|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
478-911 |
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: 898.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 478 LLSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRrSVQMYN 557
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRR-SVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 558 KIFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDML 637
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 638 REAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNGC 717
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 718 IDNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLAL 797
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 798 LQVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLRE 877
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399
|
410 420 430
....*....|....*....|....*....|....
gi 699630172 878 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 911
Cdd:cd24130 400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
479-910 |
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: 866.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNK 558
Cdd:cd24091 2 LSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:cd24091 82 IYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNGCI 718
Cdd:cd24091 162 EAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 719 DNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLALL 798
Cdd:cd24091 242 DDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 799 QVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLRET 878
Cdd:cd24091 322 QVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHET 401
|
410 420 430
....*....|....*....|....*....|..
gi 699630172 879 VKELAPQCDVTFMLSEDGSGKGAALITAVAKR 910
Cdd:cd24091 402 VKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
30-458 |
0e+00 |
|
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the first two domains of HKDC1.
Pssm-ID: 466976 [Multi-domain] Cd Length: 429 Bit Score: 821.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSQLES 109
Cdd:cd24126 1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24126 81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 270 LDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGL 349
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 350 SNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHK 429
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400
|
410 420
....*....|....*....|....*....
gi 699630172 430 VVRRLVPNCDVRFLLSVSGSGKGAAMVTA 458
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
479-911 |
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: 797.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNK 558
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:cd24127 82 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNGCI 718
Cdd:cd24127 162 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 719 DNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLALL 798
Cdd:cd24127 242 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 799 QVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLRET 878
Cdd:cd24127 322 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQT 401
|
410 420 430
....*....|....*....|....*....|...
gi 699630172 879 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 911
Cdd:cd24127 402 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
3-474 |
0e+00 |
|
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase.
Pssm-ID: 466974 [Multi-domain] Cd Length: 473 Bit Score: 776.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 3 AVHLLAFHFTKLKEDQIKKVDRYLYHMRLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLA 82
Cdd:cd24124 2 AAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 83 VDLGGSQFRAHQVKVCDDGKQSSQLESKFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTK 162
Cdd:cd24124 82 LDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 163 LEEGVLLAWTKHFKVRGVQDTDVVSSLRKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEM 242
Cdd:cd24124 162 IDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 243 RHIDLVEGDEGRMCINTEWGAFGDDGALDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNG 322
Cdd:cd24124 242 RHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 323 KVSTALLTKGKIEMKHVSAMEKYKEGLSNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKK 402
Cdd:cd24124 322 RITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699630172 403 LLRMRTTVGIDGGLYKTHPQYAKRLHKVVRRLVPNCDVRFLLSVSGSGKGAAMVTAVAYRLAAQRKQIDAAL 474
Cdd:cd24124 402 TPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
479-911 |
0e+00 |
|
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type II hexokinase.
Pssm-ID: 466978 [Multi-domain] Cd Length: 435 Bit Score: 767.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNK 558
Cdd:cd24128 2 LSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:cd24128 82 IYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNGCI 718
Cdd:cd24128 162 EAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 719 DNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLALL 798
Cdd:cd24128 242 DDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 799 QVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLRET 878
Cdd:cd24128 322 QVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHET 401
|
410 420 430
....*....|....*....|....*....|...
gi 699630172 879 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 911
Cdd:cd24128 402 VKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
30-458 |
0e+00 |
|
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of types I and II hexokinases.
Pssm-ID: 466939 [Multi-domain] Cd Length: 429 Bit Score: 730.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSQLES 109
Cdd:cd24089 1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24089 81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 270 LDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGL 349
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 350 SNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHK 429
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400
|
410 420
....*....|....*....|....*....
gi 699630172 430 VVRRLVPNCDVRFLLSVSGSGKGAAMVTA 458
Cdd:cd24089 401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
479-906 |
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: 705.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRrsVQMYNK 558
Cdd:cd24019 2 LSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQ--VKMESE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:cd24019 80 IYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEI---VEGNEGKMCINTEWGGFGDN 715
Cdd:cd24019 160 EAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGDN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 716 GCIDNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESD-R 794
Cdd:cd24019 240 GVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDnE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 795 LALLQVRRILQQLGL-DSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKkredrgVEHLQITVGVDGTLYKLHPHFSR 873
Cdd:cd24019 320 GDFSNTREILKELGLeDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNR------MNRKEVTVGVDGSLYKYHPKFHK 393
|
410 420 430
....*....|....*....|....*....|....
gi 699630172 874 VLRETVKELAP-QCDVTFMLSEDGSGKGAALITA 906
Cdd:cd24019 394 RMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
479-910 |
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: 672.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRsgrRRSVQMYNK 558
Cdd:cd24129 2 LSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVG---TAGVQITSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:cd24129 79 IYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNGCI 718
Cdd:cd24129 159 EAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 719 DNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLALL 798
Cdd:cd24129 239 AMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 799 QVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLRET 878
Cdd:cd24129 319 QVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQAT 398
|
410 420 430
....*....|....*....|....*....|..
gi 699630172 879 VKELAPQCDVTFMLSEDGSGKGAALITAVAKR 910
Cdd:cd24129 399 VRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
479-906 |
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: 643.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNK 558
Cdd:cd24089 2 LSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:cd24089 82 VYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNGCI 718
Cdd:cd24089 162 KAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 719 DNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLALL 798
Cdd:cd24089 242 EDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 799 QVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLRET 878
Cdd:cd24089 322 NAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHKA 401
|
410 420
....*....|....*....|....*...
gi 699630172 879 VKELAPQCDVTFMLSEDGSGKGAALITA 906
Cdd:cd24089 402 VRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
30-458 |
0e+00 |
|
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type II hexokinase.
Pssm-ID: 466975 [Multi-domain] Cd Length: 429 Bit Score: 635.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSQLES 109
Cdd:cd24125 1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24125 81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 270 LDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGL 349
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 350 SNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHK 429
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400
|
410 420
....*....|....*....|....*....
gi 699630172 430 VVRRLVPNCDVRFLLSVSGSGKGAAMVTA 458
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
30-458 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition.
