|
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 ... |
20-473 |
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 1958756465 20 RIDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHE 99
Cdd:cd24124 20 KIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 100 KNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGV 179
Cdd:cd24124 100 KNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 180 EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTE 259
Cdd:cd24124 180 EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 260 WGAFGDDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVS 339
Cdd:cd24124 260 WGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 340 AIEKDKEGIQNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMH 419
Cdd:cd24124 340 AIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958756465 420 PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
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 ... |
477-910 |
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 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 716
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 717 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400
|
410 420 430
....*....|....*....|....*....|....
gi 1958756465 877 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVRL 910
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 ... |
477-909 |
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 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 716
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 717 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 1958756465 877 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVR 909
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 ... |
29-457 |
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: 822.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 108
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 269 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 348
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 349 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 428
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1958756465 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 457
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 ... |
477-911 |
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 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 716
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 717 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....*
gi 1958756465 877 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVRLR 911
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 ... |
477-910 |
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: 773.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKkRTVEMHN 556
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 716
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 717 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399
|
410 420 430
....*....|....*....|....*....|....
gi 1958756465 877 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVRL 910
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 ... |
29-457 |
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 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 108
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 269 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 348
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 349 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 428
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1958756465 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 457
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
477-905 |
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: 725.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGkkRTVEMHN 556
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGG--SQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVE---MVEGNQGQMCINMEWGAFGD 713
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEkwdGDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 714 NGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESD- 792
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 793 RLALLQVRAILQQLGLNS-TCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREnrgldhLNVTVGVDGTLYKLHPHFS 871
Cdd:cd24019 319 EGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR------KEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1958756465 872 RIMHQTVKELSPK-CTVSFLLSEDGSGKGAALITA 905
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 ... |
29-457 |
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: 717.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 108
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 269 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 348
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 349 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 428
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 1958756465 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 457
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
29-457 |
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: 689.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHekNQNVSMES 108
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNG--GSQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDL---VEGDEGRMCINTEWGAFGD 265
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 266 DGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDK 345
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 346 EG-IQNAKEILTRLGVEP-SDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRdnkgtpRLRTTVGVDGSLYKMHPQYS 423
Cdd:cd24019 319 EGdFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1958756465 424 RRFHKTLRRLVP-DSDVRFLLSESGSGKGAAMVTA 457
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 ... |
477-909 |
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 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIrsgKKRTVEMHN 556
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV---GTAGVQITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 716
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 717 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397
|
410 420 430
....*....|....*....|....*....|...
gi 1958756465 877 TVKELSPKCTVSFLLSEDGSGKGAALITAVGVR 909
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 ... |
477-905 |
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 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 716
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 717 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1958756465 877 TVKELSPKCTVSFLLSEDGSGKGAALITA 905
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 ... |
477-905 |
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 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 716
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 717 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1958756465 877 TVKELSPKCTVSFLLSEDGSGKGAALITA 905
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 ... |
477-905 |
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: 604.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 KIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDNGC 716
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 717 LDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 1958756465 877 TVKELSPKCTVSFLLSEDGSGKGAALITA 905
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 ... |
458-910 |
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: 588.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 458 VAYRLAE----QHRQIEETLAHFRLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLG 533
Cdd:cd24124 6 LAYYFTElkddQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 534 GTNFRVLLVKIRSGKKRTVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCG 613
Cdd:cd24124 86 GSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 614 ILISWTKGFKATDCEGHDVASLLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVE 693
Cdd:cd24124 166 ILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHID 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 694 MVEGNQGQMCINMEWGAFGDNGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISE 773
Cdd:cd24124 246 LVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 774 PLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHL 853
Cdd:cd24124 326 ELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958756465 854 NVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCTVSFLLSEDGSGKGAALITAVGVRL 910
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 ... |
29-461 |
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 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 108
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 269 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 348
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 349 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 428
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 1958756465 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 461
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
468-909 |
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: 560.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 468 QIEETLAHFRLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSG 547
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 548 KKR--TVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKAT 625
Cdd:cd24092 81 EEGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 626 DCEGHDVASLLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCIN 705
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 706 MEWGAFGDNGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKF 785
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 786 LSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYK 865
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958756465 866 LHPHFSRIMHQTVKELSPKCTVSFLLSEDGSGKGAALITAVGVR 909
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 ... |
29-462 |
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 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 108
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 269 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 348
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 349 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 428
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....
gi 1958756465 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
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 ... |
29-462 |
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 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMES 108
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 269 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 348
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 349 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 428
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400
|
410 420 430
....*....|....*....|....*....|....
