|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02405 |
PLN02405 |
hexokinase |
1-496 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 952.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 1 MGKVAVGATVVCTAAVCAVAVLVVRRRMQSSGKWGRVLAILKAFEEDCATPISKLRQVADAMTVEMHAGLASDGGSKLKM 80
Cdd:PLN02405 1 MGKVAVGAAVVCAAAVCAAAALVVRRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATECE 160
Cdd:PLN02405 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 161 DFHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGALNKALERVGLDMRIAALVNDTVGTLAGGRY 240
Cdd:PLN02405 161 DFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 241 YNPDVVAAVILGTGTNAAYVERATAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEFDHTLDFESLNPGEQILEKIISG 320
Cdd:PLN02405 241 YNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 321 MYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCN 400
Cdd:PLN02405 321 MYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSLKMRKVVVELCN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 401 IIATRGARLSAAGIYGILKKLGRDTTKDEEVQKSVIAMDGGLFEHYTQFSECMESSLKELLGDEASGSVEVTHSNDGSGI 480
Cdd:PLN02405 401 IVATRGARLSAAGIYGILKKLGRDTVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGI 480
|
490
....*....|....*.
gi 15233457 481 GAALLAASHSLYLEDS 496
Cdd:PLN02405 481 GAALLAASHSLYLEVE 496
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
50-489 |
0e+00 |
|
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth.
Pssm-ID: 466870 [Multi-domain] Cd Length: 439 Bit Score: 823.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 50 TPISKLRQVADAMTVEMHAGLASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEV 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 130 SIPPHLMTGGSDELFNFIAEALAKFVATECEDFHlPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVG 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 210 ALNKALERVGLDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGLLPKSGEMVINMEWGNFR 289
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 290 SSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNDTSP 369
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 370 DLKIVGSKIKDILEVPTTSLKMRKVVISLCNIIATRGARLSAAGIYGILKKLGRDTTKDEEVQKSVIAMDGGLFEHYTQF 449
Cdd:cd24020 320 DLETVARILKDALGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15233457 450 SECMESSLKELLGDEASGSVEVTHSNDGSGIGAALLAASH 489
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02914 |
PLN02914 |
hexokinase |
37-492 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 609.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 37 VLAILKAFEEDCATPISKLRQVADAMTVEMHAGLASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGG 116
Cdd:PLN02914 37 VAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 117 KQERVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATECEDFHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKG 196
Cdd:PLN02914 117 KDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 197 FSIEEAVGQDVVGALNKALERVGLDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGLLPKS 276
Cdd:PLN02914 197 FAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 277 GEMVINMEWGNFrSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIR 356
Cdd:PLN02914 277 GRTIINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 357 TPHMSAMHNDTSPDLKIVGSKIKDILEVpTTSLKMRKVVISLCNIIATRGARLSAAGIYGILKKLGRDTTKDEEVQKSVI 436
Cdd:PLN02914 356 TPHLCAMQQDNSDDLQAVGSILYDVLGV-EASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFGKRTVV 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15233457 437 AMDGGLFEHYTQFSECMESSLKELLGDEASGSVEVTHSNDGSGIGAALLAASHSLY 492
Cdd:PLN02914 435 AMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATNSKY 490
|
|
| PLN02362 |
PLN02362 |
hexokinase |
1-496 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 606.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 1 MGKVAVGATVVCTAAVCAVAVLVVRRRMQSSGKWGRVLAILKAFEEDCATPISKLRQVADAMTVEMHAGLASDGGSKLKM 80
Cdd:PLN02362 1 MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATECE 160
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 161 DFHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGALNKALERVGLDMRIAALVNDTVGTLAGGRY 240
Cdd:PLN02362 161 GSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 241 YNPDVVAAVILGTGTNAAYVERATAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEFDHTLDFESLNPGEQILEKIISG 320
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 321 MYLGEILRRVLLKMAEDAAFFGdTVPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCN 400
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFG-PVSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGISEVPLKVRKLVVKICD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 401 IIATRGARLSAAGIYGILKKLGRDTT----------KDEEVQKSVIAMDGGLFEHYTQFSECMESSLKELLGDEASGSVE 470
Cdd:PLN02362 400 VVTRRAARLAAAGIVGILKKIGRDGSggitsgrsrsDIQIMRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVI 479
|
490 500
....*....|....*....|....*.
