|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
16-458 |
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: 874.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 16 VEQILAEFQLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGE 95
Cdd:cd24092 2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 96 AGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 175
Cdd:cd24092 82 EGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 176 AEGNNIVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 255
Cdd:cd24092 162 AEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 256 EWGAFGNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFV 335
Cdd:cd24092 242 EWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 336 SQVESDSGDRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 415
Cdd:cd24092 322 SQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1008870 416 HPSFKERFHASVRRLTPNCEITFIESEEGSGRGAALVSAVACK 458
Cdd:cd24092 402 HPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
24-454 |
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: 665.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeagqWSVKT 103
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGG----SQVKM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24019 77 ESEIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVEL---VEGDEGRMCVNTEWGAF 260
Cdd:cd24019 157 LLQEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 261 GNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVES 340
Cdd:cd24019 237 GDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIES 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 341 DS-GDRRQILNILSTLGLRP-SVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESrsedvmRITVGVDGSVYKLHPS 418
Cdd:cd24019 317 DNeGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRK------EVTVGVDGSLYKYHPK 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 1008870 419 FKERFHASVRRLTP-NCEITFIESEEGSGRGAALVSA 454
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 ... |
24-454 |
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: 591.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEgeAGQWSVKT 103
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVND--EKNQKVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24089 79 ESQVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24089 159 LLRKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24089 239 GSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 423
Cdd:cd24089 319 GLANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 1008870 424 HASVRRLTPNCEITFIESEEGSGRGAALVSA 454
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 ... |
24-458 |
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: 576.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGqwSVKT 103
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWR--GVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24091 79 HNKIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24091 159 LLREAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24091 239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 423
Cdd:cd24091 319 ALLQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVM 398
|
410 420 430
....*....|....*....|....*....|....*
gi 1008870 424 HASVRRLTPNCEITFIESEEGSGRGAALVSAVACK 458
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 ... |
24-458 |
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: 558.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGqwSVKT 103
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWR--GVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24128 79 HNKIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24128 159 LLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24128 239 GCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 423
Cdd:cd24128 319 ALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVM 398
|
410 420 430
....*....|....*....|....*....|....*
gi 1008870 424 HASVRRLTPNCEITFIESEEGSGRGAALVSAVACK 458
Cdd:cd24128 399 HETVKDLAPKCDVSFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
24-454 |
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: 544.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeaGQWSVKT 103
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSED--GKQKVQM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24126 79 ESQFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24126 159 SLRKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24126 239 GSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 423
Cdd:cd24126 319 GLYNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 1008870 424 HASVRRLTPNCEITFIESEEGSGRGAALVSA 454
Cdd:cd24126 399 HKVVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
24-454 |
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: 542.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeaGQWSVKT 103
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDN--GLQKVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24125 79 ENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24125 159 LLRKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24125 239 GSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 423
Cdd:cd24125 319 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 1008870 424 HASVRRLTPNCEITFIESEEGSGRGAALVSA 454
Cdd:cd24125 399 HKTVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
25-458 |
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: 539.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 25 LQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEagQWSVKTK 104
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGK--KRTVEMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 105 HQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGL 184
Cdd:cd24127 80 NKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 185 LRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNSG 264
Cdd:cd24127 160 LRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 265 ELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSGD 344
Cdd:cd24127 240 CLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 345 RRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFH 424
Cdd:cd24127 320 LLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMH 399
|
410 420 430
....*....|....*....|....*....|....
