|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
434-860 |
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: 765.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIIN 507
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 508 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 587
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 588 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 667
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 668 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 747
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 748 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 827
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 1907093304 828 TVRKLAPQCTVTFLQSEDGSGKGAALVTAVACR 860
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
434-860 |
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: 754.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY 510
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 511 SIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREA 590
Cdd:cd24129 81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 591 IRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSLGT 670
Cdd:cd24129 161 ATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCLAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 671 LSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALRQV 750
Cdd:cd24129 241 ISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALRQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 751 RAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSATVR 830
Cdd:cd24129 321 RAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQATVR 400
|
410 420 430
....*....|....*....|....*....|
gi 1907093304 831 KLAPQCTVTFLQSEDGSGKGAALVTAVACR 860
Cdd:cd24129 401 ELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
1-414 |
0e+00 |
|
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: 690.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24090 18 MEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEPRSQEFVIPQEVMLGAGQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24090 98 QLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRDAIQRQGAYNIDVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24090 178 AVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALGPVLTTFDHTLDHE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24090 258 SLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAARVRAILQDLGLSPS 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24090 338 ASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTVMLLAPECDVSFIP 417
|
410
....*....|....
gi 1907093304 401 SVDGGGRGVAMVTA 414
Cdd:cd24090 418 SVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
434-861 |
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: 661.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIIN 507
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKEthaSAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGkwrGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 508 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 587
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 588 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 667
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 668 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 747
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 748 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 827
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....
gi 1907093304 828 TVRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 861
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
434-856 |
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: 652.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGS-VQIINQV 509
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDthpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSqVKMESEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 510 YSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLRE 589
Cdd:cd24019 81 YAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 590 AIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNV---ASVPGDSGLMCINMEWGAFGDDG 666
Cdd:cd24019 161 AIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVekwDGDEGDPGQVIINTEWGAFGDNG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 667 SLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSL- 745
Cdd:cd24019 241 VLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDNEg 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 746 ALRQVRAILEDLGLTLTSD-DALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRglqeltVSVGVDGTLYKLHPHFSKL 824
Cdd:cd24019 321 DFSNTREILKELGLEDASDeDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKE------VTVGVDGSLYKYHPKFHKR 394
|
410 420 430
....*....|....*....|....*....|...
gi 1907093304 825 VSATVRKLAP-QCTVTFLQSEDGSGKGAALVTA 856
Cdd:cd24019 395 MHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
435-861 |
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: 635.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 435 LTLEQMTVVQAQMREAMIRGLQG---EASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIINQ 508
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKqthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGkkrTVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 509 VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLR 588
Cdd:cd24127 82 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 589 EAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSL 668
Cdd:cd24127 162 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 669 GTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALR 748
Cdd:cd24127 242 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 749 QVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSAT 828
Cdd:cd24127 322 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQT 401
|
410 420 430
....*....|....*....|....*....|...
gi 1907093304 829 VRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 861
Cdd:cd24127 402 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
434-861 |
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: 625.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG--SVQIINQ 508
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKEThptASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGrrSVRMYNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 509 VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLR 588
Cdd:cd24130 81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 589 EAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSL 668
Cdd:cd24130 161 EAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGCI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 669 GTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALR 748
Cdd:cd24130 241 DDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 749 QVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSAT 828
Cdd:cd24130 321 QVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQET 400
|
410 420 430
....*....|....*....|....*....|...
gi 1907093304 829 VRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 861
Cdd:cd24130 401 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
434-856 |
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: 606.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGS---VQIIN 507
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDThptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKnqkVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 508 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 587
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 588 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 667
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 668 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 747
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 748 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 827
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1907093304 828 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 856
Cdd:cd24089 401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
434-856 |
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: 551.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGEASS---LRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAE---GSVQIIN 507
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPtaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEdgkQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 508 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 587
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 588 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 667
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 668 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 747
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 748 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 827
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 1907093304 828 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 856
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
434-856 |
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: 536.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQII---N 507
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATThptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVemeN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 508 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 587
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 588 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 667
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 668 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 747
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 748 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 827
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 1907093304 828 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 856
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
1-414 |
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: 535.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGtkECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24019 18 MEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLG--GTNFRVLLVTLNG--GSQVKMESEIYAIPEEIMTGTGE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24019 94 QLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQEAIKRRGDIKVDVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSFYDEDALGPVLTTFDSAL 237
Cdd:cd24019 174 AVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEgdpGQVIINTEWGAFGDNGVLDFIRTEFDREV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 238 DRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEME-DTATGTARVHTILQDLG 316
Cdd:cd24019 254 DEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIEsDNEGDFSNTREILKELG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 317 LSPR-ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLqhsreqQTLQVAVATGGRVFERHPRFLRILKETVTLLAP-NC 394
Cdd:cd24019 334 LEDAsDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRM------NRKEVTVGVDGSLYKYHPKFHKRMHETLKELVPpGC 407
|
410 420
....*....|....*....|
gi 1907093304 395 DVSFIPSVDGGGRGVAMVTA 414
Cdd:cd24019 408 KFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
426-860 |
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: 529.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 426 LEETLAPFQLTLEQMTVVQAQMREAMIRGLQ---GEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG- 501
Cdd:cd24092 2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRletHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 502 ----SVQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASG 577
Cdd:cd24092 82 egqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 578 CEGQDVVYLLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINM 657
Cdd:cd24092 162 AEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 658 EWGAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFL 737
Cdd:cd24092 242 EWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 738 SEIESDSLALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKL 817
Cdd:cd24092 322 SQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907093304 818 HPHFSKLVSATVRKLAPQCTVTFLQSEDGSGKGAALVTAVACR 860
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 ... |
426-863 |
4.29e-175 |
|
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: 514.17 E-value: 4.29e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 426 LEETLAPFQLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVA--- 499
Cdd:cd24124 21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNhek 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 500 EGSVQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCE 579
Cdd:cd24124 101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 580 GQDVVYLLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEW 659
Cdd:cd24124 181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 660 GAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSE 739
Cdd:cd24124 261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 740 IESDSLALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHP 819
Cdd:cd24124 341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907093304 820 HFSKLVSATVRKLAPQCTVTFLQSEDGSGKGAALVTAVACRLTQ 863
Cdd:cd24124 421 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAE 464
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
1-414 |
9.44e-169 |
|
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: 496.22 E-value: 9.44e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24089 18 MEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLG--GSNFRVLWVQVNDEKNQKVEMESQVYAIPEEIMHGSGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24089 96 QLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLRKAIRRRGDYDIDIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24089 176 AVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24089 256 SLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGLANAKEILTRLGLDPS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24089 336 EDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHKAVRRLVPDCDVRFLL 415
|
410
....*....|....