gi 1958756465 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
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 ... |
29-462 |
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: 532.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNqNVSMES 108
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRR-SVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 269 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 348
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 349 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 428
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399
|
410 420 430
....*....|....*....|....*....|....
gi 1958756465 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
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 ... |
29-461 |
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 1958756465 29 RLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEknqNVSMES 108
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTA---GVQITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 109 EIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLL 188
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 269 LEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGI 348
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 349 QNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHK 428
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397
|
410 420 430
....*....|....*....|....*....|...
gi 1958756465 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 461
Cdd:cd24129 398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
20-461 |
5.64e-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: 514.43 E-value: 5.64e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 20 RIDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV--N 97
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgeG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 98 HEKNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKAS 177
Cdd:cd24092 81 EEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 178 GVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCIN 257
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 258 TEWGAFGDDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSD 337
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 338 VSAIEKDKEGIQNAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYK 417
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958756465 418 MHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 461
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. ... |
480-903 |
1.09e-158 |
|
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: 472.12 E-value: 1.09e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 480 KQTLMEVKKRLRTEMEMGLRKETNSkatVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKiY 559
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGGS---LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 560 SIPLEIMQGTGDELFDHIVSCISDFLDYMGIK---GPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLL 636
Cdd:cd24018 77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 637 RDAVKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQG------QMCINMEWGA 710
Cdd:cd24018 157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPSGsvtksdEMIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 711 FGDNGCLDDiRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIE 790
Cdd:cd24018 236 FDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 791 SDRLALLQ-VRAILQQLG--LNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREnrgLDHLNVTVGVDGTLYKLH 867
Cdd:cd24018 315 ADTSPDLDaVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS---LLPEPVTVGIDGSVYEKY 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958756465 868 PHFSRIMHQTVKELSPKCT---VSFLLSEDGSGKGAALI 903
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 ... |
477-905 |
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 1958756465 477 RLSKQTLMEVKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFLALDLG--GTNFRVLLVKIRSGKKRTVEM 554
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 555 HNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVAS 634
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 635 LLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCINMEWGAFGDN 714
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 715 GCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRL 794
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 795 ALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIM 874
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400
|
410 420 430
....*....|....*....|....*....|.
gi 1958756465 875 HQTVKELSPKCTVSFLLSEDGSGKGAALITA 905
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 ... |
33-457 |
1.42e-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: 1.42e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 33 EILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILRVQVNHEKNQNVSMESEI 110
Cdd:cd24090 5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 111 YDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNK 190
Cdd:cd24090 85 FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 191 AIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLE 270
Cdd:cd24090 165 AIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 271 DIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKEGIQN 350
Cdd:cd24090 245 PVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 351 AKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKMHPQYSRRFHKTL 430
Cdd:cd24090 325 VRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTV 404
|
410 420
....*....|....*....|....*..
gi 1958756465 431 RRLVPDSDVRFLLSESGSGKGAAMVTA 457
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. ... |
37-455 |
1.12e-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: 430.52 E-value: 1.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 37 DILTRFKKEMKNGLSRDynpTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEiYDTPEN 116
Cdd:cd24018 6 EIVKHFLSEMEKGLEGD---GGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-YKIPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 117 IVHGSGTQLFDHVADCLGDFME---KKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIK 193
Cdd:cd24018 82 AKTGTGEELFDFIAECIAEFLEehnLDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNALD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 194 KRGdYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHI---DLVEG---DEGRMCINTEWGAFgdDG 267
Cdd:cd24018 162 RRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGsvtKSDEMIINTEWGAF--DN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 268 SLEDI-RTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDKE 346
Cdd:cd24018 239 EREVLpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 347 G-IQNAKEILTRLGV--EPSDVDCVSVQHICTIVSFRSANLVAATLGAILnrLRDNKGTPRlRTTVGVDGSLYKMHPQYS 423
Cdd:cd24018 319 PdLDAVRDILKELLAidNTTLEDRKLIKRICELVSTRAARLSAAAIAAIL--LKRGSLLPE-PVTVGIDGSVYEKYPGFK 395
|
410 420 430
....*....|....*....|....*....|....*
gi 1958756465 424 RRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMV 455
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) ... |
482-904 |
4.08e-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: 4.08e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 482 TLMEVKKRLRTEMEMGLRKEtnsKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSgkKRTVEMHNKIYSI 561
Cdd:cd24000 3 DLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDG--KGIEVTISKKYEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 562 PLEIMQGTGDELFDHIVSCISDFLDYMGIKGPrMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLRDAVK 641
Cdd:cd24000 78 PDEIKTASAEEFFDFIADCIAEFLKENGLKKP-LPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 642 RREeFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNvemVEGNQGQMCINMEWGAFGDNgclDDIR 721
Cdd:cd24000 157 KRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN---SLPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 722 TDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKgflfrgqiseplktrgifetkflsqiesdrlallqvra 801
Cdd:cd24000 230 TEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE-------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 802 ilqqlglnstcddsiLVKTVCGVVSKRAAQLCGAGMAAVVEKIRENrglDHLNVTVGVDGTLYKLHPHFSRIMHQTVKEL 881
Cdd:cd24000 272 ---------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLKEL 333
|
410 420
....*....|....*....|....
