|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
11-436 |
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: 784.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENNDFQMESRIY 90
Cdd:cd24019 2 LSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQVKMESEIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 91 AIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDA 170
Cdd:cd24019 82 AIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 171 IARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFGDNGA 250
Cdd:cd24019 162 IKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFGDNGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 251 LDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEPGN 330
Cdd:cd24019 242 LDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDNEGD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 331 FTNCRLVLEELGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPTVTVGVDGSVYRFHPKFHNLMVEKISQ 410
Cdd:cd24019 322 FSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKEVTVGVDGSLYKYHPKFHKRMHETLKE 401
|
410 420
....*....|....*....|....*.
gi 24640843 411 LIKPGITFDLMLSEDGSGRGAALVAA 436
Cdd:cd24019 402 LVPPGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
11-436 |
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: 526.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENND--FQMESR 88
Cdd:cd24089 2 LSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNqkVEMESQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 89 IYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24089 82 VYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDN 248
Cdd:cd24089 162 KAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGR---MCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 249 GALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEP 328
Cdd:cd24089 239 GSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 329 GnFTNCRLVLEELGLtNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPT------VTVGVDGSVYRFHPKFHN 402
Cdd:cd24089 319 G-LANAKEILTRLGL-DPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKglerlrTTVGVDGSVYKKHPQFSK 396
|
410 420 430
....*....|....*....|....*....|....
gi 24640843 403 LMvEKISQLIKPGITFDLMLSEDGSGRGAALVAA 436
Cdd:cd24089 397 RL-HKAVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
11-440 |
9.51e-171 |
|
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: 486.28 E-value: 9.51e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENND--FQMESR 88
Cdd:cd24091 2 LSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWrgVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 89 IYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24091 82 IYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDN 248
Cdd:cd24091 162 EAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGR---MCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 249 GALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEP 328
Cdd:cd24091 239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 329 GnFTNCRLVLEELGLtNATDGDCANVRYICECVSKRAAHLVSAGIATLINK------MDEPTVTVGVDGSVYRFHPKFHN 402
Cdd:cd24091 319 A-LLQVRAILQQLGL-DSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKirenrgLDHLNVTVGVDGTLYKLHPHFSR 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 24640843 403 LMVEKISQLiKPGITFDLMLSEDGSGRGAALVAAVACR 440
Cdd:cd24091 397 VMHETVKEL-APKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
11-436 |
9.79e-168 |
|
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: 478.23 E-value: 9.79e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQEN--NDFQMESR 88
Cdd:cd24125 2 LSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNglQKVEMENQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 89 IYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24125 82 IYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDN 248
Cdd:cd24125 162 KAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGR---MCINMEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 249 GALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEP 328
Cdd:cd24125 239 GSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 329 GnFTNCRLVLEELGLtNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPT------VTVGVDGSVYRFHPKFHN 402
Cdd:cd24125 319 G-IRKAREVLMRLGL-DPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKgeerlrSTIGVDGSVYKKHPHFAR 396
|
410 420 430
....*....|....*....|....*....|....
gi 24640843 403 LMVEKISQLIkPGITFDLMLSEDGSGRGAALVAA 436
Cdd:cd24125 397 RLHKTVRRLV-PGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
11-436 |
7.85e-167 |
|
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: 476.26 E-value: 7.85e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQEN--NDFQMESR 88
Cdd:cd24126 2 LSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDgkQKVQMESQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 89 IYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24126 82 FYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDN 248
Cdd:cd24126 162 KAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGR---MCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 249 GALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEP 328
Cdd:cd24126 239 GSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 329 GnFTNCRLVLEELGLTNATDgDCANVRYICECVSKRAAHLVSAGIATLINKMDEPT------VTVGVDGSVYRFHPKFHN 402
Cdd:cd24126 319 G-LYNTREILSDLGLEPSEE-DCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKklerlrTTVGMDGTVYKTHPQYAK 396
|
410 420 430
....*....|....*....|....*....|....
