|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
480-915 |
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: 876.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNN 559
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGE 719
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLAL 799
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 800 RQVRSILQHLGLTsSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMR 879
Cdd:cd24128 321 LQVRAILQHLGLE-STCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMH 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 47085787 880 ETLRDLAPNCEVSLVQSEDGSGKGAALITAVACRLR 915
Cdd:cd24128 400 ETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
30-460 |
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: 862.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMEN 109
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDDGA 269
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 270 LDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENRKddE 349
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEK--D 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 350 GIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFARRL 429
Cdd:cd24125 319 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 47085787 430 NKMVRSLVPDCDVRFLRSEDGSGKGAAMVTA 460
Cdd:cd24125 399 HKTVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
480-913 |
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: 814.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNN 559
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGE 719
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLAL 799
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 800 RQVRSILQHLGLtSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMR 879
Cdd:cd24091 321 LQVRAILQQLGL-DSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMH 399
|
410 420 430
....*....|....*....|....*....|....
gi 47085787 880 ETLRDLAPNCEVSLVQSEDGSGKGAALITAVACR 913
Cdd:cd24091 400 ETVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
2-476 |
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: 783.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 2 IATQLLAYYFTELHHDHVQKVDKYLYHMRLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFL 81
Cdd:cd24124 1 IAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 82 ALDLGGTNFRVLLVKVSSNGMQKVEMENQIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQT 161
Cdd:cd24124 81 ALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 162 KLDESFLVSWTKGFKASGVEGKDVVSLLRKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEE 241
Cdd:cd24124 161 KIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 242 MRHLELVDGDEGRMCVNMEWGAFGDDGALDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQ 321
Cdd:cd24124 241 LRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 322 GHTTPDLLTTGHFQTSFVSAIEnrKDDEGIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRD 401
Cdd:cd24124 321 GRITPELLTRGKFNTSDVSAIE--KNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRD 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47085787 402 NKASDRLRTSIGVDGSVYKNHPEFARRLNKMVRSLVPDCDVRFLRSEDGSGKGAAMVTAVAYRLAKQHAERQRVL 476
Cdd:cd24124 399 NKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
30-460 |
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: 779.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMEN 109
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDDGA 269
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 270 LDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIEnrKDDE 349
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIE--KEKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 350 GIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFARRL 429
Cdd:cd24089 319 GLANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 47085787 430 NKMVRSLVPDCDVRFLRSEDGSGKGAAMVTA 460
Cdd:cd24089 399 HKAVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
480-914 |
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: 777.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNN 559
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGE 719
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLAL 799
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 800 RQVRSILQHLGLtSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMR 879
Cdd:cd24127 321 LQVRAILQQLGL-NSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMH 399
|
410 420 430
....*....|....*....|....*....|....*
gi 47085787 880 ETLRDLAPNCEVSLVQSEDGSGKGAALITAVACRL 914
Cdd:cd24127 400 QTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
30-460 |
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: 728.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMEN 109
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDDGA 269
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 270 LDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENRKddE 349
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYK--E 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 350 GIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFARRL 429
Cdd:cd24126 319 GLYNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 47085787 430 NKMVRSLVPDCDVRFLRSEDGSGKGAAMVTA 460
Cdd:cd24126 399 HKVVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
480-914 |
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: 721.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGkRRNVEMNN 559
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSG-RRSVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGE 719
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLAL 799
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 800 RQVRSILQHLGLtSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMR 879
Cdd:cd24130 320 LQVRRILQQLGL-DSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQ 398
|
410 420 430
....*....|....*....|....*....|....*
gi 47085787 880 ETLRDLAPNCEVSLVQSEDGSGKGAALITAVACRL 914
Cdd:cd24130 399 ETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
480-909 |
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: 719.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRrnVEMNN 559
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQ--VKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVEL---VDGDEGRMCVNMEWGAFGD 716
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 717 QGELDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESD- 795
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 796 RLALRQVRSILQHLGLTSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRglnqlsITVGVDGTLYKLHPHFA 875
Cdd:cd24019 319 EGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKE------VTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 47085787 876 TIMRETLRDLAP-NCEVSLVQSEDGSGKGAALITA 909
Cdd:cd24019 393 KRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
30-460 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition.
Pssm-ID: 466869 [Multi-domain] Cd Length: 427 Bit Score: 714.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVssNGMQKVEMEN 109
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTL--NGGSQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLEL---VDGDEGRMCVNMEWGAFGD 266
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 267 DGALDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENRK 346
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 347 DDEgIVSAEQVLRGLGL-DPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRdnkasdRLRTSIGVDGSVYKNHPEF 425
Cdd:cd24019 319 EGD-FSNTREILKELGLeDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKF 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 47085787 426 ARRLNKMVRSLVP-DCDVRFLRSEDGSGKGAAMVTA 460
Cdd:cd24019 392 HKRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
480-913 |
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: 687.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVrggKRRNVEMNN 559
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV---GTAGVQITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGE 719
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLAL 799
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 800 RQVRSILQHLGLtSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMR 879
Cdd:cd24129 318 RQVRAILEDLGL-PLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQ 396
|
410 420 430
....*....|....*....|....*....|....
