|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
14-457 |
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: 920.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 14 QVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 93
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 94 EEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 173
Cdd:cd24092 81 EEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 174 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 253
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 254 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 333
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 334 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 413
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15967161 414 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 457
Cdd:cd24092 401 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
23-453 |
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: 678.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 23 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEgqwsVKT 102
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQ----VKM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 103 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 182
Cdd:cd24019 77 ESEIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 183 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVEL---VEGDEGRMCVNTEWGAF 259
Cdd:cd24019 157 LLQEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 260 GDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVES 339
Cdd:cd24019 237 GDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIES 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 340 DT-GDRKQIYNILSTLGLRP-STTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESrsedvmRITVGVDGSVYKLHPS 417
Cdd:cd24019 317 DNeGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRK------EVTVGVDGSLYKYHPK 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 15967161 418 FKERFHASVRRLTPS-CEITFIESEEGSGRGAALVSA 453
Cdd:cd24019 391 FHKRMHETLKELVPPgCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
23-453 |
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: 602.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 23 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEgeEGQWSVKT 102
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVND--EKNQKVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 103 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 182
Cdd:cd24089 79 ESQVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 183 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDS 262
Cdd:cd24089 159 LLRKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 263 GELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTG 342
Cdd:cd24089 239 GSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 343 DRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 422
Cdd:cd24089 319 GLANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 15967161 423 HASVRRLTPSCEITFIESEEGSGRGAALVSA 453
Cdd:cd24089 399 HKAVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
23-457 |
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: 582.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 23 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGqwSVKT 102
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWR--GVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 103 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 182
Cdd:cd24091 79 HNKIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 183 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDS 262
Cdd:cd24091 159 LLREAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 263 GELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTG 342
Cdd:cd24091 239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 343 DRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 422
Cdd:cd24091 319 ALLQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVM 398
|
410 420 430
....*....|....*....|....*....|....*
gi 15967161 423 HASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 457
Cdd:cd24091 399 HETVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
23-457 |
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: 561.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 23 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGqwSVKT 102
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWR--GVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 103 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 182
Cdd:cd24128 79 HNKIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 183 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDS 262
Cdd:cd24128 159 LLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 263 GELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTG 342
Cdd:cd24128 239 GCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 343 DRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 422
Cdd:cd24128 319 ALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVM 398
|
410 420 430
....*....|....*....|....*....|....*
gi 15967161 423 HASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 457
Cdd:cd24128 399 HETVKDLAPKCDVSFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
23-453 |
0e+00 |
|
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: 549.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 23 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEgeEGQWSVKT 102
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSD--NGLQKVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 103 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 182
Cdd:cd24125 79 ENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 183 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDS 262
Cdd:cd24125 159 LLRKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 263 GELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTG 342
Cdd:cd24125 239 GSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 343 DRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 422
Cdd:cd24125 319 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 15967161 423 HASVRRLTPSCEITFIESEEGSGRGAALVSA 453
Cdd:cd24125 399 HKTVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
23-453 |
0e+00 |
|
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: 547.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 23 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEgeEGQWSVKT 102
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSE--DGKQKVQM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 103 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 182
Cdd:cd24126 79 ESQFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 183 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDS 262
Cdd:cd24126 159 SLRKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 263 GELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESdtg 342
Cdd:cd24126 239 GSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEK--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 343 DRKQIYN---ILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK 419
Cdd:cd24126 316 YKEGLYNtreILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYA 395
|
410 420 430
....*....|....*....|....*....|....
gi 15967161 420 ERFHASVRRLTPSCEITFIESEEGSGRGAALVSA 453
Cdd:cd24126 396 KRLHKVVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
24-457 |
0e+00 |
|
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: 546.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 24 LQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEegQWSVKTK 103
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGK--KRTVEMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 104 HQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 183
Cdd:cd24127 80 NKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 184 LRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDSG 263
Cdd:cd24127 160 LRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 264 ELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGD 343
Cdd:cd24127 240 CLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 344 RKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFH 423
Cdd:cd24127 320 LLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMH 399
|
410 420 430
....*....|....*....|....*....|....
