|
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. ... |
14-448 |
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: 683.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 14 VLSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVDSQI 93
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQVKMESEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 94 YAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHE 173
Cdd:cd24019 81 YAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 174 AIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADFKKTKRsVIVNAEWGAFGEG 253
Cdd:cd24019 161 AIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQ-VIINTEWGAFGDN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 254 GQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFKQSsrrpefASVLQRNEEVFETRYISE 333
Cdd:cd24019 240 GVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQ------LSEELLTRGSFETKYVSE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 334 IEDDSFPEFASTRKIVKNLfGLEKASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSNRRVIVGMDGSVYRYHPKFD 413
Cdd:cd24019 314 IESDNEGDFSNTREILKEL-GLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKEVTVGVDGSLYKYHPKFH 392
|
410 420 430
....*....|....*....|....*....|....*
gi 17864242 414 AYMRQTLQKLVKADKEWDIMLSEDGSGRGAALVAA 448
Cdd:cd24019 393 KRMHETLKELVPPGCKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
15-448 |
1.12e-153 |
|
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: 443.06 E-value: 1.12e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATV--DSQ 92
Cdd:cd24089 2 LSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVemESQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 93 IYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLH 172
Cdd:cd24089 82 VYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 173 EAIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADFKKtkrsVIVNAEWGAFGE 252
Cdd:cd24089 162 KAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGR----MCINTEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 253 GGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFKQSSRrpefASVLQRNEevFETRYIS 332
Cdd:cd24089 238 DGSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKIS----PELLTRGK--FETKDVS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 333 EIEDDSFpEFASTRKIVKNLfGLEkASVEDCQTLRYICECVAKRAATLVAIGVSGLVNR------TSNRRVIVGMDGSVY 406
Cdd:cd24089 312 AIEKEKE-GLANAKEILTRL-GLD-PSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRlrenkgLERLRTTVGVDGSVY 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 17864242 407 RYHPKFDAYMRQTLQKLVkADKEWDIMLSEDGSGRGAALVAA 448
Cdd:cd24089 389 KKHPQFSKRLHKAVRRLV-PDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
21-447 |
9.58e-143 |
|
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: 415.11 E-value: 9.58e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 21 QEVYSRFCLEVARGLKrstHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGH-HDATVDSQIYAVPKD 99
Cdd:cd24018 5 EEIVKHFLSEMEKGLE---GDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNgGIFIIVQRKYKIPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 100 LMVGPGVDLFDHIAGCLAKFVEKHD---MKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHEAIQ 176
Cdd:cd24018 82 AKTGTGEELFDFIAECIAEFLEEHNldlQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNALD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 177 RRGdADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENV---DLLRADFKKTKRsVIVNAEWGAFGeG 253
Cdd:cd24018 162 RRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGSVTKSDE-MIINTEWGAFD-N 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 254 GQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFKqssrrpEFASVLQRNEEVFETRYISE 333
Cdd:cd24018 239 EREVLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFS------GKSSELLNEPYSLDTAFLSR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 334 IEDDSFPEFASTRKIVKNLFGLEKASVEDCQTLRYICECVAKRAATLVAIGVSGLV---NRTSNRRVIVGMDGSVYRYHP 410
Cdd:cd24018 313 IEADTSPDLDAVRDILKELLAIDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILlkrGSLLPEPVTVGIDGSVYEKYP 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 17864242 411 KFDAYMRQTLQKLVKADKEWDIML--SEDGSGRGAALVA 447
Cdd:cd24018 393 GFKDRLSEALRELFGPEVKANISLvlAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
15-452 |
1.07e-141 |
|
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: 412.71 E-value: 1.07e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVD--SQ 92
Cdd:cd24091 2 LSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEmhNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 93 IYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLH 172
Cdd:cd24091 82 IYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 173 EAIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADFKKtkrsVIVNAEWGAFGE 252
Cdd:cd24091 162 EAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGR----MCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 253 GGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFK-QSSRRpefasvlQRNEEVFETRYI 331
Cdd:cd24091 238 NGCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRgQISER-------LKTRGIFETKFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 332 SEIEDDSFPeFASTRKIVKNLfGLEKASvEDCQTLRYICECVAKRAATLVAIGVSGLVNRT-SNR-----RVIVGMDGSV 405
Cdd:cd24091 311 SQIESDRLA-LLQVRAILQQL-GLDSTC-DDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIrENRgldhlNVTVGVDGTL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 17864242 406 YRYHPKFDAYMRQTLQKLV-KADKEWdiMLSEDGSGRGAALVAAVASK 452
Cdd:cd24091 388 YKLHPHFSRVMHETVKELApKCDVTF--LQSEDGSGKGAALITAVACR 433
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
15-448 |
9.10e-138 |
|
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: 402.35 E-value: 9.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLV--SLKGHHDATVDSQ 92
Cdd:cd24125 2 LSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVkvSDNGLQKVEMENQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 93 IYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLH 172
Cdd:cd24125 82 IYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 173 EAIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADfkktKRSVIVNAEWGAFGE 252
Cdd:cd24125 162 KAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGD----EGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 253 GGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFkQSSRRPEFAsvlqrNEEVFETRYIS 332