gi 15233457 471 VTHSNDGSGIGAALLAASHSLYLEDS 496
Cdd:PLN02362 480 LKATEDGSGIGSALLAASYSSYSVDT 505
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
25-488 |
0e+00 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 529.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 25 RRRMQSSGKWGRVLAILKAFEEDCATPISKLRQVADAMTVEMHAGLASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGG 104
Cdd:PLN02596 26 RWKRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 105 TNFRVMRVLLGGKQERVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVAT-ECEDFHLPEgRQRELGFTFSFPVKQT 183
Cdd:PLN02596 106 SNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEhPGDEADTPE-RVKKLGFTVSYPVDQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 184 SLSSGSLIKWtKGFSIEEAVGQDVVGALNKALERVGLDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERA 263
Cdd:PLN02596 185 AASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 264 TAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGD 343
Cdd:PLN02596 264 QAIPKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 344 TVPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCNIIATRGARLSAAGIYGILKKLGR 423
Cdd:PLN02596 344 TLPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGR 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233457 424 dttkdEEVQKSVIAMDGGLFEHYTQFSECMESSLKELLGDEASGSVEVTHSNDGSGIGAALLAAS 488
Cdd:PLN02596 424 -----IENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAAC 483
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
53-486 |
1.86e-170 |
|
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar.
Pssm-ID: 466868 [Multi-domain] Cd Length: 431 Bit Score: 487.14 E-value: 1.86e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 53 SKLRQVADAMTVEMHAGLASDGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRV-LLGGKQERVVKQEfeEVSI 131
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVtLDGNGGIFIIVQR--KYKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 132 PPHLMTGGSDELFNFIAEALAKFVATECEDFHLPEGRqrELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGAL 211
Cdd:cd24018 79 PDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSDKTI--PLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 212 NKALERVGLDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWH---GLLPKSGEMVINMEWGNF 288
Cdd:cd24018 157 QNALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsGSVTKSDEMIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 289 RSSH--LPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24018 237 DNERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 367 TSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCNIIATRGARLSAAGIYGILKKlgrdtTKDEEVQKSVIAMDGGLFEHY 446
Cdd:cd24018 317 TSPDLDAVRDILKELLAIDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLK-----RGSLLPEPVTVGIDGSVYEKY 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15233457 447 TQFSECMESSLKELLGDEASGSVEVTHSNDGSGIGAALLA 486
Cdd:cd24018 392 PGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
54-487 |
2.84e-149 |
|
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition.
Pssm-ID: 466869 [Multi-domain] Cd Length: 427 Bit Score: 433.12 E-value: 2.84e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 54 KLRQVADAMTVEMHAGLASDG--GSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGkqERVVKQEFEEVSI 131
Cdd:cd24019 6 QLEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNG--GSQVKMESEIYAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 132 PPHLMTGGSDELFNFIAEALAKFVATEC-EDFHLPegrqreLGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGA 210
Cdd:cd24019 84 PEEIMTGTGEQLFDYIAECLAEFLEKNGlKDKKLP------LGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 211 LNKALERVGL-DMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGLLPKSGEMVINMEWGNFR 289
Cdd:cd24019 158 LQEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 290 SSH---LPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24019 238 DNGvldFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 367 TSPDLkivgSKIKDILE---VPTTSLKMRKVVISLCNIIATRGARLSAAGIYGILKKLGRdttkdeevQKSVIAMDGGLF 443
Cdd:cd24019 318 NEGDF----SNTREILKelgLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR--------KEVTVGVDGSLY 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15233457 444 EHYTQFSECMESSLKELLGDEAsgSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24019 386 KYHPKFHKRMHETLKELVPPGC--KFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
55-486 |
3.93e-126 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 371.61 E-value: 3.93e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 55 LRQVADAMTVEMHAGLASDGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEfeEVSIPPH 134
Cdd:cd24000 4 LKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISK--KYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 135 LMTGGSDELFNFIAEALAKFVATECEDFHLPegrqreLGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGALNKA 214
Cdd:cd24000 81 IKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 215 LERVGLDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIpkwhglLPKSGEMVINMEWGNFRSSHLP 294
Cdd:cd24000 155 LKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKNSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 295 LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDaaffgdtvpsklripfiirtphmsamhndtspdlkiv 374
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 375 gskikdilevpttslkmrkVVISLCNIIATRGARLSAAGIYGILKKLGRDTTKdeevqKSVIAMDGGLFEHYTQFSECME 454
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTGDSPEK-----KITIAVDGSLFEKYPGYRERLE 327
|
410 420 430
....*....|....*....|....*....|..