gi 24640843 403 LMvEKISQLIKPGITFDLMLSEDGSGRGAALVAA 436
Cdd:cd24126 397 RL-HKVVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
11-440 |
7.84e-165 |
|
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: 470.91 E-value: 7.84e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENNdFQMESRIY 90
Cdd:cd24129 2 LSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAG-VQITSEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 91 AIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDA 170
Cdd:cd24129 81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 171 IARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDNGA 250
Cdd:cd24129 161 ATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGR---MCINMEWGAFGDNGC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 251 LDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEPGn 330
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLA- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 331 FTNCRLVLEELGLTNATDgDCANVRYICECVSKRAAHLVSAGIATLINKM------DEPTVTVGVDGSVYRFHPKFHNLM 404
Cdd:cd24129 317 LRQVRAILEDLGLPLTSD-DALLVLEVCQTVSQRAAQLCAAGVAAVVEKMrenrglDELAVTVGVDGTLYKLHPRFSSLV 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 24640843 405 VEKISQLiKPGITFDLMLSEDGSGRGAALVAAVACR 440
Cdd:cd24129 396 QATVREL-APRCVVTFLQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
13-435 |
1.39e-160 |
|
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar.
Pssm-ID: 466868 [Multi-domain] Cd Length: 431 Bit Score: 460.18 E-value: 1.39e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 13 DEQVQELCYRILHELRRGLAKDThpkANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENND-FQMESRIYA 91
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDG---GSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGiFIIVQRKYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 92 IPQHIMIGSGTQLFDHIAECLSNFMAEHNVY---KERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24018 78 IPDEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGdVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEE---AELFAAEDPRKKHVLINTEWGAF 245
Cdd:cd24018 158 NALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNikkLTSPSGSVTKSDEMIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 246 gDNGALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEA 325
Cdd:cd24018 237 -DNEREVLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 326 DEPGNFTNCRLVLEELGLTNA-TDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPT---VTVGVDGSVYRFHPKFH 401
Cdd:cd24018 316 DTSPDLDAVRDILKELLAIDNtTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLpepVTVGIDGSVYEKYPGFK 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 24640843 402 NLMVEKISQLIKPGITFD--LMLSEDGSGRGAALVA 435
Cdd:cd24018 396 DRLSEALRELFGPEVKANisLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
10-440 |
2.63e-160 |
|
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: 459.78 E-value: 2.63e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 10 LLTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQE-NNDFQMESR 88
Cdd:cd24130 1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSgRRSVRMYNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 89 IYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24130 81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDN 248
Cdd:cd24130 161 EAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGR---MCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 249 GALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEP 328
Cdd:cd24130 238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 329 GnFTNCRLVLEELGLTNATDgDCANVRYICECVSKRAAHLVSAGIATLINK------MDEPTVTVGVDGSVYRFHPKFHN 402
Cdd:cd24130 318 A-LLQVRRILQQLGLDSTCE-DSIIVKEVCGAVSRRAAQLCGAGLAAIVEKirenqgLDRLDITVGVDGTLYKLHPHFSR 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 24640843 403 LMVEKISQLiKPGITFDLMLSEDGSGRGAALVAAVACR 440
Cdd:cd24130 396 ILQETVKEL-APQCDVTFMLSEDGSGKGAALITAVAKR 432
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
11-440 |
4.23e-160 |
|
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: 460.62 E-value: 4.23e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHL--QENNDFQMESR 88
Cdd:cd24124 30 LSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVnhEKNQNVHMESE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 89 IYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24124 110 VYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDN 248
Cdd:cd24124 190 KAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGR---MCINTEWGAFGDD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 249 GALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEP 328
Cdd:cd24124 267 GSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 329 GnFTNCRLVLEELGLTNATDgDCANVRYICECVSKRAAHLVSAGIATLINKMDEPT------VTVGVDGSVYRFHPKFHN 402
Cdd:cd24124 347 G-LHNAKEILTRLGVEPSDD-DCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKgtprlrTTVGVDGSLYKTHPQYSR 424
|
410 420 430
....*....|....*....|....*....|....*...
