSGWVAAHVPKPKTDPDHG---IFTLASADPGRYLLAAEQETAGGALEWARD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 313 TFrLTDKEISTGLEKAMEQYlkpswsVEHVP------VFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLA 386
Cdd:cd07805 310 NL-GGDEDLGADDYELLDEL------AAEAPpgsnglLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447036295 387 MEFAHCHGCF--NIPAGRTVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETV-SLGALLIA 445
Cdd:cd07805 383 FNLRWLLEALekLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQEAgALGAALLA 444
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-481 |
3.23e-57 |
|
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: 197.38 E-value: 3.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYScHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFPVKNISIASFgeSG-- 85
Cdd:cd07808 3 LGIDLGTSSVKAVLVD-EDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGL--TGqm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 86 ---VFVDKEGVILTPMLAWYDRRGESYLSSLSKAEAEELYSITGLPPHSNYSAFKMRWLLDNYSLHERKDICWLHAPEVL 162
Cdd:cd07808 80 hglVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 163 LWRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKV------TL 236
Cdd:cd07808 160 RYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVvagagdNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 237 AGHdhmVGARAlqLQPGDVLNSTGTTEGILLLNTQPTLDVQARrdkLANGCYSDGEFFTLFASLPVGGYALEWVKKTFRL 316
Cdd:cd07808 240 AAA---LGAGV--VEPGDALISLGTSGVVFAPTDKPVPDPKGR---LHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 317 TDKEISTGLEKAmeqylkpswsvEHVP------VFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFA 390
Cdd:cd07808 312 DRESFDELDAEA-----------AKVPpgseglLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 391 HCHGCFNIPAG--RTVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIAC---------PNVVPPTVPVAER 459
Cdd:cd07808 381 DSLEVLKELGIkvKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAvgagvfddlEEAAAACIKIEKT 460
|
490 500
....*....|....*....|..
gi 447036295 460 YFPDAVRSAKLKIYQQQWLSFY 481
Cdd:cd07808 461 IEPDPERHEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
8-445 |
2.40e-55 |
|
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: 190.81 E-value: 2.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYschDVS--VLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFPVKNI---SIASFG 82
Cdd:cd07779 3 LGIDVGTTSTRAIIF---DLDgnIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIaaiGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 83 ESGVFVDKEGVILTPMLAWYDRRgesylsslskaeaeelysitglpphsnysAFKMrwlldnyslherkdicwLHAPEVL 162
Cdd:cd07779 80 STFVPVDEDGRPLRPAISWQDKR-----------------------------TAKF-----------------LTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 163 LWRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDH- 241
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQq 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 242 --MVGARAlqLQPGDVLNSTGTTEGILLLNTQPTLDVQARrdkLANGCYSDGEFFTLFASLPVGGYALEWVKKTFrLTDK 319
Cdd:cd07779 194 caALGAGV--LEPGTASLSLGTAAVVIAVSDKPVEDPERR---IPCNPSAVPGKWVLEGSINTGGSAVRWFRDEF-GQDE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 320 EISTGLEKAMEQYLkpSWSVEHVP------VFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFAHC- 392
Cdd:cd07779 268 VAEKELGVSPYELL--NEEAAKSPpgsdglLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNl 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 447036295 393 ----HGCFNIpagRTVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07779 346 eameKAGVPI---EEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILA 399
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
8-446 |
2.32e-49 |
|
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: 175.05 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYschDVS--VLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFPVKNI---SIASFG 82
Cdd:cd07802 3 LGIDNGTTNVKAVLF---DLDgrEIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIagvGVTGHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 83 ESGVFVDKEGVILTPMLAWYDRRGESYLSSLSKA-EAEELYSITGLPPHSNYSAFKMRWLLDnyslHER---KDICW-LH 157
Cdd:cd07802 80 NGLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDgTLEKVYPLTGQPLWPGQPVALLRWLKE----NEPeryDRIRTvLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 158 APEVLLWRMTGAKKTEISLASRTLcLDIARRTWSRNAAGILGIP--FGVLAPLIKPGEVAGWVTATLREELGFSHEVKVT 235
Cdd:cd07802 156 CKDWIRYRLTGEISTDYTDAGSSL-LDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 236 LAGHD---HMVGARALQlqPGDVLNSTGTTEGILLLNTQPTLDvqarRDKLANGCYSD-GEFFTLFASlPVGGYALEWVK 311
Cdd:cd07802 235 AGAFDvvaSALGAGAVD--EGQLCVILGTWSINEVVTDEPVVP----DSVGSNSLHADpGLYLIVEAS-PTSASNLDWFL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 312 KTFRLTDKEISTGLEKAMEQYLKPSWSVEHVPVFIPHLRGSG-SPNknrhTRGLLFGLTDSLPPESLLESVFIGLAMEFA 390
Cdd:cd07802 308 DTLLGEEKEAGGSDYDELDELIAAVPPGSSGVIFLPYLYGSGaNPN----ARGGFFGLTAWHTRAHLLRAVYEGIAFSHR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 447036295 391 HCHGcfNIPAGRTVKVI---GPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIAC 446
Cdd:cd07802 384 DHLE--RLLVARKPETIrltGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAA 440
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
8-445 |
8.57e-47 |
|
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: 167.78 E-value: 8.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYsCHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPF-PVKNISIAsfGESG- 85
Cdd:cd07783 3 LGIDLGTSGVRAVVV-DEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPrRVVAIAVD--GTSGt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 86 -VFVDKEGVILTPMLAWYDRRGESYLSSLSKAeAEELYSITGLPPHSNYSAFKMRWLLDNYSLHERKDICWLHAPEVLLW 164
Cdd:cd07783 80 lVLVDREGEPLRPAIMYNDARAVAEAEELAEA-AGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 165 RMTGAKK-TEISLASRTLClDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDH-- 241
Cdd:cd07783 159 RLTGDRGvTDYNNALKLGY-DPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSia 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 242 -MVGARAlqLQPGDVLNSTGTTEGILLLNTQPTLDVQARrdklaNGCYSDGE-FFTLFASLPVGGYALEWVKKTFRLTDk 319
Cdd:cd07783 238 aFLASGA--VRPGDAVTSLGTTLVLKLLSDKRVPDPGGG-----VYSHRHGDgYWLVGGASNTGGAVLRWFFSDDELAE- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 320 eistgLEKAMEQYLKPSWSV-------EHVPVFIPHLRGSGSPnkNRHTRGLLFgltdslppESLLESV-FI-GLAMEFA 390
Cdd:cd07783 310 -----LSAQADPPGPSGLIYyplplrgERFPFWDPDARGFLLP--RPHDRAEFL--------RALLEGIaFIeRLGYERL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 447036295 391 HCHGCfniPAGRTVKVIGPAVKNPYWLQLKADILQCPIEAIAfDETVSLGALLIA 445
Cdd:cd07783 375 EELGA---PPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLA 425
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
7-245 |
1.18e-43 |
|
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: 154.42 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 7 ALVIDIGTTNCKVSCYScHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFP---VKNISIASFGE 83
Cdd:pfam00370 2 YLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISlkqIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 84 SGVFVDKEGVILTPMLAWYDRRGESYLSSLSK-AEAEELYSITGLPPHSNYSAFKMRWLLDNYSLHERKDICWLHAPEVL 162
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEeGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 163 LWRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDHM 242
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQ 240
|
...
