|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
478-908 |
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: 908.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR--RRSVRMYNK 555
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRsgRRSVRMYNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 556 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLR 635
Cdd:cd24130 81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 636 EAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGCI 715
Cdd:cd24130 161 EAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGCI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 716 DDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 795
Cdd:cd24130 241 DDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 796 QVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQET 875
Cdd:cd24130 321 QVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQET 400
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 876 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 908
Cdd:cd24130 401 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
30-458 |
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: 879.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMES 109
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGL 349
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 350 ANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHK 429
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 148700155 430 VVRRLVPNCDVRFLLSESGSTKGAAMVTA 458
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
478-907 |
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: 858.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR---RRSVRMYN 554
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRsgkWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 555 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDML 634
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 635 REAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGC 714
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 715 IDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 794
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 795 LQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQE 874
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 875 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKR 907
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 ... |
30-458 |
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: 806.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMES 109
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGL 349
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 350 ANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHK 429
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 148700155 430 VVRRLVPNCDVRFLLSESGSTKGAAMVTA 458
Cdd:cd24089 401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
479-908 |
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: 793.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 479 LTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR---RRSVRMYNK 555
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRsgkKRTVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 556 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLR 635
Cdd:cd24127 82 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 636 EAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGCI 715
Cdd:cd24127 162 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 716 DDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 795
Cdd:cd24127 242 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 796 QVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQET 875
Cdd:cd24127 322 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQT 401
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 876 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 908
Cdd:cd24127 402 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
3-474 |
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: 788.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 3 AVHLVAFYFTKLKEDQIKKVDRFLYHMRLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLS 82
Cdd:cd24124 2 AAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 83 LDLGGSKFRVLKVQVSQEGQQNVQMESQFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNK 162
Cdd:cd24124 82 LDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 163 LEEGVLLSWTKKFKARGVQDTDVVNRLATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDM 242
Cdd:cd24124 162 IDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 243 SNIDLVEGDEGRMCINTEWGAFGDDGALEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGG 322
Cdd:cd24124 242 RHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 323 AKSSALHTKGKIETQHVAAMEMSKEGLANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKK 402
Cdd:cd24124 322 RITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148700155 403 LARLRTTVGMDGTLYKTHPQYPKRLHKVVRRLVPNCDVRFLLSESGSTKGAAMVTAVASRVQAQRKQIDKVL 474
Cdd:cd24124 402 TPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
478-909 |
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: 754.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR---RRSVRMYN 554
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRngkWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 555 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDML 634
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 635 REAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGC 714
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 715 IDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 794
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 795 LQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQE 874
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....*
gi 148700155 875 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRLQ 909
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
478-903 |
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: 701.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIRRRS-VRMYNKI 556
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSqVKMESEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 557 FAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLRE 636
Cdd:cd24019 81 YAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 637 AIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIEL---VDGDEGRMCVNTEWGGFGDNG 713
Cdd:cd24019 161 AIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGDNG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 714 CIDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESD-RL 792
Cdd:cd24019 241 VLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDnEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 793 ALLQVRRILQQLGL-DSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKrredqgLQHFKVTVGVDGTLYKLHPHFSRI 871
Cdd:cd24019 321 DFSNTREILKELGLeDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNR------MNRKEVTVGVDGSLYKYHPKFHKR 394
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 872 LQETVKELAP-QCDVTFMLSEDGSGKGAALITA 903
Cdd:cd24019 395 MHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
478-907 |
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: 673.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIRRRSVRMYNKIF 557
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 558 AIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLREA 637
Cdd:cd24129 81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 638 IKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGCIDD 717
Cdd:cd24129 161 ATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCLAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 718 IRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLALLQV 797
Cdd:cd24129 241 ISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALRQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 798 RRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQETVK 877
Cdd:cd24129 321 RAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQATVR 400
|
410 420 430
....*....|....*....|....*....|
gi 148700155 878 ELAPQCDVTFMLSEDGSGKGAALITAVAKR 907
Cdd:cd24129 401 ELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
30-458 |
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: 666.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMES 109
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGL 349
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 350 ANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHK 429
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 148700155 430 VVRRLVPNCDVRFLLSESGSTKGAAMVTA 458
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
30-458 |
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: 658.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVsqEGQQNVQMES 109
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTL--NGGSQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDL---VEGDEGRMCINTEWGAFGD 266
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 267 DGALEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSK 346
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 347 EG-LANTREILVDLGLEP-SESDCIAVQHVCTIVSFRSANLCAAALATILTRLRenkklaRLRTTVGMDGTLYKTHPQYP 424
Cdd:cd24019 319 EGdFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 148700155 425 KRLHKVVRRLVP-NCDVRFLLSESGSTKGAAMVTA 458
Cdd:cd24019 393 KRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
478-903 |
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: 632.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKI---RRRSVRMYN 554
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVndeKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 555 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDML 634
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 635 REAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGC 714
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 715 IDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 794
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 795 LQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQE 874
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 148700155 875 TVKELAPQCDVTFMLSEDGSGKGAALITA 903
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 ... |
478-903 |
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: 586.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR---RRSVRMYN 554
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSedgKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 555 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDML 634
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 635 REAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGC 714
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 715 IDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 794
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 795 LQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQE 874
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 148700155 875 TVKELAPQCDVTFMLSEDGSGKGAALITA 903
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 ... |
478-903 |
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: 576.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR---RRSVRMYN 554
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSdngLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 555 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDML 634
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 635 REAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDNGC 714
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 715 IDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 794
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 795 LQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRILQE 874
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 148700155 875 TVKELAPQCDVTFMLSEDGSGKGAALITA 903
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
466-915 |
0e+00 |
|
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase.
