|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
15-423 |
0e+00 |
|
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: 806.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 15 KVEQILAEFQLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 94
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 95 EAGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 174
Cdd:cd24092 81 EEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 175 GAEGNNIVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 254
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 255 TEWGAFGNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRF 334
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 335 VSQVESDSGDRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 414
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
....*....
gi 568969727 415 LHPRSASTF 423
Cdd:cd24092 401 LHPSFKERF 409
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
24-418 |
0e+00 |
|
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: 624.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeagqWSVKT 103
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGG----SQVKM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24019 77 ESEIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVEL---VEGDEGRMCVNTEWGAF 260
Cdd:cd24019 157 LLQEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 261 GNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVES 340
Cdd:cd24019 237 GDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIES 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 341 DS-GDRRQILNILSTLGLRP-SVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESrsedvmRITVGVDGSVYKLHPR 418
Cdd:cd24019 317 DNeGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRK------EVTVGVDGSLYKYHPK 390
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
24-444 |
0e+00 |
|
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: 543.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEgeAGQWSVKT 103
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVND--EKNQKVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24089 79 ESQVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24089 159 LLRKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24089 239 GSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPRSASTF 423
Cdd:cd24089 319 GLANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRL 398
|
410 420
....*....|....*....|.
gi 568969727 424 ARAPTSRAPREAPRARLSTPG 444
Cdd:cd24089 399 HKAVRRLVPDCDVRFLLSEDG 419
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
24-433 |
0e+00 |
|
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: 533.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGqwSVKT 103
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWR--GVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24091 79 HNKIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24091 159 LLREAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24091 239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPRSASTF 423
Cdd:cd24091 319 ALLQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVM 398
|
410
....*....|
gi 568969727 424 ARAPTSRAPR 433
Cdd:cd24091 399 HETVKELAPK 408
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
24-433 |
0e+00 |
|
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: 513.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGqwSVKT 103
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWR--GVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24128 79 HNKIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24128 159 LLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24128 239 GCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPRSASTF 423
Cdd:cd24128 319 ALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVM 398
|
410
....*....|
gi 568969727 424 ARAPTSRAPR 433
Cdd:cd24128 399 HETVKDLAPK 408
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
24-420 |
6.42e-176 |
|
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: 500.92 E-value: 6.42e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeaGQWSVKT 103
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSED--GKQKVQM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24126 79 ESQFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24126 159 SLRKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24126 239 GSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568969727 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPRSA 420
Cdd:cd24126 319 GLYNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYA 395
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
24-432 |
1.40e-175 |
|
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: 499.81 E-value: 1.40e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeaGQWSVKT 103
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDN--GLQKVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24125 79 ENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24125 159 LLRKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24125 239 GSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPRSASTF 423
Cdd:cd24125 319 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRL 398
|
....*....
gi 568969727 424 ARAPTSRAP 432
Cdd:cd24125 399 HKTVRRLVP 407
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
25-433 |
7.64e-174 |
|
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: 495.59 E-value: 7.64e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 25 LQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEagQWSVKTK 104
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGK--KRTVEMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 105 HQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGL 184
Cdd:cd24127 80 NKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 185 LRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNSG 264
Cdd:cd24127 160 LRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 265 ELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSGD 344
Cdd:cd24127 240 CLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 345 RRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPRSASTFA 424
Cdd:cd24127 320 LLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMH 399
|
....*....