gi 1008870 425 ASVRRLTPNCEITFIESEEGSGRGAALVSAVACK 458
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 ... |
24-458 |
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: 537.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeagqwSVKT 103
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTA-----GVQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24129 76 TSEIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24129 156 LLREAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24129 236 GCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 423
Cdd:cd24129 316 ALRQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLV 395
|
410 420 430
....*....|....*....|....*....|....*
gi 1008870 424 HASVRRLTPNCEITFIESEEGSGRGAALVSAVACK 458
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 ... |
24-456 |
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: 527.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 24 QLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgegEAGQWSVKT 103
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKI---RSGRRSVRM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 104 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVG 183
Cdd:cd24130 78 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 184 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNS 263
Cdd:cd24130 158 MLREAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 264 GELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSG 343
Cdd:cd24130 238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 344 DRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 423
Cdd:cd24130 318 ALLQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRIL 397
|
410 420 430
....*....|....*....|....*....|...
gi 1008870 424 HASVRRLTPNCEITFIESEEGSGRGAALVSAVA 456
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 ... |
16-460 |
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: 521.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 16 VEQILAEFQLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEgE 95
Cdd:cd24124 21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNH-E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 96 AGQwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 175
Cdd:cd24124 100 KNQ-NVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 176 AEGNNIVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 255
Cdd:cd24124 179 VEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 256 EWGAFGNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFV 335
Cdd:cd24124 259 EWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 336 SQVESDSGDRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 415
Cdd:cd24124 339 SAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKT 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1008870 416 HPSFKERFHASVRRLTPNCEITFIESEEGSGRGAALVSAVACKKA 460
Cdd:cd24124 419 HPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLA 463
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
28-453 |
1.31e-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: 443.23 E-value: 1.31e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 28 EDLKKVMSRMQKEMDRGLKletHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgEGEAGQwsVKTKHQM 107
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLE---GDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTL-DGNGGI--FIIVQRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 108 YSIPEDAMTGTAEMLFDYISECISDFLDKHQMKH---KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGL 184
Cdd:cd24018 76 YKIPDEAKTGTGEELFDFIAECIAEFLEEHNLDLqsdKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 185 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNV------ELVEGDEGRMCVNTEWG 258
Cdd:cd24018 156 LQNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 259 AFGNSGELDEFLlEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQV 338
Cdd:cd24018 235 AFDNEREVLPLT-KYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 339 ESD-SGDRRQILNILSTLG--LRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVmriTVGVDGSVYKL 415
Cdd:cd24018 314 EADtSPDLDAVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLPEPV---TVGIDGSVYEK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1008870 416 HPSFKERFHASVRRL---TPNCEITFIESEEGSGRGAALVS 453
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 ... |
28-454 |
3.80e-141 |
|
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: 411.62 E-value: 3.80e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 28 EDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLG--GTNFRVMLVKVgEGEAGqWSVKTKH 105
Cdd:cd24090 5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTL-TGIEG-HRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 106 QMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLL 185
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 186 RDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNSGE 265
Cdd:cd24090 163 RDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 266 LDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSGDR 345
Cdd:cd24090 243 LGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 346 RQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHA 425
Cdd:cd24090 323 ARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQG 402
|
410 420
....*....|....*....|....*....
gi 1008870 426 SVRRLTPNCEITFIESEEGSGRGAALVSA 454
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) ... |
27-452 |
2.43e-135 |
|
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: 393.95 E-value: 2.43e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 27 EEDLKKVMSRMQKEMDRGLKLEthqEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGegeaGQWSVKTKHQ 106
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLD----GKGIEVTISK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 107 MYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKhKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLLR 186
Cdd:cd24000 74 KYEIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 187 DAIKRRGDfEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNvelVEGDEGRMCVNTEWGAFGNSgel 266
Cdd:cd24000 153 DALKKRGL-PVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 267 DEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGElvrlvllklveenLLfhgeaseqlrtrgafetrfvsqvesdsgdrR 346
Cdd:cd24000 226 SLPRTEYDREVDKASENPGFQPLEKMVSGKYLGE-------------LV------------------------------R 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 347 QILNILstlglrpsvaDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEdvmRITVGVDGSVYKLHPSFKERFHAS 426
Cdd:cd24000 263 LILKDL----------ADEILRKICELVAERSARLAAAAIAALLRKTGDSPEK---KITIAVDGSLFEKYPGYRERLEEY 329
|
410 420
....*....|....*....|....*..