Pssm-ID: 466974 [Multi-domain] Cd Length: 473 Bit Score: 573.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 466 QRKQIDKVLALFQLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKI 545
Cdd:cd24124 17 QVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 546 ---RRRSVRMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKA 622
Cdd:cd24124 97 nheKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 623 TDCEGEDVVDMLREAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCV 702
Cdd:cd24124 177 SGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 703 NTEWGGFGDNGCIDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETK 782
Cdd:cd24124 257 NTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 783 FLSQIESDRLALLQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLY 862
Cdd:cd24124 337 DVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLY 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 148700155 863 KLHPHFSRILQETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRLQQPRKDI 915
Cdd:cd24124 417 KTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQI 469
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
30-462 |
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: 562.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMES 109
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGL 349
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 350 ANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHK 429
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 430 VVRRLVPNCDVRFLLSESGSTKGAAMVTAVASR 462
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
469-907 |
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: 551.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 469 QIDKVLALFQLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKI--- 545
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 546 --RRRSVRMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKAT 623
Cdd:cd24092 81 eeGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 624 DCEGEDVVDMLREAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVN 703
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 704 TEWGGFGDNGCIDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKF 783
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 784 LSQIESDRLALLQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYK 863
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 148700155 864 LHPHFSRILQETVKELAPQCDVTFMLSEDGSGKGAALITAVAKR 907
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 ... |
30-464 |
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: 539.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMES 109
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGL 349
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 350 ANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHK 429
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....*
gi 148700155 430 VVRRLVPNCDVRFLLSESGSTKGAAMVTAVASRVQ 464
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
30-463 |
1.97e-180 |
|
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: 527.94 E-value: 1.97e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMES 109
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGL 349
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 350 ANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHK 429
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400
|
410 420 430
....*....|....*....|....*....|....
gi 148700155 430 VVRRLVPNCDVRFLLSESGSTKGAAMVTAVASRV 463
Cdd:cd24127 401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
30-462 |
1.48e-179 |
|
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: 525.65 E-value: 1.48e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVsQEGQQNVQMES 109
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKI-RSGRRSVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGL 349
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 350 ANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHK 429
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 430 VVRRLVPNCDVRFLLSESGSTKGAAMVTAVASR 462
Cdd:cd24130 400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKR 432
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
21-462 |
1.36e-178 |
|
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: 523.67 E-value: 1.36e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 21 KVDRFLYHMRLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQ- 99
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 100 -EGQQNVQMESQFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKAR 178
Cdd:cd24092 81 eEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 179 GVQDTDVVNRLATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCIN 258
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 259 TEWGAFGDDGALEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQH 338
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 339 VAAMEMSKEGLANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYK 418
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 148700155 419 THPQYPKRLHKVVRRLVPNCDVRFLLSESGSTKGAAMVTAVASR 462
Cdd:cd24092 401 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
30-462 |
1.58e-178 |
|
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: 522.91 E-value: 1.58e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 30 RLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGqqnVQMES 109
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAG---VQITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 110 QFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGL 349
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 350 ANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHK 429
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 430 VVRRLVPNCDVRFLLSESGSTKGAAMVTAVASR 462
Cdd:cd24129 398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
482-901 |
4.02e-164 |
|
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: 485.99 E-value: 4.02e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 482 EQLLGVRDKMRAELEYGLKKKTHSLatvKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKI---RRRSVRMYNKiFA 558
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLEGDGGSL---PMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLdgnGGIFIIVQRK-YK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 559 IPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQ---LPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLR 635
Cdd:cd24018 78 IPDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 636 EAIKRRNeFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNI------ELVDGDEGRMCVNTEWGGF 709
Cdd:cd24018 158 NALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 710 GDNGCIDDiRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIES 789
Cdd:cd24018 237 DNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 790 DRLALLQ-VRRILQQLG--LDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREdqgLQHFKVTVGVDGTLYKLHP 866
Cdd:cd24018 316 DTSPDLDaVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS---LLPEPVTVGIDGSVYEKYP 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 148700155 867 HFSRILQETVKELAPQC---DVTFMLSEDGSGKGAALI 901
Cdd:cd24018 393 GFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
478-903 |
6.63e-154 |
|
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: 459.77 E-value: 6.63e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 478 QLTREQLLGVRDKMRAELEYGLKKKTHSLATVKMLPTYVYGMPDGTEKGKFLALDLG--GTNFRVLLVK---IRRRSVRM 552
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTltgIEGHRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 553 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVD 632
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 633 MLREAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGFGDN 712
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 713 GCIDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRL 792
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 793 ALLQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKLHPHFSRIL 872
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400
|
410 420 430
....*....|....*....|....*....|.
gi 148700155 873 QETVKELAPQCDVTFMLSEDGSGKGAALITA 903
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
34-458 |
9.11e-150 |
|
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type III hexokinase.
Pssm-ID: 466940 [Multi-domain] Cd Length: 431 Bit Score: 448.99 E-value: 9.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 34 ETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLG--GSKFRVLKVQVSQEGQQNVQMESQF 111
Cdd:cd24090 5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 112 YPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRLAT 191
Cdd:cd24090 85 FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 192 AMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGALE 271
Cdd:cd24090 165 AIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 272 DIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEMSKEGLAN 351
Cdd:cd24090 245 PVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 352 TREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKLARLRTTVGMDGTLYKTHPQYPKRLHKVV 431
Cdd:cd24090 325 VRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTV 404
|
410 420
....*....|....*....|....*..