gi 1907093304 401 SVDGGGRGVAMVTA 414
Cdd:cd24089 416 SEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
437-854 |
1.36e-165 |
|
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar.
Pssm-ID: 466868 [Multi-domain] Cd Length: 431 Bit Score: 488.30 E-value: 1.36e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 437 LEQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV--AEGSVQIINQVYSIPE 514
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLdgNGGIFIIVQRKYKIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 515 CRAQGSGQKLFDHIVDCIVDFQKRQGLSGQS---LPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAI 591
Cdd:cd24018 81 EAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 592 RRRQaVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNV------ASVPGDSGLMCINMEWGAFGDD 665
Cdd:cd24018 161 DRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWGAFDNE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 666 GS-LGTlsTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDS 744
Cdd:cd24018 240 REvLPL--TKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 745 LA-LRQVRAILEDLGLT--LTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIREnrgLQELTVSVGVDGTLYKLHPHF 821
Cdd:cd24018 318 SPdLDAVRDILKELLAIdnTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS---LLPEPVTVGIDGSVYEKYPGF 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907093304 822 SKLVSATVRKLAPQCT---VTFLQSEDGSGKGAALV 854
Cdd:cd24018 395 KDRLSEALRELFGPEVkanISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
434-856 |
1.11e-153 |
|
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: 457.46 E-value: 1.11e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 434 QLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLG--GTNFRVLLVRVA--EG-SVQI 505
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQaspAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTgiEGhRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 506 INQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVY 585
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 586 LLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDD 665
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 666 GSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSL 745
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 746 ALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLV 825
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400
|
410 420 430
....*....|....*....|....*....|.
gi 1907093304 826 SATVRKLAPQCTVTFLQSEDGSGKGAALVTA 856
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
1-414 |
1.51e-144 |
|
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: 433.94 E-value: 1.51e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24125 18 MEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLG--GTNFRVLWVKVSDNGLQKVEMENQIYAIPEDIMRGSGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24125 96 QLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLRKAIQKRGDFDIDIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24125 176 AVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGSLDDIRTEFDREIDMG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24125 256 SLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGIRKAREVLMRLGLDPT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24125 336 QEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHKTVRRLVPGCDVRFLR 415
|
410
....*....|....
gi 1907093304 401 SVDGGGRGVAMVTA 414
Cdd:cd24125 416 SEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
1-414 |
3.63e-143 |
|
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: 430.43 E-value: 3.63e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24126 18 MEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLG--GSKFRVLRVKVSEDGKQKVQMESQFYPTPEEIIHGTGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24126 96 ELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLRKAIRKHKDVDVDVL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24126 176 ALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDLG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24126 256 SLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGLYNTREILSDLGLEPS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24126 336 EEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHKVVRRLVPSCDVRFLL 415
|
410
....*....|....
gi 1907093304 401 SVDGGGRGVAMVTA 414
Cdd:cd24126 416 SESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
1-418 |
4.30e-142 |
|
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: 427.73 E-value: 4.30e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24091 18 MERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLG--GTNFRVLLVKVRSGKWRGVEMHNKIYAIPQEIMQGTGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24091 96 ELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLLREAIKRREEFDLDVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24091 176 AVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGCLDDIRTRYDVEVDEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24091 256 SLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLDST 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24091 336 CDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHETVKELAPKCDVTFLQ 415
|
410
....*....|....*...
gi 1907093304 401 SVDGGGRGVAMVTAVAAR 418
Cdd:cd24091 416 SEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
1-430 |
9.83e-142 |
|
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: 428.27 E-value: 9.83e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24124 46 MKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24124 124 QLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24124 204 AVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24124 284 SLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPS 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24124 364 DDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLL 443
|
410 420 430
....*....|....*....|....*....|
gi 1907093304 401 SVDGGGRGVAMVTAVAARLAAHRRILEETL 430
Cdd:cd24124 444 SESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
1-418 |
3.56e-133 |
|
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: 404.65 E-value: 3.56e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTgtkECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24129 18 MAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLG--GTNFRVLLVHVG---TAGVQITSEIYSIPETVAQGTGQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24129 93 QLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREAATRKQAVELNVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24129 173 AIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCLAMISTRFDASVDQA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24129 253 SINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24129 333 SDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQATVRELAPRCVVTFLQ 412
|
410
....*....|....*...
gi 1907093304 401 SVDGGGRGVAMVTAVAAR 418
Cdd:cd24129 413 SEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
1-419 |
5.04e-133 |
|
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: 404.28 E-value: 5.04e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24128 18 MERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLG--GTNFRVLLVRVRNGKWRGVEMHNKIYAIPQEVMHGTGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24128 96 ELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24128 176 AVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDDFRTEFDVAVDEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24128 256 SLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLALLQVRAILQHLGLEST 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24128 336 CDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQ 415
|
410
....*....|....*....