Pssm-ID: 466869 [Multi-domain] Cd Length: 427 Bit Score: 608.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVcdDGKQSSQLES 109
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTL--NGGSQVKMES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24019 79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDL---VEGDEGRMCINTEWGAFGD 266
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 267 DGALDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYK 346
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 347 EG-LSNTKEILTELNL-FPSEEDCIAVQHVCTIVSFRSANLCAAALAAILtrlrenKKLLRMRTTVGIDGGLYKTHPQYA 424
Cdd:cd24019 319 EGdFSNTREILKELGLeDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALL------NRMNRKEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 699630172 425 KRLHKVVRRLVP-NCDVRFLLSVSGSGKGAAMVTA 458
Cdd:cd24019 393 KRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
479-906 |
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: 590.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNK 558
Cdd:cd24126 2 LSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:cd24126 82 FYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNGCI 718
Cdd:cd24126 162 KAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 719 DNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLALL 798
Cdd:cd24126 242 EDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGLY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 799 QVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLRET 878
Cdd:cd24126 322 NTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHKV 401
|
410 420
....*....|....*....|....*...
gi 699630172 879 VKELAPQCDVTFMLSEDGSGKGAALITA 906
Cdd:cd24126 402 VRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
479-906 |
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: 589.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNK 558
Cdd:cd24125 2 LSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:cd24125 82 IYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNGCI 718
Cdd:cd24125 162 KAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 719 DNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLALL 798
Cdd:cd24125 242 DDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGIR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 799 QVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLRET 878
Cdd:cd24125 322 KAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHKT 401
|
410 420
....*....|....*....|....*...
gi 699630172 879 VKELAPQCDVTFMLSEDGSGKGAALITA 906
Cdd:cd24125 402 VRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
466-911 |
0e+00 |
|
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase.
Pssm-ID: 466974 [Multi-domain] Cd Length: 473 Bit Score: 577.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 466 QRKQIDAALAPFLLSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKI 545
Cdd:cd24124 17 QVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 546 RSGRRRSVQMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKA 625
Cdd:cd24124 97 NHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 626 TDCEGEDVVDMLREAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCI 705
Cdd:cd24124 177 SGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 706 NTEWGGFGDNGCIDNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETK 785
Cdd:cd24124 257 NTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 786 FLSQIESDRLALLQVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLY 865
Cdd:cd24124 337 DVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLY 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 699630172 866 KLHPHFSRVLRETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 911
Cdd:cd24124 417 KTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
469-910 |
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: 553.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 469 QIDAALAPFLLSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSG 548
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 549 RRR--SVQMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKAT 626
Cdd:cd24092 81 EEGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 627 DCEGEDVVDMLREAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCIN 706
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 707 TEWGGFGDNGCIDNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKF 786
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 787 LSQIESDRLALLQVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYK 866
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 699630172 867 LHPHFSRVLRETVKELAPQCDVTFMLSEDGSGKGAALITAVAKR 910
Cdd:cd24092 401 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
30-462 |
0e+00 |
|
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of types I to III hexokinases. Type I enzyme may have a catabolic function, producing H6P for energy production in glycolysis; it is bound to the mitochondrial membrane, which enables the coordination of glycolysis with the TCA cycle. Types II and III enzyme may have anabolic functions, providing H6P for glycogen or lipid synthesis.
Pssm-ID: 466941 [Multi-domain] Cd Length: 433 Bit Score: 540.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSQLES 109
Cdd:cd24091 1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24091 81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 270 LDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGL 349
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 350 SNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHK 429
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400
|
410 420 430
....*....|....*....|....*....|...
gi 699630172 430 VVRRLVPNCDVRFLLSVSGSGKGAAMVTAVAYR 462
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
30-463 |
4.80e-178 |
|
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: 522.15 E-value: 4.80e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSQLES 109
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24128 81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 270 LDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGL 349
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 350 SNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHK 429
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400
|
410 420 430
....*....|....*....|....*....|....
gi 699630172 430 VVRRLVPNCDVRFLLSVSGSGKGAAMVTAVAYRL 463
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
30-463 |
1.23e-171 |
|
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: 505.60 E-value: 1.23e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSQLES 109
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24127 81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 270 LDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGL 349
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 350 SNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHK 429
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400
|
410 420 430
....*....|....*....|....*....|....
gi 699630172 430 VVRRLVPNCDVRFLLSVSGSGKGAAMVTAVAYRL 463
Cdd:cd24127 401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
30-462 |
3.27e-171 |
|
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: 504.42 E-value: 3.27e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVcddGKQSSQLES 109
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV---GTAGVQITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24129 78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 270 LDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGL 349
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 350 SNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHK 429
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397
|
410 420 430
....*....|....*....|....*....|...
gi 699630172 430 VVRRLVPNCDVRFLLSVSGSGKGAAMVTAVAYR 462
Cdd:cd24129 398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
30-463 |
1.96e-170 |
|
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: 502.54 E-value: 1.96e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 30 RLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVcDDGKQSSQLES 109
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKI-RSGRRSVRMYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24130 80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGA 269
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 270 LDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGL 349
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 350 SNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHK 429
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399
|
410 420 430
....*....|....*....|....*....|....
gi 699630172 430 VVRRLVPNCDVRFLLSVSGSGKGAAMVTAVAYRL 463
Cdd:cd24130 400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
21-462 |
2.31e-163 |
|
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: 484.77 E-value: 2.31e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 21 KVDRYLYHMRLSDDVLLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDD 100
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 101 GKQSSQLESK--FYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVR 178
Cdd:cd24092 81 EEGQWSVKTKhqMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 179 GVQDTDVVSSLRKALQKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCIN 258
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 259 TEWGAFGDDGALDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKH 338
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 339 VSAMEKYKEGLSNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYK 418
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 699630172 419 THPQYAKRLHKVVRRLVPNCDVRFLLSVSGSGKGAAMVTAVAYR 462
Cdd:cd24092 401 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
481-904 |
4.64e-163 |
|
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: 483.29 E-value: 4.64e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 481 LETLREVKNKMRTELEYGLKRETQasaTVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNKiF 560
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGG---SLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 561 AIPLEIMQGTGEELFDHIVQCIADFLEYMGIK---GARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDML 637
Cdd:cd24018 77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 638 REAIRRRNeFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEG------KMCINTEWGG 711
Cdd:cd24018 157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPSGsvtksdEMIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 712 FGDNGCIDNiRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIE 791
Cdd:cd24018 236 FDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 792 SDRLALLQ-VRRILQQLG--LDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVeKKREDRGVEHLqiTVGVDGTLYKLH 868
Cdd:cd24018 315 ADTSPDLDaVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAIL-LKRGSLLPEPV--TVGIDGSVYEKY 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 699630172 869 PHFSRVLRETVKELAPQC---DVTFMLSEDGSGKGAALI 904
Cdd:cd24018 392 PGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
479-906 |
1.51e-158 |
|
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type III hexokinase.