gi 447036295 243 VGA 245
Cdd:pfam00370 241 AAA 243
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
10-445 |
2.49e-40 |
|
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: 150.78 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 10 IDIGTTNCKVSCYSCHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFPVKNisIASFGESG---- 85
Cdd:cd07809 5 IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRD--VAAIGISGqmhg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 86 -VFVDKEGVILTPMLAWYDRRGESYLSSLSKAEAEELYSITGLPPHSNYSAFKMRWLLDNYSLHERK--DICWLHapEVL 162
Cdd:cd07809 83 lVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARiaKILLPH--DYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 163 LWRMTGAKKTEISLASRTLCLDIARRTWSR---NAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGH 239
Cdd:cd07809 161 NWKLTGEKVTGLGDASGTFPIDPRTRDYDAellAAIDPSRDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 240 DHMVGARALQ-LQPGDVLNSTGTTEGILLLNTQPTLDVQARrdkLANGCYSDGEFFTLFASLPVGGYALEWVKKTFRLTD 318
Cdd:cd07809 241 DNMTGALGTGvVNPGTVAVSLGTSGTAYGVSDKPVSDPHGR---VATFCDSTGGMLPLINTTNCLTAWTELFRELLGVSY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 319 KEISTGLEKAmeqylkpswsvehvP------VFIPHLRGSGSPNkNRHTRGLLFGLTDS-LPPESL----LESVFIGL-- 385
Cdd:cd07809 318 EELDELAAQA--------------PpgagglLLLPFLNGERTPN-LPHGRASLVGLTLSnFTRANLaraaLEGATFGLry 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 386 AMEFAHCHGcfnIPAGRtVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07809 383 GLDILRELG---VEIDE-IRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQA 438
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
8-445 |
9.53e-39 |
|
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: 146.21 E-value: 9.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYSCHDvSVLEVRKFPTPIISSDKGE--VDFDIEALWQALRLVMAELVASVPFP---VKNISIASFG 82
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEG-KIVAIAYREWEYYTDDDYPdaKEFDPEELWEKICEAIREALKKAGISpedISAVSSTSQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 83 ESGVFVDKEGVIL--TPMLawyDRRGESYLSSLSKAEAEELYSITGLPPHSNYSAFKMRWLLDNY-SLHER-KDICWLHa 158
Cdd:cd07798 82 EGIVFLDKDGRELyaGPNI---DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAARLLWFKENRpEIFERiATVLSIS- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 159 pEVLLWRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAG 238
Cdd:cd07798 158 -DWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVVGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 239 HDHMVGARALQLQ-PGDVLNSTGTTEGILLLNTQPTLDVQARrdkLANGCYSDGEFFTLFASLPVGGYALEWVKKTFrLT 317
Cdd:cd07798 237 ADTQCALLGSGAIePGDIGIVAGTTTPVQMVTDEPIIDPERR---LWTGCHLVPGKWVLESNAGVTGLNYQWLKELL-YG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 318 DKEISTG-LEKAMEQYLKPSWSVehVPVF---IPHLRGSGSPNKnrhtrGLLFGLTDSLPP---ESLLESVFIGLAmeFA 390
Cdd:cd07798 313 DPEDSYEvLEEEASEIPPGANGV--LAFLgpqIFDARLSGLKNG-----GFLFPTPLSASEltrGDFARAILENIA--FA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 391 HCHGCFNIPA--GRTVKVI---GPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07798 384 IRANLEQLEEvsGREIPYIilcGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICA 443
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
8-445 |
3.72e-38 |
|
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: 145.30 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYScHDVSVLEV--RKFPTpiISSDKGEVDFDIEALWQALRLVMAELVASVPfpVKNISIASFG--- 82
Cdd:cd07769 3 LAIDQGTTSTRAILFD-EDGNIVASaqKEHEQ--IYPQPGWVEHDPEEIWENTLEVIREALAKAG--ISASDIAAIGitn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 83 --ESGVFVDKE-GVILTPMLAWYDRRGESYLSSLSKAEAEELY-SITGLPPHSNYSAFKMRWLLDNY----SLHERKDIC 154
Cdd:cd07769 78 qrETTVVWDKKtGKPLYNAIVWQDRRTADICEELKAKGLEERIrEKTGLPLDPYFSATKIKWILDNVpgarERAERGELL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 155 ------WlhapevLLWRMTGAKK--TEISLASRTLCLDIARRTWSRNAAGILGIPFGVLaPLIKP-GEVAGWVTATlree 225
Cdd:cd07769 158 fgtidtW------LIWKLTGGKVhvTDVTNASRTMLFNIHTLEWDDELLELFGIPRSML-PEVRPsSEVFGYTDPE---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 226 lGFSHEVKVT-LAGHDH--MVGARAlqLQPGDVLNSTGTteGI-LLLNTQPTLdVQARRDKLANGCYSDGEFFT--LFAS 299
Cdd:cd07769 227 -GLGAGIPIAgILGDQQaaLFGQGC--FEPGMAKNTYGT--GCfLLMNTGEKP-VPSKNGLLTTIAWQIGGKVTyaLEGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 300 LPVGGYALEWVKKTFRLTDKeiSTGLEKAMEQyLKPSWSVehvpVFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESL-- 377
Cdd:cd07769 301 IFIAGAAIQWLRDNLGLIED--AAETEELARS-VEDNGGV----YFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIvr 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447036295 378 --LESV-F----IGLAMEFAhchgcfnipAG---RTVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07769 374 aaLESIaYqtrdVLEAMEKD---------SGiklKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLA 442
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
255-446 |
3.66e-37 |
|
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: 135.53 E-value: 3.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 255 VLNSTGTTEGILLLNTQPTLDVQARRDKLANGCYSDgeFFTLFASLPVGGYALEWVKKTFRLTDKEISTGLEKAMEQYLK 334
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEMLPG--YWGLEGGQSAAGSLLAWLLQFHGLREELRDAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 335 PSWSVEH-VPVFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFAHCHGCFNIPAG---RTVKVIGPA 410