gi 1008870 427 VRRLTPN-CEITFIESEEGSGRGAALV 452
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) ... |
30-456 |
1.92e-115 |
|
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: 346.19 E-value: 1.92e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 30 LKKVMSRMQKEMDRGLKLETHQeaSVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGqwSVKTKHQMYS 109
Cdd:cd24020 6 LRQVADAMVVEMEAGLASEGGS--KLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGR--VDKQEYEEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 110 IPEDAMTGTAEMLFDYISECISDFLDKH----QMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLL 185
Cdd:cd24020 82 IPPELMVGTSEELFDFIAGELAKFVATEgegfHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 186 RDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGD---EGRMCVNTEWGAFgN 262
Cdd:cd24020 162 EEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-R 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 263 SGELDefLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQV-ESD 341
Cdd:cd24020 240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 342 SGDRRQILNILS-TLGL-RPSVADCDIVRRACESVSTRAAHMCSAGLAGVINR-MR-ESRSEDVMRITVGVDGSVYKLHP 417
Cdd:cd24020 318 SPDLETVARILKdALGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKlGRdGGGSSPAQRTVVAVDGGLYEHYP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1008870 418 SFKERFHASVRRL---TPNCEITFIESEEGSGRGAALVSAVA 456
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) ... |
28-456 |
6.36e-112 |
|
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: 336.65 E-value: 6.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 28 EDLKKVMSRMQKEMDRGLkleTHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGegeaGQWSVKTKHQM 107
Cdd:cd24087 2 ERLRKITDHFISELEKGL---SKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLG----GNGKFDITQSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 108 YSIPEDAMTGTAEMLFDYISECISDFLDKH--QMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLL 185
Cdd:cd24087 75 YRLPEELKTGTGEELWDFIADCLKKFVEEHfpGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 186 RDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVE----GDEGRMCVNTEWGAFG 261
Cdd:cd24087 155 QKALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 262 NsGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESD 341
Cdd:cd24087 234 N-EHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 342 SGDRRQILNIL--STLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMresrseDVMRITVGVDGSVYKLHPSF 419
Cdd:cd24087 313 PFENLEDTDDLfqHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKR------GYKTCHVAADGSVYNKYPGF 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1008870 420 KERFHASVRRL----TPNCEITFIESEEGSGRGAALVSAVA 456
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 ... |
27-452 |
1.84e-95 |
|
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: 295.07 E-value: 1.84e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 27 EEDLKKVMSRMQKEMDRGLKletHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgegeAGQWSVKTKHQ 106
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLA---KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL----HGDGTFSLRQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 107 MYSIPEDAMTG-TAEMLFDYISECISDFLDKHQMKH-------KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEG 178
Cdd:cd24088 74 KSKIPDELKTGvTAKDLFDYLAKSVEAFLTKHHGDSfaagkddDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 179 NNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMIS-CYYEDRQCE--VGMIVGTGCNACYMEEMQNV------ELVEGDEG 249
Cdd:cd24088 154 KDVVKLLQDELDRQG-IPVKVVALVNDTVGTLLArSYTSPEISGavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 250 RMCVNTEWGAFGNsgELDEF-LLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLL---FHGEASEQLR 325
Cdd:cd24088 233 HMVINTEWGSFDN--ELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 326 TRGAFETRFVSQVESD--SGDRRQILNILSTLGLR-PSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVM 402