gi 15233457 455 SSLKELLGDEAsgSVEVTHSNDGSGIGAALLA 486
Cdd:cd24000 328 EYLKELLGRGI--RIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
53-487 |
8.24e-126 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.
Pssm-ID: 466937 [Multi-domain] Cd Length: 428 Bit Score: 373.25 E-value: 8.24e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 53 SKLRQVADAMTVEMHAGLASDGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEfeEVSIP 132
Cdd:cd24087 2 ERLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQS--KYRLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 133 PHLMTGGSDELFNFIAEALAKFVateceDFHLPEGR--QRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGA 210
Cdd:cd24087 79 EELKTGTGEELWDFIADCLKKFV-----EEHFPGGKsePLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 211 LNKALERVGLDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGL-LPKSGEMVINMEWGNFR 289
Cdd:cd24087 154 LQKALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDdIPPDSPMAINCEYGAFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 290 SSH--LPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNDT 367
Cdd:cd24087 234 NEHlvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 368 SPDLKIVGSKIKDILEVPTTsLKMRKVVISLCNIIATRGARLSAAGIYGILKKLGrdttkdeeVQKSVIAMDGGLFEHYT 447
Cdd:cd24087 314 FENLEDTDDLFQHFFGLETT-VPERKFIRRLAELIGTRAARLSACGIAAICKKRG--------YKTCHVAADGSVYNKYP 384
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15233457 448 QFSECMESSLKELLGDEASGS-VEVTHSNDGSGIGAALLAA 487
Cdd:cd24087 385 GFKERAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAA 425
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
53-486 |
5.12e-125 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 (GLK-2) from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (also known as glucokinase-1, EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to glucokinase-1 and glucokinase-2.
Pssm-ID: 466938 [Multi-domain] Cd Length: 445 Bit Score: 372.11 E-value: 5.12e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 53 SKLRQVADAMTVEMHAGLASDGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEfeEVSIP 132
Cdd:cd24088 2 EKLDKLTAEFQRQMEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQE--KSKIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 133 PHLMTGG-SDELFNFIAEALAKFVATECEDfHLPEGRQRE---LGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVV 208
Cdd:cd24088 79 DELKTGVtAKDLFDYLAKSVEAFLTKHHGD-SFAAGKDDDrlkLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 209 GALNKALERVGLDMRIAALVNDTVGTLAGGRYYNPDVVAAV---ILGTGTNAAYVERATAIPKwhgLLPKS------GEM 279
Cdd:cd24088 158 KLLQDELDRQGIPVKVVALVNDTVGTLLARSYTSPEISGAVlgaIFGTGTNGAYLEDLEKIKK---LDDSSrvgkgkTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 280 VINMEWGNFRS--SHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFG---DTVPSKLRIPFI 354
Cdd:cd24088 235 VINTEWGSFDNelKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIqynDKSPSALNTPYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 355 IRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCNIIATRGARLSAAGIYGILKKLGR-DTTKDEEVQk 433
Cdd:cd24088 315 LDTAVLSAIEIDSEAELRATRKVLLDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGAlNKSYDGEIN- 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15233457 434 svIAMDGGLFEHYTQFSECMESSLKELL-GDEASGSVEVTHSNDGSGIGAALLA 486
Cdd:cd24088 394 --IGVDGSVIEFYPGFESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