gi 47085787 880 ETLRDLAPNCEVSLVQSEDGSGKGAALITAVACR 913
Cdd:cd24129 397 ATVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
480-909 |
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: 646.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNN 559
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGE 719
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLAL 799
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 800 RQVRSILQHLGLTSSTcDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMR 879
Cdd:cd24089 321 ANAKEILTRLGLDPSE-DDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLH 399
|
410 420 430
....*....|....*....|....*....|
gi 47085787 880 ETLRDLAPNCEVSLVQSEDGSGKGAALITA 909
Cdd:cd24089 400 KAVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
30-464 |
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: 630.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMEN 109
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDDGA 269
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 270 LDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENrkDDE 349
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIES--DRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 350 GIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFARRL 429
Cdd:cd24091 319 ALLQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVM 398
|
410 420 430
....*....|....*....|....*....|....*
gi 47085787 430 NKMVRSLVPDCDVRFLRSEDGSGKGAAMVTAVAYR 464
Cdd:cd24091 399 HETVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
30-465 |
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: 604.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMEN 109
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDDGA 269
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 270 LDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENrkDDE 349
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIES--DRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 350 GIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFARRL 429
Cdd:cd24128 319 ALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVM 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 47085787 430 NKMVRSLVPDCDVRFLRSEDGSGKGAAMVTAVAYRL 465
Cdd:cd24128 399 HETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
30-465 |
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: 591.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMEN 109
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDDGA 269
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 270 LDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENrkDDE 349
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIES--DRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 350 GIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFARRL 429
Cdd:cd24127 319 ALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIM 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 47085787 430 NKMVRSLVPDCDVRFLRSEDGSGKGAAMVTAVAYRL 465
Cdd:cd24127 399 HQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
480-909 |
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: 590.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNN 559
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGE 719
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLAL 799
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 800 RQVRSILQHLGLTSSTcDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMR 879
Cdd:cd24125 321 RKAREVLMRLGLDPTQ-EDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLH 399
|
410 420 430
....*....|....*....|....*....|
gi 47085787 880 ETLRDLAPNCEVSLVQSEDGSGKGAALITA 909
Cdd:cd24125 400 KTVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
480-909 |
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: 587.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 480 RLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNN 559
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 560 KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGE 719
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLAL 799
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 800 RQVRSILQHLGLTSSTcDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMR 879
Cdd:cd24126 321 YNTREILSDLGLEPSE-EDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLH 399
|
410 420 430
....*....|....*....|....*....|
gi 47085787 880 ETLRDLAPNCEVSLVQSEDGSGKGAALITA 909
Cdd:cd24126 400 KVVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
30-465 |
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: 580.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSnGMQKVEMEN 109
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRS-GRRSVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDDGA 269
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 270 LDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENrkDDE 349
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIES--DRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 350 GIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFARRL 429
Cdd:cd24130 318 ALLQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRIL 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 47085787 430 NKMVRSLVPDCDVRFLRSEDGSGKGAAMVTAVAYRL 465
Cdd:cd24130 398 QETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
21-464 |
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: 570.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 21 KVDKYLYHMRLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSN 100
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 101 --GMQKVEMENQIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKAS 178
Cdd:cd24092 81 eeGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 179 GVEGKDVVSLLRKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVN 258
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 259 MEWGAFGDDGALDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSF 338
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 339 VSAIENRKDDEGIVSaeQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSV 418
Cdd:cd24092 321 VSQVESDTGDRKQIY--NILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSV 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 47085787 419 YKNHPEFARRLNKMVRSLVPDCDVRFLRSEDGSGKGAAMVTAVAYR 464
Cdd:cd24092 399 YKLHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
30-464 |
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: 569.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQkveMEN 109
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQ---ITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 110 QIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLL 189
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 190 RKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDDGA 269
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 270 LDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENrkDDE 349
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIES--DSL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 350 GIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFARRL 429
Cdd:cd24129 316 ALRQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLV 395
|
410 420 430
....*....|....*....|....*....|....*
gi 47085787 430 NKMVRSLVPDCDVRFLRSEDGSGKGAAMVTAVAYR 464
Cdd:cd24129 396 QATVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
473-913 |
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: 567.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 473 QRVLDTLRLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKR 552
Cdd:cd24092 3 EQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 553 RN--VEMNNKIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGC 630
Cdd:cd24092 83 GQwsVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 631 EGEDVASLLKDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNME 710
Cdd:cd24092 163 EGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 711 WGAFGDQGELDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLS 790
Cdd:cd24092 243 WGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 791 QIESDRLALRQVRSILQHLGLTSSTCDDSIlVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKL 870
Cdd:cd24092 323 QVESDTGDRKQIYNILSTLGLRPSTTDCDI-VRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 47085787 871 HPHFATIMRETLRDLAPNCEVSLVQSEDGSGKGAALITAVACR 913
Cdd:cd24092 402 HPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
474-916 |
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: 564.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 474 RVLDTLRLGRDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRR 553
Cdd:cd24124 23 KYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 554 NVEMNNKIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGE 633
Cdd:cd24124 103 NVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 634 DVASLLKDAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGA 713
Cdd:cd24124 183 DVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 714 FGDQGELDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIE 793
Cdd:cd24124 263 FGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 794 SDRLALRQVRSILQHLGLTSSTcDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPH 873
Cdd:cd24124 343 KNKEGLHNAKEILTRLGVEPSD-DDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQ 421
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 47085787 874 FATIMRETLRDLAPNCEVSLVQSEDGSGKGAALITAVACRLRD 916
Cdd:cd24124 422 YSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAE 464
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
30-460 |
9.14e-166 |
|
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: 490.20 E-value: 9.14e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 30 RLSNENLMDVSKRFRKEMDKGLGRDTNPTAAVKMLPTFVRSTPDGTETGDFLALDLG--GTNFRVLLVKVSSNGMQKVEM 107
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 108 ENQIYAISENIMRGCGSELFDHIAECLANFLEKLGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVS 187
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 188 LLRKAIRKRGDFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGRMCVNMEWGAFGDD 267
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 268 GALDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENRKD 347
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 348 deGIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASDRLRTSIGVDGSVYKNHPEFAR 427
Cdd:cd24090 321 --GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCS 398
|
410 420 430
....*....|....*....|....*....|...
gi 47085787 428 RLNKMVRSLVPDCDVRFLRSEDGSGKGAAMVTA 460
Cdd:cd24090 399 ILQGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
483-909 |
2.30e-161 |
|
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: 479.03 E-value: 2.30e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 483 RDQLLEVKKRMEEEMKRGLAKKTHNNATVKMLPTFVRSTPDGTERGDFLALDLG--GTNFRVLLVRVRGGKRRNVEMNNK 560
Cdd:cd24090 4 RAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 561 IYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLLK 640
Cdd:cd24090 84 EFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 641 DAIHRCEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFGDQGEL 720
Cdd:cd24090 164 DAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 721 DDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLALR 800
Cdd:cd24090 244 GPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 801 QVRSILQHLGLTSSTcDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLNRGLNQLSITVGVDGTLYKLHPHFATIMRE 880
Cdd:cd24090 324 RVRAILQDLGLSPSA-SDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQG 402
|
410 420
....*....|....*....|....*....