gi 24640843 403 LMVEKISQLIkPGITFDLMLSEDGSGRGAALVAAVACR 440
Cdd:cd24124 425 RFHKTLRRLV-PDSDVRFLLSESGSGKGAAMVTAVAYR 461
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
1-440 |
2.59e-159 |
|
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: 457.42 E-value: 2.59e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 1 MVHELCQQLLLTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQEN 80
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 81 NDFQ----MESRIYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCA 156
Cdd:cd24092 81 EEGQwsvkTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 157 GVVNEDVVQLLKDAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhV 236
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGR---M 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 237 LINTEWGAFGDNGALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFF 316
Cdd:cd24092 238 CVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 317 TKYVSEIEADEpGNFTNCRLVLEELGLTnATDGDCANVRYICECVSKRAAHLVSAGIATLINKM------DEPTVTVGVD 390
Cdd:cd24092 318 TRFVSQVESDT-GDRKQIYNILSTLGLR-PSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMresrseDVMRITVGVD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24640843 391 GSVYRFHPKFHNLMVEKISQLiKPGITFDLMLSEDGSGRGAALVAAVACR 440
Cdd:cd24092 396 GSVYKLHPSFKERFHASVRRL-TPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
11-440 |
3.78e-159 |
|
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: 456.68 E-value: 3.78e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQ--ENNDFQMESR 88
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRsgKKRTVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 89 IYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24127 82 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDN 248
Cdd:cd24127 162 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQ---MCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 249 GALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEP 328
Cdd:cd24127 239 GCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 329 GnFTNCRLVLEELGLtNATDGDCANVRYICECVSKRAAHLVSAGIATLINK------MDEPTVTVGVDGSVYRFHPKFHN 402
Cdd:cd24127 319 A-LLQVRAILQQLGL-NSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKirenrgLDHLNVTVGVDGTLYKLHPHFSR 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 24640843 403 LMVEKISQLiKPGITFDLMLSEDGSGRGAALVAAVACR 440
Cdd:cd24127 397 IMHQTVKEL-SPKCNVSFLLSEDGSGKGAALITAVGVR 433
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
11-440 |
1.47e-157 |
|
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: 452.82 E-value: 1.47e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQ--ENNDFQMESR 88
Cdd:cd24128 2 LSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRngKWRGVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 89 IYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLK 168
Cdd:cd24128 82 IYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 169 DAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRkkhVLINTEWGAFGDN 248
Cdd:cd24128 162 EAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGR---MCVNMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 249 GALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEP 328
Cdd:cd24128 239 GCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 329 GnFTNCRLVLEELGLTNATDgDCANVRYICECVSKRAAHLVSAGIATLINK------MDEPTVTVGVDGSVYRFHPKFHN 402
Cdd:cd24128 319 A-LLQVRAILQHLGLESTCD-DSIIVKEVCTVVARRAAQLCGAGMAAVVDKirenrgLDALKVTVGVDGTLYKLHPHFAK 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 24640843 403 LMVEKISQLiKPGITFDLMLSEDGSGRGAALVAAVACR 440
Cdd:cd24128 397 VMHETVKDL-APKCDVSFLQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
13-435 |
1.22e-132 |
|
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: 386.25 E-value: 1.22e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 13 DEQVQELCYRILHELRRGLAKDthpKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENNDFQMESRIYAI 92
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISKKYEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 93 PQHIMIGSGTQLFDHIAECLSNFMAEHNVyKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDAIA 172
Cdd:cd24000 78 PDEIKTASAEEFFDFIADCIAEFLKENGL-KKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 173 RRGdVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVeeaelfAAEDPRKKHVLINTEWGAFGDNgalD 252
Cdd:cd24000 157 KRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPT------SNILLGDGGMIINTEWGNFGKN---S 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 253 FVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQagilfngqdsevlntrglfftkyvseieadepgnft 332
Cdd:cd24000 227 LPRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLAD------------------------------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 333 ncrlvleelgltnatdgdcANVRYICECVSKRAAHLVSAGIATLINKMDEPT---VTVGVDGSVYRFHPKFHNLMVEKIS 409
Cdd:cd24000 271 -------------------EILRKICELVAERSARLAAAAIAALLRKTGDSPekkITIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420
....*....|....*....|....*.