gi 148700155 432 RRLVPNCDVRFLLSESGSTKGAAMVTA 458
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. ... |
33-456 |
1.17e-145 |
|
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: 438.22 E-value: 1.17e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 33 DETLVDIMARFQAEMEKGLGKDTNptaSVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNvQMESQFY 112
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGG---SLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIF-IIVQRKY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 113 PMPNEITRGNGTELFDYVADCLADFMKTKNLTH---KKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRL 189
Cdd:cd24018 77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDLqsdKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 190 ATAMKKhKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNI---DLVEG---DEGRMCINTEWGA 263
Cdd:cd24018 157 QNALDR-RGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGsvtKSDEMIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 264 FgdDGALEDI-RTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAM 342
Cdd:cd24018 236 F--DNEREVLpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 343 EMSKEG-LANTREILVDLGLEPSES--DCIAVQHVCTIVSFRSANLCAAALATILtrLRENKKLARlRTTVGMDGTLYKT 419
Cdd:cd24018 314 EADTSPdLDAVRDILKELLAIDNTTleDRKLIKRICELVSTRAARLSAAAIAAIL--LKRGSLLPE-PVTVGIDGSVYEK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 148700155 420 HPQYPKRLHKVVRRLVPNC---DVRFLLSESGSTKGAAMV 456
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) ... |
481-902 |
1.27e-137 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 414.75 E-value: 1.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 481 REQLLGVRDKMRAELEYGLKKKTHSLatvKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR-RRSVRMYNKIFAI 559
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEPSSL---KMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDgKGIEVTISKKYEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 560 PLEIMQGTGEELFDHIVQCIADFLDYMGLKgAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLREAIK 639
Cdd:cd24000 78 PDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 640 RRNeFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIelvDGDEGRMCVNTEWGGFGDNgciDDIR 719
Cdd:cd24000 157 KRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI---LLGDGGMIINTEWGNFGKN---SLPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 720 TQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQgllfrgqiserlrtrgifetkflsqiesdrlallqvrr 799
Cdd:cd24000 230 TEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE-------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 800 ilqqlgldstcedsiVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLqhfKVTVGVDGTLYKLHPHFSRILQETVKEL 879
Cdd:cd24000 272 ---------------ILRKICELVAERSARLAAAAIAALLRKTGDSPEK---KITIAVDGSLFEKYPGYRERLEEYLKEL 333
|
410 420
....*....|....*....|....
gi 148700155 880 -APQCDVTFMLSEDGSGKGAALIT 902
Cdd:cd24000 334 lGRGIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
33-457 |
1.51e-128 |
|
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: 391.25 E-value: 1.51e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 33 DETLVDIMARFQAEMEKGLGKDTnptASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSqeGQQNVQMESQFY 112
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEP---SSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLD--GKGIEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 113 PMPNEITRGNGTELFDYVADCLADFMKtKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRLATA 192
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLK-ENGLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 193 MKKHKdLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDlveGDEGRMCINTEWGAFGDDgalED 272
Cdd:cd24000 155 LKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL---LGDGGMIINTEWGNFGKN---SL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 273 IRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVgllfggakssalhtkgkietqhvaamemskeglant 352
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 353 reilvdlglepsesdciAVQHVCTIVSFRSANLCAAALATILTRLRENKKlarLRTTVGMDGTLYKTHPQYPKRLHKVVR 432
Cdd:cd24000 272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDSPE---KKITIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420
....*....|....*....|....*.
gi 148700155 433 RLVPN-CDVRFLLSESGSTKGAAMVT 457
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) ... |
479-905 |
3.55e-127 |
|
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: 390.87 E-value: 3.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 479 LTREQLLGVRDKMRAELEYGLKKKTHSLatVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKI---RRRSVRMYNK 555
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSK--LKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLggkEGRVDKQEYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 556 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMG----LKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVV 631
Cdd:cd24020 79 EVPIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 632 DMLREAIKRRNeFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGD---EGRMCVNTEWGG 708
Cdd:cd24020 159 ELLEEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 709 FGDNGCIddiRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIE 788
Cdd:cd24020 238 FRSSHLP---RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 789 SDRLA-LLQVRRILQQ-LGL-DSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHF--KVTVGVDGTLYK 863
Cdd:cd24020 315 EDDSPdLETVARILKDaLGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPaqRTVVAVDGGLYE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 148700155 864 LHPHFSRILQETVKEL--APQCD-VTFMLSEDGSGKGAALITAVA 905
Cdd:cd24020 395 HYPKFREYMQQALVELlgDEAADsVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
482-906 |
4.13e-117 |
|
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: 364.00 E-value: 4.13e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 482 EQLLGVRDKMRAELEYGLKKKThslATVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR-RRSVRMYNKIFAIP 560
Cdd:cd24087 2 ERLRKITDHFISELEKGLSKKG---GNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGgNGKFDITQSKYRLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 561 LEIMQGTGEELFDHIVQCIADFLD--YMGLKGAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLREAI 638
Cdd:cd24087 79 EELKTGTGEELWDFIADCLKKFVEehFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 639 KRRNeFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVD----GDEGRMCVNTEWGGFgDNGC 714
Cdd:cd24087 159 KKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DNEH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 715 IDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLA- 793
Cdd:cd24087 237 LVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEn 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 794 LLQVRRILQQ-LGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLqhfkvtVGVDGTLYKLHPHFSRIL 872
Cdd:cd24087 317 LEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCH------VAADGSVYNKYPGFKERA 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 148700155 873 QETVKEL--APQCD--VTFMLSEDGSGKGAALITAVAK 906
Cdd:cd24087 391 AQALKDIfgWDGEDdpIKTVPAEDGSGVGAAIIAALTK 428
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
43-460 |
5.40e-115 |
|
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth.