gi 1958756465 882 SPK-CTVSFLLSEDGSGKGAALIT 904
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) ... |
32-456 |
3.46e-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: 395.49 E-value: 3.46e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 32 DEILIDILTRFKKEMKNGLSRDYnptASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVSMESEIY 111
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEP---SSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLD--GKGIEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 112 DTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKkLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKA 191
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLKKP-LPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 192 IKKRGdYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDlveGDEGRMCINTEWGAFGDDgslED 271
Cdd:cd24000 155 LKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL---LGDGGMIINTEWGNFGKN---SL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 272 IRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEgllfegritpelltrgkfntsdvsaiekdkegiqna 351
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 352 keiltrlgvepsdvdcvSVQHICTIVSFRSANLVAATLGAILNRLRDNkgtPRLRTTVGVDGSLYKMHPQYSRRFHKTLR 431
Cdd:cd24000 272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420
....*....|....*....|....*.
gi 1958756465 432 RLVP-DSDVRFLLSESGSGKGAAMVT 456
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) ... |
490-905 |
1.23e-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: 1.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 490 LRTEMEMGLRKETNSKatVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYSIPLEIMQGT 569
Cdd:cd24020 13 MVVEMEAGLASEGGSK--LKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVPIPPELMVGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 570 GDELFDHIVSCISDFLDYMG----IKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLRDAVKRReE 645
Cdd:cd24020 91 SEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQ-G 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 646 FDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQ---GQMCINMEWGAFgDNGCLDdiRT 722
Cdd:cd24020 170 LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLprsGEMVINTEWGNF-RSSHLP--RT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 723 DFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRLA-LLQVRA 801
Cdd:cd24020 247 EEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSPdLETVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 802 ILQQ-LGL-NSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLDHLN--VTVGVDGTLYKLHPHFSRIMHQT 877
Cdd:cd24020 327 ILKDaLGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAqrTVVAVDGGLYEHYPKFREYMQQA 406
|
410 420 430
....*....|....*....|....*....|.
gi 1958756465 878 VKELSPKCT---VSFLLSEDGSGKGAALITA 905
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) ... |
42-459 |
2.24e-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: 375.46 E-value: 2.24e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 42 FKKEMKNGLSRDynPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEIYDTPENIVHGS 121
Cdd:cd24020 13 MVVEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVPIPPELMVGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 122 GTQLFDHVADCLGDFM----EKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGd 197
Cdd:cd24020 91 SEELFDFIAGELAKFVategEGFHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 198 YDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFgDDGSLEdiRT 274
Cdd:cd24020 170 LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-RSSHLP--RT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 275 EFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAI-EKDKEGIQNAKE 353
Cdd:cd24020 247 EEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDDSPDLETVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 354 ILTR-LGVEPSDV-DCVSVQHICTIVSFRSANLVAATLGAILNRL-RDNKG-TPRLRTTVGVDGSLYKMHPQYSRRFHKT 429
Cdd:cd24020 327 ILKDaLGIDDTSLeARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGsSPAQRTVVAVDGGLYEHYPKFREYMQQA 406
|
410 420 430
....*....|....*....|....*....|...
