|
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 ... |
489-915 |
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: 766.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIIN 562
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 329755308 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTAVACR 915
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 ... |
489-915 |
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: 755.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY 565
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 566 SIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREA 645
Cdd:cd24129 81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 646 IRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSLGT 725
Cdd:cd24129 161 ATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCLAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 726 LSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALRQV 805
Cdd:cd24129 241 ISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALRQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 806 RAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSATVR 885
Cdd:cd24129 321 RAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQATVR 400
|
410 420 430
....*....|....*....|....*....|
gi 329755308 886 KLAPQCTVTFLQSEDGSGKGAALVTAVACR 915
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 ... |
39-469 |
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: 710.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400
|
410 420 430
....*....|....*....|....*....|.
gi 329755308 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
489-916 |
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: 662.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIIN 562
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKEthaSAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGkwrGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....
gi 329755308 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 916
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
489-911 |
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: 654.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGS-VQIINQV 564
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDthpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSqVKMESEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 565 YSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLRE 644
Cdd:cd24019 81 YAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 645 AIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNV---ASVPGDSGLMCINMEWGAFGDDG 721
Cdd:cd24019 161 AIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVekwDGDEGDPGQVIINTEWGAFGDNG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 722 SLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSL- 800
Cdd:cd24019 241 VLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDNEg 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 801 ALRQVRAILEDLGLTLTSD-DALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRglqeltVSVGVDGTLYKLHPHFSKL 879
Cdd:cd24019 321 DFSNTREILKELGLEDASDeDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKE------VTVGVDGSLYKYHPKFHKR 394
|
410 420 430
....*....|....*....|....*....|...
gi 329755308 880 VSATVRKLAP-QCTVTFLQSEDGSGKGAALVTA 911
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 ... |
490-916 |
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: 636.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 490 LTLEQMTVVQAQMREAMIRGLQG---EASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIINQ 563
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKqthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGkkrTVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 564 VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLR 643
Cdd:cd24127 82 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 644 EAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSL 723
Cdd:cd24127 162 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 724 GTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALR 803
Cdd:cd24127 242 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 804 QVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSAT 883
Cdd:cd24127 322 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQT 401
|
410 420 430
....*....|....*....|....*....|...
gi 329755308 884 VRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 916
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 ... |
489-916 |
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: 626.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG--SVQIINQ 563
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKEThptASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGrrSVRMYNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 564 VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLR 643
Cdd:cd24130 81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 644 EAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSL 723
Cdd:cd24130 161 EAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGCI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 724 GTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALR 803
Cdd:cd24130 241 DDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 804 QVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSAT 883
Cdd:cd24130 321 QVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQET 400
|
410 420 430
....*....|....*....|....*....|...
gi 329755308 884 VRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 916
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 ... |
489-911 |
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: 607.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGS---VQIIN 562
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDThptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKnqkVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 329755308 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 911
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 ... |
489-911 |
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: 552.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGEASS---LRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAE---GSVQIIN 562
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPtaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEdgkQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 329755308 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 911
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
39-469 |
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: 550.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGtkECRVEP 118
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLG--GTNFRVLLVTLNG--GSQVKM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24019 77 ESEIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSF 275
Cdd:cd24019 157 LLQEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEgdpGQVIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 276 YDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEME- 354
Cdd:cd24019 237 GDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIEs 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 355 DTATGTARVHTILQDLGLSPR-ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLqhsreqQTLQVAVATGGRVFERHPR 433
Cdd:cd24019 317 DNEGDFSNTREILKELGLEDAsDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRM------NRKEVTVGVDGSLYKYHPK 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 329755308 434 FLRILKETVTLLAP-NCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24019 391 FHKRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
489-911 |
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: 537.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQII---N 562
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATThptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVemeN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 329755308 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 911
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
481-915 |
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: 530.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 481 LEETLAPFQLTLEQMTVVQAQMREAMIRGLQ---GEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG- 556
Cdd:cd24092 2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRletHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 557 ----SVQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASG 632
Cdd:cd24092 82 egqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 633 CEGQDVVYLLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINM 712
Cdd:cd24092 162 AEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 713 EWGAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFL 792
Cdd:cd24092 242 EWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 793 SEIESDSLALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKL 872
Cdd:cd24092 322 SQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 329755308 873 HPHFSKLVSATVRKLAPQCTVTFLQSEDGSGKGAALVTAVACR 915
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 ... |
481-918 |
2.16e-174 |
|
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: 2.16e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 481 LEETLAPFQLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVA--- 554
Cdd:cd24124 21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNhek 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 555 EGSVQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCE 634
Cdd:cd24124 101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 635 GQDVVYLLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEW 714
Cdd:cd24124 181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 715 GAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSE 794
Cdd:cd24124 261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 795 IESDSLALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHP 874
Cdd:cd24124 341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 329755308 875 HFSKLVSATVRKLAPQCTVTFLQSEDGSGKGAALVTAVACRLTQ 918
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 ... |
44-469 |
1.13e-170 |
|
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: 503.15 E-value: 1.13e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 44 QLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREF 123
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLG--GSNFRVLWVQVNDEKNQKVEMESQVY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 124 VIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDA 203
Cdd:cd24089 84 AIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLRKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 204 IQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGP 283
Cdd:cd24089 164 IRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGSLED 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 284 VLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARV 363
Cdd:cd24089 244 IRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGLANA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 364 HTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVT 443
Cdd:cd24089 324 KEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHKAVR 403
|
410 420
....*....|....*....|....*.