Pssm-ID: 466870 [Multi-domain] Cd Length: 439 Bit Score: 358.90 E-value: 5.40e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 43 FQAEMEKGLGKDtnPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMESQFYPMPNEITRGN 122
Cdd:cd24020 13 MVVEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVPIPPELMVGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 123 GTELFDYVADCLADFMKTKN----LTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRLATAMKKHKd 198
Cdd:cd24020 91 SEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 199 LDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGD---EGRMCINTEWGAFgDDGALEdiRT 275
Cdd:cd24020 170 LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-RSSHLP--RT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 276 EFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAM-EMSKEGLANTRE 354
Cdd:cd24020 247 EEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDDSPDLETVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 355 ILVD-LGLEP-SESDCIAVQHVCTIVSFRSANLCAAALATILTRL-RENKKLARL-RTTVGMDGTLYKTHPQYPKRLHKV 430
Cdd:cd24020 327 ILKDaLGIDDtSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGSSPAqRTVVAVDGGLYEHYPKFREYMQQA 406
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 431 VRRLVPNC---DVRFLLSESGSTKGAAMVTAVA 460
Cdd:cd24020 407 LVELLGDEaadSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
494-901 |
2.87e-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: 352.08 E-value: 2.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 494 ELEYGLKKKTHSLAtvkMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR-RRSVRMYNKIFAIPLEIMQG-TGEEL 571
Cdd:cd24088 14 QMEKGLAKHGKGMA---MIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHgDGTFSLRQEKSKIPDELKTGvTAKDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 572 FDHIVQCIADFL-DYMG--LKGAQ----LPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLREAIKRRNeF 644
Cdd:cd24088 91 FDYLAKSVEAFLtKHHGdsFAAGKdddrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDRQG-I 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 645 DLDIVAIVNDTVGTMMTCGYEDPRCE---IGLIAGTGSNVCYMEEMRNIELVDGDE------GRMCVNTEWGGFgdngci 715
Cdd:cd24088 170 PVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIKKLDDSSrvgkgkTHMVINTEWGSF------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 716 DDIR-----TQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLL---FRGQISERLRTRGIFETKFLSQI 787
Cdd:cd24088 244 DNELkvlptTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNTPYGLDTAVLSAI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 788 ESDRLALLQVRR--ILQQLGL-DSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRREDQGLQHFKVTVGVDGTLYKL 864
Cdd:cd24088 324 EIDSEAELRATRkvLLDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEINIGVDGSVIEF 403
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 148700155 865 HPHFSRILQETVKELAP----QCDVTFMLSEDGSGKGAALI 901
Cdd:cd24088 404 YPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
466-905 |
6.33e-109 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 343.97 E-value: 6.33e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 466 QRKQIDKVLALFQLTREQLLGVRDKMRAELEYGLK-KKTHSLA------TVKMLPTYVYGMPDGTEKGKFLALDLGGTNF 538
Cdd:PTZ00107 7 QRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEaHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 539 RVLLVKIR--RRSVRMYNKiFAIPLEIMQG---------TGEELFDHIVQCIADFLDYMGLK---GAQLPLGFTFSFPCR 604
Cdd:PTZ00107 87 RAVRVSLRggGKMERTQSK-FSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTFSFPCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 605 QTCIDKGTLVGWTKGF---KATD--CEGEDVVDMLREAIKRrNEFDLDIVAIVNDTVGTMMTCGYEDPR----CEIGLIA 675
Cdd:PTZ00107 166 QLSVNNAILIDWTKGFetgRATNdpVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVII 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 676 GTGSNVCYMEEMrniELVDGDEGRMcVNTEWGGFgdngCIDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRIL 755
Cdd:PTZ00107 245 GTGSNACYFEPE---VSAYGYAGTP-INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 756 IdltrqgLLFRGQISERLRTRGIFETKFLSQIESDRLALLQ-VRRILQQL-GLDSTCEDSIVVKEVCGAVSRRAAQMCGA 833
Cdd:PTZ00107 317 V------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQfSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148700155 834 GMAAIVEKRREDQGlqhfKVTVGVDGTLYKLHPHFSRILQETVKE-LAPQ-CDVTFMLSEDGSGKGAALITAVA 905
Cdd:PTZ00107 391 FIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
670-904 |
6.17e-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: 327.53 E-value: 6.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 670 EIGLIAGTGSNVCYMEEMRNIELVDGD---EGRMCVNTEWGGFGDNGCIDDIRTQYDKEVDEGSLNAGKQRYEKMTSGMY 746
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 747 LGEIVRRILIDLTRQGLLFRGQiSERLRTRGIFETKFLSQIESDR-LALLQVRRILQQ-LGL-DSTCEDSIVVKEVCGAV 823
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIeTVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 824 SRRAAQMCGAGMAAIVEKRREDQglqhfKVTVGVDGTLYKLHPHFSRILQETVKE-LAPQCDVTFMLSEDGSGKGAALIT 902
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 148700155 903 AV 904
Cdd:pfam03727 235 AV 236
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
225-459 |
4.10e-99 |
|
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: 309.42 E-value: 4.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 225 EVGVIIGTGTNACYMEDMSNIDLVEGD---EGRMCINTEWGAFGDDGALEDIRTEFDRELDLGSLNPGKQLFEKMISGLY 301
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 302 MGELVRLILLKMAKVGLLFGGaKSSALHTKGKIETQHVAAMEM-SKEGLANTREILVD-LGLE-PSESDCIAVQHVCTIV 378
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIESdPSEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 379 SFRSANLCAAALATILTRLRENKklarlRTTVGMDGTLYKTHPQYPKRLHKVVRRLV-PNCDVRFLLSESGSTKGAAMVT 457
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 148700155 458 AV 459
Cdd:pfam03727 235 AV 236
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
34-460 |
6.02e-99 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.