Cdd:pfam02782 79 LAAVAPAgGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGhpiDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 447036295 411 VKNPYWLQLKADILQCPIEAIAFDETVSLGALLIAC 446
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAA 194
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
8-445 |
2.79e-35 |
|
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: 136.89 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCK---VSCyschDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFP---VKNISIASF 81
Cdd:cd07804 3 LGIDIGTTGTKgvlVDE----DGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISpkeIAAIGVSGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 82 GESGVFVDKEGVILTPMLAWYDRRGESYLSSLSKA-EAEELYSITGLPPHSNYSAFKMRWLLDNyslheRKDIcW----- 155
Cdd:cd07804 79 VPALVPVDENGKPLRPAILYGDRRATEEIEWLNENiGEDRIFEITGNPLDSQSVGPKLLWIKRN-----EPEV-Fkktrk 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 156 -LHAPEVLLWRMTGAKKTEISLASRT-LCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVK 233
Cdd:cd07804 153 fLGAYDYIVYKLTGEYVIDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 234 VTLAGHDHMVGARAL-QLQPGDVLNSTGTTEGILLLNTQPTLDVQarrdkLANGCYSDGEFFTLFASLPVGGYALEWVKK 312
Cdd:cd07804 233 VVAGTVDAAASALSAgVVEPGDLLLMLGTAGDIGVVTDKLPTDPR-----LWLDYHDIPGTYVLNGGMATSGSLLRWFRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 313 TFR--LTDKEISTGLE--KAMEQylkpswSVEHVP------VFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPE----SLL 378
Cdd:cd07804 308 EFAgeEVEAEKSGGDSayDLLDE------EAEKIPpgsdglIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAhlyrALL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 379 ESVfiglAMEFAHCHGCFN---IPAGRTVkVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07804 382 EGV----AYGLRHHLEVIReagLPIKRLV-AVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLA 446
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
50-445 |
6.44e-35 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 136.31 E-value: 6.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 50 DIEALWQAL----RLVMAELVASVpfpVKNISIASFGESGVFVDKEGVILTPMLAWYDRRGESYLSSLSK-AEAEELYSI 124
Cdd:PRK10331 48 SLDAILQRFadccRQINSELTECH---IRGITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERyISAQQLQQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 125 TGLPPHSNYSAFKMRWLLDNY-SLHERKDiCWLHAPEVLLWRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFG 203
Cdd:PRK10331 125 SGVGAFSFNTLYKLVWLKENHpQLLEQAH-AWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 204 VLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHD---HMVGARALQLQPgdVLnSTGTTEgILLLNT-QPTLDVQAR 279
Cdd:PRK10331 204 LFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISAGHDtqfALFGSGAGQNQP--VL-SSGTWE-ILMVRSaQVDTSLLSQ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 280 RDKLA------NGCYSDGEFFtlfaslpVGGYALEWVKKTFRLTDKEISTGLEKAMEqylkpswsvehVP------VFIP 347
Cdd:PRK10331 280 YAGSTceldsqSGLYNPGMQW-------LASGVLEWVRKLFWTAETPYQTMIEEARA-----------IPpgadgvKMQC 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 348 HLRGSG-------SPNKNR-HT-RGLLFGLTDSLPPE-SLLESVfiglamefahchGCFNipAGRTVkVIGPAVKNPYWL 417
Cdd:PRK10331 342 DLLACQnagwqgvTLNTTRgHFyRAALEGLTAQLKRNlQVLEKI------------GHFK--ASELL-LVGGGSRNALWN 406
|
410 420
....*....|....*....|....*...
gi 447036295 418 QLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:PRK10331 407 QIKANMLDIPIKVLDDAETTVAGAAMFG 434
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
6-240 |
7.12e-33 |
|
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: 130.34 E-value: 7.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 6 AALVIDIGTTNCKVSCYSCHD--VSVLEVRKFPTPIISSDKGEVdFDIEALWQALRLVMAELVASVPfPVKNISIASFGE 83
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGgkLELEEIHRFPNRPVEINGHLY-WDIDRLFDEIKEGLKKAAEQGG-DIDSIGIDTWGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 84 SGVFVDKEGVILTPMLAWYDRRGESYLSSL-SKAEAEELYSITGLPPHSNYSAFKMRWLLDNYSLHERKDICWLHAPEVL 162
Cdd:cd07771 79 DFGLLDKNGELLGNPVHYRDPRTEGMMEELfEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447036295 163 LWRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGfSHEVKVTL-AGHD 240
Cdd:cd07771 159 NYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELG-LKGIPVIAvASHD 236
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-445 |
3.76e-32 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 128.64 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 1 MPDYhaALVIDIGTTNCKVSCYScHDVSVLEVRK------FPTPiissdkGEVDFDIEALWQALRLVMAELVASVPFPVK 74
Cdd:COG0554 1 MKKY--ILAIDQGTTSTRAILFD-RDGNIVAVAQreftqiYPQP------GWVEHDPEEIWESVLAVIREALAKAGISAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 75 NIsiASFG-----ESGVFVDKE-GVILTPMLAWYDRRGESYLSSLSKAEAEELY-SITGLPPHSNYSAFKMRWLLDNYS- 146
Cdd:COG0554 72 DI--AAIGitnqrETTVVWDRKtGKPLYNAIVWQDRRTADICEELKADGLEDLIrEKTGLVLDPYFSATKIKWILDNVPg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 147 ---LHERKDIC------WLhapevlLWRMTGAKK--TEISLASRTLCLDIARRTWSRNAAGILGIPFGVLaPLIKP-GEV 214
Cdd:COG0554 150 areRAEAGELLfgtidsWL------IWKLTGGKVhvTDVTNASRTMLFNIHTLDWDDELLELFGIPRSML-PEVRPsSEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 215 AGWVTATLreelgFSHEVKVT-LAGHDH--MVGaralQ--LQPGDVLNSTGTteG-ILLLNTQPTLdVQARrdklaNG-- 286