gi 15967161 424 ASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 457
Cdd:cd24127 400 QTVKELSPKCNVSFLLSEDGSGKGAALITAVGVR 433
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
23-457 |
0e+00 |
|
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: 539.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 23 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeegqwSVKT 102
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTA-----GVQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 103 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 182
Cdd:cd24129 76 TSEIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 183 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDS 262
Cdd:cd24129 156 LLREAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 263 GELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTG 342
Cdd:cd24129 236 GCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 343 DRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 422
Cdd:cd24129 316 ALRQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLV 395
|
410 420 430
....*....|....*....|....*....|....*
gi 15967161 423 HASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 457
Cdd:cd24129 396 QATVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
23-455 |
0e+00 |
|
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: 527.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 23 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgegEEGQWSVKT 102
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKI---RSGRRSVRM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 103 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 182
Cdd:cd24130 78 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 183 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDS 262
Cdd:cd24130 158 MLREAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 263 GELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTG 342
Cdd:cd24130 238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 343 DRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 422
Cdd:cd24130 318 ALLQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRIL 397
|
410 420 430
....*....|....*....|....*....|...
gi 15967161 423 HASVRRLTPSCEITFIESEEGSGRGAALVSAVA 455
Cdd:cd24130 398 QETVKELAPQCDVTFMLSEDGSGKGAALITAVA 430
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
14-459 |
0e+00 |
|
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: 525.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 14 QVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEg 93
Cdd:cd24124 20 KIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNH- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 94 eEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 173
Cdd:cd24124 99 -EKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKAS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 174 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 253
Cdd:cd24124 178 GVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCIN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 254 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 333
Cdd:cd24124 258 TEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 334 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 413
Cdd:cd24124 338 VSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYK 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15967161 414 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKA 459
Cdd:cd24124 418 THPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLA 463
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
27-452 |
4.89e-153 |
|
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: 441.69 E-value: 4.89e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 27 EDLKKVMRRMQKEMDRGLRletHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgEGEEGQwsVKTKHQM 106
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLE---GDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTL-DGNGGI--FIIVQRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 107 YSIPEDAMTGTAEMLFDYISECISDFLDKHQMKH---KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 183
Cdd:cd24018 76 YKIPDEAKTGTGEELFDFIAECIAEFLEEHNLDLqsdKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 184 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNV------ELVEGDEGRMCVNTEWG 257
Cdd:cd24018 156 LQNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 258 AFGDSGELDEFLlEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQV 337
Cdd:cd24018 235 AFDNEREVLPLT-KYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 338 ESDT-GDRKQIYNILSTLGLRPSTTDCD--IVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVmriTVGVDGSVYKL 414
Cdd:cd24018 314 EADTsPDLDAVRDILKELLAIDNTTLEDrkLIKRICELVSTRAARLSAAAIAAILLKRGSLLPEPV---TVGIDGSVYEK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15967161 415 HPSFKERFHASVRRLTPSC---EITFIESEEGSGRGAALVS 452
Cdd:cd24018 391 YPGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
27-453 |
2.64e-142 |
|
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: 414.32 E-value: 2.64e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 27 EDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLG--GTNFRVMLVKVgEGEEGqWSVKTKH 104
Cdd:cd24090 5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTL-TGIEG-HRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 105 QMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLL 184
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 185 RDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDSGE 264
Cdd:cd24090 163 RDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 265 LDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDR 344
Cdd:cd24090 243 LGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 345 KQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHA 424
Cdd:cd24090 323 ARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQG 402
|
410 420
....*....|....*....|....*....