Pssm-ID: 466937 [Multi-domain] Cd Length: 428 Bit Score: 316.24 E-value: 6.02e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 34 ETLVDIMARFQAEMEKGLGKdtnPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVqMESQfYP 113
Cdd:cd24087 2 ERLRKITDHFISELEKGLSK---KGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDI-TQSK-YR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 114 MPNEITRGNGTELFDYVADCLADFMKTK--NLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRLAT 191
Cdd:cd24087 77 LPEELKTGTGEELWDFIADCLKKFVEEHfpGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 192 AMKKhKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVE----GDEGRMCINTEWGAFgDD 267
Cdd:cd24087 157 ALKK-RNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 268 GALEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEM-SK 346
Cdd:cd24087 235 EHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEdPF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 347 EGLANTREILV-DLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILtrlrenKKLARLRTTVGMDGTLYKTHPQYPK 425
Cdd:cd24087 315 ENLEDTDDLFQhFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAIC------KKRGYKTCHVAADGSVYNKYPGFKE 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 148700155 426 RLHKVVRRL----VPNCDVRFLLSESGSTKGAAMVTAVA 460
Cdd:cd24087 389 RAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
14-460 |
7.51e-98 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 313.43 E-value: 7.51e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 14 LKEDQIKKvdrflYHMRLSDETLVDIMARFQAEMEKGL-GKDtnptASVKMLPTFVrAIPDGS-ENGEFLSLDLGGSKFR 91
Cdd:COG5026 5 LVDAFLKR-----HGFDLSSIDLEEIAAKFQEEMEKGLeGKK----SSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 92 VLKVQVSQEGqqNVQMESQF-YPMPN---EITRgngTELFDYVADCLADFMKTKNlthkklPLGFTFSFPCRQNKLEEGV 167
Cdd:COG5026 75 VALVRFDGEG--TFEIENFKsFPLPGtssEITA---EEFFDFIADYIEPLLDESY------KLGFCFSFPAEQLPDKDGR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 168 LLSWTKKFKARGVQDTDVVNRLATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNC----EVGVIIGTGTNACYMEDMS 243
Cdd:COG5026 144 LIQWTKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 244 NIDLVEGDEGRMCINTEWGAFgdDGALediRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGlLFGGA 323
Cdd:COG5026 224 PIGKLPAYEGPMIINMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 324 KSSALHTKGKIETqhvAAMEMSKEGLANTREILVDLGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKKL 403
Cdd:COG5026 298 FSEVFETPYSLTT---VDMSRFLADPSDEKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTP 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 404 ARlRTTVGMDGTLYKTHPQYPKRLHKVVRR-LVPNCD--VRFLLSESGSTKGAAMVTAVA 460
Cdd:COG5026 375 LK-PHCIAIDGSTYEKMPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALN 433
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
33-456 |
1.79e-96 |
|
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: 310.48 E-value: 1.79e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 33 DETLVDIMARFQAEMEKGLgkdTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSqeGQQNVQMESQFY 112
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELH--GDGTFSLRQEKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 113 PMPNEITRGN-GTELFDYVADCLADFMKTKNLTH-------KKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTD 184
Cdd:cd24088 76 KIPDELKTGVtAKDLFDYLAKSVEAFLTKHHGDSfaagkddDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 185 VVNRLATAMKKhKDLDVDILALVNDTVGTMMTCAYDDPNCE---VGVIIGTGTNACYMEDMSNI---DLVEGDE---GRM 255
Cdd:cd24088 156 VVKLLQDELDR-QGIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklDDSSRVGkgkTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 256 CINTEWGAFgdDGALEDI-RTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAK---SSALHTK 331
Cdd:cd24088 235 VINTEWGSF--DNELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNdksPSALNTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 332 GKIETQHVAAMEMSKE-GLANTREILVD-LGLE-PSESDCIAVQHVCTIVSFRSANLCAAALATILtrLRENKKLARLRT 408
Cdd:cd24088 313 YGLDTAVLSAIEIDSEaELRATRKVLLDdLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAIL--IKTGALNKSYDG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 148700155 409 T--VGMDGTLYKTHPQYPKRLHKVVRRLVPNC----DVRFLLSESGSTKGAAMV 456
Cdd:cd24088 391 EinIGVDGSVIEFYPGFESMLREALRLLLIGAegekRIKIGIAKDGSGVGAALC 444
|
|
| PLN02914 |
PLN02914 |
hexokinase |
487-903 |
1.65e-94 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 306.81 E-value: 1.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 487 VRDKMRAELEYGLKKKTHSlaTVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIRRRSVRMYNKIF---AIPLEI 563
Cdd:PLN02914 58 VADAMAADMRAGLAVDGGG--DLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFeqvSIPQEL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 564 MQGTGEELFDHIVQCIADFLDYMGLK-----GAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLREAI 638
Cdd:PLN02914 136 MFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAM 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 639 KRRNeFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCYMEEMRNIELVDGDE---GRMCVNTEWGGFGDNGCI 715
Cdd:PLN02914 216 ERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSDGLPL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 716 ddirTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 795
Cdd:PLN02914 295 ----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNSDDL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 796 Q-VRRILQQ-LGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVEKRRED-QGLQHFKVT-VGVDGTLYKLHPHFSRI 871
Cdd:PLN02914 371 QaVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDsKGMIFGKRTvVAMDGGLYEKYPQYRRY 450
|
410 420 430
....*....|....*....|....*....|....*
gi 148700155 872 LQETVKEL---APQCDVTFMLSEDGSGKGAALITA 903
Cdd:PLN02914 451 MQDAVTELlglELSKNIAIEHTKDGSGIGAALLAA 485
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
477-905 |
2.53e-94 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 304.19 E-value: 2.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 477 FQLTREQLLGVRDKMRAELEYGLKKKTHSLatvKMLPTYVyGMPDG-TEKGKFLALDLGGTNFRVLLVKI-RRRSVRMYN 554
Cdd:COG5026 15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSL---KMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFdGEGTFEIEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 555 -KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMglkgaqLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDM 633
Cdd:COG5026 91 fKSFPLPGTSSEITAEEFFDFIADYIEPLLDES------YKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 634 LREAIKRRNEFDLDIVAIVNDTVGTMMTCGYEDP----RCEIGLIAGTGSNVCYMEEMRNIELVDGDEGRMCVNTEWGGF 709