Pssm-ID: 466940 [Multi-domain] Cd Length: 431 Bit Score: 471.71 E-value: 1.51e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASATVKMLPTYVCGTPDGTEKGKFLALDLG--GTNFRVLLVKIRSGRRRSVQMY 556
Cdd:cd24090 2 VTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 557 NKIFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDM 636
Cdd:cd24090 82 SQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 637 LREAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGGFGDNG 716
Cdd:cd24090 162 LRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 717 CIDNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLA 796
Cdd:cd24090 242 ALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 797 LLQVRRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQITVGVDGTLYKLHPHFSRVLR 876
Cdd:cd24090 322 AARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQ 401
|
410 420 430
....*....|....*....|....*....|
gi 699630172 877 ETVKELAPQCDVTFMLSEDGSGKGAALITA 906
Cdd:cd24090 402 GTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
36-458 |
1.59e-141 |
|
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: 427.80 E-value: 1.59e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 36 LLDVMARFQAEMVKGLGKDTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLG--GSQFRAHQVKVCDDGKQSSQLESKFYP 113
Cdd:cd24090 7 LQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQEFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 114 TPKEVIQGNGTELFDYIADCLLDFMETKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSLRKAL 193
Cdd:cd24090 87 IPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRDAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 194 QKHKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDEGRMCINTEWGAFGDDGALDDL 273
Cdd:cd24090 167 QRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALGPV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 274 RTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYKEGLSNTK 353
Cdd:cd24090 247 LTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAARVR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 354 EILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKTHPQYAKRLHKVVRR 433
Cdd:cd24090 327 AILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTVML 406
|
410 420
....*....|....*....|....*
gi 699630172 434 LVPNCDVRFLLSVSGSGKGAAMVTA 458
Cdd:cd24090 407 LAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
482-905 |
5.11e-138 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 415.91 E-value: 5.11e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 482 ETLREVKNKMRTELEYGLKREtqaSATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRrrSVQMYNKIFA 561
Cdd:cd24000 2 EDLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKG--IEVTISKKYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 562 IPLEIMQGTGEELFDHIVQCIADFLEYMGIKgARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLREAI 641
Cdd:cd24000 77 IPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 642 RRRNeFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIeivEGNEGKMCINTEWGGFGDNgciDNI 721
Cdd:cd24000 156 KKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI---LLGDGGMIINTEWGNFGKN---SLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 722 RTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQgllfrgqiseslrkrgifetkflsqiesdrlallqvr 801
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 802 rilqqlgldstcddsiIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDrgvEHLQITVGVDGTLYKLHPHFSRVLRETVKE 881
Cdd:cd24000 272 ----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLKE 332
|
410 420
....*....|....*....|....*
gi 699630172 882 L-APQCDVTFMLSEDGSGKGAALIT 905
Cdd:cd24000 333 LlGRGIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
33-456 |
1.66e-128 |
|
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: 393.92 E-value: 1.66e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 33 DDVLLDVMARFQAEMVKGLGKDTNptaTVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVcDDGKQSSQLESKFY 112
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGG---SLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTL-DGNGGIFIIVQRKY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 113 PTPKEVIQGNGTELFDYIADCLLDFMETKSLKH---KKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:cd24018 77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDLqsdKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKhKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHI---DLVEG---DEGRMCINTEWGA 263
Cdd:cd24018 157 QNALDR-RGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGsvtKSDEMIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 264 FGDDGALddL-RTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAM 342
Cdd:cd24018 236 FDNEREV--LpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 343 EKYKEG-LSNTKEILTEL--NLFPSEEDCIAVQHVCTIVSFRSanlCAAALAAILTRLRENKKLLRMRTTVGIDGGLYKT 419
Cdd:cd24018 314 EADTSPdLDAVRDILKELlaIDNTTLEDRKLIKRICELVSTRA---ARLSAAAIAAILLKRGSLLPEPVTVGIDGSVYEK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 699630172 420 HPQYAKRLHKVVRRLVPNC---DVRFLLSVSGSGKGAAMV 456
Cdd:cd24018 391 YPGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
479-908 |
6.10e-125 |
|
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: 385.09 E-value: 6.10e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 479 LSLETLREVKNKMRTELEYGLKRETQASatVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNK 558
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSK--LKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 559 IFAIPLEIMQGTGEELFDHIVQCIADFLEYMG----IKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVV 634
Cdd:cd24020 79 EVPIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 635 DMLREAIRRRNeFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEG---NEGKMCINTEWGG 711
Cdd:cd24020 159 ELLEEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGglpRSGEMVINTEWGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 712 FGDngciDNI-RTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQI 790
Cdd:cd24020 238 FRS----SHLpRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 791 ESDRLA-LLQVRRILQQ-LGL-DSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEHLQ--ITVGVDGTLY 865
Cdd:cd24020 314 HEDDSPdLETVARILKDaLGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAqrTVVAVDGGLY 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 699630172 866 KLHPHFSRVLRETVKEL--APQCD-VTFMLSEDGSGKGAALITAVA 908
Cdd:cd24020 394 EHYPKFREYMQQALVELlgDEAADsVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