Cdd:COG0554 223 FGETDPDL-----FGAEIPIAgIAGDQQaaLFG----QacFEPGMAKNTYGT--GcFLLMNTGDEP-VRSK-----NGll 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 287 ---CYS-DGEffTLFA---SLPVGGYALEWVKKTFRLtdkeISTGLEkaMEQYLKpswSVEH---VpVFIPHLRGSGSPN 356
Cdd:COG0554 286 ttiAWGlGGK--VTYAlegSIFVAGAAVQWLRDGLGL----IDSAAE--SEALAR---SVEDnggV-YFVPAFTGLGAPY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 357 KNRHTRGLLFGLTDSLPPESL----LESvfIGL-------AMEfAHChgcfNIPAgRTVKVIGPAVKNPYWLQLKADILQ 425
Cdd:COG0554 354 WDPDARGAIFGLTRGTTRAHIaraaLES--IAYqtrdvldAME-ADS----GIPL-KELRVDGGASANDLLMQFQADILG 425
|
490 500
....*....|....*....|
gi 447036295 426 CPIEAIAFDETVSLGALLIA 445
Cdd:COG0554 426 VPVERPKVTETTALGAAYLA 445
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
8-445 |
3.87e-30 |
|
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: 122.60 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYScHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPfpVKNISIASFG----- 82
Cdd:cd07786 3 LAIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAG--IRASDIAAIGitnqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 83 ESGVFVDKE-GVILTPMLAWYDRRGESYLSSLSKAEAEEL-YSITGLPPHSNYSAFKMRWLLDN----YSLHERKDIC-- 154
Cdd:cd07786 80 ETTVVWDREtGKPVYNAIVWQDRRTADICEELKAEGHEEMiREKTGLVLDPYFSATKIRWILDNvpgaRERAERGELAfg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 155 ----WlhapevLLWRMTGAK--KTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLaPLIKP-GEVAGWVTATLreelg 227
Cdd:cd07786 160 tidsW------LIWKLTGGKvhATDVTNASRTMLFNIHTLEWDDELLELFGIPASML-PEVKPsSEVFGYTDPDL----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 228 FSHEVKVT-LAGHDH--MVGARAlqLQPGDVLNSTGTTeGILLLNTQPTLdvQARRDKLAN--GCYSDGEF-FTLFASLP 301
Cdd:cd07786 228 LGAEIPIAgIAGDQQaaLFGQAC--FEPGMAKNTYGTG-CFMLMNTGEKP--VRSKNGLLTtiAWQLGGKVtYALEGSIF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 302 VGGYALEWVKKTFRLTDKEISTGlekAMEQYLKPSWSVehvpVFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESL---- 377
Cdd:cd07786 303 IAGAAVQWLRDGLGLIESAAETE---ALARSVPDNGGV----YFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIaraa 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447036295 378 LESVF-----IGLAMEFAhchgcfnipAGRTVKVI---GPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07786 376 LESIAyqtrdLLEAMEAD---------SGIPLKELrvdGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLA 442
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
7-445 |
2.02e-27 |
|
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: 114.24 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 7 ALVIDIGTTNCKVSCYSCHDVSVLEVRKFPTP--IISSDKGEVDFDIEALWQALRLVMAELVASVPFPVKNISIasfgeS 84
Cdd:cd07777 2 VLGIDIGTTSIKAALLDLESGRILESVSRPTPapISSDDPGRSEQDPEKILEAVRNLIDELPREYLSDVTGIGI-----T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 85 G-----VFVDKEGVILTPMLAWYDRRG-ESYLSSLSkAEAEELYSITGLPPHSNYSAFKMRWLLDNYSLHERKDICwLHA 158
Cdd:cd07777 77 GqmhgiVLWDEDGNPVSPLITWQDQRCsEEFLGGLS-TYGEELLPKSGMRLKPGYGLATLFWLLRNGPLPSKADRA-GTI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 159 PEVLLWRMTGAKK--TEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGwvtaTLREELGfsHEVKVTL 236
Cdd:cd07777 155 GDYIVARLTGLPKpvMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVG----TLSSALP--KGIPVYV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 237 AGHDHMVGARALQLQPGD--VLN-STGTTEGILLLNTQPTLDVQARrdklangCYSDGEFFTLFASLPvGGYALEWVKKT 313
Cdd:cd07777 229 ALGDNQASVLGSGLNEENdaVLNiGTGAQLSFLTPKFELSGSVEIR-------PFFDGRYLLVAASLP-GGRALAVLVDF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 314 FR---------LTDKEISTGLEKAMEQYLKPSWSVEhvPVFIPhlrgsgspnkNRHTRGLLFGLT----DSLPPESLLES 380
Cdd:cd07777 301 LRewlrelggsLSDDEIWEKLDELAESEESSDLSVD--PTFFG----------ERHDPEGRGSITnigeSNFTLGNLFRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447036295 381 VFIGLAMEFAHCHGCFNIPAGRTVKVIGP---AVKNPyWLQLK-ADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07777 369 LCRGIAENLHEMLPRLDLDLSGIERIVGSggaLRKNP-VLRRIiEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
8-445 |
1.11e-25 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 109.68 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKV-----SCYSCHDVSVLEVRKFPTPiissdkGEVDFD----IEALWQALRLVMAELVASVP-FPVKNIS 77
Cdd:PTZ00294 5 GSIDQGTTSTRFiifdeKGNVVSSHQIPHEQITPHP------GWLEHDpeeiLRNVYKCMNEAIKKLREKGPsFKIKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 78 IASFGESGVFVDKE-GVILTPMLAWYDRRGESYLSSLSKA--EAEELYSITGLPPHSNYSAFKMRWLLDNY----SLHER 150
Cdd:PTZ00294 79 ITNQRETVVAWDKVtGKPLYNAIVWLDTRTYDIVNELTKKygGSNFFQKITGLPISTYFSAFKIRWMLENVpavkDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 151 KDIC------WlhapevLLWRMTGAKK--TEISLASRTLCLDIARRTWSRNAAGILGIPFGVLaPLIKPG-EVAGWVTAT 221
Cdd:PTZ00294 159 GTLLfgtidtW------LIWNLTGGKShvTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETL-PEIKSSsENFGTISGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 222 LREELgfsHEVKVTLAGHDH---MVGARALQLqpGDVLNSTGTteGILLLNTQPTLDVQARRDKLANGCYSDGE----FF 294
Cdd:PTZ00294 232 AVPLL---EGVPITGCIGDQqaaLIGHGCFEK--GDAKNTYGT--GCFLLMNTGTEIVFSKHGLLTTVCYQLGPngptVY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 295 TLFASLPVGGYALEWVKKTFRLTD--KEISTGLEKameqyLKPSWSVehvpVFIPHLRGSGSPNKNRHTRGLLFGLTDSL 372