gi 329755308 444 LLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24089 404 RLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
492-909 |
1.68e-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: 489.84 E-value: 1.68e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 492 LEQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV--AEGSVQIINQVYSIPE 569
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLdgNGGIFIIVQRKYKIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 570 CRAQGSGQKLFDHIVDCIVDFQKRQGLSGQS---LPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAI 646
Cdd:cd24018 81 EAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 647 RRRQaVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNV------ASVPGDSGLMCINMEWGAFGDD 720
Cdd:cd24018 161 DRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWGAFDNE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 721 GS-LGTlsTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDS 799
Cdd:cd24018 240 REvLPL--TKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 800 LA-LRQVRAILEDLGLT--LTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIREnrgLQELTVSVGVDGTLYKLHPHF 876
Cdd:cd24018 318 SPdLDAVRDILKELLAIdnTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS---LLPEPVTVGIDGSVYEKYPGF 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 329755308 877 SKLVSATVRKLAPQCT---VTFLQSEDGSGKGAALV 909
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 ... |
489-911 |
1.69e-152 |
|
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type III hexokinase.
Pssm-ID: 466940 [Multi-domain] Cd Length: 431 Bit Score: 456.31 E-value: 1.69e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 489 QLTLEQMTVVQAQMREAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLG--GTNFRVLLVRVA--EG-SVQI 560
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQaspAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTgiEGhRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 561 INQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVY 640
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 641 LLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDD 720
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 721 GSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSL 800
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 801 ALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLV 880
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400
|
410 420 430
....*....|....*....|....*....|.
gi 329755308 881 SATVRKLAPQCTVTFLQSEDGSGKGAALVTA 911
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 ... |
39-469 |
4.26e-146 |
|
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: 439.71 E-value: 4.26e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLG--GTNFRVLWVKVSDNGLQKVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24125 79 ENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24125 159 LLRKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24125 239 GSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24125 319 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRL 398
|
410 420 430
....*....|....*....|....*....|.
gi 329755308 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24125 399 HKTVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
39-473 |
3.28e-145 |
|
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: 437.36 E-value: 3.28e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLG--GTNFRVLLVKVRSGKWRGVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24091 79 HNKIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24091 159 LLREAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24091 239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24091 319 ALLQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVM 398
|
410 420 430
....*....|....*....|....*....|....*
gi 329755308 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAAR 473
Cdd:cd24091 399 HETVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
44-469 |
1.98e-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: 432.74 E-value: 1.98e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 44 QLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREF 123
Cdd:cd24126 6 TLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLG--GSKFRVLRVKVSEDGKQKVQMESQFY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 124 VIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDA 203
Cdd:cd24126 84 PTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLRKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 204 IQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGP 283
Cdd:cd24126 164 IRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGSLED 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 284 VLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARV 363
Cdd:cd24126 244 IRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGLYNT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 364 HTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVT 443
Cdd:cd24126 324 REILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHKVVR 403
|
410 420
....*....|....*....|....*.
gi 329755308 444 LLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24126 404 RLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
35-485 |
8.12e-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: 430.19 E-value: 8.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 35 LQQFKVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEC 114
Cdd:cd24124 25 LYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILRVQVNHEKNQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 115 RVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQ 194
Cdd:cd24124 103 NVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 195 DVVQLLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGS 274
Cdd:cd24124 183 DVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 275 FYDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEME 354
Cdd:cd24124 263 FGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 355 DTATGTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRF 434
Cdd:cd24124 343 KNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQY 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 329755308 435 LRILKETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARLAAHRRILEETL 485
Cdd:cd24124 423 SRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
39-473 |
2.35e-135 |
|
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: 411.97 E-value: 2.35e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTgtkECRVEP 118
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLG--GTNFRVLLVHVG---TAGVQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24129 76 TSEIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24129 156 LLREAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24129 236 GCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24129 316 ALRQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLV 395
|
410 420 430
....*....|....*....|....*....|....*
gi 329755308 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAAR 473
Cdd:cd24129 396 QATVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
39-474 |
1.02e-134 |
|