51-487 |
3.48e-108 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 329.33 E-value: 3.48e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 51 PISKLRQVADAMTVEMHAGLASDGG---------SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLL--GGKQE 119
Cdd:PTZ00107 21 SKEKLKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLrgGGKME 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 120 RV---VKQEFEEVSIPPHLM--TGGSDELFNFIAEALAKFVaTECEDfHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWT 194
Cdd:PTZ00107 101 RTqskFSLPKSALLGEKGLLdkKATATDLFDHIAKSIKKMM-EENGD-PEDLNKPVPVGFTFSFPCTQLSVNNAILIDWT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 195 KGFSIEEAV-----GQDVVGALNKALERVGLDMRIAALVNDTVGTLAgGRYY-----NPDVVAAVILGTGTNAAYVERAT 264
Cdd:PTZ00107 179 KGFETGRATndpveGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLI-SCAYqkpknTPPCQVGVIIGTGSNACYFEPEV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 265 AIPKWHGllpksgeMVINMEWGNFrSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAffgdt 344
Cdd:PTZ00107 258 SAYGYAG-------TPINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKA----- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 345 vPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDI--LEVPTTSLK-MRKVvislCNIIATRGARLSAAGIYGILKKL 421
Cdd:PTZ00107 325 -PPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAwdVDLTDEDLYtIRKI----CELVRGRAAQLAAAFIAAPAKKT 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233457 422 GRDTTkdeevqKSVIAMDGGLFEHYTQFSECMESSLKELLGDEAsGSVEVTHSNDGSGIGAALLAA 487
Cdd:PTZ00107 400 RTVQG------KATVAIDGSVYVKNPWFRRLLQEYINSILGPDA-GNVVFYLADDGSGKGAAIIAA 458
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
246-488 |
7.03e-104 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.
Pssm-ID: 461028 Cd Length: 236 Bit Score: 310.19 E-value: 7.03e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 246 VAAVILGTGTNAAYVERATAIPKWHGLLPKSGEMVINMEWGNFRSSH---LPLTEFDHTLDFESLNPGEQILEKIISGMY 322
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 323 LGEILRRVLLKMAEDAAFFGDtVPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCNII 402
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 403 ATRGARLSAAGIYGILKKLGRDTtkdeevqKSVIAMDGGLFEHYTQFSECMESSLKELLGdeASGSVEVTHSNDGSGIGA 482
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-------KVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVLAEDGSGVGA 230
|
....*.
gi 15233457 483 ALLAAS 488
Cdd:pfam03727 231 ALIAAV 236
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
40-240 |
7.74e-98 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.
Pssm-ID: 459774 [Multi-domain] Cd Length: 197 Bit Score: 293.26 E-value: 7.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 40 ILKAFEEDCATPISKLRQVADAMTVEMHAGLASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGkqE 119
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGG--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 120 RVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATECEDFHlpEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSI 199
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF--EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15233457 200 EEAVGQDVVGALNKALERVGLDMRIAALVNDTVGTLAGGRY 240
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
54-487 |
8.44e-97 |
|
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of types I and II hexokinases.