482-909 |
4.55e-121 |
|
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: 374.40 E-value: 4.55e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 482 ETLREVKNKMRTELEYGLKRETQasaTVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIrSGRRRSVQMYNKiFA 561
Cdd:cd24087 2 ERLRKITDHFISELEKGLSKKGG---NIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKL-GGNGKFDITQSK-YR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 562 IPLEIMQGTGEELFDHIVQCIADFLE--YMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLRE 639
Cdd:cd24087 77 LPEELKTGTGEELWDFIADCLKKFVEehFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 640 AIRRRNeFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVE----GNEGKMCINTEWGGFgDN 715
Cdd:cd24087 157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 716 GCIDNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRL 795
Cdd:cd24087 235 EHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 796 A-LLQVRRILQQ-LGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVehlqitVGVDGTLYKLHPHF-- 871
Cdd:cd24087 315 EnLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCH------VAADGSVYNKYPGFke 388
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 699630172 872 --SRVLRETVKELAPQCDVTFMLSEDGSGKGAALITAVAK 909
Cdd:cd24087 389 raAQALKDIFGWDGEDDPIKTVPAEDGSGVGAAIIAALTK 428
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
482-904 |
1.88e-117 |
|
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: 365.57 E-value: 1.88e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 482 ETLREVKNKMRTELEYGLKREtqaSATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQmYNKiFA 561
Cdd:cd24088 2 EKLDKLTAEFQRQMEKGLAKH---GKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLR-QEK-SK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 562 IPLEIMQG-TGEELFDHIVQCIADFLE-------YMGIKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDV 633
Cdd:cd24088 77 IPDELKTGvTAKDLFDYLAKSVEAFLTkhhgdsfAAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 634 VDMLREAIRRRNeFDLDIVAVVNDTVGTMMTCGYEDPNCE---IGLIAGTGSNVCYMEDMKNI------EIVEGNEGKMC 704
Cdd:cd24088 157 VKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKTHMV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 705 INTEWGGFgdngciDNIR-----TKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLL---FRGQISESL 776
Cdd:cd24088 236 INTEWGSF------DNELkvlptTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 777 RKRGIFETKFLSQIESDRLALLQVRR--ILQQLGL-DSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKREDRGVEH 853
Cdd:cd24088 310 NTPYGLDTAVLSAIEIDSEAELRATRkvLLDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYD 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 699630172 854 LQITVGVDGTLYKLHPHFSRVLRETVKELAP----QCDVTFMLSEDGSGKGAALI 904
Cdd:cd24088 390 GEINIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
33-457 |
6.32e-112 |
|
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: 347.73 E-value: 6.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 33 DDVLLDVMARFQAEMVKGLGKDTnptATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVcdDGKQSSQLESKFY 112
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEP---SSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSL--DGKGIEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 113 PTPKEVIQGNGTELFDYIADCLLDFMEtKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSLRKA 192
Cdd:cd24000 76 EIPDEIKTASAEEFFDFIADCIAEFLK-ENGLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 193 LQKHKdIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDlveGDEGRMCINTEWGAFGDDgalDD 272
Cdd:cd24000 155 LKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL---LGDGGMIINTEWGNFGKN---SL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 273 LRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEgllfngkvstalltkgkiemkhvsamekykeglsnt 352
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 353 keiltelnlfpseedciAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLlrmRTTVGIDGGLYKTHPQYAKRLHKVVR 432
Cdd:cd24000 272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDSPEK---KITIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420
....*....|....*....|....*.
gi 699630172 433 RLVPN-CDVRFLLSVSGSGKGAAMVT 457
Cdd:cd24000 332 ELLGRgIRIELVLVEDGSLIGAALAA 357
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
462-908 |
3.91e-110 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 347.05 E-value: 3.91e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 462 RLAAQRKQidaalapFLLSLETLREVKNKMRTELEYGLK-RETQASA------TVKMLPTYVCGTPDGTEKGKFLALDLG 534
Cdd:PTZ00107 10 RLASLVNQ-------FTMSKEKLKELVDYFLYELVEGLEaHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 535 GTNFRVLLVKIRsGRRRSVQMYNKiFAIPLEIMQG---------TGEELFDHIVQCIADFLEYMGIK---GARLPLGFTF 602
Cdd:PTZ00107 83 GTNFRAVRVSLR-GGGKMERTQSK-FSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 603 SFPCRQASIDKGTLVGWTKGF---KATD--CEGEDVVDMLREAIRRrNEFDLDIVAVVNDTVGTMMTCGYED----PNCE 673
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFetgRATNdpVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 674 IGLIAGTGSNVCYMEDM-KNIeiveGNEGKMcINTEWGGFgdngCIDNIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGE 752
Cdd:PTZ00107 240 VGVIIGTGSNACYFEPEvSAY----GYAGTP-INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 753 IVRQILIdltkqgLLFRGQISESLRKRGIFETKFLSQIESDRLALLQ-VRRILQQL-GLDSTCDDSIIVKEVCGAVSKRA 830
Cdd:PTZ00107 311 ISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQfSRQVIKEAwDVDLTDEDLYTIRKICELVRGRA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 831 AQLCGAGLAAIVEKKREDRGvehlQITVGVDGTLYKLHPHFSRVLRETVKE-LAPQ-CDVTFMLSEDGSGKGAALITAVA 908
Cdd:PTZ00107 385 AQLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
673-907 |
2.92e-108 |
|
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: 333.69 E-value: 2.92e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 673 EIGLIAGTGSNVCYMEDMKNIEIVEG---NEGKMCINTEWGGFGDNGCIDNIRTKYDKEVDEGSLNPGKQRYEKMTSGMY 749
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGklpKSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 750 LGEIVRQILIDLTKQGLLFRGQiSESLRKRGIFETKFLSQIESDR-LALLQVRRILQQ-LGL-DSTCDDSIIVKEVCGAV 826
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIeTVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 827 SKRAAQLCGAGLAAIVEKKREDRGVehlqiTVGVDGTLYKLHPHFSRVLRETVKE-LAPQCDVTFMLSEDGSGKGAALIT 905
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDKKV-----TVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234
|
..