Cdd:cd24088 311 TPYGLDTAVLSAIEIDseAELRATRKVLLDDLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1008870 403 RITVGVDGSVYKLHPSFKERFHASVRRLTPNCE----ITFIESEEGSGRGAALV 452
Cdd:cd24088 391 EINIGVDGSVIEFYPGFESMLREALRLLLIGAEgekrIKIGIAKDGSGVGAALC 444
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
16-215 |
2.30e-91 |
|
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: 275.54 E-value: 2.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 16 VEQILAEFQLQEEDLKKVMSRMQKEMDRGLKLEThqEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGege 95
Cdd:pfam00349 2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 96 aGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKH---KKLPLGFTFSFPVRHEDIDKGILLNWTKGFK 172
Cdd:pfam00349 77 -GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGFD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1008870 173 ASGAEGNNIVGLLRDAIKRRGDfEMDVVAMVNDTVATMISCYY 215
Cdd:pfam00349 156 IPGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
6-456 |
3.57e-90 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 281.95 E-value: 3.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 6 TRRGAQSLTLVEQILAEFQLQEEDLKKVMSRMQKEMDRGLK-------LETHQEASVKMLPTYVRSTPEGSEVGDFLSLD 78
Cdd:PTZ00107 1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEahrrhrnLWIPNECSFKMLDSCVYNLPTGKEKGVYYAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 79 LGGTNFRVMLVKVGEGeaGQwsVKTKHQMYSIPEDAMTG---------TAEMLFDYISECISDFLDKHQMK---HKKLPL 146
Cdd:PTZ00107 81 FGGTNFRAVRVSLRGG--GK--MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 147 GFTFSFPVRHEDIDKGILLNWTKGFKASGA-----EGNNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDR--- 218
Cdd:PTZ00107 157 GFTFSFPCTQLSVNNAILIDWTKGFETGRAtndpvEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKPknt 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 219 -QCEVGMIVGTGCNACYMEEMQnveLVEGDEGRMcVNTEWGAFgnSGELDefLLEYDRMVDESSVNPGQQLYEKIIGGKY 297
Cdd:PTZ00107 236 pPCQVGVIIGTGSNACYFEPEV---SAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 298 MGELVRLVLLklveenLLFHGEASEQLRTRGAFETRFVSQVESDSGDRRQILN--ILSTLGLRPSVADCDIVRRACESVS 375
Cdd:PTZ00107 308 LGEISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFSRqvIKEAWDVDLTDEDLYTIRKICELVR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 376 TRAAHMCSAGLAGVINRMRESRSedvmRITVGVDGSVYKLHPSFKERFHASVRRLT--PNCEITFIESEEGSGRGAALVS 453
Cdd:PTZ00107 382 GRAAQLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSILgpDAGNVVFYLADDGSGKGAAIIA 457
|
...
gi 1008870 454 AVA 456
Cdd:PTZ00107 458 AMV 460
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
221-455 |
3.71e-90 |
|
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: 273.98 E-value: 3.71e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 221 EVGMIVGTGCNACYMEEMQNVELVEGD---EGRMCVNTEWGAFGNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKY 297
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 298 MGELVRLVLLKLVEENLLFHGEaSEQLRTRGAFETRFVSQVESD-SGDRRQILNILS-TLGLR-PSVADCDIVRRACESV 374
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEeLLGIEtVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 375 STRAAHMCSAGLAGVINRMRESRsedvmRITVGVDGSVYKLHPSFKERFHASVRRLT-PNCEITFIESEEGSGRGAALVS 453
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 1008870 454 AV 455
Cdd:pfam03727 235 AV 236
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
22-457 |
3.73e-90 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 281.08 E-value: 3.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 22 EFQLQEEDLKKVMSRMQKEMDRGLKletHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEgeAGQWSV 101
Cdd:COG5026 14 GFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYLGLPTGVKETGPVIALDAGGTNFRVALVRFDG--EGTFEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 102 --KTKHQMYSIPEDAmtgTAEMLFDYISECISDFLDKhqmkhkKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGN 179
Cdd:COG5026 89 enFKSFPLPGTSSEI---TAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 180 NIVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQC----EVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 255