Pssm-ID: 466939 [Multi-domain] Cd Length: 429 Bit Score: 299.00 E-value: 8.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 54 KLRQVADAMTVEMHAGLASDGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEVSI 131
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 132 PPHLMTGGSDELFNFIAEALAKFVATE-CEDFHLPegrqreLGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGA 210
Cdd:cd24089 86 PEEIMHGSGTQLFDHVAECLADFMDKQkIKDKKLP------LGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 211 LNKALERVG-LDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNFR 289
Cdd:cd24089 160 LRKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGAFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 290 ---SSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24089 237 ddgSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 367 TSpDLKIVGSKIKDILEVPttSLKMRKVVISLCNIIATRGARLSAAGIYGILKKLgrDTTKDEEVQKSVIAMDGGLFEHY 446
Cdd:cd24089 317 KE-GLANAKEILTRLGLDP--SEDDCVNVQHVCTIVSFRSANLCAATLAAILTRL--RENKGLERLRTTVGVDGSVYKKH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15233457 447 TQFSECMESSLKELLGDeasgsVEVTH--SNDGSGIGAALLAA 487
Cdd:cd24089 392 PQFSKRLHKAVRRLVPD-----CDVRFllSEDGSGKGAAMVTA 429
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
55-488 |
7.33e-96 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 296.87 E-value: 7.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 55 LRQVADAMTVEMHAGLAsDGGSKLKMLISYVdNLPSG-DEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEevsipp 133
Cdd:COG5026 22 LEEIAAKFQEEMEKGLE-GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFEIENFKS------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 134 HLMTGGS-----DELFNFIAEALAKFVatecedfhlpeGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVV 208
Cdd:COG5026 94 FPLPGTSseitaEEFFDFIADYIEPLL-----------DESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 209 GALNKALERVGLDMRI-AALVNDTVGTLAGGRYYNPDVV----AAVILGTGTNAAYVERATAIPKwhgLLPKSGEMVINM 283
Cdd:COG5026 163 ELLEAALARKGLDNVKpVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGK---LPAYEGPMIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 284 EWGNFrsSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDtVPSKLRIPFIIRTPHMSAM 363
Cdd:COG5026 240 ESGNF--NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPG-FSEVFETPYSLTTVDMSRF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 364 HNDTSPDLKIVGSKIKDILEvpttslKMRKVVISLCNIIATRGARLSAAGIYGILKKLGRDTTKDEEVqksVIAMDGGLF 443
Cdd:COG5026 317 LADPSDEKEILSQCLEAGSE------EDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLKPH---CIAIDGSTY 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 15233457 444 EHYTQFSECMESSLKELLGDEASGSVEVTHSNDGSGIGAALLAAS 488
Cdd:COG5026 388 EKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
52-487 |
1.07e-89 |
|
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of types I to III hexokinases. Type I enzyme may have a catabolic function, producing H6P for energy production in glycolysis; it is bound to the mitochondrial membrane, which enables the coordination of glycolysis with the TCA cycle. Types II and III enzyme may have anabolic functions, providing H6P for glycogen or lipid synthesis.
Pssm-ID: 466941 [Multi-domain] Cd Length: 433 Bit Score: 280.97 E-value: 1.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 52 ISKLRQVADAMTVEMHAGLA--SDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEV 129
Cdd:cd24091 4 HDQLLEVKARMRAEMERGLRkeTHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 130 SIPPHLMTGGSDELFNFIAEALAKFVateceDFHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVG 209
Cdd:cd24091 84 AIPQEIMQGTGEELFDHIVQCIADFL-----EYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 210 ALNKALERVG-LDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNF 288
Cdd:cd24091 159 LLREAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 289 RSS----HLpLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMH 364
Cdd:cd24091 236 GDNgcldDI-RTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 365 NDTSPDLKIvgSKIKDILEVPTTSlKMRKVVISLCNIIATRGARLSAAGIYGILKKLgRDTTKDEEVQKSViAMDGGLFE 444
Cdd:cd24091 315 SDRLALLQV--RAILQQLGLDSTC-DDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKI-RENRGLDHLNVTV-GVDGTLYK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15233457 445 HYTQFSECMESSLKELlgdEASGSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24091 390 LHPHFSRVMHETVKEL---APKCDVTFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
55-487 |
3.96e-89 |
|
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the first two domains of HKDC1.