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: 410.44 E-value: 1.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLG--GTNFRVLLVRVRNGKWRGVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24128 79 HNKIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24128 159 LLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24128 239 GCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24128 319 ALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVM 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 329755308 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARL 474
Cdd:cd24128 399 HETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
39-474 |
4.24e-133 |
|
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: 406.22 E-value: 4.24e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLG--GTNFRVLLVKIRSGKKRTVEM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24127 79 HNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24127 159 LLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24127 239 GCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24127 319 ALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIM 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 329755308 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARL 474
Cdd:cd24127 399 HQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
39-474 |
3.29e-130 |
|
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: 398.54 E-value: 3.29e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEcRVEP 118
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLG--GTNFRVLLVKIRSGRR-SVRM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24130 78 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24130 158 MLREAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24130 238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24130 318 ALLQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRIL 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 329755308 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARL 474
Cdd:cd24130 398 QETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
493-910 |
1.63e-129 |
|
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: 393.95 E-value: 1.63e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 493 EQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECR 571
Cdd:cd24000 2 EDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLdGKGIEVTISKKYEIPDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 572 AQGSGQKLFDHIVDCIVDFQKRQGLSgQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRQa 651
Cdd:cd24000 82 KTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALKKRG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 652 VELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNvasVPGDSGLMCINMEWGAFGDDGSLGtlsTRFD 731
Cdd:cd24000 160 LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKNSLPR---TEYD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 732 TSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLtnlgvlfrgqktqclqARDIFKTkflseiesdslalrqvrailed 811
Cdd:cd24000 234 REVDKASENPGFQPLEKMVSGKYLGELVRLILKDL----------------ADEILRK---------------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 812 lgltltsddalmvleVCQAVSRRAAQLCGAGVAAVVEKIRENrglQELTVSVGVDGTLYKLHPHFSKLVSATVRKL-APQ 890
Cdd:cd24000 276 ---------------ICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLKELlGRG 337
|
410 420
....*....|....*....|
gi 329755308 891 CTVTFLQSEDGSGKGAALVT 910
Cdd:cd24000 338 IRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
35-473 |
6.72e-125 |
|
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: 385.39 E-value: 6.72e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 35 LQQFKVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKE- 113
Cdd:cd24092 6 LAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLG--GTNFRVMLVKVGEGEEg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 114 -CRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVE 192
Cdd:cd24092 84 qWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 193 GQDVVQLLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEW 272
Cdd:cd24092 164 GNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 273 GSFYDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAE 352
Cdd:cd24092 244 GAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 353 MEDTATGTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHP 432
Cdd:cd24092 324 VESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHP 403
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 329755308 433 RFLRILKETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAAR 473
Cdd:cd24092 404 SFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
490-913 |
2.03e-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: 370.84 E-value: 2.03e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 490 LTLEQMTVVQAQMREAMIRGLQGEA-SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY--- 565
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGgSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYeev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 566 SIPECRAQGSGQKLFDHIVDCIVDFQKRQG----LSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYL 641
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 642 LREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFg 718
Cdd:cd24020 161 LEEALER-QGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 719 DDGSLGtlSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEI-ES 797
Cdd:cd24020 239 RSSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 798 DSLALRQVRAILED-LGLTLTS-DDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI-RENRGLQELTVS-VGVDGTLYKLH 873
Cdd:cd24020 317 DSPDLETVARILKDaLGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGSSPAQRTvVAVDGGLYEHY 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 329755308 874 PHFSKLVSATVRKL---APQCTVTFLQSEDGSGKGAALVTAVA 913
Cdd:cd24020 397 PKFREYMQQALVELlgdEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
43-467 |
8.94e-116 |
|
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: 360.80 E-value: 8.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 43 TQLQQIQASLLCSMEQALKGQDSpapSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKEcRVEPRSRE 122
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLEGDGG---SLPMLPSFVTERPTGKETGTYLALDLGGT--NLRVCLVTLDGNGG-IFIIVQRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 123 FVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQG---LKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQL 199
Cdd:cd24018 76 YKIPDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 200 LRDAIQRQGtYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALD------EDRGRTCVSIEWG 273
Cdd:cd24018 156 LQNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsgsvTKSDEMIINTEWG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 274 SFYDEDALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEM 353
Cdd:cd24018 235 AFDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 354 E-DTATGTARVHTILQDLGLSPRAS--DAELVQYVCVAVCTRaaqLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFER 430
Cdd:cd24018 314 EaDTSPDLDAVRDILKELLAIDNTTleDRKLIKRICELVSTR---AARLSAAAIAAILLKRGSLLPEPVTVGIDGSVYEK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 329755308 431 HPRFLRILKETVTLLAPNC---DVSFIPSVDGGGRGVAMV 467
Cdd:cd24018 391 YPGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
493-913 |
6.15e-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: 6.15e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 493 EQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECR 571
Cdd:cd24087 2 ERLRKITDHFISELEKGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLgGNGKFDITQSKYRLPEEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 572 AQGSGQKLFDHIVDCIVDF---QKRQGLSGQsLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRR 648