Cdd:cd24125 238 DGSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLF-GGKLSPELL-----NTGHFETKDVS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 333 EIEDDSfPEFASTRKIVKNLfGLEkASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSNR------RVIVGMDGSVY 406
Cdd:cd24125 312 DIEGEK-DGIRKAREVLMRL-GLD-PTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENkgeerlRSTIGVDGSVY 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 17864242 407 RYHPKFDAYMRQTLQKLVkADKEWDIMLSEDGSGRGAALVAA 448
Cdd:cd24125 389 KKHPHFARRLHKTVRRLV-PGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
15-454 |
5.43e-136 |
|
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: 398.12 E-value: 5.43e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVD--SQ 92
Cdd:cd24128 2 LSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEmhNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 93 IYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLH 172
Cdd:cd24128 82 IYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 173 EAIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADfkktKRSVIVNAEWGAFGE 252
Cdd:cd24128 162 EAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGE----EGRMCVNMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 253 GGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFK-QSSRRpefasvlQRNEEVFETRYI 331
Cdd:cd24128 238 NGCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRgRISER-------LKTRGIFETKFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 332 SEIEDDSFPeFASTRKIVKNLfGLEkASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRT-SNR-----RVIVGMDGSV 405
Cdd:cd24128 311 SQIESDRLA-LLQVRAILQHL-GLE-STCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIrENRgldalKVTVGVDGTL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 17864242 406 YRYHPKFDAYMRQTLQKLVkADKEWDIMLSEDGSGRGAALVAAVASKTK 454
Cdd:cd24128 388 YKLHPHFAKVMHETVKDLA-PKCDVSFLQSEDGSGKGAALITAVACRIR 435
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
15-452 |
7.59e-136 |
|
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: 397.77 E-value: 7.59e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLK-GHHDATVDSQI 93
Cdd:cd24130 2 LTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRsGRRSVRMYNKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 94 YAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHE 173
Cdd:cd24130 82 FAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 174 AIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADFKKtkrsVIVNAEWGAFGEG 253
Cdd:cd24130 162 AIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGR----MCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 254 GQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFK-QSSRRpefasvlQRNEEVFETRYIS 332
Cdd:cd24130 238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRgQISER-------LRTRGIFETKFLS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 333 EIEDDSFPeFASTRKIVKNLfGLEkASVEDCQTLRYICECVAKRAATLVAIGVSGLVN-RTSNR-----RVIVGMDGSVY 406
Cdd:cd24130 311 QIESDRLA-LLQVRRILQQL-GLD-STCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEkIRENQgldrlDITVGVDGTLY 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 17864242 407 RYHPKFDAYMRQTLQKLVKADKEwDIMLSEDGSGRGAALVAAVASK 452
Cdd:cd24130 388 KLHPHFSRILQETVKELAPQCDV-TFMLSEDGSGKGAALITAVAKR 432
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
15-452 |
4.62e-135 |
|
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: 397.07 E-value: 4.62e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATV--DSQ 92
Cdd:cd24124 30 LSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVhmESE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 93 IYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLH 172
Cdd:cd24124 110 VYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 173 EAIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADfkktKRSVIVNAEWGAFGE 252
Cdd:cd24124 190 KAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGD----EGRMCINTEWGAFGD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 253 GGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFkQSSRRPEfasVLQRNEevFETRYIS 332
Cdd:cd24124 266 DGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLF-EGRITPE---LLTRGK--FNTSDVS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 333 EIEDDSfpEFASTRKIVKNLFGLEkASVEDCQTLRYICECVAKRAATLVAIGVSGLVNR------TSNRRVIVGMDGSVY 406
Cdd:cd24124 340 AIEKNK--EGLHNAKEILTRLGVE-PSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRlrdnkgTPRLRTTVGVDGSLY 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 17864242 407 RYHPKFDAYMRQTLQKLVkADKEWDIMLSEDGSGRGAALVAAVASK 452
Cdd:cd24124 417 KTHPQYSRRFHKTLRRLV-PDSDVRFLLSESGSGKGAAMVTAVAYR 461
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
15-448 |
1.76e-134 |
|
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: 393.83 E-value: 1.76e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLV--SLKGHHDATVDSQ 92
Cdd:cd24126 2 LSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVkvSEDGKQKVQMESQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 93 IYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLH 172
Cdd:cd24126 82 FYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 173 EAIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADfkktKRSVIVNAEWGAFGE 252
Cdd:cd24126 162 KAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGD----EGRMCINTEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 253 GGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFKQssrrpEFASVLqRNEEVFETRYIS 332
Cdd:cd24126 238 DGSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKG-----QISPAL-RTKGKIETKHVA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 333 EIEddSFPE-FASTRKIVKNLfGLEKASvEDCQTLRYICECVAKRAATLVAIGVSGLVNR-TSNR-----RVIVGMDGSV 405
Cdd:cd24126 312 AIE--KYKEgLYNTREILSDL-GLEPSE-EDCIAVQHVCTIVSFRSANLCAAALAAILTRlRENKklerlRTTVGMDGTV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 17864242 406 YRYHPKFDAYMRQTLQKLVkADKEWDIMLSEDGSGRGAALVAA 448
Cdd:cd24126 388 YKTHPQYAKRLHKVVRRLV-PSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
5-452 |
4.24e-131 |
|
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to type IV hexokinase. It is found in the liver and pancreatic beta-cells, where it is controlled by insulin (activation) and glucagon (inhibition). In pancreatic beta-cells, type IV enzyme acts as a glucose sensor to modify insulin secretion. Mutations in type IV hexokinase have been associated with diabetes mellitus.