Cdd:COG5026 160 NIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 256 EWGAFgnsgelDEFLL-EYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENlLFHGEASEQLRTRGAFETRF 334
Cdd:COG5026 240 ESGNF------NKLPRtKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 335 VSQ-VESDSGDrrqiLNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVInRMRESRSEDVMRITVGVDGSVY 413
Cdd:COG5026 313 MSRfLADPSDE----KEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGIL-LHLGPGKTPLKPHCIAIDGSTY 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1008870 414 KLHPSFKERFHASVRR-LTPNCE--ITFIESEEGSGRGAALVSAVAC 457
Cdd:COG5026 388 EKMPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
|
|
| PLN02914 |
PLN02914 |
hexokinase |
19-458 |
1.30e-88 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 278.69 E-value: 1.30e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 19 ILAEFQLQEED----LKKVMSRMQKEMDRGLKLETHQEasVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 94
Cdd:PLN02914 40 ILTKLQKDCATplpvLRHVADAMAADMRAGLAVDGGGD--LKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 95 EagQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDK-----HQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTK 169
Cdd:PLN02914 118 D--ERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKeggkfHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 170 GFKASGAEGNNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDE- 248
Cdd:PLN02914 196 GFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKs 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 249 --GRMCVNTEWGAFGNSGELDEFlleyDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRT 326
Cdd:PLN02914 275 ssGRTIINTEWGAFSDGLPLTEF----DREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLST 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 327 RGAFETRFVSQVESD-SGDRRQILNILS-TLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVM-- 402
Cdd:PLN02914 351 PFALRTPHLCAMQQDnSDDLQAVGSILYdVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgk 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1008870 403 RITVGVDGSVYKLHPSFKERFHASVRRL---TPNCEITFIESEEGSGRGAALVSAVACK 458
Cdd:PLN02914 431 RTVVAMDGGLYEKYPQYRRYMQDAVTELlglELSKNIAIEHTKDGSGIGAALLAATNSK 489
|
|
| PLN02405 |
PLN02405 |
hexokinase |
16-454 |
2.78e-74 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 241.66 E-value: 2.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 16 VEQILAEFqlqEED-------LKKVMSRMQKEMDRGLKLETHqeASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVML 88
Cdd:PLN02405 37 AMEILKEF---EEDcatpigkLRQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 89 VKVGEGEAGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFL-----DKHQMKHKKLPLGFTFSFPVRHEDIDKGI 163
Cdd:PLN02405 112 VLLGGKDGR--VVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 164 LLNWTKGFKASGAEGNNIVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVEL 243
Cdd:PLN02405 190 LIKWTKGFSIDDAVGQDVVGELTKAMERVG-LDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 244 VEGD---EGRMCVNTEWGAFgNSGELDefLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEA 320
Cdd:PLN02405 269 WHGLlpkSGEMVINMEWGNF-RSSHLP--LTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 321 SEQLRTRGAFETRFVSQVESD-SGDRR-------QILNILSTlglrpSVADCDIVRRACESVSTRAAHMCSAGLAGVINR 392
Cdd:PLN02405 346 PPKLKIPFILRTPDMSAMHHDtSPDLKvvgsklkDILEIPNT-----SLKMRKVVVELCNIVATRGARLSAAGIYGILKK 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008870 393 M-RES-RSEDVMRITVGVDGSVYKLHPSFKERFHASVRRL-----TPNCEITfiESEEGSGRGAALVSA 454
Cdd:PLN02405 421 LgRDTvKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELlgeevSESIEVE--HSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
30-454 |
6.08e-70 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 230.92 E-value: 6.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 30 LKKVMSRMQKEMDRGLKLETHqeASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGQWSVKTKHQmyS 109
Cdd:PLN02362 55 LRQVVDAMAVEMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERH--P 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 110 IPEDAMTGTAEMLFDYISECISDFLDKHQMKH-----KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGL 184