gi 1958756465 430 LRRLVPD---SDVRFLLSESGSGKGAAMVTAVA 459
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) ... |
480-905 |
8.23e-116 |
|
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: 360.54 E-value: 8.23e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 480 KQTLMEVKKRLRTEMEMGLRKEtnsKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIrsGKKRTVEMHNKIY 559
Cdd:cd24087 1 TERLRKITDHFISELEKGLSKK---GGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKL--GGNGKFDITQSKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 560 SIPLEIMQGTGDELFDHIVSCISDFLD--YMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLR 637
Cdd:cd24087 76 RLPEELKTGTGEELWDFIADCLKKFVEehFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 638 DAVKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVE----GNQGQMCINMEWGAFgD 713
Cdd:cd24087 156 KALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 714 NGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDR 793
Cdd:cd24087 234 NEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 794 LA-LLQVRAILQQ-LGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKirenRGLDHLNvtVGVDGTLYKLHPHFS 871
Cdd:cd24087 314 FEnLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYKTCH--VAADGSVYNKYPGFK 387
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958756465 872 RIMHQTVKEL----SPKCTVSFLLSEDGSGKGAALITA 905
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 ... |
480-903 |
1.11e-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: 1.11e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 480 KQTLMEVKKRLRTEMEMGLrkeTNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIrSGKkRTVEMHNKIY 559
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL-HGD-GTFSLRQEKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 560 SIPLEIMQG-TGDELFDHIVSCISDFL-DY------MGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHD 631
Cdd:cd24088 76 KIPDELKTGvTAKDLFDYLAKSVEAFLtKHhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 632 VASLLRDAVKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCE---IGLIVGTGTNACYMEEMKNV------EMVEGNQGQM 702
Cdd:cd24088 156 VVKLLQDELDRQ-GIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 703 CINMEWGAFgdngclDDIR-----TDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFL---FRGQISEP 774
Cdd:cd24088 235 VINTEWGSF------DNELkvlptTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 775 LKTRGIFETKFLSQIESDRLALLQV--RAILQQLGLNS-TCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENRGLD 851
Cdd:cd24088 309 LNTPYGLDTAVLSAIEIDSEAELRAtrKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958756465 852 HLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCT----VSFLLSEDGSGKGAALI 903
Cdd:cd24088 389 DGEINIGVDGSVIEFYPGFESMLREALRLLLIGAEgekrIKIGIAKDGSGVGAALC 444
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
672-906 |
3.94e-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: 330.61 E-value: 3.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 672 EIGLIVGTGTNACYMEEMKNVEMVEG---NQGQMCINMEWGAFGDNGCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMY 748
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGklpKSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 749 LGEIVRNILIDFTKKGFLFRGQiSEPLKTRGIFETKFLSQIESDR-LALLQVRAILQQ-LGLNS-TCDDSILVKTVCGVV 825
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIETvTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 826 SKRAAQLCGAGMAAVVEKIRENRGldhlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPKCTVSFLLSEDGSGKGAALIT 904
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDKK-----VTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 1958756465 905 AV 906
Cdd:pfam03727 235 AV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
461-906 |
6.25e-107 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 338.57 E-value: 6.25e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 461 RLAEQHRQIEETLAHFRLSKQTLMEVKKRLRTEMEMGL---RKETN----SKATVKMLPSFVRSIPDGTEHGDFLALDLG 533
Cdd:PTZ00107 3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeahRRHRNlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 534 GTNFRVLLVKIRSGKKrtVEMHNKIYSIPLEIMQG---------TGDELFDHIVSCISDFLDYMGIK---GPRMPLGFTF 601
Cdd:PTZ00107 83 GTNFRAVRVSLRGGGK--MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 602 SFPCHQTNLDCGILISWTKGF---KATD--CEGHDVASLLRDAVKRrEEFDLDVVAVVNDTVGTMMTCAYEE----PTCE 672
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFetgRATNdpVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 673 IGLIVGTGTNACYME-EMKNVemveGNQGQMcINMEWGAFgdngCLDDIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGE 751
Cdd:PTZ00107 240 VGVIIGTGSNACYFEpEVSAY----GYAGTP-INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 752 IVRNILIDftkkgfLFRGQISEPLKTRGIFETKFLSQIESDRLALLQ-VRAILQQL-GLNSTCDDSILVKTVCGVVSKRA 829
Cdd:PTZ00107 311 ISRRLIVH------LLQLKAPPKMWQSGSFESEDASMILNDQSPDLQfSRQVIKEAwDVDLTDEDLYTIRKICELVRGRA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958756465 830 AQLCGAGMAAVVEKIRENRGLdhlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPK-CTVSFLLSEDGSGKGAALITAV 906
Cdd:PTZ00107 385 AQLAAAFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAM 459