gi 47085787 881 TLRDLAPNCEVSLVQSEDGSGKGAALITA 909
Cdd:cd24090 403 TVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
484-907 |
2.58e-160 |
|
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: 476.36 E-value: 2.58e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 484 DQLLEVKKRMEEEMKRGLAKKThnnATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNNKiYT 563
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLEGDG---GSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-YK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 564 IPQDITQGTGEELFDHIVHCIADFLEYMGMKGAS---LPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLLK 640
Cdd:cd24018 78 IPDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 641 DAIHRcEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNV------ELVDGDEGRMCVNMEWGAF 714
Cdd:cd24018 158 NALDR-RGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 715 GDQGELDDIwTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIES 794
Cdd:cd24018 237 DNEREVLPL-TKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 795 DRLA-LRQVRSILQ-HLGLTSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLnrgLNQLSITVGVDGTLYKLHP 872
Cdd:cd24018 316 DTSPdLDAVRDILKeLLAIDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS---LLPEPVTVGIDGSVYEKYP 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 47085787 873 HFATIMRETLRDLAPNC---EVSLVQSEDGSGKGAALI 907
Cdd:cd24018 393 GFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
36-458 |
1.64e-157 |
|
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: 469.04 E-value: 1.64e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 36 LMDVSKRFRKEMDKGLgrdTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQkVEMENQIYAIS 115
Cdd:cd24018 4 LEEIVKHFLSEMEKGL---EGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGI-FIIVQRKYKIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 116 ENIMRGCGSELFDHIAECLANFLEKLGIK---EKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLLRKA 192
Cdd:cd24018 80 DEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 193 IRKRGdFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEM------RHLELVDGDEGRMCVNMEWGAFGD 266
Cdd:cd24018 160 LDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVsnikklTSPSGSVTKSDEMIINTEWGAFDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 267 DGALddL-RTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENr 345
Cdd:cd24018 239 EREV--LpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEA- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 346 kDDEG-IVSAEQVLRGLG--LDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASdrlRTSIGVDGSVYKNH 422
Cdd:cd24018 316 -DTSPdLDAVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLPE---PVTVGIDGSVYEKY 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 47085787 423 PEFARRLNKMVRSLVPDC---DVRFLRSEDGSGKGAAMV 458
Cdd:cd24018 392 PGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
33-459 |
5.32e-140 |
|
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: 420.91 E-value: 5.32e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 33 NENLMDVSKRFRKEMDKGLGRDTNPtaaVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGmqKVEMENQIY 112
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEPSS---LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKG--IEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 113 AISENIMRGCGSELFDHIAECLANFLEKLGIKeKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLLRKA 192
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 193 IRKRGDfDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHlelVDGDEGRMCVNMEWGAFGDDgalDD 272
Cdd:cd24000 155 LKKRGL-PVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN---SL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 273 LRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDgllfqghttpdllttghfqtsfvsaienrkddegiv 352
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 353 saeqvlrglgldptpedcvATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKASdrlRTSIGVDGSVYKNHPEFARRLNKM 432
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTGDSPEK---KITIAVDGSLFEKYPGYRERLEEY 329
|
410 420
....*....|....*....|....*...
gi 47085787 433 VRSLV-PDCDVRFLRSEDGSGKGAAMVT 459
Cdd:cd24000 330 LKELLgRGIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
483-908 |
2.76e-135 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 408.59 E-value: 2.76e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 483 RDQLLEVKKRMEEEMKRGLAKKThnnATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGkrRNVEMNNKIY 562
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEP---SSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGK--GIEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 563 TIPQDITQGTGEELFDHIVHCIADFLEYMGMKgASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLLKDA 642
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 643 IHRcEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNvelVDGDEGRMCVNMEWGAFGDQgelDD 722
Cdd:cd24000 155 LKK-RGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN---SL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 723 IWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFtakgllfrgklserlktrgifetkflsqiesdrlalrqv 802
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDL--------------------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 803 rsilqhlgltsstcdDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIrlnRGLNQLSITVGVDGTLYKLHPHFATIMRETL 882
Cdd:cd24000 269 ---------------ADEILRKICELVAERSARLAAAAIAALLRKT---GDSPEKKITIAVDGSLFEKYPGYRERLEEYL 330
|
410 420
....*....|....*....|....*..
gi 47085787 883 RDLAPN-CEVSLVQSEDGSGKGAALIT 908
Cdd:cd24000 331 KELLGRgIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
484-911 |
3.00e-120 |
|
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: 372.76 E-value: 3.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 484 DQLLEVKKRMEEEMKRGLAKKTHnnATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNNKIYT 563
Cdd:cd24020 4 SRLRQVADAMVVEMEAGLASEGG--SKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 564 IPQDITQGTGEELFDHIVHCIADFLEYMG----MKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLL 639
Cdd:cd24020 82 IPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 640 KDAIHRcEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGD---EGRMCVNMEWGAFgD 716
Cdd:cd24020 162 EEALER-QGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-R 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 717 QGELDdiWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDR 796
Cdd:cd24020 240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 797 LA-LRQVRSILQH-LGLTSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKI-RLNRGLNQLSIT-VGVDGTLYKLHP 872
Cdd:cd24020 318 SPdLETVARILKDaLGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGSSPAQRTvVAVDGGLYEHYP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 47085787 873 HFATIMRETLRDL---APNCEVSLVQSEDGSGKGAALITAVA 911
Cdd:cd24020 398 KFREYMQQALVELlgdEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
485-911 |
2.96e-119 |
|
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: 369.78 E-value: 2.96e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 485 QLLEVKKRMEEEMKRGLAKKTHNnatVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGgkRRNVEMNNKIYTI 564
Cdd:cd24087 3 RLRKITDHFISELEKGLSKKGGN---IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGG--NGKFDITQSKYRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 565 PQDITQGTGEELFDHIVHCIADFLE--YMGMKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLLKDA 642
Cdd:cd24087 78 PEELKTGTGEELWDFIADCLKKFVEehFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 643 IHRcEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVD----GDEGRMCVNMEWGAFgDQG 718
Cdd:cd24087 158 LKK-RNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DNE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 719 ELDDIWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLA 798
Cdd:cd24087 236 HLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 799 -LRQVRSILQH-LGLTsSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKirlnRGLNqlSITVGVDGTLYKLHPHFAT 876
Cdd:cd24087 316 nLEDTDDLFQHfFGLE-TTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYK--TCHVAADGSVYNKYPGFKE 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 47085787 877 IMRETLRDL----APNCEVSLVQSEDGSGKGAALITAVA 911
Cdd:cd24087 389 RAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
43-462 |
1.14e-118 |
|
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: 368.53 E-value: 1.14e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 43 FRKEMDKGLGRDtnPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMENQIYAISENIMRGC 122
Cdd:cd24020 13 MVVEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVPIPPELMVGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 123 GSELFDHIAECLANFLEKLG----IKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLLRKAIRKRGd 198
Cdd:cd24020 91 SEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 199 FDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGD---EGRMCVNMEWGAFgDDGALDdlRT 275
Cdd:cd24020 170 LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-RSSHLP--RT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 276 EFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENRKDDEGIVSAE 355
Cdd:cd24020 247 EEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSPDLETVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 356 QVLRGLGLDPTP-EDCVATQRVCQIVSTRAAHLCAASLAAVLRQI-RDNKASDRL-RTSIGVDGSVYKNHPEFARRLNKM 432
Cdd:cd24020 327 ILKDALGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGSSPAqRTVVAVDGGLYEHYPKFREYMQQA 406
|
410 420 430
....*....|....*....|....*....|...
