|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
25-478 |
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: 947.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 25 KIDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHE 104
Cdd:cd24124 20 KIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 105 KNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGV 184
Cdd:cd24124 100 KNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 185 EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTE 264
Cdd:cd24124 180 EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 265 WGAFGDDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVS 344
Cdd:cd24124 260 WGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 345 AIEKDKEGIQNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMH 424
Cdd:cd24124 340 AIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1997589435 425 PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 478
Cdd:cd24124 420 PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
482-915 |
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: 904.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 561
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 721
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 722 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 801
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 802 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 881
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400
|
410 420 430
....*....|....*....|....*....|....
gi 1997589435 882 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVRL 915
Cdd:cd24127 401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
482-914 |
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: 869.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 561
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 721
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 722 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 801
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 802 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 881
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 1997589435 882 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVR 914
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
34-462 |
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: 822.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 113
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 273
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 274 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 353
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 354 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 433
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1997589435 434 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 462
Cdd:cd24089 401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
482-916 |
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: 802.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 561
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 721
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 722 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 801
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 802 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 881
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....*
gi 1997589435 882 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVRLR 916
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
482-915 |
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: 773.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKkRTVEMHN 561
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 721
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 722 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 801
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 802 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 881
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399
|
410 420 430
....*....|....*....|....*....|....
gi 1997589435 882 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVRL 915
Cdd:cd24130 400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
34-462 |
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: 772.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 113
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 273
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 274 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 353
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 354 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 433
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1997589435 434 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 462
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
482-910 |
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: 726.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGkkRTVEMHN 561
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGG--SQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVE---MVEGNQGQMCINMEWGAFGD 718
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEkwdGDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 719 NGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESD- 797
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 798 RLALLQVRAILQQLGLNS-TCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREnrgldhLNVTVGVDGTLYKLHPHFS 876
Cdd:cd24019 319 EGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR------KEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1997589435 877 RIMHQTVKELSPK-CTVSFLLSEDGSGKGAALITA 910
Cdd:cd24019 393 KRMHETLKELVPPgCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
34-462 |
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: 716.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 113
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 273
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 274 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 353
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 354 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 433
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 1997589435 434 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 462
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
34-462 |
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: 690.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHekNQNVSMES 113
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNG--GSQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDL---VEGDEGRMCINTEWGAFGD 270
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 271 DGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDK 350
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 351 EG-IQNAKEILTRLGVEP-SDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRdnkgtpRLRTTVGVDGSLYKMHPQYS 428
Cdd:cd24019 319 EGdFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1997589435 429 RRFHKTLRRLVP-DSDVRFLLSESGSGKGAAMVTA 462
Cdd:cd24019 393 KRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
482-914 |
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: 682.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIrsgKKRTVEMHN 561
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV---GTAGVQITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 721
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 722 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 801
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 802 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 881
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397
|
410 420 430
....*....|....*....|....*....|...
gi 1997589435 882 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVR 914
Cdd:cd24129 398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
482-910 |
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: 652.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 561
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 721
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 722 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 801
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 802 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 881
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1997589435 882 TVKELSPKCTVSFLLSEDGSGKGAALITA 910
Cdd:cd24089 401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
482-910 |
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: 605.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 561
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 721
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 722 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 801
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 802 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 881
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1997589435 882 TVKELSPKCTVSFLLSEDGSGKGAALITA 910
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
482-910 |
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: 604.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 561
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 721
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 722 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 801
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 802 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 881
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 1997589435 882 TVKELSPKCTVSFLLSEDGSGKGAALITA 910
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
463-915 |
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: 588.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 463 VAYRLAE----QHRQIEETLAHFRLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLG 538
Cdd:cd24124 6 LAYYFTElkddQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 539 GTNFRVLLVKIRSGKKRTVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCG 618
Cdd:cd24124 86 GSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 619 ILISWTKGFKATDCEGHDVASLLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVE 698
Cdd:cd24124 166 ILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHID 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 699 MVEGNQGQMCINMEWGAFGDNGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISE 778
Cdd:cd24124 246 LVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 779 PLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHL 858
Cdd:cd24124 326 ELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1997589435 859 NVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCTVSFLLSEDGSGKGAALITAVGVRL 915
Cdd:cd24124 406 RTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
34-466 |
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: 572.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 113
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 273
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 274 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 353
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 354 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 433
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 1997589435 434 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 466
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
473-914 |
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: 561.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 473 QIEETLAHFRLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSG 552
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 553 KKR--TVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKAT 630
Cdd:cd24092 81 EEGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 631 DCEGHDVASLLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCIN 710
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 711 MEWGAFGDNGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKF 790
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 791 LSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYK 870
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1997589435 871 LHPHFSRIMHQTVKELSPKCTVSFLLSEDGSGKGAALITAVGVR 914
Cdd:cd24092 401 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
34-467 |
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: 551.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 113
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 273
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 274 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 353
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 354 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 433
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....
