|
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 ... |
21-473 |
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: 984.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEK 100
Cdd:cd24124 21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180
Cdd:cd24124 101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260
Cdd:cd24124 181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340
Cdd:cd24124 261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420
Cdd:cd24124 341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15991827 421 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
Cdd:cd24124 421 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 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: 916.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 477 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 557 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 636
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 637 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 716
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 717 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400
|
410 420 430
....*....|....*....|....*....|....
gi 15991827 877 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 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: 904.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 477 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 557 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 636
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 637 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 716
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 717 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 15991827 877 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVR 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: 854.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 108
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 269 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 348
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 349 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 15991827 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 ... |
478-911 |
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: 808.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 478 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNK 557
Cdd:cd24128 2 LSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 558 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 637
Cdd:cd24128 82 IYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 638 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 717
Cdd:cd24128 162 EAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 718 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 797
Cdd:cd24128 242 DDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 798 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQT 877
Cdd:cd24128 322 QVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHET 401
|
410 420 430
....*....|....*....|....*....|....
gi 15991827 878 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRLR 911
Cdd:cd24128 402 VKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
|
|
| 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: 797.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 108
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 269 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 348
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 349 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 15991827 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 457
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
478-910 |
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: 789.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 478 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKkRTVEMHNK 557
Cdd:cd24130 2 LTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 558 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 637
Cdd:cd24130 81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 638 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 717
Cdd:cd24130 161 EAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGCI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 718 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 797
Cdd:cd24130 241 DDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 798 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQT 877
Cdd:cd24130 321 QVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQET 400
|
410 420 430
....*....|....*....|....*....|...
gi 15991827 878 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 910
Cdd:cd24130 401 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| 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: 743.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 477 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGkkRTVEMHN 556
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGG--SQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 557 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 636
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 637 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVE---MVEGDQGQMCINMEWGAFGD 713
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEkwdGDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 714 NGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESD- 792
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 793 RLALLQVRAILQQLGLNS-TCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRenrgldRLNVTVGVDGTLYKLHPHFS 871
Cdd:cd24019 319 EGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 15991827 872 RIMHQTVKELSPK-CNVSFLLSEDGSGKGAALITA 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: 734.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 108
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 269 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 348
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 349 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 15991827 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: 714.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHekNQNVHMES 108
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNG--GSQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDL---VEGDEGRMCINTEWGAFGD 265
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 266 DGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNK 345
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 346 EG-LHNAKEILTRLGVEP-SDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRdnkgtpRLRTTVGVDGSLYKTHPQYS 423
Cdd:cd24019 319 EGdFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 15991827 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 ... |
478-909 |
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: 693.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 478 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsgKKRTVEMHNK 557
Cdd:cd24129 2 LSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV---GTAGVQITSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 558 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 637
Cdd:cd24129 79 IYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 638 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 717
Cdd:cd24129 159 EAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 718 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 797
Cdd:cd24129 239 AMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 798 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQT 877
Cdd:cd24129 319 QVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQAT 398
|
410 420 430
....*....|....*....|....*....|..
gi 15991827 878 VKELSPKCNVSFLLSEDGSGKGAALITAVGVR 909
Cdd:cd24129 399 VRELAPRCVVTFLQSEDGSGKGAALVTAVACR 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: 649.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 477 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 557 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 636
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 637 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 716
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 717 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 15991827 877 TVKELSPKCNVSFLLSEDGSGKGAALITA 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: 603.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 477 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 556
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 557 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 636
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 637 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 716
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 717 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 796
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 797 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 876
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 15991827 877 TVKELSPKCNVSFLLSEDGSGKGAALITA 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 ... |
478-905 |
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: 599.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 478 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNK 557
Cdd:cd24125 2 LSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 558 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 637
Cdd:cd24125 82 IYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 638 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 717
Cdd:cd24125 162 KAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 718 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 797
Cdd:cd24125 242 DDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGIR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 798 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQT 877
Cdd:cd24125 322 KAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHKT 401
|
410 420
....*....|....*....|....*...