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
18-459 |
1.20e-106 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 337.80 E-value: 1.20e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 18 EARIDKYLYAMRLSDEILIDILTRFKKEMKNGL-SRDYNPTA------SVKMLPTFVRSIPDGSEKGDFIALDLGGSSFR 90
Cdd:PTZ00107 8 RVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 91 ILRVQVNH----EKNQN-VSMESEIYDTPENIV--HGSGTQLFDHVADCLGDFME---KKKIKDKKLPVGFTFSFPCRQS 160
Cdd:PTZ00107 88 AVRVSLRGggkmERTQSkFSLPKSALLGEKGLLdkKATATDLFDHIAKSIKKMMEengDPEDLNKPVPVGFTFSFPCTQL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 161 KIDEAVLITWTKRFKAS-----GVEGADVVKLLNKAIKkRGDYDANIVAVVNDTVGTMMTCGYDDQ----QCEVGLIIGT 231
Cdd:PTZ00107 168 SVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFK-RNNVPANVVAVLNDTVGTLISCAYQKPkntpPCQVGVIIGT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 232 GTNACYMEelrHIDLVEGDEGRMcINTEWGAFgdDGSLEdiRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVK 311
Cdd:PTZ00107 247 GSNACYFE---PEVSAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 312 MAKEGLLfegritPELLTRGKFNTSDVSAIEKDK-EGIQNAKEILTRL-GVEPSDVDCVSVQHICTIVSFRSANLVAATL 389
Cdd:PTZ00107 319 LLQLKAP------PKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958756465 390 GAILNRLRdnkgTPRLRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPD--SDVRFLLSESGSGKGAAMVTAVA 459
Cdd:PTZ00107 393 AAPAKKTR----TVQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPdaGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
224-458 |
1.33e-100 |
|
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: 313.27 E-value: 1.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 224 EVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGDDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMY 300
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 301 MGELVRLILVKMAKEGLLFEGRiTPELLTRGKFNTSDVSAIEKDK-EGIQNAKEILTR-LGVE-PSDVDCVSVQHICTIV 377
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 378 SFRSANLVAATLGAILNRLRDNKgtprlRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPDSD-VRFLLSESGSGKGAAMVT 456
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLGPGDkVVLVLAEDGSGVGAALIA 234
|
..
gi 1958756465 457 AV 458
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) ... |
33-459 |
6.31e-100 |
|
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: 318.94 E-value: 6.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 33 EILIDILTRFKKEMKNGLSRdynPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESeiYD 112
Cdd:cd24087 2 ERLRKITDHFISELEKGLSK---KGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSK--YR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 113 TPENIVHGSGTQLFDHVADCLGDFMEK--KKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNK 190
Cdd:cd24087 77 LPEELKTGTGEELWDFIADCLKKFVEEhfPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 191 AIKKRGdYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYME------ELRHIDLVEGDEgrMCINTEWGAFg 264
Cdd:cd24087 157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEvvsnipKLEHDDIPPDSP--MAINCEYGAF- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 265 DDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKD 344
Cdd:cd24087 233 DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 345 K-EGIQNAKEILTR-LGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGtprlrtTVGVDGSLYKMHPQY 422
Cdd:cd24087 313 PfENLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTC------HVAADGSVYNKYPGF 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958756465 423 SRRFHKTLRRL----VPDSDVRFLLSESGSGKGAAMVTAVA 459
Cdd:cd24087 387 KERAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
26-459 |
2.92e-98 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 314.59 E-value: 2.92e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 26 YAMRLSDEILIDILTRFKKEMKNGLSRDynpTASVKMLPTFVrSIPDGS-EKGDFIALDLGGSSFRILRVQVNheKNQNV 104
Cdd:COG5026 13 HGFDLSSIDLEEIAAKFQEEMEKGLEGK---KSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFD--GEGTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 105 SMESEIY----DTPENIvhgSGTQLFDHVADCLGDFMEKKkikdkkLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVE 180
Cdd:COG5026 87 EIENFKSfplpGTSSEI---TAEEFFDFIADYIEPLLDES------YKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQC----EVGLIIGTGTNACYMEELRHIDLVEGDEGRMCI 256
Cdd:COG5026 158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 257 NTEWGAFgdDGSLediRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGlLFEGRITPELLTRGKFNTS 336
Cdd:COG5026 238 NMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 337 DVSAIEKDKEGiqnAKEILTRLGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRLrDNKGTPRLRTTVGVDGSLY 416
Cdd:COG5026 312 DMSRFLADPSD---EKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHL-GPGKTPLKPHCIAIDGSTY 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958756465 417 -KMhPQYSRRFHKTLRRLVPDSD---VRFLLSESGSGKGAAMVTAVA 459
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 ... |
32-455 |
6.69e-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: 6.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 32 DEILIDILTRFKKEMKNGLSrdyNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVSMESEIY 111