gi 699630172 906 AV 907
Cdd:pfam03727 235 AV 236
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
43-460 |
2.70e-104 |
|
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: 330.78 E-value: 2.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 43 FQAEMVKGLGKDtnPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSQLESKFYPTPKEVIQGN 122
Cdd:cd24020 13 MVVEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVPIPPELMVGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 123 GTELFDYIADCLLDF--METKSLKHK--KLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSLRKALQKHKd 198
Cdd:cd24020 91 SEELFDFIAGELAKFvaTEGEGFHPEgeKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 199 IDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGD---EGRMCINTEWGAFgDDGALDdlRT 275
Cdd:cd24020 170 LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-RSSHLP--RT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 276 EFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAM-EKYKEGLSNTKE 354
Cdd:cd24020 247 EEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDDSPDLETVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 355 ILTELNLFP--SEEDCIAVQHVCTIVSFRSANLCAAALAAILtrlrenKKLLR--------MRTTVGIDGGLYKTHPQYA 424
Cdd:cd24020 327 ILKDALGIDdtSLEARKVVVEVCDLVAERGARLAAAGIVGIL------KKLGRdgggsspaQRTVVAVDGGLYEHYPKFR 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 699630172 425 KRLHKVVRRLVPNC---DVRFLLSVSGSGKGAAMVTAVA 460
Cdd:cd24020 401 EYMQQALVELLGDEaadSVELELSNDGSGIGAALLAAAH 439
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
477-908 |
2.92e-98 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 314.59 E-value: 2.92e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 477 FLLSLETLREVKNKMRTELEYGLKREtqaSATVKMLPTYVcGTPDG-TEKGKFLALDLGGTNFRVLLVKIrSGRRRSVQM 555
Cdd:COG5026 15 FDLSSIDLEEIAAKFQEEMEKGLEGK---KSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF-DGEGTFEIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 556 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLEYmgikgaRLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVD 635
Cdd:COG5026 90 NFKSFPLPGTSSEITAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 636 MLREAIRRRNEFDLDIVAVVNDTVGTMMTCGYEDPNC----EIGLIAGTGSNVCYMEDMKNIEIVEGNEGKMCINTEWGG 711
Cdd:COG5026 164 LLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 712 FgdNGCidnIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGlLFRGQISESLRKRGIFETKFLSQI- 790
Cdd:COG5026 244 F--NKL---PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRFl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 791 --ESDRLallqvrRILQQLGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKkrEDRGVEHLQ-ITVGVDGTLYKL 867
Cdd:COG5026 318 adPSDEK------EILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLH--LGPGKTPLKpHCIAIDGSTYEK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 699630172 868 HPHFSRVLRETVKE-LAPQCD--VTFMLSEDGSGKGAALITAVA 908
Cdd:COG5026 390 MPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALN 433
|
|
| PLN02914 |
PLN02914 |
hexokinase |
461-906 |
3.30e-96 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 311.43 E-value: 3.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 461 YRLAAQRKQIDAALAPFLLSLE--------TLREVKNKMRTELEYGLKREtqASATVKMLPTYVCGTPDGTEKGKFLALD 532
Cdd:PLN02914 24 PRSRMAVRSNAVSVAPILTKLQkdcatplpVLRHVADAMAADMRAGLAVD--GGGDLKMILSYVDSLPSGNEKGLFYALD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 533 LGGTNFRVLLVKIRSGRRRSVQMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIK-----GARLPLGFTFSFPCR 607
Cdd:PLN02914 102 LGGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 608 QASIDKGTLVGWTKGFKATDCEGEDVVDMLREAIRRRNeFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYM 687
Cdd:PLN02914 182 QTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 688 EDMKNIEIVEG---NEGKMCINTEWGGFGDNGCIdnirTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQ 764
Cdd:PLN02914 261 ERTDAIPKLQGqksSSGRTIINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAET 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 765 GLLFRGQISESLRKRGIFETKFLSQIESDRLALLQ-VRRILQQ-LGLDSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIV 842
Cdd:PLN02914 337 SDLFGHFVPEKLSTPFALRTPHLCAMQQDNSDDLQaVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGIL 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 699630172 843 EKKRED--RGVEHLQITVGVDGTLYKLHPHFSRVLRETVKEL---APQCDVTFMLSEDGSGKGAALITA 906
Cdd:PLN02914 417 EKMEEDskGMIFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELlglELSKNIAIEHTKDGSGIGAALLAA 485
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
469-667 |
2.90e-91 |
|
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: 287.09 E-value: 2.90e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 469 QIDAALAPFLLSLETLREVKNKMRTELEYGLKRETqaSATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIrsG 548
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVEL--G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 549 RRRSVQMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIK---GARLPLGFTFSFPCRQASIDKGTLVGWTKGFKA 625
Cdd:pfam00349 77 GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 699630172 626 TDCEGEDVVDMLREAIRRRNEfDLDIVAVVNDTVGTMMTCGY 667
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
39-460 |
1.46e-88 |
|
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: 288.89 E-value: 1.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 39 VMARFQAEMVKGLGKdtnPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSqLESKfYPTPKEV 118
Cdd:cd24087 7 ITDHFISELEKGLSK---KGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDI-TQSK-YRLPEEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 119 IQGNGTELFDYIADCLLDFMETKSLKHKK--LPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSLRKALQKh 196
Cdd:cd24087 82 KTGTGEELWDFIADCLKKFVEEHFPGGKSepLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKK- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 197 KDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVE----GDEGRMCINTEWGAFgDDGALDD 272
Cdd:cd24087 161 RNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DNEHLVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 273 LRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEKYK-EGLSN 351
Cdd:cd24087 240 PRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPfENLED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 352 TKEILTE-LNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILtrlrenKKLLRMRTTVGIDGGLYKTHPQYAKRLHKV 430
Cdd:cd24087 320 TDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAIC------KKRGYKTCHVAADGSVYNKYPGFKERAAQA 393
|
410 420 430
....*....|....*....|....*....|....