Cdd:COG5026 165 LEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 710 gdNGCiddIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTRQGlLFRGQISERLRTRGIFETKFLSQI-- 787
Cdd:COG5026 245 --NKL---PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRFla 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 788 -ESDRLallqvrRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQMCGAGMAAIVekRREDQGLQHFK-VTVGVDGTLYKLH 865
Cdd:COG5026 319 dPSDEK------EILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGIL--LHLGPGKTPLKpHCIAIDGSTYEKM 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 148700155 866 PHFSRILQETVKE-LAPQCD--VTFMLSEDGSGKGAALITAVA 905
Cdd:COG5026 391 PGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALN 433
|
|
| PLN02914 |
PLN02914 |
hexokinase |
38-462 |
1.77e-93 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 304.12 E-value: 1.77e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 38 DIMArfqAEMEKGLGKDTNptASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMESQFYPMPNE 117
Cdd:PLN02914 60 DAMA---ADMRAGLAVDGG--GDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIPQE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 118 ITRGNGTELFDYVADCLADFMKTK----NLTH-KKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRLATA 192
Cdd:PLN02914 135 LMFGTSEELFDFIASGLANFVAKEggkfHLPEgRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 193 MKKHkDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDE---GRMCINTEWGAFGDDGA 269
Cdd:PLN02914 215 MERQ-GLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSDGLP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 270 LedirTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEM-SKEG 348
Cdd:PLN02914 294 L----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQdNSDD 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 349 LANTREILVD-LGLEPSESDCIAVQHVCTIVSFRSANLCAAALATILTRLRENKK--LARLRTTVGMDGTLYKTHPQYPK 425
Cdd:PLN02914 370 LQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKgmIFGKRTVVAMDGGLYEKYPQYRR 449
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 148700155 426 RLHKVVRRLV-PNCDVRFLL--SESGSTKGAAMVTAVASR 462
Cdd:PLN02914 450 YMQDAVTELLgLELSKNIAIehTKDGSGIGAALLAATNSK 489
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
469-664 |
2.78e-92 |
|
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: 289.79 E-value: 2.78e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 469 QIDKVLALFQLTREQLLGVRDKMRAELEYGLKKKTHSlaTVKMLPTYVYGMPDGTEKGKFLALDLGGTNFRVLLVKIR-R 547
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSS--SLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGgD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 548 RSVRMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLK---GAQLPLGFTFSFPCRQTCIDKGTLVGWTKGFKATD 624
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148700155 625 CEGEDVVDMLREAIKRRNEfDLDIVAIVNDTVGTMMTCGY 664
Cdd:pfam00349 159 VVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
12-461 |
4.91e-90 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 293.89 E-value: 4.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 12 TKLKEDQIKKVDRFLYHMRLSDETLVDIMARFQAEMEKGL-GKDTNPTA------SVKMLPTFVRAIPDGSENGEFLSLD 84
Cdd:PTZ00107 1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 85 LGGSKFRVLKVQVSQEGQqnvqMESQF--YPMPNEITRG---------NGTELFDYVADCLADFMKTKNL---THKKLPL 150
Cdd:PTZ00107 81 FGGTNFRAVRVSLRGGGK----MERTQskFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 151 GFTFSFPCRQNKLEEGVLLSWTKKFKA-----RGVQDTDVVNRLATAMKKHKdLDVDILALVNDTVGTMMTCAYDD---- 221
Cdd:PTZ00107 157 GFTFSFPCTQLSVNNAILIDWTKGFETgratnDPVEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKpknt 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 222 PNCEVGVIIGTGTNACYMEDMSnidLVEGDEGRMcINTEWGAFgdDGALEdiRTEFDRELDLGSLNPGKQLFEKMISGLY 301
Cdd:PTZ00107 236 PPCQVGVIIGTGSNACYFEPEV---SAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 302 MGELVRLILLkmakvgLLFGGAKSSALHTKGKIETQHvAAMEMS--KEGLANTREILVDL-GLEPSESDCIAVQHVCTIV 378
Cdd:PTZ00107 308 LGEISRRLIV------HLLQLKAPPKMWQSGSFESED-ASMILNdqSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 379 SFRSANLCAAALATILTRLREnkklARLRTTVGMDGTLYKTHPQYPKRLHKVVRRLV--PNCDVRFLLSESGSTKGAAMV 456
Cdd:PTZ00107 381 RGRAAQLAAAFIAAPAKKTRT----VQGKATVAIDGSVYVKNPWFRRLLQEYINSILgpDAGNVVFYLADDGSGKGAAII 456
|
....*
gi 148700155 457 TAVAS 461
Cdd:PTZ00107 457 AAMVA 461
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
21-219 |
1.01e-81 |
|
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: 261.67 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 21 KVDRFLYHMRLSDETLVDIMARFQAEMEKGLGKDTnpTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVsqE 100
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVEL--G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 101 GQQNVQMESQFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTH---KKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKA 177
Cdd:pfam00349 77 GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148700155 178 RGVQDTDVVNRLATAMKKHKdLDVDILALVNDTVGTMMTCAY 219
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAGAY 197
|
|
| PLN02405 |
PLN02405 |
hexokinase |
452-903 |
1.55e-80 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 269.39 E-value: 1.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 452 GAAMVTAVASRVQAQRKQID----KVLALFQLTRE-------QLLGVRDKMRAELEYGLKKKTHSlaTVKMLPTYVYGMP 520
Cdd:PLN02405 12 CAAAVCAAAALVVRRRMKSSgkwaRAMEILKEFEEdcatpigKLRQVADAMTVEMHAGLASEGGS--KLKMLISYVDNLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 521 DGTEKGKFLALDLGGTNFRVLLVKIRRRSVRMYNKIFA---IPLEIMQGTGEELFDHIVQCIADFL-----DYMGLKGAQ 592
Cdd:PLN02405 90 SGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEevsIPPHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 593 LPLGFTFSFPCRQTCIDKGTLVGWTKGFKATDCEGEDVVDMLREAIKRRNeFDLDIVAIVNDTVGTMMTCGYEDPRCEIG 672
Cdd:PLN02405 170 RELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-LDMRVSALVNDTIGTLAGGRYYNPDVVAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 673 LIAGTGSNVCYMEEMRNIELVDGD---EGRMCVNTEWGGFGDNGCiddIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGE 749
Cdd:PLN02405 249 VILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFRSSHL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 750 IVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLALLQV--RRILQQLGL-DSTCEDSIVVKEVCGAVSRR 826
Cdd:PLN02405 326 ILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVvgSKLKDILEIpNTSLKMRKVVVELCNIVATR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 827 AAQMCGAGMAAIVEKRRED--QGLQHFKVTVGVDGTLYKLHPHFSRILQETVKELAPQ---CDVTFMLSEDGSGKGAALI 901
Cdd:PLN02405 406 GARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEevsESIEVEHSNDGSGIGAALL 485
|
..