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLA---KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELH--GDGTFSLRQEKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 112 DTPENIVHG-SGTQLFDHVADCLGDFME-------KKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGAD 183
Cdd:cd24088 76 KIPDELKTGvTAKDLFDYLAKSVEAFLTkhhgdsfAAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 184 VVKLLNKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQQCE---VGLIIGTGTNACYMEELRHI---DLVEGDE---GRM 254
Cdd:cd24088 156 VVKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklDDSSRVGkgkTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 255 CINTEWGAFGDDGSLEDIrTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLL---FEGRITPELLTRG 331
Cdd:cd24088 235 VINTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNTPY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 332 KFNTSDVSAIEKDKE-GIQNAKEILTR-LGVE-PSDVDCVSVQHICTIVSFRSANLVAATLGAIL---NRLRDNKGTPrl 405
Cdd:cd24088 314 GLDTAVLSAIEIDSEaELRATRKVLLDdLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAILiktGALNKSYDGE-- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958756465 406 rTTVGVDGSLYKMHPQYSRRFHKTLRRLVP----DSDVRFLLSESGSGKGAAMV 455
Cdd:cd24088 392 -INIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
468-666 |
5.84e-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: 5.84e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 468 QIEETLAHFRLSKQTLMEVKKRLRTEMEMGLRKETNSkaTVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIrsG 547
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSS--SLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVEL--G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 548 KKRTVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIK---GPRMPLGFTFSFPCHQTNLDCGILISWTKGFKA 624
Cdd:pfam00349 77 GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958756465 625 TDCEGHDVASLLRDAVKRREEfDLDVVAVVNDTVGTMMTCAY 666
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
475-902 |
2.60e-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: 2.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 475 HFRLSKQTLMEVKKRLRTEMEMGLRKEtnsKATVKMLPSFVrSIPDG-TEHGDFLALDLGGTNFRVLLVKIrsGKKRTVE 553
Cdd:COG5026 14 GFDLSSIDLEEIAAKFQEEMEKGLEGK---KSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF--DGEGTFE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 554 MHNKIySIPleiMQGTG-----DELFDHIVSCISDFLDYmgikgpRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCE 628
Cdd:COG5026 88 IENFK-SFP---LPGTSseitaEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 629 GHDVASLLRDAVKRREEFDLDVVAVVNDTVGTMMTCAYEEPTC----EIGLIVGTGTNACYMEEMKNVEMVEGNQGQMCI 704
Cdd:COG5026 158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 705 NMEWGAFgdNGCLddiRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGfLFRGQISEPLKTRGIFETK 784
Cdd:COG5026 238 NMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 785 FLSQI---ESDRLallqvrAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREnrGLDHLN-VTVGVD 860
Cdd:COG5026 312 DMSRFladPSDEK------EILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGP--GKTPLKpHCIAID 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958756465 861 GTLYKLHPHF-SRIMHQTVKELSPKCT--VSFLLSEDGSGKGAAL 902
Cdd:COG5026 384 GSTYEKMPGLaEKIEYALQEYLLGEKGryVEFVLVENASLLGAAI 428
|
|
| PLN02914 |
PLN02914 |
hexokinase |
27-457 |
4.64e-93 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 302.96 E-value: 4.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 27 AMRLSDEILIDILTRFKKE------------------MKNGLSRDynPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSS 88
Cdd:PLN02914 29 AVRSNAVSVAPILTKLQKDcatplpvlrhvadamaadMRAGLAVD--GGGDLKMILSYVDSLPSGNEKGLFYALDLGGTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 89 FRILRVQVNHEKNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFMEkKKIKDKKLP------VGFTFSFPCRQSKI 162
Cdd:PLN02914 107 FRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVA-KEGGKFHLPegrkreIGFTFSFPVKQTSI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 163 DEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELR 242
Cdd:PLN02914 186 DSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 243 HIDLVEGDE---GRMCINTEWGAFGDDGSLedirTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLF 319
Cdd:PLN02914 265 AIPKLQGQKsssGRTIINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 320 eGRITPE-LLTRGKFNTSDVSAIEKD-KEGIQNAKEILTR-LGVEPSDVDCVSVQHICTIVSFRSANLVAATLGAILNRL 396
Cdd:PLN02914 341 -GHFVPEkLSTPFALRTPHLCAMQQDnSDDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKM 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958756465 397 -RDNKGT-PRLRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTA 457
Cdd:PLN02914 420 eEDSKGMiFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLelsKNIAIEHTKDGSGIGAALLAA 485
|
|
| PLN02914 |
PLN02914 |
hexokinase |
473-905 |
2.55e-92 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 301.03 E-value: 2.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 473 LAHFRLSKQTLMEVKKRLRTEMEMGLRK--ETNSKATVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKR 550
Cdd:PLN02914 41 LTKLQKDCATPLPVLRHVADAMAADMRAglAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 551 TVEMHNKIYSIPLEIMQGTGDELFDHIVSCISDFLDYMGIK-----GPRMPLGFTFSFPCHQTNLDCGILISWTKGFKAT 625