gi 15991827 878 VKELSPKCNVSFLLSEDGSGKGAALITA 905
Cdd:cd24125 402 VRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| 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: 584.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 108
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 269 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 348
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 349 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 15991827 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 461
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| 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: 580.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 458 VAYRLAE----QHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLG 533
Cdd:cd24124 6 LAYYFTElkddQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 534 GTNFRVLLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAG 613
Cdd:cd24124 86 GSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 614 ILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVE 693
Cdd:cd24124 166 ILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHID 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 694 MVEGDQGQMCINMEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISE 773
Cdd:cd24124 246 LVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 774 TLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRL 853
Cdd:cd24124 326 ELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15991827 854 NVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 910
Cdd:cd24124 406 RTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
|
|
| 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: 569.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 468 QIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSG 547
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 548 KKR--TVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKAT 625
Cdd:cd24092 81 EEGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 626 DCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCIN 705
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 706 MEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKF 785
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 786 LSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYK 865
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15991827 866 LHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVR 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: 564.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 108
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 269 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 348
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 349 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....
gi 15991827 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: 545.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 108
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 269 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 348
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 349 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400
|
410 420 430
....*....|....*....|....*....|....
gi 15991827 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
Cdd:cd24127 401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| 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: 541.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEknqNVHMES 108
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTA---GVQITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 269 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 348
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 349 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397
|
410 420 430
....*....|....*....|....*....|...
gi 15991827 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 461
Cdd:cd24129 398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| 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: 540.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 29 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNqNVHMES 108
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRR-SVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 109 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 268
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 269 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 348
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 349 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399
|
410 420 430
....*....|....*....|....*....|....
gi 15991827 429 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
Cdd:cd24130 400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
21-461 |
6.23e-179 |
|
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: 524.44 E-value: 6.23e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV--NH 98
Cdd:cd24092 2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgeGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 99 EKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASG 178
Cdd:cd24092 82 EGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 179 VEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINT 258
Cdd:cd24092 162 AEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 259 EWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDV 338
Cdd:cd24092 242 EWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 339 SAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKT 418
Cdd:cd24092 322 SQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15991827 419 HPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 461
Cdd:cd24092 402 HPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
480-903 |
3.47e-165 |
|
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: 488.68 E-value: 3.47e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 480 KDMLLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKiY 559
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGGS---LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 560 AIPIEIMQGTGEELFDHIVSCISDFLDYMGIK---GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 636
Cdd:cd24018 77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 637 RDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVE------GDQGQMCINMEWGA 710
Cdd:cd24018 157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsgsvTKSDEMIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 711 FGDNGCLDDiRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIE 790
Cdd:cd24018 236 FDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 791 SDRLALLQ-VRAILQQLG--LNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKirenRGLDRLN-VTVGVDGTLYKL 866
Cdd:cd24018 315 ADTSPDLDaVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLK----RGSLLPEpVTVGIDGSVYEK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15991827 867 HPHFSRIMHQTVKELSP---KCNVSFLLSEDGSGKGAALI 903
Cdd:cd24018 391 YPGFKDRLSEALRELFGpevKANISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
478-905 |
1.35e-158 |
|
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: 471.71 E-value: 1.35e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 478 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLG--GTNFRVLLVKIRSGKKRTVEMH 555
Cdd:cd24090 2 VTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 556 NKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTL 635
Cdd:cd24090 82 SQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 636 LRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNG 715
Cdd:cd24090 162 LRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 716 CLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLA 795
Cdd:cd24090 242 ALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 796 LLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMH 875
Cdd:cd24090 322 AARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQ 401
|
410 420 430
....*....|....*....|....*....|
gi 15991827 876 QTVKELSPKCNVSFLLSEDGSGKGAALITA 905
Cdd:cd24090 402 GTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
33-457 |
8.13e-152 |
|
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: 454.38 E-value: 8.13e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 33 ETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILRVQVNHEKNQNVHMESEV 110
Cdd:cd24090 5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 111 YDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNK 190
Cdd:cd24090 85 FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 191 AIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLE 270
Cdd:cd24090 165 AIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 271 DIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHN 350
Cdd:cd24090 245 PVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 351 AKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTL 430
Cdd:cd24090 325 VRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTV 404
|
410 420
....*....|....*....|....*..