gi 1907093304 401 SVDGGGRGVAMVTAVAARL 419
Cdd:cd24128 416 SEDGSGKGAALITAVACRI 434
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
1-419 |
5.23e-131 |
|
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: 399.29 E-value: 5.23e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24127 18 MELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLG--GTNFRVLLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24127 96 ELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLRDAIKRREEFDLDVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24127 176 AVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDDIRTHYDRLVDEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24127 256 SLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNST 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24127 336 CDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLL 415
|
410
....*....|....*....
gi 1907093304 401 SVDGGGRGVAMVTAVAARL 419
Cdd:cd24127 416 SEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
438-855 |
9.90e-130 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 392.79 E-value: 9.90e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 438 EQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECR 516
Cdd:cd24000 2 EDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLdGKGIEVTISKKYEIPDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 517 AQGSGQKLFDHIVDCIVDFQKRQGLSgQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRQa 596
Cdd:cd24000 82 KTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALKKRG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 597 VELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNvasVPGDSGLMCINMEWGAFGDDGSLGtlsTRFD 676
Cdd:cd24000 160 LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKNSLPR---TEYD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 677 TSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLtnlgvlfrgqktqclqARDIFKTkflseiesdslalrqvrailed 756
Cdd:cd24000 234 REVDKASENPGFQPLEKMVSGKYLGELVRLILKDL----------------ADEILRK---------------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 757 lgltltsddalmvleVCQAVSRRAAQLCGAGVAAVVEKIRENrglQELTVSVGVDGTLYKLHPHFSKLVSATVRKL-APQ 835
Cdd:cd24000 276 ---------------ICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLKELlGRG 337
|
410 420
....*....|....*....|
gi 1907093304 836 CTVTFLQSEDGSGKGAALVT 855
Cdd:cd24000 338 IRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
1-419 |
6.92e-126 |
|
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: 385.82 E-value: 6.92e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEcRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24130 18 LEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLG--GTNFRVLLVKIRSGRR-SVRMYNKIFAIPLEIMQGTGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVV 160
Cdd:cd24130 95 ELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLREAIKRRNEFDLDIV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRE 240
Cdd:cd24130 175 AVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGCIDDIRTRYDREVDEG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPR 320
Cdd:cd24130 255 SLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALLQVRRILQQLGLDST 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIP 400
Cdd:cd24130 335 CEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQETVKELAPQCDVTFML 414
|
410
....*....|....*....
gi 1907093304 401 SVDGGGRGVAMVTAVAARL 419
Cdd:cd24130 415 SEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
1-418 |
3.67e-123 |
|
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: 379.22 E-value: 3.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKE--CRVEPRSREFVIPQEVILGA 78
Cdd:cd24092 27 MDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLG--GTNFRVMLVKVGEGEEgqWSVKTKHQMYSIPEDAMTGT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 79 GQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRID 158
Cdd:cd24092 105 AEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLLRDAIKRRGDFEMD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 159 VVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALD 238
Cdd:cd24092 185 VVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 239 RESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLS 318
Cdd:cd24092 265 ESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 319 PRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSF 398
Cdd:cd24092 345 PSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHASVRRLTPSCEITF 424
|
410 420
....*....|....*....|
gi 1907093304 399 IPSVDGGGRGVAMVTAVAAR 418
Cdd:cd24092 425 IESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
435-858 |
1.26e-119 |
|
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: 369.68 E-value: 1.26e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 435 LTLEQMTVVQAQMREAMIRGLQGEA-SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY--- 510
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGgSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYeev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 511 SIPECRAQGSGQKLFDHIVDCIVDFQKRQG----LSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYL 586
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 587 LREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFg 663
Cdd:cd24020 161 LEEALER-QGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 664 DDGSLGtlSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEI-ES 742
Cdd:cd24020 239 RSSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 743 DSLALRQVRAILED-LGLTLTS-DDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI-RENRGLQELTVS-VGVDGTLYKLH 818
Cdd:cd24020 317 DSPDLETVARILKDaLGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGSSPAQRTvVAVDGGLYEHY 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907093304 819 PHFSKLVSATVRKL---APQCTVTFLQSEDGSGKGAALVTAVA 858
Cdd:cd24020 397 PKFREYMQQALVELlgdEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
438-858 |
1.77e-114 |
|
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: 355.91 E-value: 1.77e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 438 EQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECR 516
Cdd:cd24087 2 ERLRKITDHFISELEKGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLgGNGKFDITQSKYRLPEEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 517 AQGSGQKLFDHIVDCIVDF---QKRQGLSGQsLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRR 593
Cdd:cd24087 82 KTGTGEELWDFIADCLKKFveeHFPGGKSEP-LPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 594 RQaVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEelrNVASVP-------GDSGLMCINMEWGAFgDDG 666
Cdd:cd24087 161 RN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYME---VVSNIPklehddiPPDSPMAINCEYGAF-DNE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 667 SLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLA 746
Cdd:cd24087 236 HLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 747 --LRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKirenRGLQelTVSVGVDGTLYKLHPHFSKL 824
Cdd:cd24087 316 nlEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYK--TCHVAADGSVYNKYPGFKER 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907093304 825 VSATVRKL----APQCTVTFLQSEDGSGKGAALVTAVA 858
Cdd:cd24087 390 AAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
1-412 |
2.00e-113 |
|
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: 353.09 E-value: 2.00e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSpapSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKEcRVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24018 15 MEKGLEGDGG---SLPMLPSFVTERPTGKETGTYLALDLGGT--NLRVCLVTLDGNGG-IFIIVQRKYKIPDEAKTGTGE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQG---LKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRI 157
Cdd:cd24018 89 ELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNALDRRG-VNV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 158 DVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALD------EDRGRTCVSIEWGSFYDEDALGPvLT 231
Cdd:cd24018 168 KVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsgsvTKSDEMIINTEWGAFDNEREVLP-LT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 232 TFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEME-DTATGTARVHT 310
Cdd:cd24018 247 KYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEaDTSPDLDAVRD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 311 ILQDLGLSPRAS--DAELVQYVCVAVCTRaaqLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVT 388
Cdd:cd24018 327 ILKELLAIDNTTleDRKLIKRICELVSTR---AARLSAAAIAAILLKRGSLLPEPVTVGIDGSVYEKYPGFKDRLSEALR 403
|
410 420
....*....|....*....|....*..