gi 1997589435 434 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 467
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
34-467 |
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: 532.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 113
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 273
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 274 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 353
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 354 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 433
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400
|
410 420 430
....*....|....*....|....*....|....
gi 1997589435 434 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 467
Cdd:cd24127 401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
34-467 |
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: 531.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNqNVSMES 113
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRR-SVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 273
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 274 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 353
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 354 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 433
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399
|
410 420 430
....*....|....*....|....*....|....
gi 1997589435 434 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 467
Cdd:cd24130 400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
34-466 |
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: 529.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 34 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEknqNVSMES 113
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTA---GVQITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 114 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 193
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 194 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 273
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 274 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 353
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 354 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 433
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397
|
410 420 430
....*....|....*....|....*....|...
gi 1997589435 434 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 466
Cdd:cd24129 398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
25-466 |
2.55e-175 |
|
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: 515.59 E-value: 2.55e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 25 KIDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV--N 102
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgeG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 103 HEKNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKAS 182
Cdd:cd24092 81 EEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 183 GVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCIN 262
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 263 TEWGAFGDDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSD 342
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 343 VSAIEKDKEGIQNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYK 422
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1997589435 423 MHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 466
Cdd:cd24092 401 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
485-908 |
8.87e-159 |
|
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: 472.50 E-value: 8.87e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 485 KQTLMEVKKRLRTEMEMGLRKETNSkatVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKiY 564
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGGS---LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 565 SIPLEIMQGTGDELFDHIVSCISDFLDYMGIK---GPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 641
Cdd:cd24018 77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 642 RDAVKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQG------QMCINMEWGA 715
Cdd:cd24018 157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPSGsvtksdEMIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 716 FGDNGCLDDiRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIE 795
Cdd:cd24018 236 FDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 796 SDRLALLQ-VRAILQQLG--LNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREnrgLDHLNVTVGVDGTLYKLH 872
Cdd:cd24018 315 ADTSPDLDaVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS---LLPEPVTVGIDGSVYEKY 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 1997589435 873 PHFSRIMHQTVKELSPKCT---VSFLLSEDGSGKGAALI 908
Cdd:cd24018 392 PGFKDRLSEALRELFGPEVkanISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
482-910 |
1.72e-157 |
|
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: 469.02 E-value: 1.72e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 482 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLG--GTNFRVLLVKIRSGKKRTVEM 559
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 560 HNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVAS 639
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 640 LLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDN 719
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 720 GCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRL 799
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 800 ALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIM 879
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400
|
410 420 430
....*....|....*....|....*....|.
gi 1997589435 880 HQTVKELSPKCTVSFLLSEDGSGKGAALITA 910
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
38-462 |
1.37e-150 |
|
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: 451.30 E-value: 1.37e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 38 EILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILRVQVNHEKNQNVSMESEI 115
Cdd:cd24090 5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 116 YDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNK 195
Cdd:cd24090 85 FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 196 AIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLE 275
Cdd:cd24090 165 AIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 276 DIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGIQN 355
Cdd:cd24090 245 PVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 356 AKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHKTL 435
Cdd:cd24090 325 VRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTV 404
|
410 420
....*....|....*....|....*..
gi 1997589435 436 RRLVPDSDVRFLLSESGSGKGAAMVTA 462
Cdd:cd24090 405 MLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
42-460 |
1.03e-142 |
|
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: 430.90 E-value: 1.03e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 42 DILTRFKKEMKNGLSRDynpTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEiYDTPEN 121
Cdd:cd24018 6 EIVKHFLSEMEKGLEGD---GGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-YKIPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 122 IVHGSGTQLFDHVADCLGDFME---KKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIK 198
Cdd:cd24018 82 AKTGTGEELFDFIAECIAEFLEehnLDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNALD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 199 KRGdYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHI---DLVEG---DEGRMCINTEWGAFgdDG 272
Cdd:cd24018 162 RRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGsvtKSDEMIINTEWGAF--DN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 273 SLEDI-RTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKE 351
Cdd:cd24018 239 EREVLpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 352 G-IQNAKEILTRLGV--EPSDVDCVSVQHICTIVSFRSANLVAATLGAILnrLRDNKGTPRlRTTVGVDGSLYKMHPQYS 428
Cdd:cd24018 319 PdLDAVRDILKELLAidNTTLEDRKLIKRICELVSTRAARLSAAAIAAIL--LKRGSLLPE-PVTVGIDGSVYEKYPGFK 395
|
410 420 430
....*....|....*....|....*....|....*
gi 1997589435 429 RRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMV 460
Cdd:cd24018 396 DRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
487-909 |
3.50e-137 |
|
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: 413.59 E-value: 3.50e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 487 TLMEVKKRLRTEMEMGLRKEtnsKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSgkKRTVEMHNKIYSI 566
Cdd:cd24000 3 DLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDG--KGIEVTISKKYEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 567 PLEIMQGTGDELFDHIVSCISDFLDYMGIKGPrMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLRDAVK 646
Cdd:cd24000 78 PDEIKTASAEEFFDFIADCIAEFLKENGLKKP-LPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 647 RREeFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNvemVEGNQGQMCINMEWGAFGDNgclDDIR 726
Cdd:cd24000 157 KRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN---SLPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 727 TDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKgflfrgqiseplktrgifetkflsqiesdrlallqvra 806
Cdd:cd24000 230 TEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE-------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 807 ilqqlglnstcddsiLVKTVCGVVSKRAAQLCGAGMAAVVEKIRENrglDHLNVTVGVDGTLYKLHPHFSRIMHQTVKEL 886
Cdd:cd24000 272 ---------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLKEL 333
|
410 420
....*....|....*....|....