Cdd:PTZ00294 305 ALEGSIAVAGAGVEWLRDNMGLIShpSEIEKLARS-----VKDTGGV----VFVPAFSGLFAPYWRPDARGTIVGMTLKT 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447036295 373 PPESLLESVFIGLAMEFAHCHGCFNIPAGRTVKVI---GPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:PTZ00294 376 TRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLrvdGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLA 451
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
10-445 |
4.11e-24 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 105.17 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 10 IDIGTTNCKVSCYScHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVAS-------VPFPVKNISIASFG 82
Cdd:PLN02295 5 IDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKaaakghnVDSGLKAIGITNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 83 ESGVFVDKE-GVILTPMLAWYDRRGESYLSSLSKAEAE---ELYSITGLPPHSNYSAFKMRWLLDNY----SLHERKDIC 154
Cdd:PLN02295 84 ETTVAWSKStGRPLYNAIVWMDSRTSSICRRLEKELSGgrkHFVETCGLPISTYFSATKLLWLLENVdavkEAVKSGDAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 155 WLHAPEVLLWRMTGAKK-----TEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTAtlreelgfS 229
Cdd:PLN02295 164 FGTIDSWLIWNLTGGASggvhvTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAK--------G 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 230 HEV-KVTLAG-----HDHMVGARAlqlQPGDVLNSTGTteG-ILLLNTQPTLdVQARRDKLANGCYSDGE----FFTLFA 298
Cdd:PLN02295 236 WPLaGVPIAGclgdqHAAMLGQRC---RPGEAKSTYGT--GcFILLNTGEEV-VPSKHGLLTTVAYKLGPdaptNYALEG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 299 SLPVGGYALEWVKKTFRLtdkeISTGLE-KAMEQYLKPSWSVEHVP----VFIPHLRGSGspnknrhtRGLLFGLTDSLP 373
Cdd:PLN02295 310 SVAIAGAAVQWLRDNLGI----IKSASEiEALAATVDDTGGVYFVPafsgLFAPRWRDDA--------RGVCVGITRFTN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 374 P----ESLLES-------VFIGL---AMEFAHCHGCFnipagrTVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSL 439
Cdd:PLN02295 378 KahiaRAVLESmcfqvkdVLDAMrkdAGEEKSHKGLF------LLRVDGGATANNLLMQIQADLLGSPVVRPADIETTAL 451
|
....*.
gi 447036295 440 GALLIA 445
Cdd:PLN02295 452 GAAYAA 457
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
6-445 |
4.14e-24 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 104.26 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 6 AALVIDIGTTNCKVSCYScHDVSVLEVRKFPTPIISSDKGEVDfDIEALWQALRLVMAELVASvpFPVKNISIASFGESG 85
Cdd:cd07772 1 VIAVFDIGKTNKKLLLFD-ENGEVLAERSTPNPEIEEDGYPCE-DVEAIWEWLLDSLAELAKR--HRIDAINFTTHGATF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 86 VFVDKEGVILTPMLawydrrgeSYLSSLSKAEAEELYSI------TGLPPHSNY--SAFKMRWLLDNYSLHERKDICWLH 157
Cdd:cd07772 77 ALLDENGELALPVY--------DYEKPIPDEINEAYYAErgpfeeTGSPPLPGGlnLGKQLYWLKREKPELFARAKTILP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 158 APEVLLWRMTGAKKTEI-SLASRTLCLDIARRTWSR--NAAGILGIPfgvlAPLIKPGEVAGWVTATLREELGFSHEVKV 234
Cdd:cd07772 149 LPQYWAWRLTGKAASEItSLGCHTDLWDFEKNEYSSlvKKEGWDKLF----PPLRKAWEVLGPLRPDLARRTGLPKDIPV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 235 TLAGHDHMVG-ARALQLQPGD-VLNSTGTTegILLLNtqPTLDVQARRDKLANGCysdgefftlFASL-----PV----- 302
Cdd:cd07772 225 GCGIHDSNAAlLPYLAAGKEPfTLLSTGTW--CIAMN--PGNDLPLTELDLARDC---------LYNLdvfgrPVktarf 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 303 -GGYALEwvKKTFRLTDKEISTGLEKAMEQYLKPSW----SVEHVPVFIPHLRGSGSPNKNRHtrgllfgltdslpPESL 377
Cdd:cd07772 292 mGGREYE--RLVERIAKSFPQLPSLADLAKLLARGTfalpSFAPGGGPFPGSGGRGVLSAFPS-------------AEEA 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447036295 378 LESVFIGLAMEFAHchgCFNIPAGRTVKVI--GPAVKNPYWLQLKADILQ-CPIEAIAFDETVSLGALLIA 445
Cdd:cd07772 357 YALAILYLALMTDY---ALDLLGSGVGRIIveGGFAKNPVFLRLLAALRPdQPVYLSDDSEGTALGAALLA 424
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
10-445 |
2.08e-23 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 103.00 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 10 IDIGTTNCKVSCYSCHDVSVL--EVRKFPTPIISSDKGEV-----DFdIEALWQALRLVMAELVASvPFPVKNISIASFG 82
Cdd:cd07781 5 IDFGTQSVRAGLVDLADGEELasAVVPYPTGYIPPRPGWAeqnpaDY-WEALEEAVRGALAEAGVD-PEDVVGIGVDTTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 83 ESGVFVDKEGVILTPMLAWYDRRgesylsslSKAEAEELYSiTGLPPHSNYSAF------------KMRWLLDNYSLHER 150
Cdd:cd07781 83 STVVPVDEDGNPLAPAILWMDHR--------AQEEAAEINE-TAHPALEYYLAYyggvyssewmwpKALWLKRNAPEVYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 151 KDICWLHAPEVLLWRMTGakkteislasrtlclDIARrtwSRNAAGI------------------LGIPFGVL-----AP 207
Cdd:cd07781 154 AAYTIVEACDWINARLTG---------------RWVR---SRCAAGHkwmynewgggppreflaaLDPGLLKLreklpGE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 208 LIKPGEVAGWVTATLREELGFSHEVKVTLAGHD-H--MVGARALQlqPGDVLNSTGTTEGILLLNTQPTLDvqarrdKLA 284
Cdd:cd07781 216 VVPVGEPAGTLTAEAAERLGLPAGIPVAQGGIDaHmgAIGAGVVE--PGTLALIMGTSTCHLMVSPKPVDI------PGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 285 NGCYSDG---EFFTLFASLPVGGYALEWVKKTFRLTDKEISTGL-----EKAMEqyLKPSwsvEHVPVFIPHLRGSGSPN 356
Cdd:cd07781 288 CGPVPDAvvpGLYGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIyallsEEAAK--LPPG---ESGLVALDWFNGNRTPL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 357 KNRHTRGLLFGLT-DSLPPE---SLLESVfiglAMEFAHCHGCFNiPAGRTVKVI----GPAVKNPYWLQLKADILQCPI 428
Cdd:cd07781 363 VDPRLRGAIVGLTlGTTPAHiyrALLEAT----AFGTRAIIERFE-EAGVPVNRVvacgGIAEKNPLWMQIYADVLGRPI 437
|
490
....*....|....*..