Cdd:cd24087 82 KTGTGEELWDFIADCLKKFveeHFPGGKSEP-LPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 649 RQaVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEelrNVASVP-------GDSGLMCINMEWGAFgDDG 721
Cdd:cd24087 161 RN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYME---VVSNIPklehddiPPDSPMAINCEYGAF-DNE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 722 SLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLA 801
Cdd:cd24087 236 HLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 802 --LRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKirenRGLQelTVSVGVDGTLYKLHPHFSKL 879
Cdd:cd24087 316 nlEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYK--TCHVAADGSVYNKYPGFKER 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 329755308 880 VSATVRKL----APQCTVTFLQSEDGSGKGAALVTAVA 913
Cdd:cd24087 390 AAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
493-909 |
1.33e-107 |
|
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: 1.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 493 EQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECR 571
Cdd:cd24088 2 EKLDKLTAEFQRQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELhGDGTFSLRQEKSKIPDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 572 AQGSGQK-LFDHIVDCIVDFQK-------RQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLR 643
Cdd:cd24088 82 KTGVTAKdLFDYLAKSVEAFLTkhhgdsfAAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 644 EAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCE---MGLIVGTGTNACYMEELRNV-----ASVPGDS-GLMCINMEW 714
Cdd:cd24088 162 DELDR-QGIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddSSRVGKGkTHMVINTEW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 715 GAFgdDGSLGTL-STRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTN---LGVLFRGQKTQCLQARDIFKTK 790
Cdd:cd24088 241 GSF--DNELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKqglFLIQYNDKSPSALNTPYGLDTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 791 FLSEIESDSLA-LRQVRAIL-EDLGL-TLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDG 867
Cdd:cd24088 319 VLSAIEIDSEAeLRATRKVLlDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEINIGVDG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 329755308 868 TLYKLHPHFSKLVSATVRKLAPQCT----VTFLQSEDGSGKGAALV 909
Cdd:cd24088 399 SVIEFYPGFESMLREALRLLLIGAEgekrIKIGIAKDGSGVGAALC 444
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
678-912 |
1.72e-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: 318.67 E-value: 1.72e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 678 EMGLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMY 754
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 755 LGEIVRHILLHLTNLGVLFRGQkTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGL-TLTSDDALMVLEVCQAV 831
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEElLGIeTVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 832 SRRAAQLCGAGVAAVVEKIRENRglqelTVSVGVDGTLYKLHPHFSKLVSATVRK-LAPQCTVTFLQSEDGSGKGAALVT 910
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 329755308 911 AV 912
Cdd:pfam03727 235 AV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
482-913 |
1.56e-101 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 324.71 E-value: 1.56e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 482 EETLAPFQLTLEQMTVVQAQMRE-------AMIRGLQG----------EASSLRMLPTYVRATPDGSERGDFLALDLGGT 544
Cdd:PTZ00107 5 IKQRVRLASLVNQFTMSKEKLKElvdyflyELVEGLEAhrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 545 NFRVLLVRVAEGSVQIINQ-VYSIPECRAQG---------SGQKLFDHIVDCIVDFQKRQGL---SGQSLPLGFTFSFPC 611
Cdd:PTZ00107 85 NFRAVRVSLRGGGKMERTQsKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPVGFTFSFPC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 612 KQLGLDQGILLNWTKGF-----NASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPR----CEMGLI 682
Cdd:PTZ00107 165 TQLSVNNAILIDWTKGFetgraTNDPVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 683 VGTGTNACYME---ELRNVASVPgdsglmcINMEWGAFgdDGSLGTlsTRFDTSVDQASINPGKQRFEKMISGMYLGEIV 759
Cdd:PTZ00107 244 IGTGSNACYFEpevSAYGYAGTP-------INMECGNF--DSKLPI--TPYDLEMDWYTPNRGRQQFEKMISGAYLGEIS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 760 RHILLHLTNLGVLFRGQKtqclqaRDIFKTKFLSEIESD-SLALRQVRAILEDL-GLTLTSDDALMVLEVCQAVSRRAAQ 837
Cdd:PTZ00107 313 RRLIVHLLQLKAPPKMWQ------SGSFESEDASMILNDqSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQ 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 329755308 838 LCGAGVAAVVEKIRENRGLqeltVSVGVDGTLYKLHPHFSKLVSATVRK-LAPQ-CTVTFLQSEDGSGKGAALVTAVA 913
Cdd:PTZ00107 387 LAAAFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
488-914 |
3.05e-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: 3.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 488 FQLTLEQMTVVQAQMREAMIRGLQGEASSLRMLPTYVrATPDGS-ERGDFLALDLGGTNFRVLLVRVA-EGSVQIIN-QV 564
Cdd:COG5026 15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFDgEGTFEIENfKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 565 YSIPECRAQGSGQKLFDHIVDCIVDfqkrqgLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLRE 644
Cdd:COG5026 94 FPLPGTSSEITAEEFFDFIADYIEP------LLDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 645 AIRRRQAVELNVVAIVNDTVGTMMSCGYDDP----RCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGdd 720
Cdd:COG5026 168 ALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNFN-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 721 gslGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGvLFRGQKTQCLQARDIFKTKFLSE-IESDS 799
Cdd:COG5026 246 ---KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRfLADPS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 800 LALRQVRAILEDlgltLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI-RENRGLQELTVSvgVDGTLYKLHPHFSK 878
Cdd:COG5026 322 DEKEILSQCLEA----GSEEDREILREIADAIVERAARLVAATLAGILLHLgPGKTPLKPHCIA--IDGSTYEKMPGLAE 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 329755308 879 LVSATVRK-LAPQCT--VTFLQSEDGSGKGAALVTAVAC 914
Cdd:COG5026 396 KIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
44-468 |
1.69e-91 |
|
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: 294.18 E-value: 1.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 44 QLQQIQASLLCSMEQALKGQDSpapSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEcrVEPRSREF 123
Cdd:cd24000 3 DLKEITDAFLEELEKGLAGEPS---SLKMLPSYVSPLPTGLESGEFLAIDLG--GTNLRVALVSLDGKGI--EVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 124 VIPQEVILGAGQQLFDFAARCLSEFLDAYPVeNQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDA 203
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLKENGL-KKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 204 IQRQGtYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVaalDEDRGRTCVSIEWGSFYDEDAlgp 283
Cdd:cd24000 155 LKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI---LLGDGGMIINTEWGNFGKNSL--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 284 VLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHgvlfdgcaspallsqgciLLDHVAEMedtatgtarv 363
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------ILRKICEL---------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 364 htilqdlgLSPRAsdAELVQYVCVAVctraaqlcaaalaavlsrLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVT 443
Cdd:cd24000 280 --------VAERS--ARLAAAAIAAL------------------LRKTGDSPEKKITIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420
....*....|....*....|....*.