gi 24640843 410 QLIKPGITFDLMLSEDGSGRGAALVA 435
Cdd:cd24000 332 ELLGRGIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
11-436 |
2.75e-126 |
|
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: 373.10 E-value: 2.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 11 LTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLG--GTNFRVLLIHLQ--ENNDFQME 86
Cdd:cd24090 2 VTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTgiEGHRVEPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 87 SRIYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQL 166
Cdd:cd24090 82 SQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 167 LKDAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMervEEAELFAAEDPRKKHVLINTEWGAFG 246
Cdd:cd24090 162 LRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYM---EEARHVAVLDEDRGRVCVSVEWGSFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 247 DNGALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEaD 326
Cdd:cd24090 239 DDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEME-D 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 327 EPGNFTNCRLVLEELGLtNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEP------TVTVGVDGSVYRFHPKF 400
Cdd:cd24090 318 PSAGAARVRAILQDLGL-SPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSreqqtlQVAVATGGRVCERHPRF 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 24640843 401 HNLMvEKISQLIKPGITFDLMLSEDGSGRGAALVAA 436
Cdd:cd24090 397 CSIL-QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
23-438 |
1.15e-122 |
|
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: 363.90 E-value: 1.15e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 23 ILHELRRGLAKDTHPKanVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENND--FQMESRIYAIPQHIMIGS 100
Cdd:cd24020 13 MVVEMEAGLASEGGSK--LKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGrvDKQEYEEVPIPPELMVGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 101 GTQLFDHIAECLSNFMAEHN----VYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDAIARRGd 176
Cdd:cd24020 91 SEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEEALERQG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 177 VQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFgDNGALDfvRT 256
Cdd:cd24020 170 LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNF-RSSHLP--RT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 257 EFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEPGNFTNCRL 336
Cdd:cd24020 247 EEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSPDLETVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 337 VLEE-LGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMD--------EPTVTVGVDGSVYRFHPKFHNLMVEK 407
Cdd:cd24020 327 ILKDaLGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGrdgggsspAQRTVVAVDGGLYEHYPKFREYMQQA 406
|
410 420 430
....*....|....*....|....*....|...
gi 24640843 408 ISQLI--KPGITFDLMLSEDGSGRGAALVAAVA 438
Cdd:cd24020 407 LVELLgdEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
14-438 |
6.85e-122 |
|
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: 361.69 E-value: 6.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 14 EQVQELCYRILHELRRGLAKdthPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENNDFQMESRIYAIP 93
Cdd:cd24087 2 ERLRKITDHFISELEKGLSK---KGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYRLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 94 QHIMIGSGTQLFDHIAECLSNFMAEH--NVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDAI 171
Cdd:cd24087 79 EELKTGTGEELWDFIADCLKKFVEEHfpGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 172 ARRGdVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAED-PRKKHVLINTEWGAFgDNGA 250
Cdd:cd24087 159 KKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDDiPPDSPMAINCEYGAF-DNEH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 251 LDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEPGN 330
Cdd:cd24087 237 LVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 331 F-TNCRLVLEELGLtNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPTVTVGVDGSVYRFHPKFHNLMVEKIS 409
Cdd:cd24087 317 LeDTDDLFQHFFGL-ETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCHVAADGSVYNKYPGFKERAAQALK 395
|
410 420 430
....*....|....*....|....*....|..