gi 1907093304 389 LLAPNC---DVSFIPSVDGGGRGVAMV 412
Cdd:cd24018 404 ELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
438-854 |
4.07e-108 |
|
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: 339.76 E-value: 4.07e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 438 EQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECR 516
Cdd:cd24088 2 EKLDKLTAEFQRQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELhGDGTFSLRQEKSKIPDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 517 AQGSGQK-LFDHIVDCIVDFQK-------RQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLR 588
Cdd:cd24088 82 KTGVTAKdLFDYLAKSVEAFLTkhhgdsfAAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 589 EAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCE---MGLIVGTGTNACYMEELRNV-----ASVPGDS-GLMCINMEW 659
Cdd:cd24088 162 DELDR-QGIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddSSRVGKGkTHMVINTEW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 660 GAFgdDGSLGTL-STRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTN---LGVLFRGQKTQCLQARDIFKTK 735
Cdd:cd24088 241 GSF--DNELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKqglFLIQYNDKSPSALNTPYGLDTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 736 FLSEIESDSLA-LRQVRAIL-EDLGL-TLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDG 812
Cdd:cd24088 319 VLSAIEIDSEAeLRATRKVLlDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEINIGVDG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907093304 813 TLYKLHPHFSKLVSATVRKLAPQCT----VTFLQSEDGSGKGAALV 854
Cdd:cd24088 399 SVIEFYPGFESMLREALRLLLIGAEgekrIKIGIAKDGSGVGAALC 444
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
623-857 |
1.69e-102 |
|
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: 317.13 E-value: 1.69e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 623 EMGLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMY 699
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 700 LGEIVRHILLHLTNLGVLFRGQkTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGL-TLTSDDALMVLEVCQAV 776
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEElLGIeTVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 777 SRRAAQLCGAGVAAVVEKIRENRglqelTVSVGVDGTLYKLHPHFSKLVSATVRK-LAPQCTVTFLQSEDGSGKGAALVT 855
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 1907093304 856 AV 857
Cdd:pfam03727 235 AV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
427-858 |
5.04e-102 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 324.71 E-value: 5.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 427 EETLAPFQLTLEQMTVVQAQMRE-------AMIRGLQG----------EASSLRMLPTYVRATPDGSERGDFLALDLGGT 489
Cdd:PTZ00107 5 IKQRVRLASLVNQFTMSKEKLKElvdyflyELVEGLEAhrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 490 NFRVLLVRVAEGSVQIINQ-VYSIPECRAQG---------SGQKLFDHIVDCIVDFQKRQGL---SGQSLPLGFTFSFPC 556
Cdd:PTZ00107 85 NFRAVRVSLRGGGKMERTQsKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPVGFTFSFPC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 557 KQLGLDQGILLNWTKGF-----NASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPR----CEMGLI 627
Cdd:PTZ00107 165 TQLSVNNAILIDWTKGFetgraTNDPVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 628 VGTGTNACYME---ELRNVASVPgdsglmcINMEWGAFgdDGSLGTlsTRFDTSVDQASINPGKQRFEKMISGMYLGEIV 704
Cdd:PTZ00107 244 IGTGSNACYFEpevSAYGYAGTP-------INMECGNF--DSKLPI--TPYDLEMDWYTPNRGRQQFEKMISGAYLGEIS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 705 RHILLHLTNLGVLFRGQKtqclqaRDIFKTKFLSEIESD-SLALRQVRAILEDL-GLTLTSDDALMVLEVCQAVSRRAAQ 782
Cdd:PTZ00107 313 RRLIVHLLQLKAPPKMWQ------SGSFESEDASMILNDqSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQ 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093304 783 LCGAGVAAVVEKIRENRGLqeltVSVGVDGTLYKLHPHFSKLVSATVRK-LAPQ-CTVTFLQSEDGSGKGAALVTAVA 858
Cdd:PTZ00107 387 LAAAFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
433-859 |
1.03e-98 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 314.97 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 433 FQLTLEQMTVVQAQMREAMIRGLQGEASSLRMLPTYVrATPDGS-ERGDFLALDLGGTNFRVLLVRVA-EGSVQIIN-QV 509
Cdd:COG5026 15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFDgEGTFEIENfKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 510 YSIPECRAQGSGQKLFDHIVDCIVDfqkrqgLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLRE 589
Cdd:COG5026 94 FPLPGTSSEITAEEFFDFIADYIEP------LLDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 590 AIRRRQAVELNVVAIVNDTVGTMMSCGYDDP----RCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGdd 665
Cdd:COG5026 168 ALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNFN-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 666 gslGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGvLFRGQKTQCLQARDIFKTKFLSE-IESDS 744
Cdd:COG5026 246 ---KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRfLADPS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 745 LALRQVRAILEDlgltLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI-RENRGLQELTVSvgVDGTLYKLHPHFSK 823