gi 15967161 425 SVRRLTPSCEITFIESEEGSGRGAALVSA 453
Cdd:cd24090 403 TVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
26-451 |
6.85e-138 |
|
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: 400.50 E-value: 6.85e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 26 EEDLKKVMRRMQKEMDRGLRletHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgegeEGQWSVKTKHQ 105
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLA---GEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSL----DGKGIEVTISK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 106 MYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKhKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLLR 185
Cdd:cd24000 74 KYEIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 186 DAIKRRGDfEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNvelVEGDEGRMCVNTEWGAFGDSgel 265
Cdd:cd24000 153 DALKKRGL-PVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 266 DEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGElvrlvllrlvdenllfhgeaseqlrtrgafetrfvsqvesdtgdrk 345
Cdd:cd24000 226 SLPRTEYDREVDKASENPGFQPLEKMVSGKYLGE---------------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 346 QIYNILSTLglrpsttDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEdvmRITVGVDGSVYKLHPSFKERFHAS 425
Cdd:cd24000 260 LVRLILKDL-------ADEILRKICELVAERSARLAAAAIAALLRKTGDSPEK---KITIAVDGSLFEKYPGYRERLEEY 329
|
410 420
....*....|....*....|....*..
gi 15967161 426 VRRLTPS-CEITFIESEEGSGRGAALV 451
Cdd:cd24000 330 LKELLGRgIRIELVLVEDGSLIGAALA 356
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
29-455 |
9.66e-117 |
|
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: 349.27 E-value: 9.66e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 29 LKKVMRRMQKEMDRGLRLETHeeASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGqwSVKTKHQMYS 108
Cdd:cd24020 6 LRQVADAMVVEMEAGLASEGG--SKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGR--VDKQEYEEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 109 IPEDAMTGTAEMLFDYISECISDFLDKH----QMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLL 184
Cdd:cd24020 82 IPPELMVGTSEELFDFIAGELAKFVATEgegfHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 185 RDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGD---EGRMCVNTEWGAFgD 261
Cdd:cd24020 162 EEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-R 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 262 SGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDT 341
Cdd:cd24020 240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 342 G-DRKQIYNILSTLGLRPSTT--DCDIVRRACESVSTRAAHMCSAGLAGVINR-MR-ESRSEDVMRITVGVDGSVYKLHP 416
Cdd:cd24020 318 SpDLETVARILKDALGIDDTSleARKVVVEVCDLVAERGARLAAAGIVGILKKlGRdGGGSSPAQRTVVAVDGGLYEHYP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15967161 417 SFKERFHASVRRL---TPSCEITFIESEEGSGRGAALVSAVA 455
Cdd:cd24020 398 KFREYMQQALVELlgdEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
27-455 |
6.00e-113 |
|
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: 339.35 E-value: 6.00e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 27 EDLKKVMRRMQKEMDRGLrleTHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGegeeGQWSVKTKHQM 106
Cdd:cd24087 2 ERLRKITDHFISELEKGL---SKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLG----GNGKFDITQSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 107 YSIPEDAMTGTAEMLFDYISECISDFLDKH--QMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLL 184
Cdd:cd24087 75 YRLPEELKTGTGEELWDFIADCLKKFVEEHfpGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 185 RDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVE----GDEGRMCVNTEWGAFg 260
Cdd:cd24087 155 QKALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 261 DSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESD 340
Cdd:cd24087 233 DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 341 -TGDRKQIYNILST-LGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMresrseDVMRITVGVDGSVYKLHPSF 418
Cdd:cd24087 313 pFENLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKR------GYKTCHVAADGSVYNKYPGF 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15967161 419 KERFHASVRRL----TPSCEITFIESEEGSGRGAALVSAVA 455
Cdd:cd24087 387 KERAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
26-451 |
5.68e-97 |
|
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: 298.93 E-value: 5.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 26 EEDLKKVMRRMQKEMDRGLrleTHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgegeEGQWSVKTKHQ 105
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL----HGDGTFSLRQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 106 MYSIPEDAMTG-TAEMLFDYISECISDFLDKHQMKH-------KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEG 177
Cdd:cd24088 74 KSKIPDELKTGvTAKDLFDYLAKSVEAFLTKHHGDSfaagkddDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 178 NNVVGLLRDAIKRRGdFEMDVVAMVNDTVATMIS-CYYEDHQCE--VGMIVGTGCNACYMEEMQNV------ELVEGDEG 248
Cdd:cd24088 154 KDVVKLLQDELDRQG-IPVKVVALVNDTVGTLLArSYTSPEISGavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 249 RMCVNTEWGAFGDsgELDEF-LLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLL---FHGEASEQLR 324
Cdd:cd24088 233 HMVINTEWGSFDN--ELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 325 TRGAFETRFVSQVESD-TGDRKQIYNIL-STLGLR-PSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVM 401
Cdd:cd24088 311 TPYGLDTAVLSAIEIDsEAELRATRKVLlDDLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15967161 402 RITVGVDGSVYKLHPSFKERFHASVRRLTPSCE----ITFIESEEGSGRGAALV 451
Cdd:cd24088 391 EINIGVDGSVIEFYPGFESMLREALRLLLIGAEgekrIKIGIAKDGSGVGAALC 444
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
10-455 |
8.20e-93 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 288.88 E-value: 8.20e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 10 QPNSQVEQILAEFQLQEEDLKKVMRRMQKEMDRGLrlETH---------EEASVKMLPTYVRSTPEGSEVGDFLSLDLGG 80
Cdd:PTZ00107 6 KQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGL--EAHrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 81 TNFRVMLVKVGEGEEgqwsVKTKHQMYSIPEDAMTG---------TAEMLFDYISECISDFLDKHQMK---HKKLPLGFT 148
Cdd:PTZ00107 84 TNFRAVRVSLRGGGK----MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 149 FSFPVRHEDIDKGILLNWTKGFKASGA-----EGNNVVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDH----QC 219
Cdd:PTZ00107 160 FSFPCTQLSVNNAILIDWTKGFETGRAtndpvEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKPkntpPC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 220 EVGMIVGTGCNACYMEEMQnveLVEGDEGRMcVNTEWGAFgDSgELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGE 299
Cdd:PTZ00107 239 QVGVIIGTGSNACYFEPEV---SAYGYAGTP-INMECGNF-DS-KLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 300 LVRLVLLrlvdenLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYN--ILSTLGLRPSTTDCDIVRRACESVSTRA 377
Cdd:PTZ00107 311 ISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFSRqvIKEAWDVDLTDEDLYTIRKICELVRGRA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 378 AHMCSAGLAGVINRMRESRSedvmRITVGVDGSVYKLHPSFKERFHASVRRLT--PSCEITFIESEEGSGRGAALVSAVA 455
Cdd:PTZ00107 385 AQLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSILgpDAGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
14-214 |
9.12e-93 |
|
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: 9.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 14 QVEQILAEFQLQEEDLKKVMRRMQKEMDRGLrlETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeg 93
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGL--AKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 94 eeGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKH---KKLPLGFTFSFPVRHEDIDKGILLNWTKGF 170
Cdd:pfam00349 77 --GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15967161 171 KASGAEGNNVVGLLRDAIKRRGDfEMDVVAMVNDTVATMISCYY 214
Cdd:pfam00349 155 DIPGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
9-456 |
2.60e-92 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 286.47 E-value: 2.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 9 PQPNSQVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRletHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLV 88
Cdd:COG5026 2 KKLLVDAFLKRHGFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYLGLPTGVKETGPVIALDAGGTNFRVALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 89 KVGEgeEGQWSV--KTKHQMYSIPEDAmtgTAEMLFDYISECISDFLDKhqmkhkKLPLGFTFSFPVRHEDIDKGILLNW 166
Cdd:COG5026 79 RFDG--EGTFEIenFKSFPLPGTSSEI---TAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 167 TKGFKASGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQC----EVGMIVGTGCNACYMEEMQNVEL 242
Cdd:COG5026 148 TKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 243 VEGDEGRMCVNTEWGAFgdsgelDEFLL-EYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENlLFHGEASE 321