gi 1997589435 887 SPK-CTVSFLLSEDGSGKGAALIT 909
Cdd:cd24000 334 LGRgIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
37-461 |
3.03e-130 |
|
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: 395.88 E-value: 3.03e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 37 DEILIDILTRFKKEMKNGLSRDYnptASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVSMESEIY 116
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEP---SSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLD--GKGIEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 117 DTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKkLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKA 196
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLKKP-LPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 197 IKKRGdYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDlveGDEGRMCINTEWGAFGDDgslED 276
Cdd:cd24000 155 LKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL---LGDGGMIINTEWGNFGKN---SL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 277 IRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEgllfegritpelltrgkfntsdvsaiekdkegiqna 356
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 357 keiltrlgvepsdvdcvSVQHICTIVSFRSANLVAATLGAILNRLRDNkgtPRLRTTVGVDGSLYKMHPQYSRRFHKTLR 436
Cdd:cd24000 272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420
....*....|....*....|....*.
gi 1997589435 437 RLVP-DSDVRFLLSESGSGKGAAMVT 461
Cdd:cd24000 332 ELLGrGIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
495-910 |
8.87e-122 |
|
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: 377.00 E-value: 8.87e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 495 LRTEMEMGLRKETNSKatVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYSIPLEIMQGT 574
Cdd:cd24020 13 MVVEMEAGLASEGGSK--LKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVPIPPELMVGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 575 GDELFDHIVSCISDFLDYMG----IKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLRDAVKRReE 650
Cdd:cd24020 91 SEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQ-G 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 651 FDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQ---GQMCINMEWGAFgDNGCLDdiRT 727
Cdd:cd24020 170 LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLprsGEMVINTEWGNF-RSSHLP--RT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 728 DFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLA-LLQVRA 806
Cdd:cd24020 247 EEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSPdLETVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 807 ILQQ-LGL-NSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLN--VTVGVDGTLYKLHPHFSRIMHQT 882
Cdd:cd24020 327 ILKDaLGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAqrTVVAVDGGLYEHYPKFREYMQQA 406
|
410 420 430
....*....|....*....|....*....|.
gi 1997589435 883 VKELSPKCT---VSFLLSEDGSGKGAALITA 910
Cdd:cd24020 407 LVELLGDEAadsVELELSNDGSGIGAALLAA 437
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
47-464 |
1.63e-121 |
|
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: 376.23 E-value: 1.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 47 FKKEMKNGLSRDynPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEIYDTPENIVHGS 126
Cdd:cd24020 13 MVVEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVPIPPELMVGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 127 GTQLFDHVADCLGDFM----EKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGd 202
Cdd:cd24020 91 SEELFDFIAGELAKFVategEGFHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 203 YDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFgDDGSLEdiRT 279
Cdd:cd24020 170 LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-RSSHLP--RT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 280 EFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAI-EKDKEGIQNAKE 358
Cdd:cd24020 247 EEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDDSPDLETVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 359 ILTR-LGVEPSDV-DCVSVQHICTIVSFRSANLVAATLGAILNRL-RDNKG-TPRLRTTVGVDGSLYKMHPQYSRRFHKT 434
Cdd:cd24020 327 ILKDaLGIDDTSLeARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGsSPAQRTVVAVDGGLYEHYPKFREYMQQA 406
|
410 420 430
....*....|....*....|....*....|...