gi 329755308 444 -LLAPNCDVSFIPSVDGGGRGVAMVT 468
Cdd:cd24000 332 eLLGRGIRIELVLVEDGSLIGAALAA 357
|
|
| PLN02914 |
PLN02914 |
hexokinase |
452-911 |
3.71e-91 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 297.95 E-value: 3.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 452 SFIPSVDGGGRGVAMvTAVAARLAAHRRILEETLAPFQLTLEQMTVVQAQMREAMIRGLQGE-ASSLRMLPTYVRATPDG 530
Cdd:PLN02914 13 SFTFSSRPRRRPRSR-MAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDgGGDLKMILSYVDSLPSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 531 SERGDFLALDLGGTNFRVLLVRVAEGSVQII----NQVySIPECRAQGSGQKLFDHIVDCIVDFQKRQG-----LSGQSL 601
Cdd:PLN02914 92 NEKGLFYALDLGGTNFRVLRVQLGGKDERVIatefEQV-SIPQELMFGTSEELFDFIASGLANFVAKEGgkfhlPEGRKR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 602 PLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGL 681
Cdd:PLN02914 171 EIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMER-QGLDMRVSALVNDTVGTLAGARYWDDDVMVAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 682 IVGTGTNACYMEELRNVASVPG---DSGLMCINMEWGAFGDdgslGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEI 758
Cdd:PLN02914 250 ILGTGTNACYVERTDAIPKLQGqksSSGRTIINTEWGAFSD----GLPLTEFDREMDAASINPGEQIFEKTISGMYLGEI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 759 VRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGLTLTSDDALMVLEVCQAVSRRAA 836
Cdd:PLN02914 326 VRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDnSDDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 837 QLCGAGVAAVVEKIRENR---GLQELTVsVGVDGTLYKLHPHFSK-LVSATVRKLAPQCT--VTFLQSEDGSGKGAALVT 910
Cdd:PLN02914 406 RLAGAGIVGILEKMEEDSkgmIFGKRTV-VAMDGGLYEKYPQYRRyMQDAVTELLGLELSknIAIEHTKDGSGIGAALLA 484
|
.
gi 329755308 911 A 911
Cdd:PLN02914 485 A 485
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
44-476 |
9.97e-88 |
|
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: 286.86 E-value: 9.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 44 QLQQIQASLLCSMEQALKGQdsPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGtKECRVEPR-SRE 122
Cdd:cd24020 5 RLRQVADAMVVEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLG--GTNFRVLRVQLGG-KEGRVDKQeYEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 123 FVIPQEVILGAGQQLFDFAARCLSEFLDAYP----VENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24020 80 VPIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGtYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRT---CVSIEWGSF 275
Cdd:cd24020 160 LLEEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSgemVINTEWGNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 276 YdeDALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEM-E 354
Cdd:cd24020 239 R--SSHLP-RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 355 DTATGTARVHTILQDLGLSPRAS--DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQH--SREQQTLQVAVATGGRVFER 430
Cdd:cd24020 316 DDSPDLETVARILKDALGIDDTSleARKVVVEVCDLVAERGARLAAAGIVGILKKLGRdgGGSSPAQRTVVAVDGGLYEH 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 329755308 431 HPRFLRILKETVT-LLAPNC--DVSFIPSVDGGGRGvamvtavAARLAA 476
Cdd:cd24020 396 YPKFREYMQQALVeLLGDEAadSVELELSNDGSGIG-------AALLAA 437
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
480-672 |
3.49e-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: 271.30 E-value: 3.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 480 ILEETLAPFQLTLEQMTVVQAQMREAMIRGLQGE-ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVA-EGS 557
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEgSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGgDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 558 VQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLS---GQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCE 634
Cdd:pfam00349 81 FEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGVV 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 329755308 635 GQDVVYLLREAIRRRQaVELNVVAIVNDTVGTMMSCGY 672
Cdd:pfam00349 161 GKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
44-445 |
9.02e-78 |
|
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: 260.41 E-value: 9.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 44 QLQQIQASLLCSMEQALKGQDSPAPsvrMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKECRVepRSREF 123
Cdd:cd24088 3 KLDKLTAEFQRQMEKGLAKHGKGMA---MIPTYVTGVPDGTETGTYLALDLGGT--NFRVCSVELHGDGTFSL--RQEKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 124 VIPQEVILGA-GQQLFDFAARCLSEFL-----DAYPVENQG--LKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQD 195
Cdd:cd24088 76 KIPDELKTGVtAKDLFDYLAKSVEAFLtkhhgDSFAAGKDDdrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 196 VVQLLRDAIQRQGTyRIDVVAMVNDTVGTMMGCELGTRPCE---VGLIVDTGTNACYMEEARHVAALD------EDRGRT 266
Cdd:cd24088 156 VVKLLQDELDRQGI-PVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIKKLDdssrvgKGKTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 267 CVSIEWGSFYDEDALGPVlTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGC--ASPALLSQGC 344
Cdd:cd24088 235 VINTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYndKSPSALNTPY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 345 IL----LDHVAemEDTATGTARV-HTILQDLGL-SPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQ 418
Cdd:cd24088 314 GLdtavLSAIE--IDSEAELRATrKVLLDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGE 391
|
410 420
....*....|....*....|....*..