gi 699630172 431 VRRLVPNCDVRFLLSVS----GSGKGAAMVTAVA 460
Cdd:cd24087 394 LKDIFGWDGEDDPIKTVpaedGSGVGAAIIAALT 427
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
33-456 |
4.05e-86 |
|
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: 282.75 E-value: 4.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 33 DDVLLDVMARFQAEMVKGLgkdTNPTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRahqvkVCD---DGKQSSQLES 109
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFR-----VCSvelHGDGTFSLRQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 110 KFYPTPKEVIQGN-GTELFDYIADCLLDFMETKSLKH-------KKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQ 181
Cdd:cd24088 73 EKSKIPDELKTGVtAKDLFDYLAKSVEAFLTKHHGDSfaagkddDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 182 DTDVVSSLRKALQKhKDIDVDVLALVNDTVGTMMTCGYDDPRCE---VGLIIGTGTNACYMEEMRHI---DLVEGDE--- 252
Cdd:cd24088 153 GKDVVKLLQDELDR-QGIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklDDSSRVGkgk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 253 GRMCINTEWGAFgdDGALDDL-RTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLL---FNGKVSTAL 328
Cdd:cd24088 232 THMVINTEWGSF--DNELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 329 LTKGKIEMKHVSAMEKYKE-GLSNTKEILTELNLFPSE--EDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLR 405
Cdd:cd24088 310 NTPYGLDTAVLSAIEIDSEaELRATRKVLLDDLGLPAPslEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYD 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 699630172 406 MRTTVGIDGGLYKTHPQYAKRLHKVVRRLVPNC----DVRFLLSVSGSGKGAAMV 456
Cdd:cd24088 390 GEINIGVDGSVIEFYPGFESMLREALRLLLIGAegekRIKIGIAKDGSGVGAALC 444
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
12-460 |
1.01e-85 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 282.34 E-value: 1.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 12 TKLKEDQIKKVDRYLYHMRLSDDVLLDVMARFQAEMVKGL-GKDTNPTA------TVKMLPSFVRSLPDGSEKGDFLAVD 84
Cdd:PTZ00107 1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 85 LGGSQFRAHQVkVCDDGKQSSQLESKFyPTPKEVIQG---------NGTELFDYIADCLLDFMETKSLK---HKKLPLGF 152
Cdd:PTZ00107 81 FGGTNFRAVRV-SLRGGGKMERTQSKF-SLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 153 TFSFPCKQTKLEEGVLLAWTKHFKV-----RGVQDTDVVSSLRKALQKHKdIDVDVLALVNDTVGTMMTCGYDDPR---- 223
Cdd:PTZ00107 159 TFSFPCTQLSVNNAILIDWTKGFETgratnDPVEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKPKntpp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 224 CEVGLIIGTGTNACYMEEMRhidLVEGDEGRMcINTEWGAFgdDGALDdlRTEFDRELDLGSLNPGKQLFEKMISSLYLG 303
Cdd:PTZ00107 238 CQVGVIIGTGSNACYFEPEV---SAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 304 ELVRLILLkmtkegLLFNGKVSTALLTKGKIEMKHVSAM-EKYKEGLSNTKEILTEL-NLFPSEEDCIAVQHVCTIVSFR 381
Cdd:PTZ00107 310 EISRRLIV------HLLQLKAPPKMWQSGSFESEDASMIlNDQSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 382 SANLCAAALAAILTRLREnkklLRMRTTVGIDGGLYKTHPQYAKRLHKVVRRLV--PNCDVRFLLSVSGSGKGAAMVTAV 459
Cdd:PTZ00107 384 AAQLAAAFIAAPAKKTRT----VQGKATVAIDGSVYVKNPWFRRLLQEYINSILgpDAGNVVFYLADDGSGKGAAIIAAM 459
|
.
gi 699630172 460 A 460
Cdd:PTZ00107 460 V 460
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
14-460 |
1.12e-83 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 276.07 E-value: 1.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 14 LKEDQIKKvdrylYHMRLSDDVLLDVMARFQAEMVKGL-GKDtnptATVKMLPSFVrSLPDGS-EKGDFLAVDLGGSQFR 91
Cdd:COG5026 5 LVDAFLKR-----HGFDLSSIDLEEIAAKFQEEMEKGLeGKK----SSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 92 AHQVKVcdDGKQSSQLESKF-YPTPKEVIQGNGTELFDYIADCLldfmetKSLKHKKLPLGFTFSFPCKQTKLEEGVLLA 170
Cdd:COG5026 75 VALVRF--DGEGTFEIENFKsFPLPGTSSEITAEEFFDFIADYI------EPLLDESYKLGFCFSFPAEQLPDKDGRLIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 171 WTKHFKVRGVQDTDVVSSLRKALQKHKDIDVDVLALVNDTVGTMMTCGYDDP----RCEVGLIIGTGTNACYMEEMRHID 246
Cdd:COG5026 147 WTKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 247 LVEGDEGRMCINTEWGAFgdDGAlddLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGlLFNGKVST 326
Cdd:COG5026 227 KLPAYEGPMIINMESGNF--NKL---PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 327 ALLTKGKIEMKHVSAmekYKEGLSNTKEILTELNLFPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLLRm 406
Cdd:COG5026 301 VFETPYSLTTVDMSR---FLADPSDEKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK- 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 699630172 407 RTTVGIDGGLYKTHPQYAKRLHKVVRR-LVPNCD--VRFLLSVSGSGKGAAMVTAVA 460
Cdd:COG5026 377 PHCIAIDGSTYEKMPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALN 433
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
225-459 |
6.56e-83 |
|
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: 266.66 E-value: 6.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 225 EVGLIIGTGTNACYMEEMRHIDLVEGD---EGRMCINTEWGAFGDDGALDDLRTEFDRELDLGSLNPGKQLFEKMISSLY 301
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 302 LGELVRLILLKMTKEGLLFNGKvSTALLTKGKIEMKHVSAMEKYK-EGLSNTKEILTE-LNLF-PSEEDCIAVQHVCTIV 378
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 379 SFRSAnlcaaalaailtrlrenkKL---------LRMR----TTVGIDGGLYKTHPQYAKRLHKVVRRLV-PNCDVRFLL 444
Cdd:pfam03727 160 STRAA------------------RLvaagiaailKKIGrdkkVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVL 221
|
250
....*....|....*
gi 699630172 445 SVSGSGKGAAMVTAV 459
Cdd:pfam03727 222 AEDGSGVGAALIAAV 236
|
|
| PLN02914 |
PLN02914 |
hexokinase |
35-458 |
2.46e-82 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 274.07 E-value: 2.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 35 VLLDVMARFQAEMVKGLGKDTNptATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDDGKQSSQLESKFYPT 114
Cdd:PLN02914 54 VLRHVADAMAADMRAGLAVDGG--GDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 115 PKEVIQGNGTELFDYIADCLLDFMETKSLKH-----KKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSL 189
Cdd:PLN02914 132 PQELMFGTSEELFDFIASGLANFVAKEGGKFhlpegRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 190 RKALQKHkDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGDE---GRMCINTEWGAFGD 266
Cdd:PLN02914 212 NEAMERQ-GLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 267 DGALddlrTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEK-Y 345
Cdd:PLN02914 291 GLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQdN 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 346 KEGLSNTKEILTelNLFPSEEDCIA---VQHVCTIVSFRSANLCAAALAAILTRLRENKK--LLRMRTTVGIDGGLYKTH 420
Cdd:PLN02914 367 SDDLQAVGSILY--DVLGVEASLSArrrVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKgmIFGKRTVVAMDGGLYEKY 444
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 699630172 421 PQYAKRLHKVVRRLV-PNCDVRFLL--SVSGSGKGAAMVTA 458
Cdd:PLN02914 445 PQYRRYMQDAVTELLgLELSKNIAIehTKDGSGIGAALLAA 485
|
|
| PLN02405 |
PLN02405 |
hexokinase |
484-906 |
5.76e-79 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 265.16 E-value: 5.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 484 LREVKNKMRTELEYGLKREtqASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNKIFAIP 563
Cdd:PLN02405 55 LRQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 564 LEIMQGTGEELFDHIVQCIADFLEYMG-----IKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDMLR 638
Cdd:PLN02405 133 PHLMTGSSDALFDFIAAALAKFVATEGedfhlPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 639 EAIRRRNeFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEG---NEGKMCINTEWGGFGDN 715
Cdd:PLN02405 213 KAMERVG-LDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFRSS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 716 GCidnIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRL 795
Cdd:PLN02405 292 HL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 796 ALLQV--RRILQQLGL-DSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKRED--RGVEHLQITVGVDGTLYKLHPH 870
Cdd:PLN02405 369 PDLKVvgSKLKDILEIpNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHYTE 448
|
410 420 430
....*....|....*....|....*....|....*....