gi 1997589435 435 LRRLVPD---SDVRFLLSESGSGKGAAMVTAVA 464
Cdd:cd24020 407 LVELLGDeaaDSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
485-910 |
1.33e-115 |
|
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: 360.15 E-value: 1.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 485 KQTLMEVKKRLRTEMEMGLRKEtnsKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIrsGKKRTVEMHNKIY 564
Cdd:cd24087 1 TERLRKITDHFISELEKGLSKK---GGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKL--GGNGKFDITQSKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 565 SIPLEIMQGTGDELFDHIVSCISDFLD--YMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLR 642
Cdd:cd24087 76 RLPEELKTGTGEELWDFIADCLKKFVEehFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 643 DAVKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVE----GNQGQMCINMEWGAFgD 718
Cdd:cd24087 156 KALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 719 NGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDR 798
Cdd:cd24087 234 NEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 799 LA-LLQVRAILQQ-LGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKirenRGLDHLNvtVGVDGTLYKLHPHFS 876
Cdd:cd24087 314 FEnLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYKTCH--VAADGSVYNKYPGFK 387
|
410 420 430
....*....|....*....|....*....|....*...
gi 1997589435 877 RIMHQTVKEL----SPKCTVSFLLSEDGSGKGAALITA 910
Cdd:cd24087 388 ERAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAA 425
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
485-908 |
1.24e-111 |
|
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: 350.54 E-value: 1.24e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 485 KQTLMEVKKRLRTEMEMGLrkeTNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIrSGKkRTVEMHNKIY 564
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL-HGD-GTFSLRQEKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 565 SIPLEIMQG-TGDELFDHIVSCISDFL-DY------MGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHD 636
Cdd:cd24088 76 KIPDELKTGvTAKDLFDYLAKSVEAFLtKHhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 637 VASLLRDAVKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCE---IGLIVGTGTNACYMEEMKNV------EMVEGNQGQM 707
Cdd:cd24088 156 VVKLLQDELDRQ-GIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 708 CINMEWGAFgdngclDDIR-----TDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFL---FRGQISEP 779
Cdd:cd24088 235 VINTEWGSF------DNELkvlptTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 780 LKTRGIFETKFLSQIESDRLALLQV--RAILQQLGLNS-TCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLD 856
Cdd:cd24088 309 LNTPYGLDTAVLSAIEIDSEAELRAtrKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1997589435 857 HLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCT----VSFLLSEDGSGKGAALI 908
Cdd:cd24088 389 DGEINIGVDGSVIEFYPGFESMLREALRLLLIGAEgekrIKIGIAKDGSGVGAALC 444
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
677-911 |
2.60e-107 |
|
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: 331.38 E-value: 2.60e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 677 EIGLIVGTGTNACYMEEMKNVEMVEG---NQGQMCINMEWGAFGDNGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMY 753
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGklpKSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 754 LGEIVRNILIDFTKKGFLFRGQiSEPLKTRGIFETKFLSQIESDR-LALLQVRAILQQ-LGLNS-TCDDSILVKTVCGVV 830
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIETvTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 831 SKRAAQLCGAGMAAVVEKIRENRGldhlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPKCTVSFLLSEDGSGKGAALIT 909
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDKK-----VTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 1997589435 910 AV 911
Cdd:pfam03727 235 AV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
466-911 |
5.93e-107 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 338.96 E-value: 5.93e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 466 RLAEQHRQIEETLAHFRLSKQTLMEVKKRLRTEMEMGL---RKETN----SKATVKMLPSFVRSIPDGTEHGDFLALDLG 538
Cdd:PTZ00107 3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeahRRHRNlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 539 GTNFRVLLVKIRSGKKrtVEMHNKIYSIPLEIMQG---------TGDELFDHIVSCISDFLDYMGIK---GPRMPLGFTF 606
Cdd:PTZ00107 83 GTNFRAVRVSLRGGGK--MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 607 SFPCHQTNLDCGILISWTKGF---KATD--CEGHDVASLLRDAVKRrEEFDLDVVAVVNDTVGTMMTCAYEE----PTCE 677
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFetgRATNdpVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 678 IGLIVGTGTNACYME-EMKNVemveGNQGQMcINMEWGAFgdngCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGE 756
Cdd:PTZ00107 240 VGVIIGTGSNACYFEpEVSAY----GYAGTP-INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 757 IVRNILIDftkkgfLFRGQISEPLKTRGIFETKFLSQIESDRLALLQ-VRAILQQL-GLNSTCDDSILVKTVCGVVSKRA 834
Cdd:PTZ00107 311 ISRRLIVH------LLQLKAPPKMWQSGSFESEDASMILNDQSPDLQfSRQVIKEAwDVDLTDEDLYTIRKICELVRGRA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1997589435 835 AQLCGAGMAAVVEKIRENRGLdhlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPK-CTVSFLLSEDGSGKGAALITAV 911