Cdd:COG5026 322 DEKEILSQCLEA----GSEEDREILREIADAIVERAARLVAATLAGILLHLgPGKTPLKPHCIA--IDGSTYEKMPGLAE 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907093304 824 LVSATVRK-LAPQCT--VTFLQSEDGSGKGAALVTAVAC 859
Cdd:COG5026 396 KIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
|
|
| PLN02914 |
PLN02914 |
hexokinase |
397-856 |
1.86e-91 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 297.57 E-value: 1.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 397 SFIPSVDGGGRGVAMvTAVAARLAAHRRILEETLAPFQLTLEQMTVVQAQMREAMIRGLQGE-ASSLRMLPTYVRATPDG 475
Cdd:PLN02914 13 SFTFSSRPRRRPRSR-MAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDgGGDLKMILSYVDSLPSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 476 SERGDFLALDLGGTNFRVLLVRVAEGSVQII----NQVySIPECRAQGSGQKLFDHIVDCIVDFQKRQG-----LSGQSL 546
Cdd:PLN02914 92 NEKGLFYALDLGGTNFRVLRVQLGGKDERVIatefEQV-SIPQELMFGTSEELFDFIASGLANFVAKEGgkfhlPEGRKR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 547 PLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGL 626
Cdd:PLN02914 171 EIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMER-QGLDMRVSALVNDTVGTLAGARYWDDDVMVAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 627 IVGTGTNACYMEELRNVASVPG---DSGLMCINMEWGAFGDdgslGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEI 703
Cdd:PLN02914 250 ILGTGTNACYVERTDAIPKLQGqksSSGRTIINTEWGAFSD----GLPLTEFDREMDAASINPGEQIFEKTISGMYLGEI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 704 VRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGLTLTSDDALMVLEVCQAVSRRAA 781
Cdd:PLN02914 326 VRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDnSDDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 782 QLCGAGVAAVVEKIRENR---GLQELTVsVGVDGTLYKLHPHFSK-LVSATVRKLAPQCT--VTFLQSEDGSGKGAALVT 855
Cdd:PLN02914 406 RLAGAGIVGILEKMEEDSkgmIFGKRTV-VAMDGGLYEKYPQYRRyMQDAVTELLGLELSknIAIEHTKDGSGIGAALLA 484
|
.
gi 1907093304 856 A 856
Cdd:PLN02914 485 A 485
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
1-413 |
3.11e-90 |
|
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: 289.56 E-value: 3.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSpapSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEcrVEPRSREFVIPQEVILGAGQ 80
Cdd:cd24000 15 LEKGLAGEPS---SLKMLPSYVSPLPTGLESGEFLAIDLG--GTNLRVALVSLDGKGI--EVTISKKYEIPDEIKTASAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVeNQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRIDVV 160
Cdd:cd24000 88 EFFDFIADCIAEFLKENGL-KKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALKKRG-LPVKVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 161 AMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVaalDEDRGRTCVSIEWGSFYDEDAlgpVLTTFDSALDRE 240
Cdd:cd24000 166 AVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI---LLGDGGMIINTEWGNFGKNSL---PRTEYDREVDKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 241 SLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHgvlfdgcaspallsqgciLLDHVAEMedtatgtarvhtilqdlgLSPR 320
Cdd:cd24000 240 SENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------ILRKICEL------------------VAER 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 321 AsdAELVQYVCVAVctraaqlcaaalaavlsrLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVT-LLAPNCDVSFI 399
Cdd:cd24000 284 S--ARLAAAAIAAL------------------LRKTGDSPEKKITIAVDGSLFEKYPGYRERLEEYLKeLLGRGIRIELV 343
|
410
....*....|....
gi 1907093304 400 PSVDGGGRGVAMVT 413
Cdd:cd24000 344 LVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
14-421 |
1.78e-86 |
|
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: 282.63 E-value: 1.78e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 14 SVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGtKECRVEPR-SREFVIPQEVILGAGQQLFDFAARCLSE 92
Cdd:cd24020 28 KLKMLPSYVDNLPSGDEKGLFYALDLG--GTNFRVLRVQLGG-KEGRVDKQeYEEVPIPPELMVGTSEELFDFIAGELAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 93 FLDAYP----VENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRIDVVAMVNDTVG 168
Cdd:cd24020 105 FVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQG-LDMRVAALVNDTVG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 169 TMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRT---CVSIEWGSFYdeDALGPvLTTFDSALDRESLTPG 245
Cdd:cd24020 184 TLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSgemVINTEWGNFR--SSHLP-RTEEDRELDAESLNPG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 246 AQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEM-EDTATGTARVHTILQDLGLSPRAS-- 322
Cdd:cd24020 261 EQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDDSPDLETVARILKDALGIDDTSle 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 323 DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQH--SREQQTLQVAVATGGRVFERHPRFLRILKETVT-LLAPNC--DVS 397
Cdd:cd24020 341 ARKVVVEVCDLVAERGARLAAAGIVGILKKLGRdgGGSSPAQRTVVAVDGGLYEHYPKFREYMQQALVeLLGDEAadSVE 420
|
410 420
....*....|....*....|....