Cdd:COG5026 228 LPAYEGPMIINMESGNF------NKLPRtKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 322 QLRTRGAFETRFVSQVESDTGDRKqiyNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVInRMRESRSEDVM 401
Cdd:COG5026 301 VFETPYSLTTVDMSRFLADPSDEK---EILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGIL-LHLGPGKTPLK 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15967161 402 RITVGVDGSVYKLHPSFKERFHASVRR-LTPSCE--ITFIESEEGSGRGAALVSAVAC 456
Cdd:COG5026 377 PHCIAIDGSTYEKMPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
|
|
| PLN02914 |
PLN02914 |
hexokinase |
2-457 |
5.21e-92 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 287.55 E-value: 5.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 2 PRPRSQLPQPNSQVEQILAEFQLQEEDLKKVMRRMQKEMDRGLR--LETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLG 79
Cdd:PLN02914 24 PRSRMAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRagLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 80 GTNFRVMLVKVGEGEEGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDK-----HQMKHKKLPLGFTFSFPVR 154
Cdd:PLN02914 104 GTNFRVLRVQLGGKDER--VIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKeggkfHLPEGRKREIGFTFSFPVK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 155 HEDIDKGILLNWTKGFKASGAEGNNVVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYM 234
Cdd:PLN02914 182 QTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 235 EEMQNVELVEGDE---GRMCVNTEWGAFGDSGELDEFlleyDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDE 311
Cdd:PLN02914 261 ERTDAIPKLQGQKsssGRTIINTEWGAFSDGLPLTEF----DREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAET 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 312 NLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQ-----IYNIlstLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLA 386
Cdd:PLN02914 337 SDLFGHFVPEKLSTPFALRTPHLCAMQQDNSDDLQavgsiLYDV---LGVEASLSARRRVVEVCDTIVKRGGRLAGAGIV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15967161 387 GVINRMRESRSEDVM--RITVGVDGSVYKLHPSFKERFHASVRRL---TPSCEITFIESEEGSGRGAALVSAVACK 457
Cdd:PLN02914 414 GILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTELlglELSKNIAIEHTKDGSGIGAALLAATNSK 489
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
220-454 |
5.64e-92 |
|
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: 278.61 E-value: 5.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 220 EVGMIVGTGCNACYMEEMQNVELVEGD---EGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKY 296
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 297 MGELVRLVLLRLVDENLLFHGEaSEQLRTRGAFETRFVSQVESD-TGDRKQIYNILS-TLGLRPSTT-DCDIVRRACESV 373
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEeLLGIETVTEeDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 374 STRAAHMCSAGLAGVINRMRESRsedvmRITVGVDGSVYKLHPSFKERFHASVRRLT-PSCEITFIESEEGSGRGAALVS 452
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 15967161 453 AV 454
Cdd:pfam03727 235 AV 236
|
|
| PLN02405 |
PLN02405 |
hexokinase |
13-453 |
1.54e-74 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 242.43 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 13 SQVEQILAEFqlqEED-------LKKVMRRMQKEMDRGLRLETHeeASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRV 85
Cdd:PLN02405 35 ARAMEILKEF---EEDcatpigkLRQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 86 MLVKVGEGEEGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFL-----DKHQMKHKKLPLGFTFSFPVRHEDIDK 160
Cdd:PLN02405 110 LRVLLGGKDGR--VVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 161 GILLNWTKGFKASGAEGNNVVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNV 240
Cdd:PLN02405 188 GTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-LDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 241 ELVEGD---EGRMCVNTEWGAFgDSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHG 317
Cdd:PLN02405 267 PKWHGLlpkSGEMVINMEWGNF-RSSHLP--LTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 318 EASEQLRTRGAFETRFVSQVESDTG-DRKQIYNILSTLgLRPSTTDCD---IVRRACESVSTRAAHMCSAGLAGVINRM- 392
Cdd:PLN02405 344 TVPPKLKIPFILRTPDMSAMHHDTSpDLKVVGSKLKDI-LEIPNTSLKmrkVVVELCNIVATRGARLSAAGIYGILKKLg 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15967161 393 RES-RSEDVMRITVGVDGSVYKLHPSFKERFHASVRRL---TPSCEITFIESEEGSGRGAALVSA 453
Cdd:PLN02405 423 RDTvKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELlgeEVSESIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
29-453 |