gi 329755308 419 VAVATGGRVFERHPRFLRILKETVTLL 445
Cdd:cd24088 392 INIGVDGSVIEFYPGFESMLREALRLL 418
|
|
| PLN02405 |
PLN02405 |
hexokinase |
463-911 |
1.78e-77 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 261.30 E-value: 1.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 463 GVAMVTAVAARLAAHR--------------RILEETLAPFQLTLEQmtvVQAQMREAMIRGLQGEA-SSLRMLPTYVRAT 527
Cdd:PLN02405 12 CAAAVCAAAALVVRRRmkssgkwarameilKEFEEDCATPIGKLRQ---VADAMTVEMHAGLASEGgSKLKMLISYVDNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 528 PDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY---SIPECRAQGSGQKLFDHIVDCIVDFQKRQG-----LSGQ 599
Cdd:PLN02405 89 PSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFeevSIPPHLMTGSSDALFDFIAAALAKFVATEGedfhlPPGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 600 SLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEM 679
Cdd:PLN02405 169 QRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMER-VGLDMRVSALVNDTIGTLAGGRYYNPDVVA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 680 GLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFGddgSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLG 756
Cdd:PLN02405 248 AVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR---SSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 757 EIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGLTLTS-DDALMVLEVCQAVSR 833
Cdd:PLN02405 325 EILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDtSPDLKVVGSKLKDiLEIPNTSlKMRKVVVELCNIVAT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 834 RAAQLCGAGVAAVVEKI-RENRGLQELTVSV-GVDGTLYKLHPHFSKLVSATVRKLAPQ---CTVTFLQSEDGSGKGAAL 908
Cdd:PLN02405 405 RGARLSAAGIYGILKKLgRDTVKDGEKQKSViAMDGGLFEHYTEFSKCMESTLKELLGEevsESIEVEHSNDGSGIGAAL 484
|
...
gi 329755308 909 VTA 911
Cdd:PLN02405 485 LAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
463-911 |
1.59e-74 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 253.65 E-value: 1.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 463 GVAMVTAVAA----------RLAAHRR------ILEETLAPFQLTLEQMTVVQAQMREAMIRGLQGEA-SSLRMLPTYVR 525
Cdd:PLN02362 7 GLAAAAAVAAcavaavmvgrRVKSRRKwrrvvgVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGgSKLKMLLTFVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 526 ATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQ---VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLP 602
Cdd:PLN02362 87 DLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQdveRHPIPQHLMNSTSEVLFDFIASSLKQFVEKEENGSEFSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 603 -----LGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRqAVELNVVAIVNDTVGTMMSCGYDDPRC 677
Cdd:PLN02362 167 vrrreLGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 678 EMGLIVGTGTNACYMEELRNVASVPG---DSGLMCINMEWGAFgddGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMY 754
Cdd:PLN02362 246 VAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---WSSHLPRTSYDIDLDAESPNPNDQGFEKMISGMY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 755 LGEIVRHILLHLTNLGVLFrGQKTQCLQARDIFKTKFLSEI-ESDSLALRQVRAIL-EDLGLtltSDDAL----MVLEVC 828
Cdd:PLN02362 323 LGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARILkETLGI---SEVPLkvrkLVVKIC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 829 QAVSRRAAQLCGAGVAAVVEKI-------------RENRGLQELTVsVGVDGTLYKLHPHFSKLVSATVRKLAPQCT--- 892
Cdd:PLN02362 399 DVVTRRAARLAAAGIVGILKKIgrdgsggitsgrsRSDIQIMRRTV-VAVEGGLYTNYTMFREYLHEALNEILGEDVaqh 477
|
490
....*....|....*....
gi 329755308 893 VTFLQSEDGSGKGAALVTA 911
Cdd:PLN02362 478 VILKATEDGSGIGSALLAA 496
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
33-228 |
4.15e-74 |
|
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: 241.64 E-value: 4.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 33 ECLQQFKVTRTQLQQIQASLLCSMEQALKGQDSPapSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGtk 112
Cdd:pfam00349 4 ELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSS--SLKMLPTYVTSLPTGTEKGTFLALDLGGT--NFRVCLVELGG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 113 ECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQG---LKLGFNFSFPCHQTGLDRSTLISWTKGFRCS 189
Cdd:pfam00349 78 DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEekeLPLGFTFSFPVEQTSLDSGTLIRWTKGFDIP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 329755308 190 GVEGQDVVQLLRDAIQRQGtYRIDVVAMVNDTVGTMMGC 228
Cdd:pfam00349 158 GVVGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAG 195
|
|
| PLN02914 |
PLN02914 |
hexokinase |
70-469 |
1.79e-70 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 242.10 E-value: 1.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 70 VRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFL 149
Cdd:PLN02914 78 LKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 150 ----DAYPVEnQGLK--LGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRIDVVAMVNDTVG 223
Cdd:PLN02914 156 akegGKFHLP-EGRKreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 224 TMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSFYDedalGPVLTTFDSALDRESLTPG 300
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD----GLPLTEFDREMDAASINPG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 301 AQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCIL-LDHVAEM-EDTATGTARVHTILQD-LGLSPRAS 377
Cdd:PLN02914 310 EQIFEKTISGMYLGEIVRRVLLKMAETSDLF-GHFVPEKLSTPFALrTPHLCAMqQDNSDDLQAVGSILYDvLGVEASLS 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 378 DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTL--QVAVATGGRVFERHPRFLRILKETVT-LLAP--NCDVS 452
Cdd:PLN02914 389 ARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTeLLGLelSKNIA 468
|
410
....*....|....*..