gi 447036295 429 EAIAFDETVSLGALLIA 445
Cdd:cd07781 438 KVPKSDQAPALGAAILA 454
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
10-445 |
1.54e-22 |
|
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: 100.01 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 10 IDIGTTNCKVSCYScHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASV---PFPVKNISIASFGESGV 86
Cdd:cd24121 5 IDAGTSVVKAVAFD-LDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLdvlPDRVAAIGVTGQGDGTW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 87 FVDKEGVILTPMLAWYDRRGESYLSSLSK-AEAEELYSITGLPPHSNYSAFKMRWLLDNYSlhERKDICW--LHAPEVLL 163
Cdd:cd24121 84 LVDEDGRPVRDAILWLDGRAADIVERWQAdGIAEAVFEITGTGLFPGSQAAQLAWLKENEP--ERLERARtaLHCKDWLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 164 WRMTGAKKTEISLASRTlCLDIARRTWSRNAAGILGIP--FGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDh 241
Cdd:cd24121 162 YKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 242 mVGARALQL---QPGD---VLNSTGTTEgilllntqpTLDVQARRDKLANG---CYSDGEFFTLFASLPVGGYALEWVKK 312
Cdd:cd24121 240 -VVATALGSgaiEPGDacsILGTTGVHE---------VVVDEPDLEPEGVGytiCLGVPGRWLRAMANMAGTPNLDWFLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 313 TFRLTDKEISTGLEKAMEQYLKPswSVEHVP------VFIPHLRGSG--SPNKNRHTRGLLFGLTDSLPPESLLESVFIG 384
Cdd:cd24121 310 ELGEVLKEGAEPAGSDLFQDLEE--LAASSPpgaegvLYHPYLSPAGerAPFVNPNARAQFTGLSLEHTRADLLRAVYEG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447036295 385 LAMEFAHCHGCFNIPAGRtVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd24121 388 VALAMRDCYEHMGEDPGE-LRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNA 447
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
10-445 |
2.82e-22 |
|
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: 99.52 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 10 IDIGTTNCKVSCY--SCHDVSV--LEV-RKFPTPiissdkGEVDFDIEALWQALRLVMAELVASV------PFPVKNISI 78
Cdd:cd07792 6 IDQGTTSTRFIVFdsTGELVAShqVEHkQIYPKP------GWVEHDPMEILESVYECIEEAVEKLkalgisPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 79 ASFGESGVFVDKE-GVILTPMLAWYDRRGESYLSSLSKAE---AEELYSITGLPPHSNYSAFKMRWLLDNY----SLHER 150
Cdd:cd07792 80 TNQRETTVVWDKStGKPLYNAIVWLDTRTSDTVEELSAKTpggKDHFRKKTGLPISTYFSAVKLRWLLDNVpevkKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 151 KDIC------WlhapevLLWRMTGAKK-----TEISLASRTLCLDIARRTWSRNAAGILGIPFGVLaPLIKP-GEVAGWV 218
Cdd:cd07792 160 GRLLfgtvdsW------LIWNLTGGKNggvhvTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSIL-PEIRSsSEVYGKI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 219 TATlreelgfsHEVKVTLAG-----HDHMVGARAlqLQPGDVLNSTGTteG-ILLLNTQPTLdVQARRDKLANGCYSDGE 292
Cdd:cd07792 233 ASG--------PLAGVPISGclgdqQAALVGQGC--FKPGEAKNTYGT--GcFLLYNTGEEP-VFSKHGLLTTVAYKLGP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 293 ----FFTLFASLPVGGYALEWVKKTFRLtdkeISTGLEkaMEQYLKpswSVEH------VPVF----IPHLRGSGspnkn 358
Cdd:cd07792 300 dappVYALEGSIAIAGAAVQWLRDNLGI----ISSASE--VETLAA---SVPDtggvyfVPAFsglfAPYWRPDA----- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 359 rhtRGLLFGLTDSLPPE----SLLESVfiglamefahchgCF---------NIPAG---RTVKVIGPAVKNPYWLQLKAD 422
Cdd:cd07792 366 ---RGTIVGLTQFTTKAhiarAALEAV-------------CFqtreildamNKDSGiplTSLRVDGGMTKNNLLMQIQAD 429
|
490 500
....*....|....*....|...
gi 447036295 423 ILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07792 430 ILGIPVERPSMVETTALGAAIAA 452
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-441 |
6.91e-22 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 98.36 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 1 MPDYHAAlvIDIGTTNC----------KVScyschdVSVLEVRK-FPTPiissdkGEVDFDIEALWQALRLVMAELVASv 69
Cdd:PRK00047 3 MKKYILA--LDQGTTSSraiifdhdgnIVS------VAQKEFTQiFPQP------GWVEHDPNEIWASQLSVIAEALAK- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 70 pfpvKNIS---IASFG-----ESGVFVDKE-GVILTPMLAWYDRRGESYLSSLSKAEAEEL-YSITGLPPHSNYSAFKMR 139
Cdd:PRK00047 68 ----AGISpdqIAAIGitnqrETTVVWDKEtGRPIYNAIVWQDRRTADICEELKRDGYEDYiREKTGLVIDPYFSGTKIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 140 WLLDNYSL----HERKDI------CWlhapevLLWRMTGAKK--TEISLASRTLCLDIARRTWSRNAAGILGIPFGVLaP 207
Cdd:PRK00047 144 WILDNVEGarerAEKGELlfgtidTW------LVWKLTGGKVhvTDYTNASRTMLFNIHTLDWDDELLELLDIPRSML-P 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 208 LIKPG-EVAGwVTATLReelGFSHEVKVT-LAGHDH--MVGaralQL--QPGDVLNSTGTTeGILLLNTQPTLdVQARRD 281
Cdd:PRK00047 217 EVRPSsEVYG-KTNPYG---FFGGEVPIAgIAGDQQaaLFG----QLcfEPGMAKNTYGTG-CFMLMNTGEKA-VKSENG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 282 KLANGCYS-DGE-FFTLFASLPVGGYALEWVKKTFRLtdkeISTGLEKamEQYLKPSWSVEHVpVFIPHLRGSGSPNKNR 359
Cdd:PRK00047 287 LLTTIAWGiDGKvVYALEGSIFVAGSAIQWLRDGLKI----ISDASDS--EALARKVEDNDGV-YVVPAFTGLGAPYWDS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 360 HTRGLLFGLTDSLPPESL----LESvfIGL-------AMEfahchgcfnIPAG---RTVKVIGPAVKNPYWLQLKADILQ 425
Cdd:PRK00047 360 DARGAIFGLTRGTTKEHIiratLES--IAYqtrdvldAMQ---------ADSGirlKELRVDGGAVANNFLMQFQADILG 428
|
490
....*....|....*.