Pssm-ID: 466976 [Multi-domain] Cd Length: 429 Bit Score: 279.43 E-value: 3.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 55 LRQVADAMTVEMHAGLASDGGSK--LKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEVSIP 132
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 133 PHLMTGGSDELFNFIAEALAKFVATE-CEDFHLPegrqreLGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGAL 211
Cdd:cd24126 87 EEIIHGTGTELFDYVAECLADFMKKKgIKHKKLP------LGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 212 NKALERVG-LDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24126 161 RKAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 291 SHLP---LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNdt 367
Cdd:cd24126 238 DGSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEK-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 368 spdLKIVGSKIKDILevptTSLKMRK------VVISLCNIIATRGARLSAAGIYGILKKLgRDTTKDEEVQKSViAMDGG 441
Cdd:cd24126 316 ---YKEGLYNTREIL----SDLGLEPseedciAVQHVCTIVSFRSANLCAAALAAILTRL-RENKKLERLRTTV-GMDGT 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15233457 442 LFEHYTQFSECMESSLKELLgdeASGSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24126 387 VYKTHPQYAKRLHKVVRRLV---PSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
54-487 |
2.84e-86 |
|
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type III hexokinase.
Pssm-ID: 466979 [Multi-domain] Cd Length: 430 Bit Score: 271.76 E-value: 2.84e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 54 KLRQVADAMTVEMHAGLASD--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFeevSI 131
Cdd:cd24129 6 QLAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIY---SI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 132 PPHLMTGGSDELFNFIAEALAKFvaTECEDFhlpEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGAL 211
Cdd:cd24129 83 PETVAQGTGQQLFDHIVDCIVDF--QQKQGL---SGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 212 NKA-LERVGLDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIpkwhGLLP-KSGEMVINMEWGNF- 288
Cdd:cd24129 158 REAaTRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV----AGVPgDSGRMCINMEWGAFg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 289 --RSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24129 234 dnGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 367 TSPdLKIVGSKIKDiLEVPTT---SLKMRKVvislCNIIATRGARLSAAGIYGILKKLGRDTTKDEevQKSVIAMDGGLF 443
Cdd:cd24129 314 SLA-LRQVRAILED-LGLPLTsddALLVLEV----CQTVSQRAAQLCAAGVAAVVEKMRENRGLDE--LAVTVGVDGTLY 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15233457 444 EHYTQFSECMESSLKELlgdEASGSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24129 386 KLHPRFSSLVQATVREL---APRCVVTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
55-487 |
2.43e-83 |
|
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type II hexokinase.
Pssm-ID: 466975 [Multi-domain] Cd Length: 429 Bit Score: 264.45 E-value: 2.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 55 LRQVADAMTVEMHAGLASDGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEVSIP 132
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 133 PHLMTGGSDELFNFIAEALAKFVAT-ECEDFHLPegrqreLGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGAL 211
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDKlQIKDKKLP------LGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 212 NKALERVG-LDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24125 161 RKAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 291 SHL---PLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNDT 367
Cdd:cd24125 238 DGSlddIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 368 SPDLKIVGSKIKDILE-VPTTSLKMRKVvislCNIIATRGARLSAAGIYGILKKLGRDttKDEEVQKSVIAMDGGLFEHY 446
Cdd:cd24125 318 DGIRKAREVLMRLGLDpTQEDCVATHRI----CQIVSTRSASLCAATLAAVLQRIKEN--KGEERLRSTIGVDGSVYKKH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15233457 447 TQFSECMESSLKELLGDeasGSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24125 392 PHFARRLHKTVRRLVPG---CDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
54-487 |
1.90e-82 |
|
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type II hexokinase.
Pssm-ID: 466978 [Multi-domain] Cd Length: 435 Bit Score: 262.14 E-value: 1.90e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 54 KLRQVADAMTVEMHAGLA--SDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEVSI 131
Cdd:cd24128 6 QLLEVKRRMKVEMERGLSkeTHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 132 PPHLMTGGSDELFNFIAEALAKFVateceDFHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGAL 211
Cdd:cd24128 86 PQEVMHGTGEELFDHIVHCIADFL-----EYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 212 NKALERV-GLDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24128 161 KEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 291 SHLP---LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNDt 367
Cdd:cd24128 238 NGCLddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESD- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 368 spdlKIVGSKIKDILEV--PTTSLKMRKVVISLCNIIATRGARLSAAGIYGILKKLGRDttKDEEVQKSVIAMDGGLFEH 445
Cdd:cd24128 317 ----RLALLQVRAILQHlgLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIREN--RGLDALKVTVGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15233457 446 YTQFSECMESSLKELlgdEASGSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24128 391 HPHFAKVMHETVKDL---APKCDVSFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
55-487 |
9.92e-82 |
|
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase.