gi 15991827 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. ... |
32-455 |
1.42e-148 |
|
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: 445.93 E-value: 1.42e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 32 DETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVhMESEVY 111
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGD---GGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFI-IVQRKY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 112 DTPENIVHGSGSQLFDHVAECLGDFMEKRKIK---DKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24018 77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHI---DLVEG---DEGRMCINTEWGA 262
Cdd:cd24018 157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGsvtKSDEMIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 263 FgdDGSLEDI-RTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAI 341
Cdd:cd24018 236 F--DNEREVLpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 342 EKNKEG-LHNAKEILTRLGV--EPSDDDCVSVQHVCTIVSFRSANLVAATLGAILnrLRDNKGTPRlRTTVGVDGSLYKT 418
Cdd:cd24018 314 EADTSPdLDAVRDILKELLAidNTTLEDRKLIKRICELVSTRAARLSAAAIAAIL--LKRGSLLPE-PVTVGIDGSVYEK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15991827 419 HPQYSRRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMV 455
Cdd:cd24018 391 YPGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
480-904 |
2.46e-138 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 416.68 E-value: 2.46e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 480 KDMLLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSgkKRTVEMHNKIY 559
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEPSS---LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDG--KGIEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 560 AIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPrMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDA 639
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLKKP-LPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 640 IKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNvemVEGDQGQMCINMEWGAFGDNgclDD 719
Cdd:cd24000 155 LKKR-GLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN---SL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 720 IRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKgflfrgqisetlktrgifetkflsqiesdrlallqv 799
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 800 railqqlglnstcddsiLVKTVCGVVSRRAAQLCGAGMAAVVDKIRENrglDRLNVTVGVDGTLYKLHPHFSRIMHQTVK 879
Cdd:cd24000 272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420
....*....|....*....|....*.
gi 15991827 880 ELSPK-CNVSFLLSEDGSGKGAALIT 904
Cdd:cd24000 332 ELLGRgIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
32-456 |
4.27e-134 |
|
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: 405.51 E-value: 4.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 32 DETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVHMESEVY 111
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLD--GKGIEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 112 DTPENIVHGSGSQLFDHVAECLGDFMEKRKIKdKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKA 191
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 192 IKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDlveGDEGRMCINTEWGAFGDDgslED 271
Cdd:cd24000 155 LKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL---LGDGGMIINTEWGNFGKN---SL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 272 IRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEgllfegritpelltrgkfntsdvsaieknkeglhna 351
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 352 keiltrlgvepsdddcvSVQHVCTIVSFRSANLVAATLGAILNRLRDNkgtPRLRTTVGVDGSLYKTHPQYSRRFHKTLR 431
Cdd:cd24000 272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420
....*....|....*....|....*.
gi 15991827 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) ... |
33-459 |
8.11e-123 |
|
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: 379.31 E-value: 8.11e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 33 ETLIDIMTrfrKEMKNGLSRDfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYD 112
Cdd:cd24020 7 RQVADAMV---VEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 113 TPENIVHGSGSQLFDHVAECLGDFMEK----RKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
Cdd:cd24020 82 IPPELMVGTSEELFDFIAGELAKFVATegegFHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 189 NKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFgD 265
Cdd:cd24020 162 EEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-R 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 266 DGSLEdiRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAI-EKN 344
Cdd:cd24020 240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 345 KEGLHNAKEILTR-LGVEPSD-DDCVSVQHVCTIVSFRSANLVAATLGAILNRL-RDNKG-TPRLRTTVGVDGSLYKTHP 420
Cdd:cd24020 318 SPDLETVARILKDaLGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGsSPAQRTVVAVDGGLYEHYP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15991827 421 QYSRRFHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTAVA 459
Cdd:cd24020 398 KFREYMQQALVELLGDeaaDSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
478-905 |
1.16e-122 |
|
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth.