gi 447036295 426 CPIEAIAFDETVSLGA 441
Cdd:PRK00047 429 VPVERPVVAETTALGA 444
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
10-475 |
1.94e-20 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 93.88 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 10 IDIGTTNCKVSCYSCH-DVSVLEVRKF----PTPIISSDkgevdfDIEALWQALRLVMAELVASVPF-PVKNISIASFGE 83
Cdd:PRK15027 5 IDLGTSGVKVILLNEQgEVVASQTEKLtvsrPHPLWSEQ------DPEQWWQATDRAMKALGDQHSLqDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 84 SGVFVDKEGVILTPMLAWYDRR-GESylSSLSKAEAEELYSITGLPPHSNYSAFKMRWLldnySLHE----RKDICWLHA 158
Cdd:PRK15027 79 GATLLDAQQRVLRPAILWNDGRcAQE--CALLEARVPQSRVITGNLMMPGFTAPKLLWV----QRHEpeifRQIDKVLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 159 PEVLLWRMTGAKKTEISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFShEVKVTLAG 238
Cdd:PRK15027 153 KDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMA-TVPVVAGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 239 HDHMVGARAL-QLQPGDVLNSTGTT-------EGILllnTQPTLDVQARrdklangCYSDGEFFTLFASLPVGGYALEWV 310
Cdd:PRK15027 232 GDNAAGAVGVgMVDANQAMLSLGTSgvyfavsEGFL---SKPESAVHSF-------CHALPQRWHLMSVMLSAASCLDWA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 311 KKTFRLTDKEISTGLEKAMEQYLKPSWsvehvpvFIPHLRGSGSPNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFA 390
Cdd:PRK15027 302 AKLTGLSNVPALIAAAQQADESAEPVW-------FLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 391 H----CHGCFNIPAgrTVKVIGPAVKNPYWLQLKADI--LQ---------------CPIEAIAFDETVSLGALLiacpnv 449
Cdd:PRK15027 375 DgmdvVHACGIKPQ--SVTLIGGGARSEYWRQMLADIsgQQldyrtggdvgpalgaARLAQIAANPEKSLIELL------ 446
|
490 500 510
....*....|....*....|....*....|....
gi 447036295 450 vpPTVPVAERYFPDAVRSAKL--------KIYQQ 475
Cdd:PRK15027 447 --PQLPLEQSHLPDAQRYAAYqprretfrRLYQQ 478
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
8-445 |
5.40e-19 |
|
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: 89.54 E-value: 5.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 8 LVIDIGTTNCKVSCYScHDVSVLEVRKFPTPIISSDKGEVDFDIEALWQALRLVMAELVASVPFPVKNisIASFGES--- 84
Cdd:cd07793 3 LAVDVGTTNIRCHIFD-KKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPED--IAAIGIStqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 85 GVFV--DKE-GVILTPMLAWYDRRGE--------SYLSSLSKAEAEELYSITGLPPH---------SNYSAFKMRWLLDN 144
Cdd:cd07793 80 NTFLtwDKKtGKPLHNFITWQDLRAAelceswnrSLLLKALRGGSKFLHFLTRNKRFlaasvlkfsTAHVSIRLLWILQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 145 Y----SLHERKDIC------WlhapevLLWRMTGAKK--TEISLASRTLCLDIARRTWSRNAAGILGIPFGVLaPLIKP- 211
Cdd:cd07793 160 NpelkEAAEKGELLfgtidtW------LLWKLTGGKVhaTDYSNASATGLFDPFTLEWSPILLSLFGIPSSIL-PEVKDt 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 212 ----GEVagwvtatlrEELGFSHEVKVTLAGHDH---MVGARAlqLQPGDVLNSTGTteGILL-LNTQPTLDVQARrdkl 283
Cdd:cd07793 233 sgdfGST---------DPSIFGAEIPITAVVADQqaaLFGECC--FDKGDVKITMGT--GTFIdINTGSKPHASVK---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 284 anGCYS------DGEF-FTLFASLPVGGYALEWVKKTFRLTDKEISTGLEKameqylkpswSVEHVP--VFIPHLRGSGS 354
Cdd:cd07793 296 --GLYPlvgwkiGGEItYLAEGNASDTGTVIDWAKSIGLFDDPSETEDIAE----------SVEDTNgvYFVPAFSGLQA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 355 PNKNRHTRGLLFGLTDSLPPESLLESVFIGLAMEFAHCHGCF----NIPAgRTVKVIGPAVKNPYWLQLKADILQCPIEA 430
Cdd:cd07793 364 PYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMeketSIKI-SSIRVDGGVSNNDFILQLIADLLGKPVER 442
|
490
....*....|....*
gi 447036295 431 IAFDETVSLGALLIA 445
Cdd:cd07793 443 PKNTEMSALGAAFLA 457
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
45-446 |
1.37e-17 |
|
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: 85.08 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 45 GEVDFDIEALWQALRLVMAELVASVPFPVKNI---SIASFGESGVFVDKEGVILtpmlaW----YDRRGESYLSSLSKAE 117
Cdd:cd07775 41 GSMDFDTEKNWKLICECIREALKKAGIAPKSIaaiSTTSMREGIVLYDNEGEEI-----WacanVDARAAEEVSELKELY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 118 ---AEELYSITGlpphsnysafkmrwllDNYSLHERKDICWL--HAPEV-------------LLWRMTGAKKTEISLASR 179
Cdd:cd07775 116 ntlEEEVYRISG----------------QTFALGAIPRLLWLknNRPEIyrkaakitmlsdwIAYKLSGELAVEPSNGST 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 180 TLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDHMVGARAL-QLQPGDVLNS 258
Cdd:cd07775 180 TGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLgVVRPGQTAVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 259 TGTTEGILLLNTQPTLDVQARRdKLANGCYSDGEFFTLFASLPvgGYALEWVKKTFRLTDKEISTGLEKAMEQYLK---- 334
Cdd:cd07775 260 GGSFWQQEVNTAAPVTDPAMNI-RVNCHVIPDMWQAEGISFFP--GLVMRWFRDAFCAEEKEIAERLGIDAYDLLEemak 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 335 --PSWSVEHVPVFiphlrgSGSPN-KN-RHTRGLLFGLtDSLPPESLLESVFIGLaMEFA----HCH-----GCFNIPAG 401