gi 148700155 902 TA 903
Cdd:PLN02405 486 AA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
459-903 |
2.09e-77 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 261.35 E-value: 2.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 459 VASRVQAQRK--QIDKVLALFQLTREQLLG----VRDKMRAELEYGLKKKTHSlaTVKMLPTYVYGMPDGTEKGKFLALD 532
Cdd:PLN02362 24 VGRRVKSRRKwrRVVGVLKELEEACETPVGrlrqVVDAMAVEMHAGLASEGGS--KLKMLLTFVDDLPTGSEIGTYYALD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 533 LGGTNFRVLLVKI--RRRSVRMYN-KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGlKGAQLP------LGFTFSFPC 603
Cdd:PLN02362 102 LGGTNFRVLRVQLggQRSSILSQDvERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEE-NGSEFSqvrrreLGFTFSFPV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 604 RQTCIDKGTLVGWTKGFKATDCEGEDVVDMLREAIKRRNeFDLDIVAIVNDTVGTMMTCGYEDPRCEIGLIAGTGSNVCY 683
Cdd:PLN02362 181 KQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 684 MEEMRNIELVDG---DEGRMCVNTEWGGFGDNGCiddIRTQYDKEVDEGSLNAGKQRYEKMTSGMYLGEIVRRILIDLTR 760
Cdd:PLN02362 260 LERTDAIIKCQGlltTSGSMVVNMEWGNFWSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 761 QGLLFrGQISERLRTRGIFETKFLSQI-ESDRLALLQVRRILQQ-LGL-DSTCEDSIVVKEVCGAVSRRAAQMCGAGMAA 837
Cdd:PLN02362 337 ESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARILKEtLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 838 IVEK-------------RREDQGLQHfKVTVGVDGTLYKLHPHFSRILQETVKELAPQ---CDVTFMLSEDGSGKGAALI 901
Cdd:PLN02362 416 ILKKigrdgsggitsgrSRSDIQIMR-RTVVAVEGGLYTNYTMFREYLHEALNEILGEdvaQHVILKATEDGSGIGSALL 494
|
..
gi 148700155 902 TA 903
Cdd:PLN02362 495 AA 496
|
|
| PLN02405 |
PLN02405 |
hexokinase |
46-461 |
4.04e-74 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 252.06 E-value: 4.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 46 EMEKGLGKDTNptASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMESQFYPMPNEITRGNGTE 125
Cdd:PLN02405 65 EMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 126 LFDYVADCLADFMKTKN-----LTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRLATAMKKhKDLD 200
Cdd:PLN02405 143 LFDFIAAALAKFVATEGedfhlPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMER-VGLD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 201 VDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGD---EGRMCINTEWGAFGDDGAledIRTEF 277
Cdd:PLN02405 222 MRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFRSSHL---PLTEY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 278 DRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAKSSALHTKGKIETQHVAAMEM-SKEGLANTREIL 356
Cdd:PLN02405 299 DHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHdTSPDLKVVGSKL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 357 VDLgLEPSESDC---IAVQHVCTIVSFRSANLCAAALATILTRLREN--KKLARLRTTVGMDGTLYKTHPQYPKRLHKVV 431
Cdd:PLN02405 379 KDI-LEIPNTSLkmrKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHYTEFSKCMESTL 457
|
410 420 430
....*....|....*....|....*....|...