Pssm-ID: 466870 [Multi-domain] Cd Length: 439 Bit Score: 378.93 E-value: 1.16e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 478 LTKDMLLEVKKRMRAEMELGLRKQTHNNavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNK 557
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSK--LKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 558 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMG----IKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVV 633
Cdd:cd24020 79 EVPIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 634 TLLRDAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQ---GQMCINMEWGA 710
Cdd:cd24020 159 ELLEEALERQ-GLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLprsGEMVINTEWGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 711 FgDNGCLDdiRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIE 790
Cdd:cd24020 238 F-RSSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 791 SDRLA-LLQVRAILQQ-LGL-NSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLN--VTVGVDGTLYK 865
Cdd:cd24020 315 EDDSPdLETVARILKDaLGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAqrTVVAVDGGLYE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15991827 866 LHPHFSRIMHQTVKELSPKC---NVSFLLSEDGSGKGAALITA 905
Cdd:cd24020 395 HYPKFREYMQQALVELLGDEaadSVELELSNDGSGIGAALLAA 437
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
483-905 |
1.49e-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: 362.46 E-value: 1.49e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 483 LLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsGKKRTVEMHNKIYAIP 562
Cdd:cd24087 4 LRKITDHFISELEKGLSKKGGN---IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKL--GGNGKFDITQSKYRLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 563 IEIMQGTGEELFDHIVSCISDFLD--YMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAI 640
Cdd:cd24087 79 EELKTGTGEELWDFIADCLKKFVEehFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 641 KRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVE----GDQGQMCINMEWGAFgDNGC 716
Cdd:cd24087 159 KKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DNEH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 717 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLA- 795
Cdd:cd24087 237 LVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEn 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 796 LLQVRAILQQ-LGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKirenRGLDRLNvtVGVDGTLYKLHPHFSRIM 874
Cdd:cd24087 317 LEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYKTCH--VAADGSVYNKYPGFKERA 390
|
410 420 430
....*....|....*....|....*....|....*
gi 15991827 875 HQTVKEL----SPKCNVSFLLSEDGSGKGAALITA 905
Cdd:cd24087 391 AQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAA 425
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
483-903 |
9.89e-112 |
|
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: 9.89e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 483 LLEVKKRMRAEMELGLrkqTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrSGKkRTVEMHNKIYAIP 562
Cdd:cd24088 4 LDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL-HGD-GTFSLRQEKSKIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 563 IEIMQG-TGEELFDHIVSCISDFL-DY------MGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVT 634
Cdd:cd24088 79 DELKTGvTAKDLFDYLAKSVEAFLtKHhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 635 LLRDAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCE---VGLIVGTGSNACYMEEMKNV------EMVEGDQGQMCIN 705
Cdd:cd24088 159 LLQDELDRQ-GIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKTHMVIN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 706 MEWGAFgdngclDDIRTH-----YDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFL---FRGQISETLKT 777
Cdd:cd24088 238 TEWGSF------DNELKVlpttpYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 778 RGIFETKFLSQIESDRLALLQV--RAILQQLGLNS-TCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLN 854
Cdd:cd24088 312 PYGLDTAVLSAIEIDSEAELRAtrKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGE 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15991827 855 VTVGVDGTLYKLHPHFSRIMHQTVKELSP----KCNVSFLLSEDGSGKGAALI 903
Cdd:cd24088 392 INIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
21-459 |
1.85e-108 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 342.81 E-value: 1.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGL-SRDFNPTA------TVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILR 93
Cdd:PTZ00107 11 LASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 94 VQVNH----EKNQN--VHMESEVYdTPENIV--HGSGSQLFDHVAECLGDFMEKRKIKD---KKLPVGFTFSFPCQQSKI 162
Cdd:PTZ00107 91 VSLRGggkmERTQSkfSLPKSALL-GEKGLLdkKATATDLFDHIAKSIKKMMEENGDPEdlnKPVPVGFTFSFPCTQLSV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 163 DEAILITWTKRFKAS-----GVEGADVVKLLNKAIKkRGDYDANIVAVVNDTVGTMMTCGYDDQH----CEVGLIIGTGT 233
Cdd:PTZ00107 170 NNAILIDWTKGFETGratndPVEGKDVGELLNDAFK-RNNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVIIGTGS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 234 NACYMEelrHIDLVEGDEGRMcINTEWGAFgdDGSLEdiRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMA 313