gi 568969727 425 RAPTSRAPR 433
Cdd:cd24127 400 QTVKELSPK 408
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
24-433 |
1.12e-173 |
|
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: 495.17 E-value: 1.12e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeagqwSVKT 103
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTA-----GVQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24129 76 TSEIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24129 156 LLREAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24129 236 GCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPRSASTF 423
Cdd:cd24129 316 ALRQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLV 395
|
410
....*....|
gi 568969727 424 ARAPTSRAPR 433
Cdd:cd24129 396 QATVRELAPR 405
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
24-433 |
3.20e-171 |
|
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: 489.06 E-value: 3.20e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgegEAGQWSVKT 103
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKI---RSGRRSVRM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24130 78 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24130 158 MLREAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24130 238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPRSASTF 423
Cdd:cd24130 318 ALLQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRIL 397
|
410
....*....|
gi 568969727 424 ARAPTSRAPR 433
Cdd:cd24130 398 QETVKELAPQ 407
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
14-457 |
1.37e-167 |
|
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: 481.42 E-value: 1.37e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 14 EKVEQILAEFQLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGE 93
Cdd:cd24124 19 KKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 94 gEAGQwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKA 173
Cdd:cd24124 99 -EKNQ-NVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 174 SGAEGNNIVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCV 253
Cdd:cd24124 177 SGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 254 NTEWGAFGNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETR 333
Cdd:cd24124 257 NTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 334 FVSQVESDSGDRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVY 413
Cdd:cd24124 337 DVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLY 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568969727 414 KLHPRSASTFARAPTSRAPREAPRARLSTPGFCEPILLDSPWAW 457
Cdd:cd24124 417 KTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAY 460
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
28-417 |
5.74e-144 |
|
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: 419.35 E-value: 5.74e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 28 EDLKKVMSRMQKEMDRGLKletHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgEGEAGQwsVKTKHQM 107
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLE---GDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTL-DGNGGI--FIIVQRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 108 YSIPEDAMTGTAEMLFDYISECISDFLDKHQMKH---KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGL 184
Cdd:cd24018 76 YKIPDEAKTGTGEELFDFIAECIAEFLEEHNLDLqsdKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 185 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNV------ELVEGDEGRMCVNTEWG 258
Cdd:cd24018 156 LQNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 259 AFGNSGELDEFLlEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQV 338
Cdd:cd24018 235 AFDNEREVLPLT-KYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 339 ESD-SGDRRQILNILSTLG--LRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVmriTVGVDGSVYKL 415
Cdd:cd24018 314 EADtSPDLDAVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLPEPV---TVGIDGSVYEK 390
|
..
gi 568969727 416 HP 417
Cdd:cd24018 391 YP 392
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
28-418 |
2.09e-129 |
|
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: 382.35 E-value: 2.09e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 28 EDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLG--GTNFRVMLVKVgEGEAGqWSVKTKH 105
Cdd:cd24090 5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTL-TGIEG-HRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 106 QMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLL 185
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 186 RDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNSGE 265
Cdd:cd24090 163 RDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 266 LDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSGDR 345
Cdd:cd24090 243 LGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGA 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568969727 346 RQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPR 418
Cdd:cd24090 323 ARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPR 395
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
27-418 |
4.18e-125 |
|
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: 368.53 E-value: 4.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 27 EEDLKKVMSRMQKEMDRGLKLEthqEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGegeaGQWSVKTKHQ 106
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLD----GKGIEVTISK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 107 MYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKhKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLLR 186
Cdd:cd24000 74 KYEIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 187 DAIKRRGDfEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNvelVEGDEGRMCVNTEWGAFGNSgel 266
Cdd:cd24000 153 DALKKRGL-PVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 267 DEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGElvrlvllklveenLLfhgeaseqlrtrgafetrfvsqvesdsgdrR 346
Cdd:cd24000 226 SLPRTEYDREVDKASENPGFQPLEKMVSGKYLGE-------------LV------------------------------R 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568969727 347 QILNILstlglrpsvaDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEdvmRITVGVDGSVYKLHPR 418
Cdd:cd24000 263 LILKDL----------ADEILRKICELVAERSARLAAAAIAALLRKTGDSPEK---KITIAVDGSLFEKYPG 321
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
30-418 |
3.84e-109 |
|
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: 330.78 E-value: 3.84e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 30 LKKVMSRMQKEMDRGLKLETHQeaSVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGqwSVKTKHQMYS 109
Cdd:cd24020 6 LRQVADAMVVEMEAGLASEGGS--KLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGR--VDKQEYEEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 110 IPEDAMTGTAEMLFDYISECISDFLDKH----QMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLL 185
Cdd:cd24020 82 IPPELMVGTSEELFDFIAGELAKFVATEgegfHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 186 RDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGD---EGRMCVNTEWGAFgN 262
Cdd:cd24020 162 EEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-R 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 263 SGELDefLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQV-ESD 341
Cdd:cd24020 240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 342 SGDRRQILNILS-TLGL-RPSVADCDIVRRACESVSTRAAHMCSAGLAGVINR-MR-ESRSEDVMRITVGVDGSVYKLHP 417
Cdd:cd24020 318 SPDLETVARILKdALGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKlGRdGGGSSPAQRTVVAVDGGLYEHYP 397
|
.
gi 568969727 418 R 418
Cdd:cd24020 398 K 398
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
28-426 |
3.32e-103 |
|
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: 315.08 E-value: 3.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 28 EDLKKVMSRMQKEMDRGLkleTHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGegeaGQWSVKTKHQM 107
Cdd:cd24087 2 ERLRKITDHFISELEKGL---SKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLG----GNGKFDITQSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 108 YSIPEDAMTGTAEMLFDYISECISDFLDKH--QMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLL 185
Cdd:cd24087 75 YRLPEELKTGTGEELWDFIADCLKKFVEEHfpGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 186 RDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVE----GDEGRMCVNTEWGAFG 261
Cdd:cd24087 155 QKALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 262 NsGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESD 341
Cdd:cd24087 234 N-EHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 342 SGDRRQILNIL--STLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMresrseDVMRITVGVDGSVYKLHPRS 419
Cdd:cd24087 313 PFENLEDTDDLfqHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKR------GYKTCHVAADGSVYNKYPGF 386
|
....*..