gi 47085787 433 VRSLVPDC---DVRFLRSEDGSGKGAAMVTAVA 462
Cdd:cd24020 407 LVELLGDEaadSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
34-462 |
5.04e-115 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.
Pssm-ID: 466937 [Multi-domain] Cd Length: 428 Bit Score: 358.61 E-value: 5.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 34 ENLMDVSKRFRKEMDKGLgrdTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGmqKVEMENQIYA 113
Cdd:cd24087 2 ERLRKITDHFISELEKGL---SKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNG--KFDITQSKYR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 114 ISENIMRGCGSELFDHIAECLANFLEK--LGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLLRK 191
Cdd:cd24087 77 LPEELKTGTGEELWDFIADCLKKFVEEhfPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 192 AIRKRGdFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVD----GDEGRMCVNMEWGAFgDD 267
Cdd:cd24087 157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 268 GALDDLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENRKD 347
Cdd:cd24087 235 EHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 348 DEGIVSAEQVLRGLGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNKAsdrlrtSIGVDGSVYKNHPEFAR 427
Cdd:cd24087 315 ENLEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTC------HVAADGSVYNKYPGFKE 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 47085787 428 RLNKMVRSL----VPDCDVRFLRSEDGSGKGAAMVTAVA 462
Cdd:cd24087 389 RAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
485-907 |
4.47e-114 |
|
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: 356.71 E-value: 4.47e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 485 QLLEVKKRMEEEMKRGLAkktHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGgkRRNVEMNNKIYTI 564
Cdd:cd24088 3 KLDKLTAEFQRQMEKGLA---KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHG--DGTFSLRQEKSKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 565 PQDITQG-TGEELFDHIVHCIADFL-EYMGMKGAS------LPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVA 636
Cdd:cd24088 78 PDELKTGvTAKDLFDYLAKSVEAFLtKHHGDSFAAgkdddrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 637 SLLKDAIHRcEEFDLDVVAVVNDTVGTMMTCGYEDPQCE---VGLIVGTGTNACYMEEMSNVELVDGDE------GRMCV 707
Cdd:cd24088 158 KLLQDELDR-QGIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIKKLDDSSrvgkgkTHMVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 708 NMEWGAFGDQGELDDIwTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLL---FRGKLSERLKTRGIF 784
Cdd:cd24088 237 NTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNTPYGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 785 ETKFLSQIESDRLA-LRQVR-SILQHLGLTSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKI-RLNRGLNQlSITV 861
Cdd:cd24088 316 DTAVLSAIEIDSEAeLRATRkVLLDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTgALNKSYDG-EINI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 47085787 862 GVDGTLYKLHPHFATIMRETLRDLAPNCE----VSLVQSEDGSGKGAALI 907
Cdd:cd24088 395 GVDGSVIEFYPGFESMLREALRLLLIGAEgekrIKIGIAKDGSGVGAALC 444
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
34-458 |
3.79e-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: 351.70 E-value: 3.79e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 34 ENLMDVSKRFRKEMDKGLgrdTNPTAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGmqKVEMENQIYA 113
Cdd:cd24088 2 EKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDG--TFSLRQEKSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 114 ISENIMRGCGS-ELFDHIAECLANFLEK-------LGIKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDV 185
Cdd:cd24088 77 IPDELKTGVTAkDLFDYLAKSVEAFLTKhhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 186 VSLLRKAIRKRGdFDIDIVAVINDTVGTMMTCGYDDHHCE---IGLIVGTGTNACYMEEMRHLELVDGDE------GRMC 256
Cdd:cd24088 157 VKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIKKLDDSSrvgkgkTHMV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 257 VNMEWGAFgdDGALDDL-RTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHT--TPDLLTTgH 333
Cdd:cd24088 236 INTEWGSF--DNELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNdkSPSALNT-P 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 334 FQ--TSFVSAIENrkDDE-GIVSAEQVL-RGLGL-DPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLrqIRDNKASDRL 408
Cdd:cd24088 313 YGldTAVLSAIEI--DSEaELRATRKVLlDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAIL--IKTGALNKSY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 47085787 409 --RTSIGVDGSVYKNHPEFARRLNKMVRSLVP----DCDVRFLRSEDGSGKGAAMV 458
Cdd:cd24088 389 dgEINIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
12-462 |
7.85e-108 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 341.27 E-value: 7.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 12 TELHHDHVQKVDKYLYHMRLSNENLMDVSKRFRKEMDKGL-GRDTNPTA------AVKMLPTFVRSTPDGTETGDFLALD 84
Cdd:PTZ00107 1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 85 LGGTNFRVLLVKVSSNGmqKVEMENQIYAISENIMRGC---------GSELFDHIAECLANFLEKLGIKE---KKLPLGF 152
Cdd:PTZ00107 81 FGGTNFRAVRVSLRGGG--KMERTQSKFSLPKSALLGEkglldkkatATDLFDHIAKSIKKMMEENGDPEdlnKPVPVGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 153 TFSFPCQQTKLDESFLVSWTKGFKAS-----GVEGKDVVSLLRKAIrKRGDFDIDIVAVINDTVGTMMTCGYDDHH---- 223
Cdd:PTZ00107 159 TFSFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAF-KRNNVPANVVAVLNDTVGTLISCAYQKPKntpp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 224 CEIGLIVGTGTNACYMEEMrhlELVDGDEGRMcVNMEWGAFgdDGALDdlRTEFDREIDAGSLNPGKQLFEKMISGMYMG 303
Cdd:PTZ00107 238 CQVGVIIGTGSNACYFEPE---VSAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 304 ELVRLILVkmakdgLLFQGHTTPDLLTTGHFQTSFVSAIENRKdDEGIVSAEQVL-RGLGLDPTPEDCVATQRVCQIVST 382
Cdd:PTZ00107 310 EISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQ-SPDLQFSRQVIkEAWDVDLTDEDLYTIRKICELVRG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 383 RAAHLCAASLAAVLRQIRdnkaSDRLRTSIGVDGSVYKNHPEFARRLNKMVRSLVPD--CDVRFLRSEDGSGKGAAMVTA 460
Cdd:PTZ00107 383 RAAQLAAAFIAAPAKKTR----TVQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPdaGNVVFYLADDGSGKGAAIIAA 458
|
..