Cdd:PTZ00107 249 NACYFE---PEVSAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 314 KEGLLfegritPELLTRGKFNTSDVSAIEKNK-EGLHNAKEILTRL-GVEPSDDDCVSVQHVCTIVSFRSANLVAATLGA 391
Cdd:PTZ00107 321 QLKAP------PKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 392 ILNRLRdnkgTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPD--SDVRFLLSESGSGKGAAMVTAVA 459
Cdd:PTZ00107 395 PAKKTR----TVQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPdaGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
672-906 |
1.95e-106 |
|
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: 328.68 E-value: 1.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 672 EVGLIVGTGSNACYMEEMKNVEMVEGDQ---GQMCINMEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMY 748
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLpksGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 749 LGEIVRNILIDFTKKGFLFRGQiSETLKTRGIFETKFLSQIESDR-LALLQVRAILQQ-LGLNS-TCDDSILVKTVCGVV 825
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIETvTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 826 SRRAAQLCGAGMAAVVDKIRENRGldrlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPKCNVSFLLSEDGSGKGAALIT 904
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDKK-----VTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 15991827 905 AV 906
Cdd:pfam03727 235 AV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
461-906 |
1.63e-102 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 327.02 E-value: 1.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 461 RLAEQHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLR-KQTHNNAV------VKMLPSFVRRTPDGTENGDFLALDLG 533
Cdd:PTZ00107 3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEaHRRHRNLWipnecsFKMLDSCVYNLPTGKEKGVYYAIDFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 534 GTNFRVLLVKIRSGKKrtVEMHNKIYAIPIEIMQG---------TGEELFDHIVSCISDFLDYMGIK---GPRMPLGFTF 601
Cdd:PTZ00107 83 GTNFRAVRVSLRGGGK--MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 602 SFPCQQTSLDAGILITWTKGFK----ATDCV-GHDVVTLLRDAIKRrEEFDLDVVAVVNDTVGTMMTCAYEE----PTCE 672
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFEtgraTNDPVeGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 673 VGLIVGTGSNACYMEEM----KNVEMVegdqgqmcINMEWGAFgdngCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMY 748
Cdd:PTZ00107 240 VGVIIGTGSNACYFEPEvsayGYAGTP--------INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 749 LGEIVRNILIDftkkgfLFRGQISETLKTRGIFETKFLSQIESDRLALLQ-VRAILQQL-GLNSTCDDSILVKTVCGVVS 826
Cdd:PTZ00107 308 LGEISRRLIVH------LLQLKAPPKMWQSGSFESEDASMILNDQSPDLQfSRQVIKEAwDVDLTDEDLYTIRKICELVR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 827 RRAAQLCGAGMAAVVDKIRENRGLdrlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPK-CNVSFLLSEDGSGKGAALIT 904
Cdd:PTZ00107 382 GRAAQLAAAFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIA 457
|
..
gi 15991827 905 AV 906
Cdd:PTZ00107 458 AM 459
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
33-459 |
1.72e-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: 320.48 E-value: 1.72e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 33 ETLIDIMTRFRKEMKNGLSRdfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVhMESEvYD 112
Cdd:cd24087 2 ERLRKITDHFISELEKGLSK---KGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDI-TQSK-YR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 113 TPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKK--LPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNK 190
Cdd:cd24087 77 LPEELKTGTGEELWDFIADCLKKFVEEHFPGGKSepLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 191 AIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME------ELRHIDLVEGDEgrMCINTEWGAFg 264
Cdd:cd24087 157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEvvsnipKLEHDDIPPDSP--MAINCEYGAF- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 265 DDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKN 344
Cdd:cd24087 233 DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 345 K-EGLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRlRDNKGtprlrTTVGVDGSLYKTHPQY 422
Cdd:cd24087 313 PfENLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK-RGYKT-----CHVAADGSVYNKYPGF 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15991827 423 SRRFHKTLRRL----VPDSDVRFLLSESGSGKGAAMVTAVA 459
Cdd:cd24087 387 KERAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
224-458 |
2.19e-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: 312.89 E-value: 2.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 224 EVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMY 300
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 301 LGELVRLILVKMAKEGLLFEGRiTPELLTRGKFNTSDVSAIEK-NKEGLHNAKEILTR-LGVE-PSDDDCVSVQHVCTIV 377
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESdPSEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 378 SFRSANLVAATLGAILNRLRDNKgtprlRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSD-VRFLLSESGSGKGAAMVT 456
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLGPGDkVVLVLAEDGSGVGAALIA 234
|
..