Cdd:PLN02914 121 VIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 626 DCEGHDVASLLRDAVKrREEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEGNQ---GQM 702
Cdd:PLN02914 201 GTAGKDVVACLNEAME-RQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 703 CINMEWGAFGDNGCLddirTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFE 782
Cdd:PLN02914 280 IINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 783 TKFLSQIESDRLALLQ-VRAILQQ-LGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREN-RGLDHLNVT-VG 858
Cdd:PLN02914 356 TPHLCAMQQDNSDDLQaVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDsKGMIFGKRTvVA 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958756465 859 VDGTLYKLHPHFSRIMHQTVKE-LSPKCTVSFLL--SEDGSGKGAALITA 905
Cdd:PLN02914 436 MDGGLYEKYPQYRRYMQDAVTElLGLELSKNIAIehTKDGSGIGAALLAA 485
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
21-218 |
7.93e-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: 256.66 E-value: 7.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 21 IDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDynPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheK 100
Cdd:pfam00349 2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKE--GSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELG--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 101 NQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFME---KKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKAS 177
Cdd:pfam00349 78 DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKehgLEDFEEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958756465 178 GVEGADVVKLLNKAIKKRGDyDANIVAVVNDTVGTMMTCGY 218
Cdd:pfam00349 158 GVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| PLN02405 |
PLN02405 |
hexokinase |
483-905 |
2.67e-79 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 266.31 E-value: 2.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 483 LMEVKKRLRTEMEMGLRKETNSKatVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYSIP 562
Cdd:PLN02405 55 LRQVADAMTVEMHAGLASEGGSK--LKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 563 LEIMQGTGDELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHDVASLLR 637
Cdd:PLN02405 133 PHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 638 DAVKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEG---NQGQMCINMEWGAFGDN 714
Cdd:PLN02405 213 KAMERV-GLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFRSS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 715 GClddIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRL 794
Cdd:PLN02405 292 HL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 795 ALLQV-----RAILQQlgLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREN--RGLDHLNVTVGVDGTLYKLH 867
Cdd:PLN02405 369 PDLKVvgsklKDILEI--PNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHY 446
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958756465 868 PHFSRIMHQTVKEL---SPKCTVSFLLSEDGSGKGAALITA 905
Cdd:PLN02405 447 TEFSKCMESTLKELlgeEVSESIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
483-905 |
1.92e-77 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 261.35 E-value: 1.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 483 LMEVKKRLRTEMEMGLRKETNSKatVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLlvKIRSGKKRT------VEMHn 556
Cdd:PLN02362 55 LRQVVDAMAVEMHAGLASEGGSK--LKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVL--RVQLGGQRSsilsqdVERH- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 557 kiySIPLEIMQGTGDELFDHIVSCISDFLDYMG-----IKGPRMPLGFTFSFPCHQTNLDCGILISWTKGFKATDCEGHD 631
Cdd:PLN02362 130 ---PIPQHLMNSTSEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 632 VASLLRDAVKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEG---NQGQMCINMEW 708
Cdd:PLN02362 207 VAECLQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEW 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 709 GAFGDNGClddIRTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFrGQISEPLKTRGIFETKFLSQ 788
Cdd:PLN02362 286 GNFWSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 789 I-ESDRLALLQVRAILQQ-LGLNST-CDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKI-RE---------NRGLDHL-- 853
Cdd:PLN02362 362 MhEDDSPELQEVARILKEtLGISEVpLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgRDgsggitsgrSRSDIQImr 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958756465 854 NVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCTVSFLL---SEDGSGKGAALITA 905
Cdd:PLN02362 442 RTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVIlkaTEDGSGIGSALLAA 496
|
|
| PLN02405 |
PLN02405 |
hexokinase |
45-457 |
2.93e-76 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 257.84 E-value: 2.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 45 EMKNGLSRDYNptASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEIYDTPENIVHGSGTQ 124
Cdd:PLN02405 65 EMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 125 LFDHVADCLGDFMEKKKIKDKKLP-----VGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGdYD 199