gi 47085787 461 VA 462
Cdd:PTZ00107 459 MV 460
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
675-910 |
2.22e-107 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.
Pssm-ID: 461028 Cd Length: 236 Bit Score: 331.38 E-value: 2.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 675 EVGLIVGTGTNACYMEEMSNVELVDGD---EGRMCVNMEWGAFGDQGELDDIWTEFDRAVDDQSTYPGRQRYEKMISGMY 751
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 752 LGEIVRNVLLHFTAKGLLFRGKlSERLKTRGIFETKFLSQIESDR-LALRQVRSILQ-HLGLTSSTCDDSILVKEVCSVV 829
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEeLLGIETVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 830 SKRAAQLCGAGLAAVVDKIRlnrglNQLSITVGVDGTLYKLHPHFATIMRETLRD-LAPNCEVSLVQSEDGSGKGAALIT 908
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIG-----RDKKVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 47085787 909 AV 910
Cdd:pfam03727 235 AV 236
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
225-461 |
9.79e-105 |
|
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: 324.44 E-value: 9.79e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 225 EIGLIVGTGTNACYMEEMRHLELVDGD---EGRMCVNMEWGAFGDDGALDDLRTEFDREIDAGSLNPGKQLFEKMISGMY 301
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 302 MGELVRLILVKMAKDGLLFQGHtTPDLLTTGHFQTSFVSAIENRkDDEGIVSAEQVL-RGLGL-DPTPEDCVATQRVCQI 379
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESD-PSEDLETTREILeELLGIeTVTEEDRKIVRRICEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 380 VSTRAAHLCAASLAAVLRQIRDNKasdrlRTSIGVDGSVYKNHPEFARRLNKMVRSLV-PDCDVRFLRSEDGSGKGAAMV 458
Cdd:pfam03727 159 VSTRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVLAEDGSGVGAALI 233
|
...
gi 47085787 459 TAV 461
Cdd:pfam03727 234 AAV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
464-911 |
5.59e-102 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 325.86 E-value: 5.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 464 RLAKQHAERQRVLDTLRLGRDQLLEVKKRMEEEMKRGL-AKKTHNNA------TVKMLPTFVRSTPDGTERGDFLALDLG 536
Cdd:PTZ00107 3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 537 GTNFRVLLVRVRGGKRrnVEMNNKIYTIPQDITQG---------TGEELFDHIVHCIADFLEYMGMK---GASLPLGFTF 604
Cdd:PTZ00107 83 GTNFRAVRVSLRGGGK--MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 605 SFPCHQDKLDQGILIKWTKGFKAS-----GCEGEDVASLLKDAIHRcEEFDLDVVAVVNDTVGTMMTCGYED----PQCE 675
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 676 VGLIVGTGTNACYMEEMSnveLVDGDEGRMcVNMEWGAFGDQGELddiwTEFDRAVDDQSTYPGRQRYEKMISGMYLGEI 755
Cdd:PTZ00107 240 VGVIIGTGSNACYFEPEV---SAYGYAGTP-INMECGNFDSKLPI----TPYDLEMDWYTPNRGRQQFEKMISGAYLGEI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 756 VRNVLLHftakglLFRGKLSERLKTRGIFETKFLSQIESDRL-ALRQVRSILQHLGLTSSTCDDSILVKEVCSVVSKRAA 834
Cdd:PTZ00107 312 SRRLIVH------LLQLKAPPKMWQSGSFESEDASMILNDQSpDLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAA 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47085787 835 QLCGAGLAAVVDKIRLNRGLnqlsITVGVDGTLYKLHPHFATIMRETLRD-LAPN-CEVSLVQSEDGSGKGAALITAVA 911
Cdd:PTZ00107 386 QLAAAFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
27-462 |
8.66e-101 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 321.52 E-value: 8.66e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 27 YHMRLSNENLMDVSKRFRKEMDKGL-GRDtnptAAVKMLPTFVrSTPDG-TETGDFLALDLGGTNFRVLLVKVSSNGmqK 104
Cdd:COG5026 13 HGFDLSSIDLEEIAAKFQEEMEKGLeGKK----SSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEG--T 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 105 VEMEN-QIYAiseniMRGCGS-----ELFDHIAECLANFLEKlgikekKLPLGFTFSFPCQQTKLDESFLVSWTKGFKAS 178
Cdd:COG5026 86 FEIENfKSFP-----LPGTSSeitaeEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 179 GVEGKDVVSLLRKAIRKRGDFDIDIVAVINDTVGTMMTCGY----DDHHCEIGLIVGTGTNACYMEEMRHLELVDGDEGR 254
Cdd:COG5026 155 GVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYadpdDGYSGYIGSILGTGHNTCYLEPNAPIGKLPAYEGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 255 MCVNMEWGAFgdDGAlddLRTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGlLFQGHTTPDLLTTGHF 334
Cdd:COG5026 235 MIINMESGNF--NKL---PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 335 QTSFVSA-IENRKDDEGIVSaeQVLRglglDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIrDNKASDRLRTSIG 413
Cdd:COG5026 309 TTVDMSRfLADPSDEKEILS--QCLE----AGSEEDREILREIADAIVERAARLVAATLAGILLHL-GPGKTPLKPHCIA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 47085787 414 VDGSVYKNHPEFARRLNK-MVRSLVPDCD--VRFLRSEDGSGKGAAMVTAVA 462
Cdd:COG5026 382 IDGSTYEKMPGLAEKIEYaLQEYLLGEKGryVEFVLVENASLLGAAIAAALN 433
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
485-912 |
2.33e-97 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 312.28 E-value: 2.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 485 QLLEVKKRMEEEMKRGLAkktHNNATVKMLPTFVrSTPDG-TERGDFLALDLGGTNFRVLLVRVrGGKRRNVEMNNKIYT 563
Cdd:COG5026 21 DLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF-DGEGTFEIENFKSFP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 564 IPQDITQGTGEELFDHIVHCIADFLEYmgmkgaSLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLLKDAI 643