gi 15991827 457 AV 458
Cdd:pfam03727 235 AV 236
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
26-459 |
6.31e-100 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 319.21 E-value: 6.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 26 YAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVrSIPDGS-EKGDFIALDLGGSSFRILRVQVNheKNQNV 104
Cdd:COG5026 13 HGFDLSSIDLEEIAAKFQEEMEKGLEGK---KSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFD--GEGTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 105 HMESEVY----DTPENIvhgSGSQLFDHVAECLGDFmekrkiKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180
Cdd:COG5026 87 EIENFKSfplpGTSSEI---TAEEFFDFIADYIEPL------LDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQ----HCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCI 256
Cdd:COG5026 158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 257 NTEWGAFgdDGSLediRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGlLFEGRITPELLTRGKFNTS 336
Cdd:COG5026 238 NMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 337 DVSAIEKNKEGlhnAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLrDNKGTPRLRTTVGVDGSLY 416
Cdd:COG5026 312 DMSRFLADPSD---EKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHL-GPGKTPLKPHCIAIDGSTY 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15991827 417 KTHPQYSRRFHKTLRRLVPDSD---VRFLLSESGSGKGAAMVTAVA 459
Cdd:COG5026 388 EKMPGLAEKIEYALQEYLLGEKgryVEFVLVENASLLGAAIAAALN 433
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
32-455 |
2.79e-98 |
|
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: 315.10 E-value: 2.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 32 DETLIDIMTRFRKEMKNGLSrdfNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVHMESEVY 111
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLA---KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELH--GDGTFSLRQEKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 112 DTPENIVHGSGSQ-LFDHVAECLGDFMEK-------RKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGAD 183
Cdd:cd24088 76 KIPDELKTGVTAKdLFDYLAKSVEAFLTKhhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 184 VVKLLNKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCE---VGLIIGTGTNACYMEELRHI---DLVEGDE---GRM 254
Cdd:cd24088 156 VVKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklDDSSRVGkgkTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 255 CINTEWGAFGDDGSLEDIrTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLL---FEGRITPELLTRG 331
Cdd:cd24088 235 VINTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNTPY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 332 KFNTSDVSAIEKNKE-GLHNAKEILTR-LGVE-PSDDDCVSVQHVCTIVSFRSANLVAATLGAIL---NRLRDNKGTPrl 405
Cdd:cd24088 314 GLDTAVLSAIEIDSEaELRATRKVLLDdLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAILiktGALNKSYDGE-- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15991827 406 rTTVGVDGSLYKTHPQYSRRFHKTLRRLVP----DSDVRFLLSESGSGKGAAMV 455
Cdd:cd24088 392 -INIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
|
|
| PLN02914 |
PLN02914 |
hexokinase |
27-457 |
1.20e-97 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 315.29 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 27 AMRLSDETLIDIMTRFRKE------------------MKNGLSRDfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSS 88
Cdd:PLN02914 29 AVRSNAVSVAPILTKLQKDcatplpvlrhvadamaadMRAGLAVD--GGGDLKMILSYVDSLPSGNEKGLFYALDLGGTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 89 FRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIK-----DKKLPVGFTFSFPCQQSKID 163
Cdd:PLN02914 107 FRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSID 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 164 EAILITWTKRFKASGVEGADVVKLLNKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRH 243
Cdd:PLN02914 187 SGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 244 IDLVEGDE---GRMCINTEWGAFGDDGSLedirTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFe 320
Cdd:PLN02914 266 IPKLQGQKsssGRTIINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLF- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 321 GRITPE-LLTRGKFNTSDVSAIEK-NKEGLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRL- 396
Cdd:PLN02914 341 GHFVPEkLSTPFALRTPHLCAMQQdNSDDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMe 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15991827 397 RDNKGT-PRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTA 457
Cdd:PLN02914 421 EDSKGMiFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLelsKNIAIEHTKDGSGIGAALLAA 485
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
468-666 |
1.32e-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: 295.95 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 468 QIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQThnNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsG 547
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVEL--G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 548 KKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIK---GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKA 624
Cdd:pfam00349 77 GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15991827 625 TDCVGHDVVTLLRDAIKRREEfDLDVVAVVNDTVGTMMTCAY 666
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
475-902 |
3.53e-92 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 298.41 E-value: 3.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 475 HFHLTKDMLLEVKKRMRAEMELGLRkqtHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsGKKRTVEM 554
Cdd:COG5026 14 GFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYLGLPTGVKETGPVIALDAGGTNFRVALVRF--DGEGTFEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 555 HNKIyAIPieiMQGTG-----EELFDHIVSCISDFLDYmgikgpRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVG 629
Cdd:COG5026 89 ENFK-SFP---LPGTSseitaEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 630 HDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTC----EVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCIN 705
Cdd:COG5026 159 KNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIIN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 706 MEWGAFgdNGCLddiRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGfLFRGQISETLKTRGIFETKF 785
Cdd:COG5026 239 MESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 786 LSQI---ESDRLallqvrAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRlNVTVGVDGT 862
Cdd:COG5026 313 MSRFladPSDEK------EILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-PHCIAIDGS 385
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15991827 863 LYKLHPHF-SRIMHQTVKELSPKCN--VSFLLSEDGSGKGAAL 902
Cdd:COG5026 386 TYEKMPGLaEKIEYALQEYLLGEKGryVEFVLVENASLLGAAI 428
|
|
| PLN02914 |
PLN02914 |
hexokinase |
483-905 |
4.10e-91 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 297.57 E-value: 4.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 483 LLEVKKRMRAEMELGLRKQTHNNavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIP 562
Cdd:PLN02914 55 LRHVADAMAADMRAGLAVDGGGD--LKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 563 IEIMQGTGEELFDHIVSCISDFLDYMGIK-----GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 637
Cdd:PLN02914 133 QELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 638 DAIKrREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQ---GQMCINMEWGAFGDN 714
Cdd:PLN02914 213 EAME-RQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSDG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 715 GCLddirTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 794
Cdd:PLN02914 292 LPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 795 ALLQ-VRAILQQ-LGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIREN-RGLDRLNVT-VGVDGTLYKLHPHF 870
Cdd:PLN02914 368 DDLQaVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDsKGMIFGKRTvVAMDGGLYEKYPQY 447
|
410 420 430
....*....|....*....|....*....|....*...