2.54e-70 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 231.69 E-value: 2.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 29 LKKVMRRMQKEMDRGLRLETHeeASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQmyS 108
Cdd:PLN02362 55 LRQVVDAMAVEMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERH--P 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 109 IPEDAMTGTAEMLFDYISECISDFLDKHQMKH-----KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 183
Cdd:PLN02362 131 IPQHLMNSTSEVLFDFIASSLKQFVEKEENGSefsqvRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAEC 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 184 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFG 260
Cdd:PLN02362 211 LQGALNRRG-LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFW 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 261 DSgELDEflLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFhGEASEQLRTRGAFETRFVSQV-ES 339
Cdd:PLN02362 290 SS-HLPR--TSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhED 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 340 DTGDRKQIYNIL-STLGLRPSTTDC-DIVRRACESVSTRAAHMCSAGLAGVINRMRE----------SRSEDVM--RITV 405
Cdd:PLN02362 366 DSPELQEVARILkETLGISEVPLKVrKLVVKICDVVTRRAARLAAAGIVGILKKIGRdgsggitsgrSRSDIQImrRTVV 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15967161 406 GVDGSVYKLHPSFKERFHASVRRL---TPSCEITFIESEEGSGRGAALVSA 453
Cdd:PLN02362 446 AVEGGLYTNYTMFREYLHEALNEIlgeDVAQHVILKATEDGSGIGSALLAA 496
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
46-453 |
5.73e-43 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 158.12 E-value: 5.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 46 LETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEgqwSVKTKH-QMYSIPEDAMTGTAEMLFDY 124
Cdd:PLN02596 71 LTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNE---PISDLYrEEISIPSNVLNGTSQELFDY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 125 ISECISDFLDKHQMKHKKLP-----LGFTFSFPVRHEDIDKGILLNWtKGFKASGAEGNNVVGLLRDAIKRRGdFEMDVV 199
Cdd:PLN02596 148 IALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 200 AMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFgDSGELDefLLEYDRLV 276
Cdd:PLN02596 226 ALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF-NSCHLP--ITEFDASL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 277 DESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYN--ILSTL 354
Cdd:PLN02596 303 DAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNekLKEIF 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 355 GLRPSTTDC-DIVRRACESVSTRAAHMCSAGLAGVINRMreSRSEDVMRItVGVDGSVYKLHPSFKERFHASVRRLTPS- 432
Cdd:PLN02596 383 GITDSTPMArEVVAEVCDIVAERGARLAGAGIVGIIKKL--GRIENKKSV-VTVEGGLYEHYRVFRNYLHSSVWEMLGSe 459
|
410 420
....*....|....*....|...
gi 15967161 433 -CEITFIE-SEEGSGRGAALVSA 453
Cdd:PLN02596 460 lSDNVVIEhSHGGSGAGALFLAA 482
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
73-265 |
3.85e-06 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 48.44 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 73 FLSLDLGGTNFRVMLVKvgegEEGQWSVKTKHQmysipedamtgTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFP 152
Cdd:PRK09698 6 VLGIDMGGTHIRFCLVD----AEGEILHCEKKR-----------TAEVIAPDLVSGLGEMIDEYLRRFNARCHGIVMGFP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 153 --VrheDIDKGILLNwTKGFKASGAEGNNVVGLLRDAIKRRGDFEMDV-VAMVNDTVAtmiscYYEDHQCEVGMIVGTGC 229
Cdd:PRK09698 71 alV---SKDRRTVIS-TPNLPLTALDLYDLADKLENTLNCPVFFSRDVnLQLLWDVKE-----NNLTQQLVLGAYLGTGM 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 15967161 230 -NACYMeemqnvelvegdEGRMCVntewGAFGDSGEL 265
Cdd:PRK09698 142 gFAVWM------------NGAPWT----GAHGVAGEL 162
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
73-232 |
2.79e-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: 39.49 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 73 FLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQmysipedamtGTAEMLFDYISECISDFLDKHQMKHKKL-PLGFTFSF 151
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIPTPAG----------AGPEAVLEAIAELIEELLAEAGISRGRIlGIGIGVPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15967161 152 PVrheDIDKGILLNwtkgfkasgaeGNNVVGL----LRDAIKRRGDFEmdvVAMVNDTVAtmiSCYYE-------DHQCE 220
Cdd:COG1940 77 PV---DPETGVVLN-----------APNLPGWrgvpLAELLEERLGLP---VFVENDANA---AALAEawfgagrGADNV 136
|
170
....*....|..
gi 15967161 221 VGMIVGTGCNAC 232
Cdd:COG1940 137 VYLTLGTGIGGG 148
|
|
| |