Cdd:COG5026 96 LPGTSSEITAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 644 HRCEEFDLDVVAVVNDTVGTMMTCGYEDPQC----EVGLIVGTGTNACYMEEMSNVELVDGDEGRMCVNMEWGAFgDQGE 719
Cdd:COG5026 170 ARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNF-NKLP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 720 LddiwTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGlLFRGKLSERLKTRGIFETK----FLSQIESD 795
Cdd:COG5026 249 R----TKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVdmsrFLADPSDE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 796 RLALRQVrsilqhlgLTSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVdkIRLNRGLNQLS-ITVGVDGTLYKLHPHF 874
Cdd:COG5026 324 KEILSQC--------LEAGSEEDREILREIADAIVERAARLVAATLAGIL--LHLGPGKTPLKpHCIAIDGSTYEKMPGL 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 47085787 875 ATIMRETLRD-LAPNCE--VSLVQSEDGSGKGAALITAVAC 912
Cdd:COG5026 394 AEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
|
|
| PLN02914 |
PLN02914 |
hexokinase |
486-909 |
3.57e-96 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 311.43 E-value: 3.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 486 LLEVKKRMEEEMKRGLAkkTHNNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNNKIYTIP 565
Cdd:PLN02914 55 LRHVADAMAADMRAGLA--VDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 566 QDITQGTGEELFDHIVHCIADFLEYMGMK-----GASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLLK 640
Cdd:PLN02914 133 QELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 641 DAIHRcEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIVGTGTNACYMEEMSNVELVDGDE---GRMCVNMEWGAFGDQ 717
Cdd:PLN02914 213 EAMER-QGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSDG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 718 GELddiwTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRL 797
Cdd:PLN02914 292 LPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 798 -ALRQVRSILQHLGLTSSTCDDSILVKEVCSVVSKRAAQLCGAGLAAVVDKIRLN-RGLNQLSIT-VGVDGTLYKLHPHF 874
Cdd:PLN02914 368 dDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDsKGMIFGKRTvVAMDGGLYEKYPQY 447
|
410 420 430
....*....|....*....|....*....|....*...
gi 47085787 875 ATIMRETLRDL---APNCEVSLVQSEDGSGKGAALITA 909
Cdd:PLN02914 448 RRYMQDAVTELlglELSKNIAIEHTKDGSGIGAALLAA 485
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
21-219 |
9.59e-94 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.
Pssm-ID: 459774 [Multi-domain] Cd Length: 197 Bit Score: 294.03 E-value: 9.59e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 21 KVDKYLYHMRLSNENLMDVSKRFRKEMDKGLGRDTNPTaaVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSN 100
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSS--LKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 101 GmqKVEMENQIYAISENIMRGCGSELFDHIAECLANFLEKLGIK---EKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKA 177
Cdd:pfam00349 79 G--KFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 47085787 178 SGVEGKDVVSLLRKAIRKRGDfDIDIVAVINDTVGTMMTCGY 219
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
473-669 |
1.50e-90 |
|
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: 285.55 E-value: 1.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 473 QRVLDTLRLGRDQLLEVKKRMEEEMKRGLAKKThnNATVKMLPTFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKR 552
Cdd:pfam00349 3 EELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 553 rnVEMNNKIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMK---GASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASG 629
Cdd:pfam00349 81 --FEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47085787 630 CEGEDVASLLKDAIHRCEEfDLDVVAVVNDTVGTMMTCGY 669
Cdd:pfam00349 159 VVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| PLN02914 |
PLN02914 |
hexokinase |
36-460 |
5.32e-90 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 294.87 E-value: 5.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 36 LMDVSKRFRKEMDKGLGRDTNptAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMENQIYAIS 115
Cdd:PLN02914 55 LRHVADAMAADMRAGLAVDGG--GDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 116 ENIMRGCGSELFDHIAECLANFLEKLGIK-----EKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLLR 190
Cdd:PLN02914 133 QELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 191 KAIRKRGdFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEE---MRHLELVDGDEGRMCVNMEWGAFGDD 267
Cdd:PLN02914 213 EAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERtdaIPKLQGQKSSSGRTIINTEWGAFSDG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 268 GALddlrTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFqGHTTPDLLTTGH-FQTSFVSAIENRK 346
Cdd:PLN02914 292 LPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLF-GHFVPEKLSTPFaLRTPHLCAMQQDN 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 347 DDEgIVSAEQVLRG-LGLDPTPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIRDNkaSDRL----RTSIGVDGSVYKN 421
Cdd:PLN02914 367 SDD-LQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEED--SKGMifgkRTVVAMDGGLYEK 443