gi 568969727 420 ASTFARA 426
Cdd:cd24087 387 KERAAQA 393
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
15-215 |
2.31e-92 |
|
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: 279.00 E-value: 2.31e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 15 KVEQILAEFQLQEEDLKKVMSRMQKEMDRGLKLEThqEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeg 94
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 95 eaGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKH---KKLPLGFTFSFPVRHEDIDKGILLNWTKGF 171
Cdd:pfam00349 77 --GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568969727 172 KASGAEGNNIVGLLRDAIKRRGDfEMDVVAMVNDTVATMISCYY 215
Cdd:pfam00349 155 DIPGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
27-418 |
9.28e-91 |
|
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: 283.52 E-value: 9.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 27 EEDLKKVMSRMQKEMDRGLKletHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgegeAGQWSVKTKHQ 106
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLA---KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL----HGDGTFSLRQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 107 MYSIPEDAMTG-TAEMLFDYISECISDFLDKHQMKH-------KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEG 178
Cdd:cd24088 74 KSKIPDELKTGvTAKDLFDYLAKSVEAFLTKHHGDSfaagkddDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 179 NNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMIS-CYYEDRQCE--VGMIVGTGCNACYMEEMQNV------ELVEGDEG 249
Cdd:cd24088 154 KDVVKLLQDELDRQG-IPVKVVALVNDTVGTLLArSYTSPEISGavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 250 RMCVNTEWGAFGNsgELDEF-LLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLL---FHGEASEQLR 325
Cdd:cd24088 233 HMVINTEWGSFDN--ELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 326 TRGAFETRFVSQVESD--SGDRRQILNILSTLGLR-PSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVM 402
Cdd:cd24088 311 TPYGLDTAVLSAIEIDseAELRATRKVLLDDLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDG 390
|
410
....*....|....*.
gi 568969727 403 RITVGVDGSVYKLHPR 418
Cdd:cd24088 391 EINIGVDGSVIEFYPG 406
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
22-426 |
1.10e-84 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 267.59 E-value: 1.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 22 EFQLQEEDLKKVMSRMQKEMDRGLKletHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEgeAGQWSV 101
Cdd:COG5026 14 GFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYLGLPTGVKETGPVIALDAGGTNFRVALVRFDG--EGTFEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 102 --KTKHQMYSIPEDAmtgTAEMLFDYISECISDFLDKhqmkhkKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGN 179
Cdd:COG5026 89 enFKSFPLPGTSSEI---TAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 180 NIVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQC----EVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 255
Cdd:COG5026 160 NIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 256 EWGAFgnsgelDEFLL-EYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENlLFHGEASEQLRTRGAFETRF 334
Cdd:COG5026 240 ESGNF------NKLPRtKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 335 VSQ-VESDSGDrrqiLNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVInRMRESRSEDVMRITVGVDGSVY 413
Cdd:COG5026 313 MSRfLADPSDE----KEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGIL-LHLGPGKTPLKPHCIAIDGSTY 387
|
410
....*....|...
gi 568969727 414 KLHPRSASTFARA 426
Cdd:COG5026 388 EKMPGLAEKIEYA 400
|
|
| PLN02914 |
PLN02914 |
hexokinase |
19-418 |
2.95e-84 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 268.29 E-value: 2.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 19 ILAEFQLQEED----LKKVMSRMQKEMDRGLKLETHQEasVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 94
Cdd:PLN02914 40 ILTKLQKDCATplpvLRHVADAMAADMRAGLAVDGGGD--LKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 95 EagQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDK-----HQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTK 169
Cdd:PLN02914 118 D--ERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKeggkfHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 170 GFKASGAEGNNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDE- 248
Cdd:PLN02914 196 GFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKs 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 249 --GRMCVNTEWGAFGNSGELDEFlleyDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRT 326
Cdd:PLN02914 275 ssGRTIINTEWGAFSDGLPLTEF----DREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLST 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 327 RGAFETRFVSQVESD-SGDRRQILNILS-TLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVM-- 402
Cdd:PLN02914 351 PFALRTPHLCAMQQDnSDDLQAVGSILYdVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgk 430
|
410
....*....|....*.