gi 24640843 410 QLIKPGITFDLMLS---EDGSGRGAALVAAVA 438
Cdd:cd24087 396 DIFGWDGEDDPIKTvpaEDGSGVGAAIIAALT 427
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
203-437 |
7.62e-122 |
|
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: 354.11 E-value: 7.62e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 203 KIGLIVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFGDNGALDFVRTEFDRDIDVHSINPGKQTFEKMISGMY 282
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 283 MGELVRLVLVKMTQAGILFNGQdSEVLNTRGLFFTKYVSEIEADEPGNFTNCRLVLEE-LGLTNATDGDCANVRYICECV 361
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPSEDLETTREILEElLGIETVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640843 362 SKRAAHLVSAGIATLINKMDE-PTVTVGVDGSVYRFHPKFHNLMVEKISQLIKPGITFDLMLSEDGSGRGAALVAAV 437
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRdKKVTVGVDGSVYEKYPGFRERLQEALRELLGPGDKVVLVLAEDGSGVGAALIAAV 236
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
13-435 |
1.19e-121 |
|
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: 361.71 E-value: 1.19e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 13 DEQVQELCYRILHELRRGLAKDTHPKANVKcfvTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENNDFQMESRIYAI 92
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLAKHGKGMAMIP---TYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQEKSKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 93 PQHIMIG-SGTQLFDHIAECLSNFMAEH--NVYK-----ERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVV 164
Cdd:cd24088 78 PDELKTGvTAKDLFDYLAKSVEAFLTKHhgDSFAagkddDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 165 QLLKDAIARRGdVQIDVCAILNDTTGTLMSCAWKNHNC---KIGLIVGTGANACYMERVEE-AELFAAEDPRKK--HVLI 238
Cdd:cd24088 158 KLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEIsgaVLGAIFGTGTNGAYLEDLEKiKKLDDSSRVGKGktHMVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 239 NTEWGAFgDNGALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAG---ILFNGQDSEVLNTRGLF 315
Cdd:cd24088 237 NTEWGSF-DNELKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGlflIQYNDKSPSALNTPYGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 316 FTKYVSEIEADEPGNFTNCRLVL-EELGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLI------NKMDEPTVTVG 388
Cdd:cd24088 316 DTAVLSAIEIDSEAELRATRKVLlDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILiktgalNKSYDGEINIG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 24640843 389 VDGSVYRFHPKFHNLMVEKIsQLIKPGIT----FDLMLSEDGSGRGAALVA 435
Cdd:cd24088 396 VDGSVIEFYPGFESMLREAL-RLLLIGAEgekrIKIGIAKDGSGVGAALCA 445
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
8-438 |
2.12e-104 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 318.16 E-value: 2.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 8 QLLLTDEQVQELCYRILHELRRGL-AKDTHPKAN------VKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQEN 80
Cdd:PTZ00107 17 QFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLWipnecsFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 81 N-DFQMESRiYAIPQHIMIG---------SGTQLFDHIAECLSNFMAEHNVY---KERLPLGFTFSFPLRQLGLTKGLLE 147
Cdd:PTZ00107 97 GkMERTQSK-FSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTFSFPCTQLSVNNAILI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 148 TWTKGF-----NCAGVVNEDVVQLLKDAIaRRGDVQIDVCAILNDTTGTLMSCAWK----NHNCKIGLIVGTGANACYME 218
Cdd:PTZ00107 176 DWTKGFetgraTNDPVEGKDVGELLNDAF-KRNNVPANVVAVLNDTVGTLISCAYQkpknTPPCQVGVIIGTGSNACYFE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 219 rvEEAELFAAedprkKHVLINTEWGAFgDNgalDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAG 298
Cdd:PTZ00107 255 --PEVSAYGY-----AGTPINMECGNF-DS---KLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 299 ILfngqdsEVLNTRGLFFTKYVSEIEADEPGNFTNCRLVLEELGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLIN 378
Cdd:PTZ00107 324 AP------PKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAK 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640843 379 KMDEPT--VTVGVDGSVYRFHPKFHNLMVEKISQLIKPGITF-DLMLSEDGSGRGAALVAAVA 438
Cdd:PTZ00107 398 KTRTVQgkATVAIDGSVYVKNPWFRRLLQEYINSILGPDAGNvVFYLADDGSGKGAAIIAAMV 460
|
|
| PLN02914 |
PLN02914 |
hexokinase |
26-436 |
1.29e-97 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 301.42 E-value: 1.29e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 26 ELRRGLAKDThpKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHL--QENNDFQMESRIYAIPQHIMIGSGTQ 103
Cdd:PLN02914 65 DMRAGLAVDG--GGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLggKDERVIATEFEQVSIPQELMFGTSEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 104 LFDHIAECLSNFMAEHNvYKERLP------LGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDAIARRGdV 177