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 47085787 422 HPEFARRLNKMVRSLVPD---CDVRFLRSEDGSGKGAAMVTA 460
Cdd:PLN02914 444 YPQYRRYMQDAVTELLGLelsKNIAIEHTKDGSGIGAALLAA 485
|
|
| PLN02362 |
PLN02362 |
hexokinase |
456-909 |
5.74e-81 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 270.98 E-value: 5.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 456 AMVTAVAYRLAKQHAERQRVLDTLR---------LGRdqLLEVKKRMEEEMKRGLAkkTHNNATVKMLPTFVRSTPDGTE 526
Cdd:PLN02362 18 AVAAVMVGRRVKSRRKWRRVVGVLKeleeacetpVGR--LRQVVDAMAVEMHAGLA--SEGGSKLKMLLTFVDDLPTGSE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 527 RGDFLALDLGGTNFRVLLVRVrGGKRRNVEMNN-KIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLP-----L 600
Cdd:PLN02362 94 IGTYYALDLGGTNFRVLRVQL-GGQRSSILSQDvERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEENGSEFSQvrrreL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 601 GFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLLKDAIHRcEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLIV 680
Cdd:PLN02362 173 GFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNR-RGLDMRVAALVNDTVGTLALGHYHDPDTVAAVII 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 681 GTGTNACYMEEMSNVELVDG---DEGRMCVNMEWGAFgdqgelddiW------TEFDRAVDDQSTYPGRQRYEKMISGMY 751
Cdd:PLN02362 252 GTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---------WsshlprTSYDIDLDAESPNPNDQGFEKMISGMY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 752 LGEIVRNVLLHFTAKGLLFrGKLSERLKTRGIFETKFLSQI-ESDRLALRQVRSILQH-LGLTSSTCDDSILVKEVCSVV 829
Cdd:PLN02362 323 LGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARILKEtLGISEVPLKVRKLVVKICDVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 830 SKRAAQLCGAGLAAVVDKI------RLNRGLNQLSI------TVGVDGTLYKLHPHFATIMRETLRDLAPN---CEVSLV 894
Cdd:PLN02362 402 TRRAARLAAAGIVGILKKIgrdgsgGITSGRSRSDIqimrrtVVAVEGGLYTNYTMFREYLHEALNEILGEdvaQHVILK 481
|
490
....*....|....*
gi 47085787 895 QSEDGSGKGAALITA 909
Cdd:PLN02362 482 ATEDGSGIGSALLAA 496
|
|
| PLN02405 |
PLN02405 |
hexokinase |
454-909 |
1.10e-77 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 261.69 E-value: 1.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 454 GAAMVTAVAYRLAKQHAERQRVLDTLRLGRdqLLEVKKRMEE------------------EMKRGLAkkTHNNATVKMLP 515
Cdd:PLN02405 7 GAAVVCAAAVCAAAALVVRRRMKSSGKWAR--AMEILKEFEEdcatpigklrqvadamtvEMHAGLA--SEGGSKLKMLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 516 TFVRSTPDGTERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNNKIYTIPQDITQGTGEELFDHIVHCIADFLEYMG--- 592
Cdd:PLN02405 83 SYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGedf 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 593 --MKGASLPLGFTFSFPCHQDKLDQGILIKWTKGFKASGCEGEDVASLLKDAIHRcEEFDLDVVAVVNDTVGTMMTCGYE 670
Cdd:PLN02405 163 hlPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMER-VGLDMRVSALVNDTIGTLAGGRYY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 671 DPQCEVGLIVGTGTNACYMEEMSNVELVDGD---EGRMCVNMEWGAFgDQGELDdiWTEFDRAVDDQSTYPGRQRYEKMI 747
Cdd:PLN02405 242 NPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNF-RSSHLP--LTEYDHALDVESLNPGEQIFEKII 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 748 SGMYLGEIVRNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLA-LRQVRSILQH-LGLTSSTCDDSILVKEV 825
Cdd:PLN02405 319 SGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPdLKVVGSKLKDiLEIPNTSLKMRKVVVEL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 826 CSVVSKRAAQLCGAGLAAVVDKI---RLNRGLNQLSItVGVDGTLYKLHPHFATIMRETLRDLAPNcEVS----LVQSED 898
Cdd:PLN02405 399 CNIVATRGARLSAAGIYGILKKLgrdTVKDGEKQKSV-IAMDGGLFEHYTEFSKCMESTLKELLGE-EVSesieVEHSND 476
|
490
....*....|.
gi 47085787 899 GSGKGAALITA 909
Cdd:PLN02405 477 GSGIGAALLAA 487
|
|
| PLN02405 |
PLN02405 |
hexokinase |
46-460 |
5.62e-77 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 259.76 E-value: 5.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 46 EMDKGLGRDTNptAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMENQIYAISENIMRGCGSE 125
Cdd:PLN02405 65 EMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 126 LFDHIAECLANFLEKLGiKEKKLP------LGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLLRKAIRKRGdF 199
Cdd:PLN02405 143 LFDFIAAALAKFVATEG-EDFHLPpgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-L 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 200 DIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDGD---EGRMCVNMEWGAFGDDGALddlRTE 276
Cdd:PLN02405 221 DMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFRSSHLP---LTE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 277 FDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFQGHTTPDLLTTGHFQTSFVSAIENRKDDEGIVSAEQ 356
Cdd:PLN02405 298 YDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 357 VLRGLGLDPTPedcVATQRV----CQIVSTRAAHLCAASLAAVLRQI-RDN-KASDRLRTSIGVDGSVYKNHPEFARRLN 430
Cdd:PLN02405 378 LKDILEIPNTS---LKMRKVvvelCNIVATRGARLSAAGIYGILKKLgRDTvKDGEKQKSVIAMDGGLFEHYTEFSKCME 454
|
410 420 430
....*....|....*....|....*....|...