Cdd:PLN02362 131 IPQHLMNSTSEVLFDFIASSLKQFVEKEENGSefsqvRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAEC 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 185 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFG 261
Cdd:PLN02362 211 LQGALNRRG-LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFW 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 262 NSgELDEflLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFhGEASEQLRTRGAFETRFVSQV-ES 340
Cdd:PLN02362 290 SS-HLPR--TSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhED 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 341 DSGDRRQILNIL-STLGLRP-SVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRE----------SRSEDVM--RITV 406
Cdd:PLN02362 366 DSPELQEVARILkETLGISEvPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGRdgsggitsgrSRSDIQImrRTVV 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1008870 407 GVDGSVYKLHPSFKERFHASVRRLTPN---CEITFIESEEGSGRGAALVSA 454
Cdd:PLN02362 446 AVEGGLYTNYTMFREYLHEALNEILGEdvaQHVILKATEDGSGIGSALLAA 496
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
47-454 |
4.24e-42 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 155.80 E-value: 4.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 47 LETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAgqwSVKTKH-QMYSIPEDAMTGTAEMLFDY 125
Cdd:PLN02596 71 LTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNE---PISDLYrEEISIPSNVLNGTSQELFDY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 126 ISECISDFLDKHQMKHKKLP-----LGFTFSFPVRHEDIDKGILLNWtKGFKASGAEGNNIVGLLRDAIKRRGdFEMDVV 200
Cdd:PLN02596 148 IALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 201 AMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFgNSGELDefLLEYDRMV 277
Cdd:PLN02596 226 ALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF-NSCHLP--ITEFDASL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 278 DESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSGDRRQILN--ILSTL 355
Cdd:PLN02596 303 DAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNekLKEIF 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 356 GLRPSV-ADCDIVRRACESVSTRAAHMCSAGLAGVINRMreSRSEDVMRItVGVDGSVYKLHPSFKERFHASVRRLTPN- 433
Cdd:PLN02596 383 GITDSTpMAREVVAEVCDIVAERGARLAGAGIVGIIKKL--GRIENKKSV-VTVEGGLYEHYRVFRNYLHSSVWEMLGSe 459
|
410 420
....*....|....*....|...
gi 1008870 434 -CEITFIE-SEEGSGRGAALVSA 454
Cdd:PLN02596 460 lSDNVVIEhSHGGSGAGALFLAA 482
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
74-266 |
5.21e-05 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 44.97 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 74 FLSLDLGGTNFRVMLVKvgegEAGQWSVKTKHQmysipedamtgTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFP 153
Cdd:PRK09698 6 VLGIDMGGTHIRFCLVD----AEGEILHCEKKR-----------TAEVIAPDLVSGLGEMIDEYLRRFNARCHGIVMGFP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 154 --VrheDIDKGILLNwTKGFKASGAEGNNIVGLLRDAIKRRGDFEMDV-VAMVNDTVAtmiscYYEDRQCEVGMIVGTGC 230
Cdd:PRK09698 71 alV---SKDRRTVIS-TPNLPLTALDLYDLADKLENTLNCPVFFSRDVnLQLLWDVKE-----NNLTQQLVLGAYLGTGM 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 1008870 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 |
5.82e-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: 41.81 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 74 FLSLDLGGTNFRVMLVKVGEGEAGQWSVKTKHQmysipedamtGTAEMLFDYISECISDFLDKHQMKHKKL-PLGFTFSF 152
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIPTPAG----------AGPEAVLEAIAELIEELLAEAGISRGRIlGIGIGVPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008870 153 PVrheDIDKGILLNwtkgfkasgaeGNNIVGL----LRDAIKRRGDFEmdvVAMVNDTVATMIS--CYYEDRQCE--VGM 224
Cdd:COG1940 77 PV---DPETGVVLN-----------APNLPGWrgvpLAELLEERLGLP---VFVENDANAAALAeaWFGAGRGADnvVYL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1008870 225 IVGTGCNACYmeeMQNVELVEgdegrmcvntewGAFGNSGEL 266
Cdd:COG1940 140 TLGTGIGGGI---VINGKLLR------------GANGNAGEI 166
|
|
| |