gi 699630172 871 FSRVLRETVKELAPQ---CDVTFMLSEDGSGKGAALITA 906
Cdd:PLN02405 449 FSKCMESTLKELLGEevsESIEVEHSNDGSGIGAALLAA 487
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
21-219 |
8.44e-79 |
|
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: 253.97 E-value: 8.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 21 KVDRYLYHMRLSDDVLLDVMARFQAEMVKGLGKDTnpTATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVCDD 100
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 101 GKQSsqLESKFYPTPKEVIQGNGTELFDYIADCLLDFMETKSLKH---KKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKV 177
Cdd:pfam00349 79 GKFE--ITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 699630172 178 RGVQDTDVVSSLRKALQKHKDiDVDVLALVNDTVGTMMTCGY 219
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| PLN02362 |
PLN02362 |
hexokinase |
484-906 |
3.00e-78 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 263.67 E-value: 3.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 484 LREVKNKMRTELEYGLKREtqASATVKMLPTYVCGTPDGTEKGKFLALDLGGTNFRVLLVKIrSGRRRSVQMYN-KIFAI 562
Cdd:PLN02362 55 LRQVVDAMAVEMHAGLASE--GGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQL-GGQRSSILSQDvERHPI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 563 PLEIMQGTGEELFDHIVQCIADFLEYMG-----IKGARLPLGFTFSFPCRQASIDKGTLVGWTKGFKATDCEGEDVVDML 637
Cdd:PLN02362 132 PQHLMNSTSEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 638 REAIRRRNeFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNVCYMEDMKNIEIVEG---NEGKMCINTEWGGFGD 714
Cdd:PLN02362 212 QGALNRRG-LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFWS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 715 NGCidnIRTKYDKEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFrGQISESLRKRGIFETKFLSQI-ESD 793
Cdd:PLN02362 291 SHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 794 RLALLQVRRILQQ-LGL-DSTCDDSIIVKEVCGAVSKRAAQLCGAGLAAIVEKKRED--------RGVEHLQI----TVG 859
Cdd:PLN02362 367 SPELQEVARILKEtLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGRDgsggitsgRSRSDIQImrrtVVA 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 699630172 860 VDGTLYKLHPHFSRVLRETVKELAPQ---CDVTFMLSEDGSGKGAALITA 906
Cdd:PLN02362 447 VEGGLYTNYTMFREYLHEALNEILGEdvaQHVILKATEDGSGIGSALLAA 496
|
|
| PLN02405 |
PLN02405 |
hexokinase |
46-458 |
5.90e-66 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 229.72 E-value: 5.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 46 EMVKGLGKDTNptATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVcdDGKQSSQLESKF--YPTPKEVIQGNG 123
Cdd:PLN02405 65 EMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLL--GGKDGRVVKQEFeeVSIPPHLMTGSS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 124 TELFDYIADCLLDFMETKSLKHKKLP-----LGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVSSLRKALQKhKD 198
Cdd:PLN02405 141 DALFDFIAAALAKFVATEGEDFHLPPgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMER-VG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 199 IDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEGD---EGRMCINTEWGAFGDDGALddlRT 275
Cdd:PLN02405 220 LDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFRSSHLP---LT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 276 EFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFNGKVSTALLTKGKIEMKHVSAMEK-----YKEGLS 350
Cdd:PLN02405 297 EYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHdtspdLKVVGS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 351 NTKEILTELNlfPSEEDCIAVQHVCTIVSFRSANLCAAALAAILtrlrenKKLLR--------MRTTVGIDGGLYKTHPQ 422
Cdd:PLN02405 377 KLKDILEIPN--TSLKMRKVVVELCNIVATRGARLSAAGIYGIL------KKLGRdtvkdgekQKSVIAMDGGLFEHYTE 448
|
410 420 430
....*....|....*....|....*....|....*....