gi 47085787 431 KMVRSLVPD---CDVRFLRSEDGSGKGAAMVTA 460
Cdd:PLN02405 455 STLKELLGEevsESIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
46-460 |
6.48e-72 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 246.33 E-value: 6.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 46 EMDKGLGRDTNptAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKV----SSNGMQKVEMEnqiyAISENIMRG 121
Cdd:PLN02362 65 EMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLggqrSSILSQDVERH----PIPQHLMNS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 122 CGSELFDHIAECLANFLEKLG-----IKEKKLPLGFTFSFPCQQTKLDESFLVSWTKGFKASGVEGKDVVSLLRKAIRKR 196
Cdd:PLN02362 139 TSEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 197 GdFDIDIVAVINDTVGTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDG---DEGRMCVNMEWGAFGDDGALddl 273
Cdd:PLN02362 219 G-LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFWSSHLP--- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 274 RTEFDREIDAGSLNPGKQLFEKMISGMYMGELVRLILVKMAKDGLLFqGHTTPDLLTTGHFQTSFVSAIENRKDDEGIVS 353
Cdd:PLN02362 295 RTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMHEDDSPELQEV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 354 AEQVLRGLGLDPTPEDCVA-TQRVCQIVSTRAAHLCAASLAAVLRQI-RD---------NKASDRL--RTSIGVDGSVYK 420
Cdd:PLN02362 374 ARILKETLGISEVPLKVRKlVVKICDVVTRRAARLAAAGIVGILKKIgRDgsggitsgrSRSDIQImrRTVVAVEGGLYT 453
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 47085787 421 NHPEFARRLNKMVRSLVPDCDVRFL---RSEDGSGKGAAMVTA 460
Cdd:PLN02362 454 NYTMFREYLHEALNEILGEDVAQHVilkATEDGSGIGSALLAA 496
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
455-909 |
3.79e-54 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 196.25 E-value: 3.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 455 AAMVTAVAYRLAKQHAERQRVlDTLRLGRD----------QLLEVKKRMEEEMKRGLAKKthNNATVKMLPTFVRSTPDG 524
Cdd:PLN02596 16 AAVAAAVLMGRWKRRKERQWK-HTQRILRKfarecatpvsKLWEVADALVSDMTASLTAE--ETTTLNMLVSYVASLPSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 525 TERGDFLALDLGGTNFRVLLVRVRGGKRRNVEMNNKIYTIPQDITQGTGEELFDHIVHCIADFLEYMGMKGASLP----- 599
Cdd:PLN02596 93 DEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkk 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 600 LGFTFSFPCHQDKLDQGILIKWtKGFKASGCEGEDVASLLKDAIHRcEEFDLDVVAVVNDTVGTMMTCGYEDPQCEVGLI 679
Cdd:PLN02596 173 LGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 680 VGTGTNACYMEEMSNVELVDG---DEGRMCVNMEWGAFgDQGELDdiWTEFDRAVDDQSTYPGRQRYEKMISGMYLGEIV 756
Cdd:PLN02596 251 LGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF-NSCHLP--ITEFDASLDAESSNPGSRIFEKLTSGMYLGEIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 757 RNVLLHFTAKGLLFRGKLSERLKTRGIFETKFLSQIESDRLALRQV--RSILQHLGLTSSTCDDSILVKEVCSVVSKRAA 834
Cdd:PLN02596 328 RRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVvnEKLKEIFGITDSTPMAREVVAEVCDIVAERGA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 835 QLCGAGLAAVVDKirLNRGLNQLSItVGVDGTLYKLHPHFATIMRETL-----RDLAPNceVSLVQSEDGSGKGAALITA 909
Cdd:PLN02596 408 RLAGAGIVGIIKK--LGRIENKKSV-VTVEGGLYEHYRVFRNYLHSSVwemlgSELSDN--VVIEHSHGGSGAGALFLAA 482
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
58-460 |
7.86e-48 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 178.15 E-value: 7.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 58 TAAVKMLPTFVRSTPDGTETGDFLALDLGGTNFRVLLVKVSSNGMQKVEMENQIYAISENIMRGCGSELFDHIAECLANF 137
Cdd:PLN02596 76 TTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 138 L------EKLGIKEKKlPLGFTFSFPCQQTKLDESFLVSWtKGFKASGVEGKDVVSLLRKAIRKRGdFDIDIVAVINDTV 211
Cdd:PLN02596 156 VaehpgdEADTPERVK-KLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDTI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 212 GTMMTCGYDDHHCEIGLIVGTGTNACYMEEMRHLELVDG---DEGRMCVNMEWGAFGddgALDDLRTEFDREIDAGSLNP 288
Cdd:PLN02596 233 GNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN---SCHLPITEFDASLDAESSNP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 289 GKQLFEKMISGMYMGELVRLILVKMAKDGLLFqGHTTPDLLTTGHFQTS--FVSAIENRKDDEGIVSaEQVLRGLGL-DP 365
Cdd:PLN02596 310 GSRIFEKLTSGMYLGEIVRRVLLKMAEETALF-GDTLPPKLTTPYLLRSpdMAAMHQDTSEDHEVVN-EKLKEIFGItDS 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 366 TPEDCVATQRVCQIVSTRAAHLCAASLAAVLRQIR--DNKasdrlRTSIGVDGSVYKNHPEFARRLN----KMVRSLVPD 439
Cdd:PLN02596 388 TPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGriENK-----KSVVTVEGGLYEHYRVFRNYLHssvwEMLGSELSD 462
|
410 420
....*....|....*....|.
gi 47085787 440 cDVRFLRSEDGSGKGAAMVTA 460
Cdd:PLN02596 463 -NVVIEHSHGGSGAGALFLAA 482
|
|
| ASKHA_NBD_NAGK_meta |
cd24078 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
624-718 |
5.84e-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: 39.87 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085787 624 GFKASGCEGEDVASLLKDAIHRCEEFDLDVVAVVNDTVGTMMTCgyedpqCEVG---LIVGTGtnacymeemSNVELVDG 700
Cdd:cd24078 69 GLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATA------FENGgivLISGTG---------SNCQLINP 133
|
90 100
....*....|....*....|
gi 47085787 701 D-EGRMCVNmeWGAF-GDQG 718
Cdd:cd24078 134 DgSTAGCGG--WGHMlGDEG 151
|
|
| |