Cdd:PTZ00107 385 AQLAAAFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAM 459
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
23-464 |
1.09e-105 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 335.49 E-value: 1.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 23 EDKIDKYLYAMRLSDEILIDILTRFKKEMKNGL-SRDYNPTA------SVKMLPTFVRSIPDGSEKGDFIALDLGGSSFR 95
Cdd:PTZ00107 8 RVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 96 ILRVQVNH----EKNQN-VSMESEIYDTPENIV--HGSGTQLFDHVADCLGDFME---KKKIKDKKLPVGFTFSFPCRQS 165
Cdd:PTZ00107 88 AVRVSLRGggkmERTQSkFSLPKSALLGEKGLLdkKATATDLFDHIAKSIKKMMEengDPEDLNKPVPVGFTFSFPCTQL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 166 KIDEAVLITWTKRFKAS-----GVEGADVVKLLNKAIKkRGDYDANIVAVVNDTVGTMMTCGYDDQ----QCEVGLIIGT 236
Cdd:PTZ00107 168 SVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFK-RNNVPANVVAVLNDTVGTLISCAYQKPkntpPCQVGVIIGT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 237 GTNACYMEelrHIDLVEGDEGRMcINTEWGAFgdDGSLEdiRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVK 316
Cdd:PTZ00107 247 GSNACYFE---PEVSAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 317 MAKEGLLfegritPELLTRGKFNTSDVSAIEKDK-EGIQNAKEILTRL-GVEPSDVDCVSVQHICTIVSFRSANLVAATL 394
Cdd:PTZ00107 319 LLQLKAP------PKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997589435 395 GAILNRLRdnkgTPRLRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPD--SDVRFLLSESGSGKGAAMVTAVA 464
Cdd:PTZ00107 393 AAPAKKTR----TVQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPdaGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
229-463 |
8.47e-101 |
|
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: 314.04 E-value: 8.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 229 EVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGDDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMY 305
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 306 MGELVRLILVKMAKEGLLFEGRiTPELLTRGKFNTSDVSAIEKDK-EGIQNAKEILTR-LGVE-PSDVDCVSVQHICTIV 382
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 383 SFRSANLVAATLGAILNRLRDNKgtprlRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPDSD-VRFLLSESGSGKGAAMVT 461
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLGPGDkVVLVLAEDGSGVGAALIA 234
|
..
gi 1997589435 462 AV 463
Cdd:pfam03727 235 AV 236
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
38-464 |
1.01e-99 |
|
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: 318.55 E-value: 1.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 38 EILIDILTRFKKEMKNGLSRdynPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESeiYD 117
Cdd:cd24087 2 ERLRKITDHFISELEKGLSK---KGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSK--YR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 118 TPENIVHGSGTQLFDHVADCLGDFMEK--KKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNK 195
Cdd:cd24087 77 LPEELKTGTGEELWDFIADCLKKFVEEhfPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 196 AIKKRGdYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYME------ELRHIDLVEGDEgrMCINTEWGAFg 269
Cdd:cd24087 157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEvvsnipKLEHDDIPPDSP--MAINCEYGAF- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 270 DDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKD 349
Cdd:cd24087 233 DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 350 K-EGIQNAKEILTR-LGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGtprlrtTVGVDGSLYKMHPQY 427
Cdd:cd24087 313 PfENLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTC------HVAADGSVYNKYPGF 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1997589435 428 SRRFHKTLRRL----VPDSDVRFLLSESGSGKGAAMVTAVA 464
Cdd:cd24087 387 KERAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
31-464 |
3.01e-98 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 314.97 E-value: 3.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 31 YAMRLSDEILIDILTRFKKEMKNGLSRDynpTASVKMLPTFVrSIPDGS-EKGDFIALDLGGSSFRILRVQVNheKNQNV 109
Cdd:COG5026 13 HGFDLSSIDLEEIAAKFQEEMEKGLEGK---KSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFD--GEGTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 110 SMESEIY----DTPENIvhgSGTQLFDHVADCLGDFMEKKkikdkkLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVE 185
Cdd:COG5026 87 EIENFKSfplpGTSSEI---TAEEFFDFIADYIEPLLDES------YKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 186 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQC----EVGLIIGTGTNACYMEELRHIDLVEGDEGRMCI 261
Cdd:COG5026 158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 262 NTEWGAFgdDGSLediRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGlLFEGRITPELLTRGKFNTS 341
Cdd:COG5026 238 NMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 342 DVSAIEKDKEGiqnAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLrDNKGTPRLRTTVGVDGSLY 421
Cdd:COG5026 312 DMSRFLADPSD---EKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHL-GPGKTPLKPHCIAIDGSTY 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1997589435 422 -KMhPQYSRRFHKTLRRLVPDSD---VRFLLSESGSGKGAAMVTAVA 464
Cdd:COG5026 388 eKM-PGLAEKIEYALQEYLLGEKgryVEFVLVENASLLGAAIAAALN 433
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
37-460 |