gi 329755308 453 FIPSVDGGGRGVAMVTA 469
Cdd:PLN02914 469 IEHTKDGSGIGAALLAA 485
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
37-472 |
2.90e-69 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 237.65 E-value: 2.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 37 QFKVTRTQLQQIQASLLCSMEQALKGQDS------PAP-SVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLT 109
Cdd:PTZ00107 17 QFTMSKEKLKELVDYFLYELVEGLEAHRRhrnlwiPNEcSFKMLDSCVYNLPTGKEKGVYYAIDFG--GTNFRAVRVSLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 110 GTKEcrVEPRSREFVIPQEVILGA---------GQQLFDFAARCLSEFLD--AYPVE-NQGLKLGFNFSFPCHQTGLDRS 177
Cdd:PTZ00107 95 GGGK--MERTQSKFSLPKSALLGEkglldkkatATDLFDHIAKSIKKMMEenGDPEDlNKPVPVGFTFSFPCTQLSVNNA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 178 TLISWTKGFRCS-----GVEGQDVVQLLRDAIQRQGTyRIDVVAMVNDTVGTMMGC----ELGTRPCEVGLIVDTGTNAC 248
Cdd:PTZ00107 173 ILIDWTKGFETGratndPVEGKDVGELLNDAFKRNNV-PANVVAVLNDTVGTLISCayqkPKNTPPCQVGVIIGTGSNAC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 249 YMEEArhVAAldedRGR--TCVSIEWGSFydeDALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQ 326
Cdd:PTZ00107 252 YFEPE--VSA----YGYagTPINMECGNF---DSKLP-ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 327 HGvlfdgcASPALLSQGCILLDHVAEM-EDTATGTARVHTILQDL-GLSPRASDAELVQYVCVAVCTRAAQLCAAALAAV 404
Cdd:PTZ00107 322 LK------APPKMWQSGSFESEDASMIlNDQSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAP 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 405 LSRLQHSREQQTlqvaVATGGRVFERHPRFLRILKETVTL-LAPN-CDVSFIPSVDGGGRGVAMVTAVAA 472
Cdd:PTZ00107 396 AKKTRTVQGKAT----VAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMVA 461
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
44-472 |
2.71e-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: 231.11 E-value: 2.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 44 QLQQIQASLLCSMEQAL--KGQDSPapsvrMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKEcrVEPRSR 121
Cdd:cd24087 3 RLRKITDHFISELEKGLskKGGNIP-----MIPTWVMGFPTGKETGDYLALDLGGT--NLRVCLVKLGGNGK--FDITQS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 122 EFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVEN--QGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQL 199
Cdd:cd24087 74 KYRLPEELKTGTGEELWDFIADCLKKFVEEHFPGGksEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 200 LRDAIQRQGTyRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAAL-------DEDRGRTCvsiEW 272
Cdd:cd24087 154 LQKALKKRNV-PIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLehddippDSPMAINC---EY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 273 GSFYDEDALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDG----------CASPALLSQ 342
Cdd:cd24087 230 GAFDNEHLVLP-RTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGqdtsklekpyVMDTSFLSR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 343 gcILLDHVAEMEDTATgtarvhTILQDLGLSPRASDAELVQYVCVAVCTRaaqlcaaalaavLSRL---------QHSRE 413
Cdd:cd24087 309 --IEEDPFENLEDTDD------LFQHFFGLETTVPERKFIRRLAELIGTR------------AARLsacgiaaicKKRGY 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 329755308 414 QQTLqvaVATGGRVFERHPRF-------LR-ILKETVTllapNCDVSFIPSVDGGGRGVAMVTAVAA 472
Cdd:cd24087 369 KTCH---VAADGSVYNKYPGFkeraaqaLKdIFGWDGE----DDPIKTVPAEDGSGVGAAIIAALTK 428
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
36-392 |
1.66e-62 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 218.29 E-value: 1.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 36 QQFKVTRTQLQQIQASLLCSMEQALKGQDSpapSVRMLPTYVrSTPHG-TEQGDFLVLELGATgaSLRVLWVTLTGTKEC 114
Cdd:COG5026 13 HGFDLSSIDLEEIAAKFQEEMEKGLEGKKS---SLKMLPSYL-GLPTGvKETGPVIALDAGGT--NFRVALVRFDGEGTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 115 RVEpRSREFVIP---QEVilgAGQQLFDFAARCLSEFLDaypvenQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGV 191
Cdd:COG5026 87 EIE-NFKSFPLPgtsSEI---TAEEFFDFIADYIEPLLD------ESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 192 EGQDVVQLLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPC----EVGLIVDTGTNACYMEEARHVAALDEDRGRTC 267
Cdd:COG5026 157 EGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 268 VSIEWGSFydedALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGvLFDGCASPALLSQGCIll 347
Cdd:COG5026 237 INMESGNF----NKLP-RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSL-- 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 329755308 348 dHVAEMEDTATGTARVHTILQDLGLSPRASDAELVQYVCVAVCTR 392
Cdd:COG5026 309 -TTVDMSRFLADPSDEKEILSQCLEAGSEEDREILREIADAIVER 352
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
236-470 |
7.86e-60 |
|
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: 203.88 E-value: 7.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 236 EVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSFYDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLY 312
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLpksGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 313 LGELVRLVLVHLTQHGVLFDGcASPALLSQGCILLDHVAEME-DTATGTARVHTILQD-LGLSPRAS-DAELVQYVCVAV 389
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIEsDPSEDLETTREILEElLGIETVTEeDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 390 CTRaaqlcaaalaavLSRL---------QHSREQQTLQVAVatGGRVFERHPRFLRILKETV-TLLAPNCDVSFIPSVDG 459
Cdd:pfam03727 160 STR------------AARLvaagiaailKKIGRDKKVTVGV--DGSVYEKYPGFRERLQEALrELLGPGDKVVLVLAEDG 225
|
250
....*....|.