Cdd:PLN02914 143 LFDFIASGLANFVAKEG-GKFHLPegrkreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-L 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 178 QIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFGDNGALdfvrTE 257
Cdd:PLN02914 221 DMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSSGRTIINTEWGAFSDGLPL----TE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 258 FDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEPGNFTNCRLV 337
Cdd:PLN02914 297 FDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNSDDLQAVGSI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 338 LEELGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPT--------VTVGVDGSVYRFHPKFHNLMVEKIS 409
Cdd:PLN02914 377 LYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSkgmifgkrTVVAMDGGLYEKYPQYRRYMQDAVT 456
|
410 420
....*....|....*....|....*....
gi 24640843 410 QLIKPGITFDLML--SEDGSGRGAALVAA 436
Cdd:PLN02914 457 ELLGLELSKNIAIehTKDGSGIGAALLAA 485
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
2-197 |
4.00e-95 |
|
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: 284.78 E-value: 4.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 2 VHELCQQLLLTDEQVQELCYRILHELRRGLAKDThpKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENN 81
Cdd:pfam00349 2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 82 DFQMESRIYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYK---ERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGV 158
Cdd:pfam00349 80 KFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 24640843 159 VNEDVVQLLKDAIARRGdVQIDVCAILNDTTGTLMSCAW 197
Cdd:pfam00349 160 VGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAGAY 197
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
7-439 |
3.61e-88 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 275.30 E-value: 3.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 7 QQLLLTDEQVQELCYRILHELRRGLAkdtHPKANVKCFVTYVQdLPNG-NERGKFLALDLGGTNFRVLLIHLQENNDFQM 85
Cdd:COG5026 13 HGFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYLG-LPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 86 ESRIyaipQHIMIGSG-----TQLFDHIAECLSNFMaehnvyKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVN 160
Cdd:COG5026 89 ENFK----SFPLPGTSseitaEEFFDFIADYIEPLL------DESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 161 EDVVQLLKDAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCK----IGLIVGTGANACYMERVEEAELFAAEdprKKHV 236
Cdd:COG5026 159 KNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKLPAY---EGPM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 237 LINTEWGAFgdNGAldfVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGiLFNGQDSEVLNTRGLFF 316
Cdd:COG5026 236 IINMESGNF--NKL---PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 317 TKYVSEIEADEPGNftncrlvLEELG--LTNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDE-----PTVTVGV 389
Cdd:COG5026 310 TVDMSRFLADPSDE-------KEILSqcLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGPgktplKPHCIAI 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24640843 390 DGSVYRFHPKFHNLMVEKISQLI--KPGITFDLMLSEDGSGRGAALVAAVAC 439
Cdd:COG5026 383 DGSTYEKMPGLAEKIEYALQEYLlgEKGRYVEFVLVENASLLGAAIAAALNE 434
|
|
| PLN02405 |
PLN02405 |
hexokinase |
26-436 |
7.42e-82 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 260.92 E-value: 7.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 26 ELRRGLAKDTHPKanVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHL--QENNDFQMESRIYAIPQHIMIGSGTQ 103
Cdd:PLN02405 65 EMHAGLASEGGSK--LKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLggKDGRVVKQEFEEVSIPPHLMTGSSDA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 104 LFDHIAECLSNFMAEHNVYKERLP-----LGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDAIARRGdVQ 178
Cdd:PLN02405 143 LFDFIAAALAKFVATEGEDFHLPPgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-LD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 179 IDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFGDNgalDFVRTEF 258
Cdd:PLN02405 222 MRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSS---HLPLTEY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 259 DRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEPGNFTNCRLVL 338
Cdd:PLN02405 299 DHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 339 EE-LGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPTV--------TVGVDGSVYRFHPKFHNLMVEKIS 409
Cdd:PLN02405 379 KDiLEIPNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDTVkdgekqksVIAMDGGLFEHYTEFSKCMESTLK 458
|
410 420
....*....|....*....|....*....