gi 15991827 871 SRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 905
Cdd:PLN02914 448 RRYMQDAVTELlglELSKNIAIEHTKDGSGIGAALLAA 485
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
21-218 |
4.20e-83 |
|
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: 265.52 E-value: 4.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheK 100
Cdd:pfam00349 2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKE--GSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELG--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKD---KKLPVGFTFSFPCQQSKIDEAILITWTKRFKAS 177
Cdd:pfam00349 78 DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15991827 178 GVEGADVVKLLNKAIKKRGDyDANIVAVVNDTVGTMMTCGY 218
Cdd:pfam00349 158 GVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| PLN02405 |
PLN02405 |
hexokinase |
483-905 |
1.19e-79 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 267.08 E-value: 1.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 483 LLEVKKRMRAEMELGLrkQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIP 562
Cdd:PLN02405 55 LRQVADAMTVEMHAGL--ASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 563 IEIMQGTGEELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 637
Cdd:PLN02405 133 PHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 638 DAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGD---QGQMCINMEWGAFGDN 714
Cdd:PLN02405 213 KAMERV-GLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFRSS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 715 GClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 794
Cdd:PLN02405 292 HL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 795 ALLQV-----RAILQQlgLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDRLNVTVGVDGTLYKLH 867
Cdd:PLN02405 369 PDLKVvgsklKDILEI--PNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHY 446
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15991827 868 PHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 905
Cdd:PLN02405 447 TEFSKCMESTLKELlgeEVSESIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
483-905 |
2.47e-79 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 266.75 E-value: 2.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 483 LLEVKKRMRAEMELGLrkQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLlvKIRSGKKRT------VEMHn 556
Cdd:PLN02362 55 LRQVVDAMAVEMHAGL--ASEGGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVL--RVQLGGQRSsilsqdVERH- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 557 kiyAIPIEIMQGTGEELFDHIVSCISDFLDYMG-----IKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHD 631
Cdd:PLN02362 130 ---PIPQHLMNSTSEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 632 VVTLLRDAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEW 708
Cdd:PLN02362 207 VAECLQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEW 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 709 GAFGDNGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFrGQISETLKTRGIFETKFLSQ 788
Cdd:PLN02362 286 GNFWSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 789 I-ESDRLALLQVRAILQQ-LGLNST-CDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKI-------------RENRGLDR 852
Cdd:PLN02362 362 MhEDDSPELQEVARILKEtLGISEVpLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgrdgsggitsgrsRSDIQIMR 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15991827 853 LNVtVGVDGTLYKLHPHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 905
Cdd:PLN02362 442 RTV-VAVEGGLYTNYTMFREYLHEALNEIlgeDVAQHVILKATEDGSGIGSALLAA 496
|
|
| PLN02405 |
PLN02405 |
hexokinase |
37-457 |
1.18e-74 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 253.60 E-value: 1.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 37 DIMTrfrKEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPEN 116
Cdd:PLN02405 60 DAMT---VEMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 117 IVHGSGSQLFDHVAECLGDFMEKRKiKDKKLP------VGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNK 190
Cdd:PLN02405 135 LMTGSSDALFDFIAAALAKFVATEG-EDFHLPpgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 191 AIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGddg 267
Cdd:PLN02405 214 AMERVG-LDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR--- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 268 SLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEknkeg 347
Cdd:PLN02405 290 SSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMH----- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 348 lHNAKEILTRLGVEPSDDDCVS---------VQHVCTIVSFRSANLVAATLGAILNRL-RDN-KGTPRLRTTVGVDGSLY 416