gi 1907093304 398 FIPSVDGGGRGvamvtavAARLAA 421
Cdd:cd24020 421 LELSNDGSGIG-------AALLAA 437
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
425-617 |
2.66e-85 |
|
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: 270.53 E-value: 2.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 425 ILEETLAPFQLTLEQMTVVQAQMREAMIRGLQGE-ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVA-EGS 502
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEgSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGgDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 503 VQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLS---GQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCE 579
Cdd:pfam00349 81 FEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGVV 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907093304 580 GQDVVYLLREAIRRRQaVELNVVAIVNDTVGTMMSCGY 617
Cdd:pfam00349 161 GKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAGAY 197
|
|
| PLN02405 |
PLN02405 |
hexokinase |
408-856 |
1.46e-77 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 260.53 E-value: 1.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 408 GVAMVTAVAARLAAHR--------------RILEETLAPFQLTLEQmtvVQAQMREAMIRGLQGEA-SSLRMLPTYVRAT 472
Cdd:PLN02405 12 CAAAVCAAAALVVRRRmkssgkwarameilKEFEEDCATPIGKLRQ---VADAMTVEMHAGLASEGgSKLKMLISYVDNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 473 PDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY---SIPECRAQGSGQKLFDHIVDCIVDFQKRQG-----LSGQ 544
Cdd:PLN02405 89 PSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFeevSIPPHLMTGSSDALFDFIAAALAKFVATEGedfhlPPGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 545 SLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEM 624
Cdd:PLN02405 169 QRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMER-VGLDMRVSALVNDTIGTLAGGRYYNPDVVA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 625 GLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFGddgSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLG 701
Cdd:PLN02405 248 AVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR---SSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 702 EIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGLTLTS-DDALMVLEVCQAVSR 778
Cdd:PLN02405 325 EILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDtSPDLKVVGSKLKDiLEIPNTSlKMRKVVVELCNIVAT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 779 RAAQLCGAGVAAVVEKI-RENRGLQELTVSV-GVDGTLYKLHPHFSKLVSATVRKLAPQ---CTVTFLQSEDGSGKGAAL 853
Cdd:PLN02405 405 RGARLSAAGIYGILKKLgRDTVKDGEKQKSViAMDGGLFEHYTEFSKCMESTLKELLGEevsESIEVEHSNDGSGIGAAL 484
|
...
gi 1907093304 854 VTA 856
Cdd:PLN02405 485 LAA 487
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
2-390 |
2.88e-77 |
|
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: 258.09 E-value: 2.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 2 EQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKECRVepRSREFVIPQEVILGA-GQ 80
Cdd:cd24088 13 RQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGT--NFRVCSVELHGDGTFSL--RQEKSKIPDELKTGVtAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFL-----DAYPVENQG--LKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQG 153
Cdd:cd24088 89 DLFDYLAKSVEAFLtkhhgDSFAAGKDDdrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDRQG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 154 TyRIDVVAMVNDTVGTMMGCELGTRPCE---VGLIVDTGTNACYMEEARHVAALD------EDRGRTCVSIEWGSFYDED 224
Cdd:cd24088 169 I-PVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIKKLDdssrvgKGKTHMVINTEWGSFDNEL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 225 ALGPVlTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGC--ASPALLSQGCIL----LDHVAem 298
Cdd:cd24088 248 KVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYndKSPSALNTPYGLdtavLSAIE-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 299 EDTATGTARV-HTILQDLGL-SPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERH 376
Cdd:cd24088 325 IDSEAELRATrKVLLDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEINIGVDGSVIEFY 404
|
410
....*....|....
gi 1907093304 377 PRFLRILKETVTLL 390
Cdd:cd24088 405 PGFESMLREALRLL 418
|
|
| PLN02362 |
PLN02362 |
hexokinase |
408-856 |
1.48e-74 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 252.88 E-value: 1.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 408 GVAMVTAVAA----------RLAAHRR------ILEETLAPFQLTLEQMTVVQAQMREAMIRGLQGEA-SSLRMLPTYVR 470
Cdd:PLN02362 7 GLAAAAAVAAcavaavmvgrRVKSRRKwrrvvgVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGgSKLKMLLTFVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 471 ATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQ---VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLP 547
Cdd:PLN02362 87 DLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQdveRHPIPQHLMNSTSEVLFDFIASSLKQFVEKEENGSEFSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 548 -----LGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRqAVELNVVAIVNDTVGTMMSCGYDDPRC 622
Cdd:PLN02362 167 vrrreLGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 623 EMGLIVGTGTNACYMEELRNVASVPG---DSGLMCINMEWGAFgddGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMY 699
Cdd:PLN02362 246 VAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---WSSHLPRTSYDIDLDAESPNPNDQGFEKMISGMY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 700 LGEIVRHILLHLTNLGVLFrGQKTQCLQARDIFKTKFLSEI-ESDSLALRQVRAIL-EDLGLtltSDDAL----MVLEVC 773
Cdd:PLN02362 323 LGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARILkETLGI---SEVPLkvrkLVVKIC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 774 QAVSRRAAQLCGAGVAAVVEKI-------------RENRGLQELTVsVGVDGTLYKLHPHFSKLVSATVRKLAPQCT--- 837
Cdd:PLN02362 399 DVVTRRAARLAAAGIVGILKKIgrdgsggitsgrsRSDIQIMRRTV-VAVEGGLYTNYTMFREYLHEALNEILGEDVaqh 477
|
490
....*....|....*....
gi 1907093304 838 VTFLQSEDGSGKGAALVTA 856
Cdd:PLN02362 478 VILKATEDGSGIGSALLAA 496
|
|
| PLN02914 |
PLN02914 |
hexokinase |
15-414 |
1.25e-70 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 241.71 E-value: 1.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 15 VRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFL 94
Cdd:PLN02914 78 LKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 95 ----DAYPVEnQGLK--LGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRIDVVAMVNDTVG 168
Cdd:PLN02914 156 akegGKFHLP-EGRKreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 169 TMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSFYDedalGPVLTTFDSALDRESLTPG 245
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD----GLPLTEFDREMDAASINPG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 246 AQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCIL-LDHVAEM-EDTATGTARVHTILQD-LGLSPRAS 322
Cdd:PLN02914 310 EQIFEKTISGMYLGEIVRRVLLKMAETSDLF-GHFVPEKLSTPFALrTPHLCAMqQDNSDDLQAVGSILYDvLGVEASLS 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 323 DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTL--QVAVATGGRVFERHPRFLRILKETVT-LLAP--NCDVS 397
Cdd:PLN02914 389 ARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTeLLGLelSKNIA 468
|
410
....*....|....*..