7.19e-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: 311.64 E-value: 7.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 37 DEILIDILTRFKKEMKNGLSrdyNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVSMESEIY 116
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLA---KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELH--GDGTFSLRQEKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 117 DTPENIVHG-SGTQLFDHVADCLGDFME-------KKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGAD 188
Cdd:cd24088 76 KIPDELKTGvTAKDLFDYLAKSVEAFLTkhhgdsfAAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 189 VVKLLNKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQQCE---VGLIIGTGTNACYMEELRHI---DLVEGDE---GRM 259
Cdd:cd24088 156 VVKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklDDSSRVGkgkTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 260 CINTEWGAFGDDGSLEDIrTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLL---FEGRITPELLTRG 336
Cdd:cd24088 235 VINTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNTPY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 337 KFNTSDVSAIEKDKE-GIQNAKEILTR-LGVE-PSDVDCVSVQHICTIVSFRSANLVAATLGAIL---NRLRDNKGTPrl 410
Cdd:cd24088 314 GLDTAVLSAIEIDSEaELRATRKVLLDdLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAILiktGALNKSYDGE-- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1997589435 411 rTTVGVDGSLYKMHPQYSRRFHKTLRRLVP----DSDVRFLLSESGSGKGAAMV 460
Cdd:cd24088 392 -INIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
473-671 |
6.78e-94 |
|
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: 294.41 E-value: 6.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 473 QIEETLAHFRLSKQTLMEVKKRLRTEMEMGLRKETNSkaTVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIrsG 552
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSS--SLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVEL--G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 553 KKRTVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIK---GPRMPLGFTFSFPCHQTNLDCGILISWTKGFKA 629
Cdd:pfam00349 77 GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1997589435 630 TDCEGHDVASLLRDAVKRREEfDLDVVAVVNDTVGTMMTCAY 671
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
480-907 |
2.82e-93 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 301.49 E-value: 2.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 480 HFRLSKQTLMEVKKRLRTEMEMGLRKEtnsKATVKMLPSFVrSIPDG-TEHGDFLALDLGGTNFRVLLVKIrsGKKRTVE 558
Cdd:COG5026 14 GFDLSSIDLEEIAAKFQEEMEKGLEGK---KSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF--DGEGTFE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 559 MHNKIySIPleiMQGTG-----DELFDHIVSCISDFLDYmgikgpRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCE 633
Cdd:COG5026 88 IENFK-SFP---LPGTSseitaEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 634 GHDVASLLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTC----EIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCI 709
Cdd:COG5026 158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 710 NMEWGAFgdNGCLddiRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGfLFRGQISEPLKTRGIFETK 789
Cdd:COG5026 238 NMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 790 FLSQI---ESDRLallqvrAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREnrGLDHLN-VTVGVD 865
Cdd:COG5026 312 DMSRFladPSDEK------EILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGP--GKTPLKpHCIAID 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1997589435 866 GTLYKLHPHF-SRIMHQTVKELSPKCT--VSFLLSEDGSGKGAAL 907
Cdd:COG5026 384 GSTYEKMPGLaEKIEYALQEYLLGEKGryVEFVLVENASLLGAAI 428
|
|
| PLN02914 |
PLN02914 |
hexokinase |
32-462 |
4.17e-93 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 302.96 E-value: 4.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 32 AMRLSDEILIDILTRFKKE------------------MKNGLSRDynPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSS 93
Cdd:PLN02914 29 AVRSNAVSVAPILTKLQKDcatplpvlrhvadamaadMRAGLAVD--GGGDLKMILSYVDSLPSGNEKGLFYALDLGGTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 94 FRILRVQVNHEKNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFMEkKKIKDKKLP------VGFTFSFPCRQSKI 167
Cdd:PLN02914 107 FRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVA-KEGGKFHLPegrkreIGFTFSFPVKQTSI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 168 DEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELR 247
Cdd:PLN02914 186 DSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 248 HIDLVEGDE---GRMCINTEWGAFGDDGSLedirTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLF 324
Cdd:PLN02914 265 AIPKLQGQKsssGRTIINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 325 eGRITPE-LLTRGKFNTSDVSAIEKD-KEGIQNAKEILTR-LGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRL 401
Cdd:PLN02914 341 -GHFVPEkLSTPFALRTPHLCAMQQDnSDDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKM 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997589435 402 -RDNKGT-PRLRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTA 462
Cdd:PLN02914 420 eEDSKGMiFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLelsKNIAIEHTKDGSGIGAALLAA 485
|
|
| PLN02914 |
PLN02914 |
hexokinase |
478-910 |
2.37e-92 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 301.03 E-value: 2.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 478 LAHFRLSKQTLMEVKKRLRTEMEMGLRK--ETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKR 555