Cdd:cd07775 337 dvPPGSYGIMPIF------SDVMNyKNwRHAAPSFLNL-DIDPEKCNKATFFRAI-MENAaivsAGNleriaEFSGIFPD 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 447036295 402 rTVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIAC 446
Cdd:cd07775 409 -SLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAG 452
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
51-441 |
8.32e-07 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 51.39 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 51 IEALWQALRLVMAElvASV-PFPVKNISIASFGESGVFVDKEGVIL--TPMLA---------WYDRRgesylsslSKAEA 118
Cdd:PRK04123 59 IESLEAAIPAVLKE--AGVdPAAVVGIGVDFTGSTPAPVDADGTPLalLPEFAenphamvklWKDHT--------AQEEA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 119 EELYSITglppHSNYSAFKMRWLLDNYS--------LHerkdicWL-HAPEV-------------LLWRMTGakkteisl 176
Cdd:PRK04123 129 EEINRLA----HERGEADLSRYIGGIYSsewfwakiLH------VLrEDPAVyeaaaswveacdwVVALLTG-------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 177 asRTLCLDIARrtwSRNAAG--------ILGIP----FGVLAPLIK-------------PGEVAGWVTATLREELGFSHE 231
Cdd:PRK04123 191 --TTDPQDIVR---SRCAAGhkalwhesWGGLPsadfFDALDPLLArglrdklftetwtAGEPAGTLTAEWAQRLGLPEG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 232 VKVTLAGHD-HM--VGARAlqlQPGDVLNSTGTTEGILLLntqptldvqARRDKLANG-CYS-DG----EFFTLFASLPV 302
Cdd:PRK04123 266 VAVSVGAFDaHMgaVGAGA---EPGTLVKVMGTSTCDILL---------ADKQRAVPGiCGQvDGsivpGLIGYEAGQSA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 303 GGYALEWVKKtfRLTDKEISTGLEKAMEQ---YLKPSWS----VEHVPVFIPHLRGSGSPNKNRHTRGLLFGLT-DSLPP 374
Cdd:PRK04123 334 VGDIFAWFAR--LLVPPEYKDEAEARGKQlleLLTEAAAkqppGEHGLVALDWFNGRRTPLADQRLKGVITGLTlGTDAP 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447036295 375 E---SLLESVFIG--LAMEfahchgCFN---IPAGRTVKVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGA 441
Cdd:PRK04123 412 DiyrALIEATAFGtrAIME------CFEdqgVPVEEVIAAGGIARKNPVLMQIYADVLNRPIQVVASDQCPALGA 480
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
173-445 |
1.06e-06 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 51.02 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 173 EISLASRTLCLDIARRTWSRNAAGILGIP--FGVLAPLIKPGEVAGWVTATLREELGFSHEVKV---------TLAGhdh 241
Cdd:cd07776 204 DESDGSGMNLMDIRSRKWSPELLDAATAPdlKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVvaftgdnpaSLAG--- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 242 mvgaraLQLQPGDVLNSTGTTEGILLLNTQPTLDVQA--------RRDKLANGCYSDGefftlfaSLpvggyALEWVKKT 313
Cdd:cd07776 281 ------LGLEPGDVAVSLGTSDTVFLVLDEPKPGPEGhvfanpvdPGSYMAMLCYKNG-------SL-----ARERVRDR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 314 FRLTD--------KEISTGLEKAMEQYLkpswsveHVPVFIPHLRGSGspnknrHTRGLLFGLTDSLPPE----SLLESV 381
Cdd:cd07776 343 YAGGSwekfnellESTPPGNNGNLGLYF-------DEPEITPPVPGGG------RRFFGDDGVDAFFDPAvevrAVVESQ 409
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447036295 382 FigLAMefaHCHGC---FNIPAGRTVkVIGPAVKNPYWLQLKADILQCPIEAIAFDETVSLGALLIA 445
Cdd:cd07776 410 F--LSM---RLHAErlgSDIPPTRIL-ATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRA 470
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
45-261 |
1.35e-06 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 50.77 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 45 GEVDFDIEALWQALRLVMAELVASV---PFPVKNISIASFGESGVFVDKEGvilTPMLAWYD---RRGE--SYLSSLSKA 116
Cdd:PRK10939 44 GSMEFDLEKNWQLACQCIRQALQKAgipASDIAAVSATSMREGIVLYDRNG---TEIWACANvdaRASRevSELKELHNN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 117 EAEELYSITGlpphsnysafkmrwllDNYSLHERKDICWL--HAPEV-------------LLWRMTGAKKTEISLASRTL 181
Cdd:PRK10939 121 FEEEVYRCSG----------------QTLALGALPRLLWLahHRPDIyrqahtitmisdwIAYMLSGELAVDPSNAGTTG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 182 CLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAGWVTATLREELGFSHEVKVTLAGHDHMVGARALQL-QPGDVLNSTG 260
Cdd:PRK10939 185 LLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLRAGTPVVMGGGDVQLGCLGLGVvRPGQTAVLGG 264
|
.
gi 447036295 261 T 261
Cdd:PRK10939 265 T 265
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
24-240 |
1.61e-04 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 43.94 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 24 CHDVSVLEVRKFPTPIISSDkGEVDFDIEALWQALRLVMAELVASVPFPVkNISIASFGESGVFVDKEGVILTPMLAWYD 103
Cdd:PRK10640 9 CRSLTLREIHRFNNGLHSQD-GFDTWDVDSLESAIRLGLNKVCEEGIRID-SIGIDTWGVDYVLLDKQGQRVGLPVSYRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447036295 104 RRGESYLSslsKAEA----EELYSITG---LPPHSNYsafKMRWLLDNYSlHERKDICwlHA---PEVLLWRMTGAKKTE 173
Cdd:PRK10640 87 SRTDGVMA---QAQQqlgkRDIYRRSGiqfLPFNTLY---QLRALTEQQP-ELIAQVA--HAlliPDYFSYRLTGKMNWE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447036295 174 ISLASRTLCLDIARRTWSRNAAGILGIPFGVLAPLIKPGEVAG-WVTATLReelgfshEVKV-TLAGHD 240
Cdd:PRK10640 158 YTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGhWICPQGN-------EIPVvAVASHD 219
|
|
| |