gi 699630172 423 YAKRLHKVVRRLV---PNCDVRFLLSVSGSGKGAAMVTA 458
Cdd:PLN02405 449 FSKCMESTLKELLgeeVSESIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
36-458 |
7.76e-65 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 226.69 E-value: 7.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 36 LLDVMArfqAEMVKGLGKDTNptATVKMLPSFVRSLPDGSEKGDFLAVDLGGSQFRAHQVKVcddGKQSSQLESK---FY 112
Cdd:PLN02362 58 VVDAMA---VEMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQL---GGQRSSILSQdveRH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 113 PTPKEVIQGNGTELFDYIADCLLDFME-----TKSLKHKKLPLGFTFSFPCKQTKLEEGVLLAWTKHFKVRGVQDTDVVS 187
Cdd:PLN02362 130 PIPQHLMNSTSEVLFDFIASSLKQFVEkeengSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 188 SLRKALQKhKDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTGTNACYMEEMRHIDLVEG---DEGRMCINTEWGAF 264
Cdd:PLN02362 210 CLQGALNR-RGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 265 GDDGALddlRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLILLKMTKEGLLFnGKVSTALLTKGKIEMKHVSAM-E 343
Cdd:PLN02362 289 WSSHLP---RTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 344 KYKEGLSNTKEILTE---LNLFPSEEDCIAVQhVCTIVSFRSANLCAA-------------ALAAILTRLRENKKLLRmR 407
Cdd:PLN02362 365 DDSPELQEVARILKEtlgISEVPLKVRKLVVK-ICDVVTRRAARLAAAgivgilkkigrdgSGGITSGRSRSDIQIMR-R 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 699630172 408 TTVGIDGGLYKTHPQYAKRLHKVVRRLVPNcDV--RFLLSVS--GSGKGAAMVTA 458
Cdd:PLN02362 443 TVVAVEGGLYTNYTMFREYLHEALNEILGE-DVaqHVILKATedGSGIGSALLAA 496
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
453-906 |
1.75e-49 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 182.77 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 453 AAMVTAVAYRLAA------------QRKQIDAALAPFLLSLET----LREVKNKMRTELEYGLKRETqaSATVKMLPTYV 516
Cdd:PLN02596 9 AATVATVAAVAAAvlmgrwkrrkerQWKHTQRILRKFARECATpvskLWEVADALVSDMTASLTAEE--TTTLNMLVSYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 517 CGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRRSVQMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLEYMGIKGARL 596
Cdd:PLN02596 87 ASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 597 P-----LGFTFSFPCRQASIDKGTLVGWtKGFKATDCEGEDVVDMLREAIRRRNeFDLDIVAVVNDTVGTMMTCGYEDPN 671
Cdd:PLN02596 167 PervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDTIGNLAGGRYYNKD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 672 CEIGLIAGTGSNVCYMEDMKNIEIVEG---NEGKMCINTEWGGFgdNGCIDNIrTKYDKEVDEGSLNPGKQRYEKMTSGM 748
Cdd:PLN02596 245 TVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF--NSCHLPI-TEFDASLDAESSNPGSRIFEKLTSGM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 749 YLGEIVRQILIDLTKQGLLFRGQISESLRKRGIFETKFLSQIESDRLALLQV--RRILQQLGL-DSTCDDSIIVKEVCGA 825
Cdd:PLN02596 322 YLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVvnEKLKEIFGItDSTPMAREVVAEVCDI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 826 VSKRAAQLCGAGLAAIVEKKREdrgVEHLQITVGVDGTLYKLHPHFSRVLRETVKELAP---QCDVTFMLSEDGSGKGAA 902
Cdd:PLN02596 402 VAERGARLAGAGIVGIIKKLGR---IENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGselSDNVVIEHSHGGSGAGAL 478
|
....
gi 699630172 903 LITA 906
Cdd:PLN02596 479 FLAA 482
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
3-458 |
4.76e-46 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 172.75 E-value: 4.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 3 AVHLLAFHFTKLKEDQIKKVDRYL--YHMRLSDDV--LLDVMARFQAEMVKGLGKDTnpTATVKMLPSFVRSLPDGSEKG 78
Cdd:PLN02596 19 AAAVLMGRWKRRKERQWKHTQRILrkFARECATPVskLWEVADALVSDMTASLTAEE--TTTLNMLVSYVASLPSGDEKG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 79 DFLAVDLGGSQFRAHQVKVCDDGKQSSQLESKFYPTPKEVIQGNGTELFDYIADCLLDFM-----ETKSLKHKKLPLGFT 153
Cdd:PLN02596 97 LYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVaehpgDEADTPERVKKLGFT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 154 FSFPCKQTKLEEGVLLAWtKHFKVRGVQDTDVVSSLRKALQKHkDIDVDVLALVNDTVGTMMTCGYDDPRCEVGLIIGTG 233
Cdd:PLN02596 177 VSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKH-GLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 234 TNACYMEEMRHIDLVEG---DEGRMCINTEWGAFGddgALDDLRTEFDRELDLGSLNPGKQLFEKMISSLYLGELVRLIL 310
Cdd:PLN02596 255 TNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN---SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 311 LKMTKEGLLFNGKVSTALLTKGKIEMKHVSAM-----EKYKEGLSNTKEILTELNLFPSEEDCIAvqHVCTIVSFRSANL 385
Cdd:PLN02596 332 LKMAEETALFGDTLPPKLTTPYLLRSPDMAAMhqdtsEDHEVVNEKLKEIFGITDSTPMAREVVA--EVCDIVAERGARL 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 699630172 386 CAAALAAILtrlrenKKLLRM---RTTVGIDGGLYKTHPQYAKRLHKVVRRLVPN---CDVRFLLSVSGSGKGAAMVTA 458
Cdd:PLN02596 410 AGAGIVGII------KKLGRIenkKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSelsDNVVIEHSHGGSGAGALFLAA 482
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
523-657 |
1.02e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 42.19 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699630172 523 TEKGKFLALDLGGTNFRVLLV----KIRSgRRRsvqmynkifaIPLEImQGTGEELFDHIVQCIADFLEYMGIKGARLpL 598
Cdd:COG1940 2 PDAGYVIGIDIGGTKIKAALVdldgEVLA-RER----------IPTPA-GAGPEAVLEAIAELIEELLAEAGISRGRI-L 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699630172 599 GFTFSFPcrqASIDKGT--------LVGWtkgfkatdcEGEDVVDMLREAirrrneFDLDiVAVVND 657
Cdd:COG1940 69 GIGIGVP---GPVDPETgvvlnapnLPGW---------RGVPLAELLEER------LGLP-VFVEND 116
|
|
| ASKHA_NBD_NAGK_meta |
cd24078 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
628-683 |
3.93e-03 |
|
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. Members in this family are mainly from metazoa.
Pssm-ID: 466928 [Multi-domain] Cd Length: 314 Bit Score: 40.26 E-value: 3.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 699630172 628 CEGEDVVDMLREAIRRRNEFDLDIVAVVNDTVGTMMTCgyedpnCEIG---LIAGTGSN 683
Cdd:cd24078 75 AEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATA------FENGgivLISGTGSN 127
|
|
| |