Cdd:PLN02914 41 LTKLQKDCATPLPVLRHVADAMAADMRAglAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 556 TVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIK-----GPRMPLGFTFSFPCHQTNLDCGILISWTKGFKAT 630
Cdd:PLN02914 121 VIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 631 DCEGHDVASLLRDAVKrREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQ---GQM 707
Cdd:PLN02914 201 GTAGKDVVACLNEAME-RQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 708 CINMEWGAFGDNGCLddirTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFE 787
Cdd:PLN02914 280 IINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 788 TKFLSQIESDRLALLQ-VRAILQQ-LGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREN-RGLDHLNVT-VG 863
Cdd:PLN02914 356 TPHLCAMQQDNSDDLQaVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDsKGMIFGKRTvVA 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1997589435 864 VDGTLYKLHPHFSRIMHQTVKE-LSPKCTVSFLL--SEDGSGKGAALITA 910
Cdd:PLN02914 436 MDGGLYEKYPQYRRYMQDAVTElLGLELSKNIAIehTKDGSGIGAALLAA 485
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
25-223 |
5.45e-80 |
|
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: 257.43 E-value: 5.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 25 KIDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDynPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNhe 104
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKE--GSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 105 KNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFME---KKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKA 181
Cdd:pfam00349 77 GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKehgLEDFEEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1997589435 182 SGVEGADVVKLLNKAIKKRGDyDANIVAVVNDTVGTMMTCGY 223
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| PLN02405 |
PLN02405 |
hexokinase |
488-910 |
2.52e-79 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 266.31 E-value: 2.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 488 LMEVKKRLRTEMEMGLRKETNSKatVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYSIP 567
Cdd:PLN02405 55 LRQVADAMTVEMHAGLASEGGSK--LKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 568 LEIMQGTGDELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLR 642
Cdd:PLN02405 133 PHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 643 DAVKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEG---NQGQMCINMEWGAFGDN 719
Cdd:PLN02405 213 KAMERV-GLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFRSS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 720 GClddIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRL 799
Cdd:PLN02405 292 HL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 800 ALLQV-----RAILQQlgLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREN--RGLDHLNVTVGVDGTLYKLH 872
Cdd:PLN02405 369 PDLKVvgsklKDILEI--PNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHY 446
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1997589435 873 PHFSRIMHQTVKEL---SPKCTVSFLLSEDGSGKGAALITA 910
Cdd:PLN02405 447 TEFSKCMESTLKELlgeEVSESIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
488-910 |
1.70e-77 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 261.74 E-value: 1.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 488 LMEVKKRLRTEMEMGLRKETNSKatVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLlvKIRSGKKRT------VEMHn 561
Cdd:PLN02362 55 LRQVVDAMAVEMHAGLASEGGSK--LKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVL--RVQLGGQRSsilsqdVERH- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 562 kiySIPLEIMQGTGDELFDHIVSCISDFLDYMG-----IKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHD 636
Cdd:PLN02362 130 ---PIPQHLMNSTSEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 637 VASLLRDAVKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEG---NQGQMCINMEW 713
Cdd:PLN02362 207 VAECLQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEW 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 714 GAFGDNGClddIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFrGQISEPLKTRGIFETKFLSQ 793
Cdd:PLN02362 286 GNFWSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 794 I-ESDRLALLQVRAILQQ-LGLNST-CDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKI-RE---------NRGLDHL-- 858
Cdd:PLN02362 362 MhEDDSPELQEVARILKEtLGISEVpLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgRDgsggitsgrSRSDIQImr 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1997589435 859 NVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCTVSFLL---SEDGSGKGAALITA 910
Cdd:PLN02362 442 RTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVIlkaTEDGSGIGSALLAA 496
|
|
| PLN02405 |
PLN02405 |
hexokinase |
50-462 |
2.64e-76 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 258.22 E-value: 2.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 50 EMKNGLSRDYNptASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEIYDTPENIVHGSGTQ 129
Cdd:PLN02405 65 EMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 130 LFDHVADCLGDFMEKKKIKDKKLP-----VGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGdYD 204