gi 568969727 403 RITVGVDGSVYKLHPR 418
Cdd:PLN02914 431 RTVVAMDGGLYEKYPQ 446
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
7-413 |
1.35e-78 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 252.67 E-value: 1.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 7 RMEATKKEKVEQILAEFQLQEEDLKKVMSRMQKEMDRGLK-------LETHQEASVKMLPTYVRSTPEGSEVGDFLSLDL 79
Cdd:PTZ00107 2 MRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEahrrhrnLWIPNECSFKMLDSCVYNLPTGKEKGVYYAIDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 80 GGTNFRVMLVKVGEGeaGQwsVKTKHQMYSIPEDAMTG---------TAEMLFDYISECISDFLDKHQMK---HKKLPLG 147
Cdd:PTZ00107 82 GGTNFRAVRVSLRGG--GK--MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 148 FTFSFPVRHEDIDKGILLNWTKGFKASGA-----EGNNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDR---- 218
Cdd:PTZ00107 158 FTFSFPCTQLSVNNAILIDWTKGFETGRAtndpvEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKPkntp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 219 QCEVGMIVGTGCNACYMEEMQnveLVEGDEGRMcVNTEWGAFgnSGELDefLLEYDRMVDESSVNPGQQLYEKIIGGKYM 298
Cdd:PTZ00107 237 PCQVGVIIGTGSNACYFEPEV---SAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 299 GELVRLVLLklveenLLFHGEASEQLRTRGAFETRFVSQVESD-SGDRRQILNIL-STLGLRPSVADCDIVRRACESVST 376
Cdd:PTZ00107 309 GEISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDqSPDLQFSRQVIkEAWDVDLTDEDLYTIRKICELVRG 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 568969727 377 RAAHMCSAGLAGVINRMRESRSedvmRITVGVDGSVY 413
Cdd:PTZ00107 383 RAAQLAAAFIAAPAKKTRTVQG----KATVAIDGSVY 415
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
221-418 |
3.90e-75 |
|
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: 236.23 E-value: 3.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 221 EVGMIVGTGCNACYMEEMQNVELVEGD---EGRMCVNTEWGAFGNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKY 297
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 298 MGELVRLVLLKLVEENLLFHGEaSEQLRTRGAFETRFVSQVESD-SGDRRQILNILS-TLGLR-PSVADCDIVRRACESV 374
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEeLLGIEtVTEEDRKIVRRICEAV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568969727 375 STRAAHMCSAGLAGVINRMRESRsedvmRITVGVDGSVYKLHPR 418
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPG 198
|
|
| PLN02405 |
PLN02405 |
hexokinase |
5-414 |
4.31e-71 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 233.96 E-value: 4.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 5 RARMEATKK-EKVEQILAEFqlqEED-------LKKVMSRMQKEMDRGLKLETHqeASVKMLPTYVRSTPEGSEVGDFLS 76
Cdd:PLN02405 25 RRRMKSSGKwARAMEILKEF---EEDcatpigkLRQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 77 LDLGGTNFRVMLVKVGEGEAGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFL-----DKHQMKHKKLPLGFTFS 151
Cdd:PLN02405 100 LDLGGTNFRVLRVLLGGKDGR--VVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 152 FPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCN 231
Cdd:PLN02405 178 FPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-LDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 232 ACYMEEMQNVELVEGD---EGRMCVNTEWGAFgNSGELDefLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLK 308
Cdd:PLN02405 257 AAYVERAQAIPKWHGLlpkSGEMVINMEWGNF-RSSHLP--LTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 309 LVEENLLFHGEASEQLRTRGAFETRFVSQVESD-SGDRR-------QILNILSTlglrpSVADCDIVRRACESVSTRAAH 380
Cdd:PLN02405 334 MAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDtSPDLKvvgsklkDILEIPNT-----SLKMRKVVVELCNIVATRGAR 408
|
410 420 430
....*....|....*....|....*....|....*.