gi 148700155 432 RRLV---PNCDVRFLLSESGSTKGAAMVTAVAS 461
Cdd:PLN02405 458 KELLgeeVSESIEVEHSNDGSGIGAALLAASHS 490
|
|
| PLN02362 |
PLN02362 |
hexokinase |
36-470 |
7.10e-72 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 246.33 E-value: 7.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 36 LVDIMArfqAEMEKGLGKDTNptASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVsqeGQQNVQMESQ---FY 112
Cdd:PLN02362 58 VVDAMA---VEMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQL---GGQRSSILSQdveRH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 113 PMPNEITRGNGTELFDYVADCLADFM-KTKNLTH----KKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVN 187
Cdd:PLN02362 130 PIPQHLMNSTSEVLFDFIASSLKQFVeKEENGSEfsqvRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 188 RLATAMKKhKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEG---DEGRMCINTEWGAF 264
Cdd:PLN02362 210 CLQGALNR-RGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 265 GDDGAledIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGGAkSSALHTKGKIETQHVAAM-E 343
Cdd:PLN02362 289 WSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGPV-SSRLSTPFVLRTPSVAAMhE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 344 MSKEGLANTREILVDlGLEPSESDCIA---VQHVCTIVSFRSANLCAAALATILTRL-------------RENKKLARlR 407
Cdd:PLN02362 365 DDSPELQEVARILKE-TLGISEVPLKVrklVVKICDVVTRRAARLAAAGIVGILKKIgrdgsggitsgrsRSDIQIMR-R 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148700155 408 TTVGMDGTLYKTHPQYPKRLHKVVRRLVPNCDVRFLL---SESGSTKGAAMVTAVASRVQAQRKQI 470
Cdd:PLN02362 443 TVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVIlkaTEDGSGIGSALLAASYSSYSVDTVQL 508
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
449-903 |
2.82e-50 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 185.08 E-value: 2.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 449 STKGAAMVTAVA-------SRVQAQRKQIDKVLALFqlTRE------QLLGVRDKMRAELEYGLKKKTHSlaTVKMLPTY 515
Cdd:PLN02596 10 ATVATVAAVAAAvlmgrwkRRKERQWKHTQRILRKF--AREcatpvsKLWEVADALVSDMTASLTAEETT--TLNMLVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 516 VYGMPDGTEKGKFLALDLGGTNFRVLLVKIRRRS---VRMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAQ 592
Cdd:PLN02596 86 VASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNepiSDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 593 LP-----LGFTFSFPCRQTCIDKGTLVGWtKGFKATDCEGEDVVDMLREAIKRRNeFDLDIVAIVNDTVGTMMTCGYEDP 667
Cdd:PLN02596 166 TPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDTIGNLAGGRYYNK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 668 RCEIGLIAGTGSNVCYMEEMRNIELVDG---DEGRMCVNTEWGGFgdNGCIDDIrTQYDKEVDEGSLNAGKQRYEKMTSG 744
Cdd:PLN02596 244 DTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF--NSCHLPI-TEFDASLDAESSNPGSRIFEKLTSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 745 MYLGEIVRRILIDLTRQGLLFRGQISERLRTRGIFETKFLSQIESDRLALLQV--RRILQQLGL-DSTCEDSIVVKEVCG 821
Cdd:PLN02596 321 MYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVvnEKLKEIFGItDSTPMAREVVAEVCD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 822 AVSRRAAQMCGAGMAAIVEK--RREDQglqhfKVTVGVDGTLYKLHPHFSRILQETVKELAP---QCDVTFMLSEDGSGK 896
Cdd:PLN02596 401 IVAERGARLAGAGIVGIIKKlgRIENK-----KSVVTVEGGLYEHYRVFRNYLHSSVWEMLGselSDNVVIEHSHGGSGA 475
|
....*..
gi 148700155 897 GAALITA 903
Cdd:PLN02596 476 GALFLAA 482
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
15-458 |
4.51e-47 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 175.84 E-value: 4.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 15 KEDQIKKVDRFLYHMRLSDET----LVDIMARFQAEMEKGLGKDTnpTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKF 90
Cdd:PLN02596 31 KERQWKHTQRILRKFARECATpvskLWEVADALVSDMTASLTAEE--TTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 91 RVLKVQVSQEGQQNVQMESQFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLP-----LGFTFSFPCRQNKLEE 165
Cdd:PLN02596 109 LLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 166 GVLLSWtKKFKARGVQDTDVVNRLATAMKKHkDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNI 245
Cdd:PLN02596 189 GSAIKW-KSFSADDTVGKALVNDINRALEKH-GLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 246 DLVEG---DEGRMCINTEWGAFGddgALEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLFGG 322
Cdd:PLN02596 267 PKWQSpspESQEIVISTEWGNFN---SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 323 AKSSALHTKGKIETQHVAAM--EMSKE-GLANTR--EILVDLGLEPSESDCIAvqHVCTIVSFRSANLCAAALATILtrl 397
Cdd:PLN02596 344 TLPPKLTTPYLLRSPDMAAMhqDTSEDhEVVNEKlkEIFGITDSTPMAREVVA--EVCDIVAERGARLAGAGIVGII--- 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148700155 398 renKKLARL---RTTVGMDGTLYKTHPQYPKRLHKVVRRLVPN---CDVRFLLSESGSTKGAAMVTA 458
Cdd:PLN02596 419 ---KKLGRIenkKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSelsDNVVIEHSHGGSGAGALFLAA 482
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
523-654 |
8.37e-04 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 42.58 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148700155 523 TEKGKFLALDLGGTNFRVLLV----KIRRRSVrmynkifaIPLEImQGTGEELFDHIVQCIADFLDYMGLKGAQLpLGFT 598
Cdd:COG1940 2 PDAGYVIGIDIGGTKIKAALVdldgEVLARER--------IPTPA-GAGPEAVLEAIAELIEELLAEAGISRGRI-LGIG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148700155 599 FSFP-----CRQTCIDKGTLVGWtkgfkatdcEGEDVVDMLREAIKRRnefdldiVAIVND 654
Cdd:COG1940 72 IGVPgpvdpETGVVLNAPNLPGW---------RGVPLAELLEERLGLP-------VFVEND 116
|
|
| ASKHA_NBD_NAGK_meta |
cd24078 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
625-680 |
3.43e-03 |
|
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. Members in this family are mainly from metazoa.
Pssm-ID: 466928 [Multi-domain] Cd Length: 314 Bit Score: 40.64 E-value: 3.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 148700155 625 CEGEDVVDMLREAIKRRNEFDLDIVAIVNDTVGTMMTCgyedprCEIG---LIAGTGSN 680
Cdd:cd24078 75 AEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATA------FENGgivLISGTGSN 127
|
|
| |