gi 329755308 460 GGRGVAMVTAV 470
Cdd:pfam03727 226 SGVGAALIAAV 236
|
|
| PLN02405 |
PLN02405 |
hexokinase |
44-469 |
3.03e-53 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 193.89 E-value: 3.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 44 QLQQIQASLLCSMEQALKGQDspAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREF 123
Cdd:PLN02405 54 KLRQVADAMTVEMHAGLASEG--GSKLKMLISYVDNLPSGDEKGLFYALDLG--GTNFRVLRVLLGGKDGRVVKQEFEEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 124 VIPQEVILGAGQQLFDFAARCLSEFL-----DAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:PLN02405 130 SIPPHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 199 LLRDAIQRQGTyRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVA---ALDEDRGRTCVSIEWGSF 275
Cdd:PLN02405 210 ELTKAMERVGL-DMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPkwhGLLPKSGEMVINMEWGNF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 276 YDEDAlgpVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEM-E 354
Cdd:PLN02405 289 RSSHL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMhH 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 355 DTATGTARVHTILQDLGLSPRAS--DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHS--REQQTLQVAVATGGRVFER 430
Cdd:PLN02405 366 DTSPDLKVVGSKLKDILEIPNTSlkMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEH 445
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 329755308 431 HPRFLRILKETVT-LLAPNC--DVSFIPSVDGGGRGVAMVTA 469
Cdd:PLN02405 446 YTEFSKCMESTLKeLLGEEVseSIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
478-911 |
2.33e-46 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 173.91 E-value: 2.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 478 RRILEETLAPFQLTLEQMTVVQAQMREAMIrglQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAeGS 557
Cdd:PLN02596 43 RKFARECATPVSKLWEVADALVSDMTASLT---AEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLG-GK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 558 VQIINQVY----SIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLP-----LGFTFSFPCKQLGLDQGILLNWtKGF 628
Cdd:PLN02596 119 NEPISDLYreeiSIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 629 NASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPG---DS 705
Cdd:PLN02596 198 SADDTVGKALVNDINRALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspES 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 706 GLMCINMEWGAFGddgSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARD 785
Cdd:PLN02596 277 QEIVISTEWGNFN---SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 786 IFKTKFLSEIESDSLALRQV--RAILEDLGLTLTSDDAL-MVLEVCQAVSRRAAQLCGAGVAAVVEKIREnrgLQELTVS 862
Cdd:PLN02596 354 LLRSPDMAAMHQDTSEDHEVvnEKLKEIFGITDSTPMAReVVAEVCDIVAERGARLAGAGIVGIIKKLGR---IENKKSV 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 329755308 863 VGVDGTLYKLHPHFSKLVSATV-RKLAPQCT--VTFLQSEDGSGKGAALVTA 911
Cdd:PLN02596 431 VTVEGGLYEHYRVFRNYLHSSVwEMLGSELSdnVVIEHSHGGSGAGALFLAA 482
|
|
| PLN02362 |
PLN02362 |
hexokinase |
44-392 |
2.60e-44 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 168.14 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 44 QLQQIQASLLCSMEQALKGQDspAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKE----CRVEPR 119
Cdd:PLN02362 54 RLRQVVDAMAVEMHAGLASEG--GSKLKMLLTFVDDLPTGSEIGTYYALDLG--GTNFRVLRVQLGGQRSsilsQDVERH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 120 SrefvIPQEVILGAGQQLFDFAARCLSEFL-----DAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQ 194
Cdd:PLN02362 130 P----IPQHLMNSTSEVLFDFIASSLKQFVekeenGSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 195 DVVQLLRDAIQRQGtYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHV---AALDEDRGRTCVSIE 271
Cdd:PLN02362 206 DVAECLQGALNRRG-LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIikcQGLLTTSGSMVVNME 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 272 WGSFYDEDAlgpVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCILLDHVA 351
Cdd:PLN02362 285 WGNFWSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVA 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 329755308 352 EM-EDTATGTARVHTILQD-LGLSPRASDA-ELVQYVCVAVCTR 392
Cdd:PLN02362 361 AMhEDDSPELQEVARILKEtLGISEVPLKVrKLVVKICDVVTRR 404
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
43-392 |
5.18e-38 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 149.26 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 43 TQLQQIQASLLCSMEQALKGQDSPapSVRMLPTYVRSTPHGTEQGDFLVLELgaTGASLRVLWVTLTGTKECRVEPRSRE 122
Cdd:PLN02596 54 SKLWEVADALVSDMTASLTAEETT--TLNMLVSYVASLPSGDEKGLYYGLNL--RGSNFLLLRARLGGKNEPISDLYREE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 123 FVIPQEVILGAGQQLFDFAARCLSEFLDAYPVEN-----QGLKLGFNFSFPCHQTGLDRSTLISWtKGFRCSGVEGQDVV 197
Cdd:PLN02596 130 ISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEadtpeRVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 198 QLLRDAIQRQGTyRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDE---DRGRTCVSIEWGS 274
Cdd:PLN02596 209 NDINRALEKHGL-KIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329755308 275 FydeDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCILLDH-VAEM 353
Cdd:PLN02596 288 F---NSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALF-GDTLPPKLTTPYLLRSPdMAAM 363
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 329755308 354 -EDTATGTARVHTILQD-LGLSPRASDA-ELVQYVCVAVCTR 392
Cdd:PLN02596 364 hQDTSEDHEVVNEKLKEiFGITDSTPMArEVVAEVCDIVAER 405
|
|
| |