gi 1907093304 398 FIPSVDGGGRGVAMVTA 414
Cdd:PLN02914 469 IEHTKDGSGIGAALLAA 485
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
1-173 |
1.78e-68 |
|
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: 225.46 E-value: 1.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPapSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGtkECRVEPRSREFVIPQEVILGAGQ 80
Cdd:pfam00349 27 MEKGLAKEGSS--SLKMLPTYVTSLPTGTEKGTFLALDLGGT--NFRVCLVELGG--DGKFEITQEKYKIPEELMTGTGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVENQG---LKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRI 157
Cdd:pfam00349 101 ELFDFIADCIAEFLKEHGLEDFEekeLPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGVVGKDVVQLLQEALERRG-LPV 179
|
170
....*....|....*.
gi 1907093304 158 DVVAMVNDTVGTMMGC 173
Cdd:pfam00349 180 KVVALVNDTVGTLMAG 195
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
6-417 |
8.65e-67 |
|
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: 229.18 E-value: 8.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 6 KGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKEcrVEPRSREFVIPQEVILGAGQQLFDF 85
Cdd:cd24087 17 KGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGT--NLRVCLVKLGGNGK--FDITQSKYRLPEELKTGTGEELWDF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 86 AARCLSEFLDAYPVEN--QGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTyRIDVVAMV 163
Cdd:cd24087 93 IADCLKKFVEEHFPGGksEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKKRNV-PIELVALI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 164 NDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAAL-------DEDRGRTCvsiEWGSFYDEDALGPvLTTFDSA 236
Cdd:cd24087 172 NDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLehddippDSPMAINC---EYGAFDNEHLVLP-RTKYDVI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 237 LDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDG----------CASPALLSQgcILLDHVAEMEDTATgta 306
Cdd:cd24087 248 IDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGqdtsklekpyVMDTSFLSR--IEEDPFENLEDTDD--- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 307 rvhTILQDLGLSPRASDAELVQYVCVAVCTRaaqlcaaalaavLSRL---------QHSREQQTLqvaVATGGRVFERHP 377
Cdd:cd24087 323 ---LFQHFFGLETTVPERKFIRRLAELIGTR------------AARLsacgiaaicKKRGYKTCH---VAADGSVYNKYP 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907093304 378 RF-------LR-ILKETVTllapNCDVSFIPSVDGGGRGVAMVTAVAA 417
Cdd:cd24087 385 GFkeraaqaLKdIFGWDGE----DDPIKTVPAEDGSGVGAAIIAALTK 428
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
14-417 |
1.66e-66 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 229.56 E-value: 1.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 14 SVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEcrVEPRSREFVIPQEVILGA---------GQQLFD 84
Cdd:PTZ00107 56 SFKMLDSCVYNLPTGKEKGVYYAIDFG--GTNFRAVRVSLRGGGK--MERTQSKFSLPKSALLGEkglldkkatATDLFD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 85 FAARCLSEFLD--AYPVE-NQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCS-----GVEGQDVVQLLRDAIQRQGTyR 156
Cdd:PTZ00107 132 HIAKSIKKMMEenGDPEDlNKPVPVGFTFSFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFKRNNV-P 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 157 IDVVAMVNDTVGTMMGC----ELGTRPCEVGLIVDTGTNACYMEEArhVAAldedRGR--TCVSIEWGSFydeDALGPvL 230
Cdd:PTZ00107 211 ANVVAVLNDTVGTLISCayqkPKNTPPCQVGVIIGTGSNACYFEPE--VSA----YGYagTPINMECGNF---DSKLP-I 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 231 TTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGvlfdgcASPALLSQGCILLDHVAEM-EDTATGTARVH 309
Cdd:PTZ00107 281 TPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLK------APPKMWQSGSFESEDASMIlNDQSPDLQFSR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 310 TILQDL-GLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTlqvaVATGGRVFERHPRFLRILKETVT 388
Cdd:PTZ00107 355 QVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKTRTVQGKAT----VAIDGSVYVKNPWFRRLLQEYIN 430
|
410 420 430
....*....|....*....|....*....|.
gi 1907093304 389 L-LAPN-CDVSFIPSVDGGGRGVAMVTAVAA 417
Cdd:PTZ00107 431 SiLGPDaGNVVFYLADDGSGKGAAIIAAMVA 461
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
181-415 |
1.06e-59 |
|
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: 203.11 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 181 EVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSFYDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLY 257
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLpksGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 258 LGELVRLVLVHLTQHGVLFDGcASPALLSQGCILLDHVAEME-DTATGTARVHTILQD-LGLSPRAS-DAELVQYVCVAV 334
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIEsDPSEDLETTREILEElLGIETVTEeDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 335 CTRaaqlcaaalaavLSRL---------QHSREQQTLQVAVatGGRVFERHPRFLRILKETV-TLLAPNCDVSFIPSVDG 404
Cdd:pfam03727 160 STR------------AARLvaagiaailKKIGRDKKVTVGV--DGSVYEKYPGFRERLQEALrELLGPGDKVVLVLAEDG 225
|
250
....*....|.