Cdd:PLN02405 143 LFDFIAAALAKFVATEGEDFHLPPgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-LD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 205 ANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGddgSLEDIRTEF 281
Cdd:PLN02405 222 MRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR---SSHLPLTEY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 282 DRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDkegiqnAKEILT 361
Cdd:PLN02405 299 DHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHD------TSPDLK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 362 RLGVEPSDVDCVS---------VQHICTIVSFRSANLVAATLGAILNRL-RDN-KGTPRLRTTVGVDGSLYKMHPQYSRR 430
Cdd:PLN02405 373 VVGSKLKDILEIPntslkmrkvVVELCNIVATRGARLSAAGIYGILKKLgRDTvKDGEKQKSVIAMDGGLFEHYTEFSKC 452
|
410 420 430
....*....|....*....|....*....|....*
gi 1997589435 431 FHKTLRRLVPDS---DVRFLLSESGSGKGAAMVTA 462
Cdd:PLN02405 453 MESTLKELLGEEvseSIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
50-462 |
4.72e-73 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 249.80 E-value: 4.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 50 EMKNGLSRDYNptASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEIYDTPENIVHGSGTQ 129
Cdd:PLN02362 65 EMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 130 LFDHVADCLGDFMEKKKIKDKKLPV-----GFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGdYD 204
Cdd:PLN02362 143 LFDFIASSLKQFVEKEENGSEFSQVrrrelGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 205 ANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFgddGSLEDIRTEF 281
Cdd:PLN02362 222 MRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---WSSHLPRTSY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 282 DRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFeGRITPELLTRGKFNTSDVSAI-EKDKEGIQNAKEIL 360
Cdd:PLN02362 299 DIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARIL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 361 T-RLGVE--PSDVDCVSVQhICTIVSFRSANLVAATLGAILNRL-RDNKGT-----------PRLRTTVGVDGSLYKMHP 425
Cdd:PLN02362 378 KeTLGISevPLKVRKLVVK-ICDVVTRRAARLAAAGIVGILKKIgRDGSGGitsgrsrsdiqIMRRTVVAVEGGLYTNYT 456
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1997589435 426 QYSRRFHKTLRRLVPDSDVRFLL---SESGSGKGAAMVTA 462
Cdd:PLN02362 457 MFREYLHEALNEILGEDVAQHVIlkaTEDGSGIGSALLAA 496
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
488-912 |
1.22e-50 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 186.24 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 488 LMEVKKRLRTEMEMGLRKETNSkaTVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYSIP 567
Cdd:PLN02596 56 LWEVADALVSDMTASLTAEETT--TLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 568 LEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMP-----LGFTFSFPCHQTNLDCGILISWtKGFKATDCEGHDVASLLR 642
Cdd:PLN02596 134 SNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDIN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 643 DAVKRrEEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEG---NQGQMCINMEWGAFgdN 719
Cdd:PLN02596 213 RALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF--N 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 720 GCLDDIrTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRL 799
Cdd:PLN02596 290 SCHLPI-TEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 800 ALLQV--RAILQQLGL-NSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREnrgLDHLNVTVGVDGTLYKLHPHFS 876
Cdd:PLN02596 369 EDHEVvnEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGR---IENKKSVVTVEGGLYEHYRVFR 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1997589435 877 RIMHQTV-----KELSPKCTVSFllSEDGSGKGAALITAVG 912
Cdd:PLN02596 446 NYLHSSVwemlgSELSDNVVIEH--SHGGSGAGALFLAACQ 484
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
62-462 |
1.08e-48 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 180.46 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 62 TASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHeKNQNVS-MESEIYDTPENIVHGSGTQLFDHVADCLGD 140
Cdd:PLN02596 76 TTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGG-KNEPISdLYREEISIPSNVLNGTSQELFDYIALELAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 141 FMEKKKIKDKKLP-----VGFTFSFPCRQSKIDEAVLITWtKRFKASGVEGADVVKLLNKAIKKRGdYDANIVAVVNDTV 215
Cdd:PLN02596 155 FVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDTI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 216 GTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGddgSLEDIRTEFDRELDRGSLNP 292
Cdd:PLN02596 233 GNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN---SCHLPITEFDASLDAESSNP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 293 GKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKD---KEGIQNAK--EILTRLGVEP 367
Cdd:PLN02596 310 GSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDtseDHEVVNEKlkEIFGITDSTP 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997589435 368 SDVDCVSvqHICTIVSFRSANLVAATLGAILNRLR--DNKgtprlRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPD--SD 443
Cdd:PLN02596 390 MAREVVA--EVCDIVAERGARLAGAGIVGIIKKLGriENK-----KSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSelSD 462
|
410 420
....*....|....*....|
gi 1997589435 444 -VRFLLSESGSGKGAAMVTA 462
Cdd:PLN02596 463 nVVIEHSHGGSGAGALFLAA 482
|
|
| |