gi 24640843 410 QLIKPGI--TFDLMLSEDGSGRGAALVAA 436
Cdd:PLN02405 459 ELLGEEVseSIEVEHSNDGSGIGAALLAA 487
|
|
| PLN02362 |
PLN02362 |
hexokinase |
26-436 |
3.79e-79 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 254.42 E-value: 3.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 26 ELRRGLAKDTHPKanVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHL--QENNDFQMESRIYAIPQHIMIGSGTQ 103
Cdd:PLN02362 65 EMHAGLASEGGSK--LKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLggQRSSILSQDVERHPIPQHLMNSTSEV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 104 LFDHIAECLSNFMAEHNVYKE-----RLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDAIARRGdVQ 178
Cdd:PLN02362 143 LFDFIASSLKQFVEKEENGSEfsqvrRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 179 IDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEaeLFAAEDPRKK--HVLINTEWGAFGDNgalDFVRT 256
Cdd:PLN02362 222 MRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDA--IIKCQGLLTTsgSMVVNMEWGNFWSS---HLPRT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 257 EFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFnGQDSEVLNTRGLFFTKYVSEIEADEPGNFTN-CR 335
Cdd:PLN02362 297 SYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMHEDDSPELQEvAR 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 336 LVLEELGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLINK-------------------MDEPTVtVGVDGSVYRF 396
Cdd:PLN02362 376 ILKETLGISEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKigrdgsggitsgrsrsdiqIMRRTV-VAVEGGLYTN 454
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 24640843 397 HPKFHNLMVEKISQLIKPGITFDLML--SEDGSGRGAALVAA 436
Cdd:PLN02362 455 YTMFREYLHEALNEILGEDVAQHVILkaTEDGSGIGSALLAA 496
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
45-436 |
3.50e-54 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 188.16 E-value: 3.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 45 VTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENND--FQMESRIYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVY 122
Cdd:PLN02596 83 VSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEpiSDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 123 KERLP-----LGFTFSFPLRQLGLTKGLLETWtKGFNCAGVVNEDVVQLLKDAIARRGdVQIDVCAILNDTTGTLMSCAW 197
Cdd:PLN02596 163 EADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDTIGNLAGGRY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 198 KNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFGdngALDFVRTEFDRDIDVHSINPGKQTFEKM 277
Cdd:PLN02596 241 YNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPESQEIVISTEWGNFN---SCHLPITEFDASLDAESSNPGSRIFEKL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 278 ISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEAD--EPGNFTNCRLvLEELGLTNATDGDCANVR 355
Cdd:PLN02596 318 TSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDtsEDHEVVNEKL-KEIFGITDSTPMAREVVA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640843 356 YICECVSKRAAHLVSAGIATLINKM---DEPTVTVGVDGSVYRFHPKFHNLMVEKISQLIKPGITFDLML--SEDGSGRG 430
Cdd:PLN02596 397 EVCDIVAERGARLAGAGIVGIIKKLgriENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIehSHGGSGAG 476
|
....*.
gi 24640843 431 AALVAA 436
Cdd:PLN02596 477 ALFLAA 482
|
|
| |