gi 1907093304 405 GGRGVAMVTAV 415
Cdd:pfam03727 226 SGVGAALIAAV 236
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
1-337 |
2.29e-59 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 208.66 E-value: 2.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSpapSVRMLPTYVrSTPHG-TEQGDFLVLELGATgaSLRVLWVTLTGTKECRVEpRSREFVIP---QEVil 76
Cdd:COG5026 33 MEKGLEGKKS---SLKMLPSYL-GLPTGvKETGPVIALDAGGT--NFRVALVRFDGEGTFEIE-NFKSFPLPgtsSEI-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 77 gAGQQLFDFAARCLSEFLDaypvenQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYR 156
Cdd:COG5026 104 -TAEEFFDFIADYIEPLLD------ESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEAALARKGLDN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 157 IDVVAMVNDTVGTMMGCELGTRPC----EVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFydedALGPvLTT 232
Cdd:COG5026 177 VKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNF----NKLP-RTK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 233 FDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGvLFDGCASPALLSQGCIlldHVAEMEDTATGTARVHTIL 312
Cdd:COG5026 252 IDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSL---TTVDMSRFLADPSDEKEIL 327
|
330 340
....*....|....*....|....*
gi 1907093304 313 QDLGLSPRASDAELVQYVCVAVCTR 337
Cdd:COG5026 328 SQCLEAGSEEDREILREIADAIVER 352
|
|
| PLN02405 |
PLN02405 |
hexokinase |
15-414 |
6.96e-53 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 192.35 E-value: 6.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 15 VRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFL 94
Cdd:PLN02405 78 LKMLISYVDNLPSGDEKGLFYALDLG--GTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 95 -----DAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTyRIDVVAMVNDTVGT 169
Cdd:PLN02405 156 ategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGL-DMRVSALVNDTIGT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 170 MMGCELGTRPCEVGLIVDTGTNACYMEEARHVA---ALDEDRGRTCVSIEWGSFYDEDAlgpVLTTFDSALDRESLTPGA 246
Cdd:PLN02405 235 LAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPkwhGLLPKSGEMVINMEWGNFRSSHL---PLTEYDHALDVESLNPGE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 247 QRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEM-EDTATGTARVHTILQDLGLSPRAS--D 323
Cdd:PLN02405 312 QIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMhHDTSPDLKVVGSKLKDILEIPNTSlkM 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 324 AELVQYVCVAVCTRAAQLCAAALAAVLSRLQHS--REQQTLQVAVATGGRVFERHPRFLRILKETVT-LLAPNC--DVSF 398
Cdd:PLN02405 392 RKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKeLLGEEVseSIEV 471
|
410
....*....|....*.
gi 1907093304 399 IPSVDGGGRGVAMVTA 414
Cdd:PLN02405 472 EHSNDGSGIGAALLAA 487
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
423-856 |
2.34e-46 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 173.52 E-value: 2.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 423 RRILEETLAPFQLTLEQMTVVQAQMREAMIrglQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAeGS 502
Cdd:PLN02596 43 RKFARECATPVSKLWEVADALVSDMTASLT---AEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLG-GK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 503 VQIINQVY----SIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLP-----LGFTFSFPCKQLGLDQGILLNWtKGF 573
Cdd:PLN02596 119 NEPISDLYreeiSIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 574 NASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPG---DS 650
Cdd:PLN02596 198 SADDTVGKALVNDINRALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspES 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 651 GLMCINMEWGAFGddgSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARD 730
Cdd:PLN02596 277 QEIVISTEWGNFN---SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 731 IFKTKFLSEIESDSLALRQV--RAILEDLGLTLTSDDAL-MVLEVCQAVSRRAAQLCGAGVAAVVEKIREnrgLQELTVS 807
Cdd:PLN02596 354 LLRSPDMAAMHQDTSEDHEVvnEKLKEIFGITDSTPMAReVVAEVCDIVAERGARLAGAGIVGIIKKLGR---IENKKSV 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907093304 808 VGVDGTLYKLHPHFSKLVSATV-RKLAPQCT--VTFLQSEDGSGKGAALVTA 856
Cdd:PLN02596 431 VTVEGGLYEHYRVFRNYLHSSVwEMLGSELSdnVVIEHSHGGSGAGALFLAA 482
|
|
| PLN02362 |
PLN02362 |
hexokinase |
15-337 |
4.64e-44 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 167.37 E-value: 4.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 15 VRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKE----CRVEPRSrefvIPQEVILGAGQQLFDFAARCL 90
Cdd:PLN02362 78 LKMLLTFVDDLPTGSEIGTYYALDLG--GTNFRVLRVQLGGQRSsilsQDVERHP----IPQHLMNSTSEVLFDFIASSL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 91 SEFL-----DAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRIDVVAMVND 165
Cdd:PLN02362 152 KQFVekeenGSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LDMRVAALVND 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 166 TVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHV---AALDEDRGRTCVSIEWGSFYDEDAlgpVLTTFDSALDRESL 242
Cdd:PLN02362 231 TVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIikcQGLLTTSGSMVVNMEWGNFWSSHL---PRTSYDIDLDAESP 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 243 TPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCILLDHVAEM-EDTATGTARVHTILQD-LGLSPR 320
Cdd:PLN02362 308 NPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARILKEtLGISEV 386
|
330
....*....|....*...
gi 1907093304 321 ASDA-ELVQYVCVAVCTR 337
Cdd:PLN02362 387 PLKVrKLVVKICDVVTRR 404
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
1-337 |
3.46e-37 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 146.56 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 1 MEQALKGQDSPapSVRMLPTYVRSTPHGTEQGDFLVLELgaTGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQ 80
Cdd:PLN02596 67 MTASLTAEETT--TLNMLVSYVASLPSGDEKGLYYGLNL--RGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 81 QLFDFAARCLSEFLDAYPVEN-----QGLKLGFNFSFPCHQTGLDRSTLISWtKGFRCSGVEGQDVVQLLRDAIQRQGTy 155
Cdd:PLN02596 143 ELFDYIALELAKFVAEHPGDEadtpeRVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGL- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 156 RIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDE---DRGRTCVSIEWGSFydeDALGPVLTT 232
Cdd:PLN02596 221 KIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF---NSCHLPITE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093304 233 FDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCILLDH-VAEM-EDTATGTARVHT 310
Cdd:PLN02596 298 FDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALF-GDTLPPKLTTPYLLRSPdMAAMhQDTSEDHEVVNE 376
|
330 340
....*....|....*....|....*....
gi 1907093304 311 ILQD-LGLSPRASDA-ELVQYVCVAVCTR 337
Cdd:PLN02596 377 KLKEiFGITDSTPMArEVVAEVCDIVAER 405
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