Pssm-ID: 466974 [Multi-domain] Cd Length: 473 Bit Score: 261.48 E-value: 9.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 55 LRQVADAMTVEMHAGLASDGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEVSIP 132
Cdd:cd24124 35 LIDIMTRFRKEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 133 PHLMTGGSDELFNFIAEALAKFV-ATECEDFHLPegrqreLGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGAL 211
Cdd:cd24124 115 ENIVHGSGSQLFDHVAECLGDFMeKRKIKDKKLP------VGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 212 NKALERVG-LDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNF-- 288
Cdd:cd24124 189 NKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFgd 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 289 -RSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNDt 367
Cdd:cd24124 266 dGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKN- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 368 spdlKIVGSKIKDILevptTSLKMRK------VVISLCNIIATRGARLSAAGIYGILKKLgRDtTKDEEVQKSVIAMDGG 441
Cdd:cd24124 345 ----KEGLHNAKEIL----TRLGVEPsdddcvSVQHVCTIVSFRSANLVAATLGAILNRL-RD-NKGTPRLRTTVGVDGS 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15233457 442 LFEHYTQFSECMESSLKELLGDEasgSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24124 415 LYKTHPQYSRRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
54-487 |
1.61e-80 |
|
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type I hexokinase.
Pssm-ID: 466977 [Multi-domain] Cd Length: 434 Bit Score: 257.15 E-value: 1.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 54 KLRQVADAMTVEMHAGL--ASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQERVVKQEFEEVSI 131
Cdd:cd24127 6 MLLEVKKRMRAEMELGLrkQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 132 PPHLMTGGSDELFNFIAEALAKFVateceDFHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGAL 211
Cdd:cd24127 86 PIEIMQGTGEELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 212 NKALERVG-LDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24127 161 RDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 291 SHL---PLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNDt 367
Cdd:cd24127 238 NGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESD- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 368 spdlKIVGSKIKDILEV--PTTSLKMRKVVISLCNIIATRGARLSAAGIYGILKKLgRDTTKDEEVQKSViAMDGGLFEH 445
Cdd:cd24127 317 ----RLALLQVRAILQQlgLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKI-RENRGLDHLNVTV-GVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15233457 446 YTQFSECMESSLKELlgdEASGSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24127 391 HPHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
54-487 |
7.17e-80 |
|
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the second two domains of HKDC1.
Pssm-ID: 466980 [Multi-domain] Cd Length: 433 Bit Score: 255.63 E-value: 7.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 54 KLRQVADAMTVEMHAGLA--SDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQeRVVKQEFEEVSI 131
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKkeTHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYNKIFAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 132 PPHLMTGGSDELFNFIAEALAKFVateceDFHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGAL 211
Cdd:cd24130 85 PLEIMQGTGEELFDHIVQCIADFL-----DYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 212 NKALERVG-LDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24130 160 REAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGFGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 291 SHLP---LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHNDT 367
Cdd:cd24130 237 NGCIddiRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 368 SPDLKIvgSKIKDILEVPTTSlKMRKVVISLCNIIATRGARLSAAGIYGILKKLGRDttKDEEVQKSVIAMDGGLFEHYT 447
Cdd:cd24130 317 LALLQV--RRILQQLGLDSTC-EDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIREN--QGLDRLDITVGVDGTLYKLHP 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15233457 448 QFSECMESSLKELlgdEASGSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24130 392 HFSRILQETVKEL---APQCDVTFMLSEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
55-487 |
2.74e-77 |
|
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to type IV hexokinase. It is found in the liver and pancreatic beta-cells, where it is controlled by insulin (activation) and glucagon (inhibition). In pancreatic beta-cells, type IV enzyme acts as a glucose sensor to modify insulin secretion. Mutations in type IV hexokinase have been associated with diabetes mellitus.