gi 568969727 381 MCSAGLAGVINRM-RES-RSEDVMRITVGVDGSVYK 414
Cdd:PLN02405 409 LSAAGIYGILKKLgRDTvKDGEKQKSVIAMDGGLFE 444
|
|
| PLN02362 |
PLN02362 |
hexokinase |
5-413 |
4.66e-66 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 221.29 E-value: 4.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 5 RARMEATKK-EKVEQILAEFQLQEED----LKKVMSRMQKEMDRGLKLETHqeASVKMLPTYVRSTPEGSEVGDFLSLDL 79
Cdd:PLN02362 25 GRRVKSRRKwRRVVGVLKELEEACETpvgrLRQVVDAMAVEMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 80 GGTNFRVMLVKVGEGEAGQWSVKTKHQmySIPEDAMTGTAEMLFDYISECISDFLDKHQMKH-----KKLPLGFTFSFPV 154
Cdd:PLN02362 103 GGTNFRVLRVQLGGQRSSILSQDVERH--PIPQHLMNSTSEVLFDFIASSLKQFVEKEENGSefsqvRRRELGFTFSFPV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 155 RHEDIDKGILLNWTKGFKASGAEGNNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACY 234
Cdd:PLN02362 181 KQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 235 MEEMQNVELVEG---DEGRMCVNTEWGAFGNSgELDEflLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVE 311
Cdd:PLN02362 260 LERTDAIIKCQGlltTSGSMVVNMEWGNFWSS-HLPR--TSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 312 ENLLFhGEASEQLRTRGAFETRFVSQV-ESDSGDRRQILNIL-STLGLRP-SVADCDIVRRACESVSTRAAHMCSAGLAG 388
Cdd:PLN02362 337 ESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARILkETLGISEvPLKVRKLVVKICDVVTRRAARLAAAGIVG 415
|
410 420 430
....*....|....*....|....*....|....*..
gi 568969727 389 VINRMRE----------SRSEDVM--RITVGVDGSVY 413
Cdd:PLN02362 416 ILKKIGRdgsggitsgrSRSDIQImrRTVVAVEGGLY 452
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
47-413 |
3.41e-38 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 145.40 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 47 LETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAgqwSVKTKH-QMYSIPEDAMTGTAEMLFDY 125
Cdd:PLN02596 71 LTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNE---PISDLYrEEISIPSNVLNGTSQELFDY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 126 ISECISDFLDKHQMKHKKLP-----LGFTFSFPVRHEDIDKGILLNWtKGFKASGAEGNNIVGLLRDAIKRRGdFEMDVV 200
Cdd:PLN02596 148 IALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 201 AMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFgNSGELDefLLEYDRMV 277
Cdd:PLN02596 226 ALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF-NSCHLP--ITEFDASL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 278 DESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSGDRRQILN--ILSTL 355
Cdd:PLN02596 303 DAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNekLKEIF 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 568969727 356 GLRPSV-ADCDIVRRACESVSTRAAHMCSAGLAGVINRMreSRSEDVMRItVGVDGSVY 413
Cdd:PLN02596 383 GITDSTpMAREVVAEVCDIVAERGARLAGAGIVGIIKKL--GRIENKKSV-VTVEGGLY 438
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
74-266 |
5.52e-05 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 44.97 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 74 FLSLDLGGTNFRVMLVKvgegEAGQWSVKTKHQmysipedamtgTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFP 153
Cdd:PRK09698 6 VLGIDMGGTHIRFCLVD----AEGEILHCEKKR-----------TAEVIAPDLVSGLGEMIDEYLRRFNARCHGIVMGFP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 154 --VrheDIDKGILLNwTKGFKASGAEGNNIVGLLRDAIKRRGDFEMDV-VAMVNDTVAtmiscYYEDRQCEVGMIVGTGC 230
Cdd:PRK09698 71 alV---SKDRRTVIS-TPNLPLTALDLYDLADKLENTLNCPVFFSRDVnLQLLWDVKE-----NNLTQQLVLGAYLGTGM 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 568969727 231 -NACYMeemqnvelvegdEGRMCVntewGAFGNSGEL 266
Cdd:PRK09698 142 gFAVWM------------NGAPWT----GAHGVAGEL 162
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
74-266 |
4.43e-04 |
|
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: 42.19 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 74 FLSLDLGGTNFRVMLVKVGEGEAGQWSVKTKHQmysipedamtGTAEMLFDYISECISDFLDKHQMKHKKL-PLGFTFSF 152
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIPTPAG----------AGPEAVLEAIAELIEELLAEAGISRGRIlGIGIGVPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969727 153 PVrheDIDKGILLNwtkgfkasgaeGNNIVGL----LRDAIKRRGDFEmdvVAMVNDTVATMIS--CYYEDRQCE--VGM 224
Cdd:COG1940 77 PV---DPETGVVLN-----------APNLPGWrgvpLAELLEERLGLP---VFVENDANAAALAeaWFGAGRGADnvVYL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568969727 225 IVGTGCNACYmeeMQNVELVEgdegrmcvntewGAFGNSGEL 266
Cdd:COG1940 140 TLGTGIGGGI---VINGKLLR------------GANGNAGEI 166
|
|
| |