Cdd:PLN02405 365 -HDTSPDLKVVGSKLKDILEIPntslkmrkvVVELCNIVATRGARLSAAGIYGILKKLgRDTvKDGEKQKSVIAMDGGLF 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15991827 417 KTHPQYSRRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMVTA 457
Cdd:PLN02405 444 EHYTEFSKCMESTLKELLGEEvseSIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
45-457 |
2.44e-71 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 244.79 E-value: 2.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 45 EMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQ 124
Cdd:PLN02362 65 EMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 125 LFDHVAECLGDFMEKRKIKDKKLPV-----GFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGdYD 199
Cdd:PLN02362 143 LFDFIASSLKQFVEKEENGSEFSQVrrrelGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 200 ANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFgddGSLEDIRTEF 276
Cdd:PLN02362 222 MRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---WSSHLPRTSY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 277 DREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFeGRITPELLTRGKFNTSDVSAI-EKNKEGLHNAKEIL 355
Cdd:PLN02362 299 DIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARIL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 356 T-RLGV-EPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRL-RDNKG-----------TPRLRTTVGVDGSLYKTHPQ 421
Cdd:PLN02362 378 KeTLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgRDGSGgitsgrsrsdiQIMRRTVVAVEGGLYTNYTM 457
|
410 420 430
....*....|....*....|....*....|....*....
gi 15991827 422 YSRRFHKTLRRLVPDSDVRFLL---SESGSGKGAAMVTA 457
Cdd:PLN02362 458 FREYLHEALNEILGEDVAQHVIlkaTEDGSGIGSALLAA 496
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
57-457 |
7.55e-50 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 183.92 E-value: 7.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 57 TATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV--NHEKNQNVHMEsEVyDTPENIVHGSGSQLFDHVAECLG 134
Cdd:PLN02596 76 TTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLggKNEPISDLYRE-EI-SIPSNVLNGTSQELFDYIALELA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 135 DFMEKRKIKDKKLP-----VGFTFSFPCQQSKIDEAILITWtKRFKASGVEGADVVKLLNKAIKKRGdYDANIVAVVNDT 209
Cdd:PLN02596 154 KFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 210 VGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGddgSLEDIRTEFDREIDRGSLN 286
Cdd:PLN02596 232 IGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN---SCHLPITEFDASLDAESSN 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 287 PGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA----IEKNKEGLHNA-KEILTRLGVE 361
Cdd:PLN02596 309 PGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAmhqdTSEDHEVVNEKlKEIFGITDST 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 362 PSDDDCVSvqHVCTIVSFRSANLVAATLGAILNRLR--DNKgtprlRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPD--S 437
Cdd:PLN02596 389 PMAREVVA--EVCDIVAERGARLAGAGIVGIIKKLGriENK-----KSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSelS 461
|
410 420
....*....|....*....|.
gi 15991827 438 D-VRFLLSESGSGKGAAMVTA 457
Cdd:PLN02596 462 DnVVIEHSHGGSGAGALFLAA 482
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
483-907 |
1.91e-48 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 179.69 E-value: 1.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 483 LLEVKKRMRAEMELGLRKQTHNNavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIP 562
Cdd:PLN02596 56 LWEVADALVSDMTASLTAEETTT--LNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 563 IEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMP-----LGFTFSFPCQQTSLDAGILITWtKGFKATDCVGHDVVTLLR 637
Cdd:PLN02596 134 SNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDIN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 638 DAIKRrEEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFgdN 714
Cdd:PLN02596 213 RALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF--N 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 715 GCLDDIrTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 794
Cdd:PLN02596 290 SCHLPI-TEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15991827 795 ALLQV--RAILQQLGL-NSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIreNRGLDRLNVtVGVDGTLYKLHPHFS 871
Cdd:PLN02596 369 EDHEVvnEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKL--GRIENKKSV-VTVEGGLYEHYRVFR 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15991827 872 RIMHQTV-----KELSPkcNVSFLLSEDGSGKGAALITAVG 907
Cdd:PLN02596 446 NYLHSSVwemlgSELSD--NVVIEHSHGGSGAGALFLAACQ 484
|
|
| |