Cdd:PLN02405 143 LFDFIAAALAKFVATEGEDFHLPPgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-LD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 200 ANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGddgSLEDIRTEF 276
Cdd:PLN02405 222 MRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR---SSHLPLTEY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 277 DRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKDkegiqnAKEILT 356
Cdd:PLN02405 299 DHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHD------TSPDLK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 357 RLGVEPSDVDCVS---------VQHICTIVSFRSANLVAATLGAILNRL-RDN-KGTPRLRTTVGVDGSLYKMHPQYSRR 425
Cdd:PLN02405 373 VVGSKLKDILEIPntslkmrkvVVELCNIVATRGARLSAAGIYGILKKLgRDTvKDGEKQKSVIAMDGGLFEHYTEFSKC 452
|
410 420 430
....*....|....*....|....*....|....*
gi 1958756465 426 FHKTLRRLVPDS---DVRFLLSESGSGKGAAMVTA 457
Cdd:PLN02405 453 MESTLKELLGEEvseSIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
45-457 |
5.53e-73 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 249.41 E-value: 5.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 45 EMKNGLSRDYNptASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEIYDTPENIVHGSGTQ 124
Cdd:PLN02362 65 EMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 125 LFDHVADCLGDFMEKKKIKDKKLPV-----GFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGdYD 199
Cdd:PLN02362 143 LFDFIASSLKQFVEKEENGSEFSQVrrrelGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 200 ANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFgddGSLEDIRTEF 276
Cdd:PLN02362 222 MRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---WSSHLPRTSY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 277 DRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFeGRITPELLTRGKFNTSDVSAI-EKDKEGIQNAKEIL 355
Cdd:PLN02362 299 DIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARIL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 356 T-RLGVE--PSDVDCVSVQhICTIVSFRSANLVAATLGAILNRL-RDNKG-----------TPRLRTTVGVDGSLYKMHP 420
Cdd:PLN02362 378 KeTLGISevPLKVRKLVVK-ICDVVTRRAARLAAAGIVGILKKIgRDGSGgitsgrsrsdiQIMRRTVVAVEGGLYTNYT 456
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1958756465 421 QYSRRFHKTLRRLVPDSDVRFLL---SESGSGKGAAMVTA 457
Cdd:PLN02362 457 MFREYLHEALNEILGEDVAQHVIlkaTEDGSGIGSALLAA 496
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
483-907 |
1.36e-50 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 185.85 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 483 LMEVKKRLRTEMEMGLRKETNSkaTVKMLPSFVRSIPDGTEHGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYSIP 562
Cdd:PLN02596 56 LWEVADALVSDMTASLTAEETT--TLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 563 LEIMQGTGDELFDHIVSCISDFLDYMGIKGPRMP-----LGFTFSFPCHQTNLDCGILISWtKGFKATDCEGHDVASLLR 637
Cdd:PLN02596 134 SNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDIN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 638 DAVKRrEEFDLDVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEEMKNVEMVEG---NQGQMCINMEWGAFgdN 714
Cdd:PLN02596 213 RALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF--N 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 715 GCLDDIrTDFDKVVDEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFRGQISEPLKTRGIFETKFLSQIESDRL 794
Cdd:PLN02596 290 SCHLPI-TEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 795 ALLQV--RAILQQLGL-NSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIREnrgLDHLNVTVGVDGTLYKLHPHFS 871
Cdd:PLN02596 369 EDHEVvnEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGR---IENKKSVVTVEGGLYEHYRVFR 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958756465 872 RIMHQTV-----KELSPKCTVSFllSEDGSGKGAALITAVG 907
Cdd:PLN02596 446 NYLHSSVwemlgSELSDNVVIEH--SHGGSGAGALFLAACQ 484
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
57-457 |
1.31e-48 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 180.46 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 57 TASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHeKNQNVS-MESEIYDTPENIVHGSGTQLFDHVADCLGD 135
Cdd:PLN02596 76 TTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGG-KNEPISdLYREEISIPSNVLNGTSQELFDYIALELAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 136 FMEKKKIKDKKLP-----VGFTFSFPCRQSKIDEAVLITWtKRFKASGVEGADVVKLLNKAIKKRGdYDANIVAVVNDTV 210
Cdd:PLN02596 155 FVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDTI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 211 GTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGddgSLEDIRTEFDRELDRGSLNP 287
Cdd:PLN02596 233 GNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN---SCHLPITEFDASLDAESSNP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 288 GKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKD---KEGIQNAK--EILTRLGVEP 362
Cdd:PLN02596 310 GSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDtseDHEVVNEKlkEIFGITDSTP 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756465 363 SDVDCVSvqHICTIVSFRSANLVAATLGAILNRLR--DNKgtprlRTTVGVDGSLYKMHPQYSRRFHKTLRRLVPD--SD 438
Cdd:PLN02596 390 MAREVVA--EVCDIVAERGARLAGAGIVGIIKKLGriENK-----KSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSelSD 462
|
410 420
....*....|....*....|
gi 1958756465 439 -VRFLLSESGSGKGAAMVTA 457
Cdd:PLN02596 463 nVVIEHSHGGSGAGALFLAA 482
|
|
| |