Pssm-ID: 466942 [Multi-domain] Cd Length: 444 Bit Score: 249.03 E-value: 2.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 55 LRQVADAMTVEMHAGL--ASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQER--VVKQEFEEVS 130
Cdd:cd24092 16 LKKVMRRMQKEMDRGLrlETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGqwSVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 131 IPPHLMTGGSDELFNFIAEALAKFVateceDFHLPEGRQRELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQDVVGA 210
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFL-----DKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 211 LNKALERVG-LDMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKWHGllpKSGEMVINMEWGNF- 288
Cdd:cd24092 171 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 289 RSSHLP--LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24092 248 DSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 367 TSpDLKivgsKIKDILevptTSLKMR------KVVISLCNIIATRGARLSAAGIYGILKKLgRDtTKDEEVQKSVIAMDG 440
Cdd:cd24092 328 TG-DRK----QIYNIL----STLGLRpsttdcDIVRRACESVSTRAAHMCSAGLAGVINRM-RE-SRSEDVMRITVGVDG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 15233457 441 GLFEHYTQFSECMESSLKELlgdeaSGSVEVT--HSNDGSGIGAALLAA 487
Cdd:cd24092 397 SVYKLHPSFKERFHASVRRL-----TPSCEITfiESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-487 |
5.18e-74 |
|
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type III hexokinase.
Pssm-ID: 466940 [Multi-domain] Cd Length: 431 Bit Score: 240.21 E-value: 5.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 51 PISKLRQVADAMTVEMHAGLASDGG--SKLKMLISYVDNLPSGDEKGLFYALDLG--GTNFRVMRVLLGGKQERVVKQEF 126
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 127 EEVSIPPHLMTGGSDELFNFIAEALAKFVATecedfhLPEGRQR-ELGFTFSFPVKQTSLSSGSLIKWTKGFSIEEAVGQ 205
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDG------QPVPKQGlQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 206 DVVGALNKALERVGL-DMRIAALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERATAIPKwhgLLPKSGEMVINME 284
Cdd:cd24090 157 DVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 285 WGNFR---SSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEDAAFFGDTVPSKLRIPFIIRTPHMS 361
Cdd:cd24090 234 WGSFSddgALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 362 AMHnDTSPDLKIVGSKIKDILEVPTTSLKMRkvVISLCNIIATRGARLSAAGIYGILKKLgRDTTKDEEVQKSViAMDGG 441
Cdd:cd24090 314 EME-DPSAGAARVRAILQDLGLSPSASDVEL--VQHVCRAVCTRAAQLCAAALAAVLSHL-QHSREQQTLQVAV-ATGGR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15233457 442 LFEHYTQFSECMESSLKeLLGDEAsgSVEVTHSNDGSGIGAALLAA 487
Cdd:cd24090 389 VCERHPRFCSILQGTVM-LLAPEC--DVSFIPSVDGGGRGVAMVTA 431
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
210-263 |
1.92e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 40.25 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15233457 210 ALNKALERVGLDMRIAaLVNDTVGTLAGGryYNPDVVAAVILGTGTNAAYVERA 263
Cdd:COG2971 82 ALEAALRELFPFARVV-VVNDALAALAGA--LGGEDGIVVIAGTGSIAAGRDGD 132
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
93-260 |
2.58e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 39.88 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 93 EKGLFYALDLGGTNFRVMRVLLGGKqerVVKQefEEVSIPPHlmtGGSDELFNFIAEALAKFVATECEDFHLPEGrqreL 172
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGE---VLAR--ERIPTPAG---AGPEAVLEAIAELIEELLAEAGISRGRILG----I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233457 173 GFTFSFPV---KQTSLSSGSLIKWTkgfsieeavGQDVVGALNKALervGLDMRIAalvND-TVGTLA-----GGRYYnp 243
Cdd:COG1940 71 GIGVPGPVdpeTGVVLNAPNLPGWR---------GVPLAELLEERL---GLPVFVE---NDaNAAALAeawfgAGRGA-- 133
|
170
....*....|....*..
gi 15233457 244 DVVAAVILGTGTNAAYV 260
Cdd:COG1940 134 DNVVYLTLGTGIGGGIV 150
|
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