Pssm-ID: 466942 [Multi-domain] Cd Length: 444 Bit Score: 385.77 E-value: 4.24e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 5 EVRELMQPFVLSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSL--- 81
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 82 -KGHHDATVDSQIYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCA 160
Cdd:cd24092 81 eEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 161 GVEGEDVGRMLHEAIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADfkktKRS 240
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGD----EGR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 241 VIVNAEWGAFGEGGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFKQSsrrpefASVLQ 320
Cdd:cd24092 237 MCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGE------ASEQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 321 RNEEVFETRYISEIEDDSfpefaSTRKIVKNL---FGLeKASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSNRR- 396
Cdd:cd24092 311 RTRGAFETRFVSQVESDT-----GDRKQIYNIlstLGL-RPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRs 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17864242 397 -----VIVGMDGSVYRYHPKFDAYMRQTLQKLVKAdKEWDIMLSEDGSGRGAALVAAVASK 452
Cdd:cd24092 385 edvmrITVGVDGSVYKLHPSFKERFHASVRRLTPS-CEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
15-452 |
3.29e-130 |
|
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: 383.49 E-value: 3.29e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVD--SQ 92
Cdd:cd24127 2 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEmhNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 93 IYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLH 172
Cdd:cd24127 82 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 173 EAIQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADfkktKRSVIVNAEWGAFGE 252
Cdd:cd24127 162 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGD----QGQMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 253 GGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFkqssrRPEFASVLqRNEEVFETRYIS 332
Cdd:cd24127 238 NGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLF-----RGQISETL-KTRGIFETKFLS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 333 EIEDDSFPeFASTRKIVKNLfGLEkASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSNRR------VIVGMDGSVY 406
Cdd:cd24127 312 QIESDRLA-LLQVRAILQQL-GLN-STCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRgldhlnVTVGVDGTLY 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 17864242 407 RYHPKFDAYMRQTLQKLV-KADKEWdiMLSEDGSGRGAALVAAVASK 452
Cdd:cd24127 389 KLHPHFSRIMHQTVKELSpKCNVSF--LLSEDGSGKGAALITAVGVR 433
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
15-452 |
1.73e-129 |
|
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: 381.15 E-value: 1.73e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 15 LSDYQVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLkGHHDATVDSQIY 94
Cdd:cd24129 2 LSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV-GTAGVQITSEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 95 AVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHEA 174
Cdd:cd24129 81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 175 IQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADfkktKRSVIVNAEWGAFGEGG 254
Cdd:cd24129 161 ATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGD----SGRMCINMEWGAFGDNG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 255 QLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIF--KQSSRrpefasVLQRNeeVFETRYIS 332
Cdd:cd24129 237 CLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFrgKQIQR------LQTRD--IFKTKFLS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 333 EIEDDSFPeFASTRKIVKNLfGLeKASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSNRR------VIVGMDGSVY 406
Cdd:cd24129 309 EIESDSLA-LRQVRAILEDL-GL-PLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRgldelaVTVGVDGTLY 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 17864242 407 RYHPKFDAYMRQTLQKLV-KADKEWdiMLSEDGSGRGAALVAAVASK 452
Cdd:cd24129 386 KLHPRFSSLVQATVRELApRCVVTF--LQSEDGSGKGAALVTAVACR 430
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
17-447 |
7.58e-124 |
|
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: 364.29 E-value: 7.58e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 17 DYQVQEVYSRFCLEVARGLKRSthpQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVDSQIYAV 96
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISKKYEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 97 PKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTaYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHEAIQ 176
Cdd:cd24000 78 PDEIKTASAEEFFDFIADCIAEFLKENGLKK-PLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 177 RRGDaDIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADfkktkrsVIVNAEWGAFGEggqL 256
Cdd:cd24000 157 KRGL-PVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNILLGDGG-------MIINTEWGNFGK---N 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 257 DFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGnlvrlvllralerklifkqssrrpefasvlqrneevfetryisEIed 336
Cdd:cd24000 226 SLPRTEYDREVDKASENPGFQPLEKMVSGKYLG-------------------------------------------EL-- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 337 dsfpefasTRKIVKNLFglekasvedCQTLRYICECVAKRAATLVAIGVSGLVNRTS---NRRVIVGMDGSVYRYHPKFD 413
Cdd:cd24000 261 --------VRLILKDLA---------DEILRKICELVAERSARLAAAAIAALLRKTGdspEKKITIAVDGSLFEKYPGYR 323
|
410 420 430
....*....|....*....|....*....|....
gi 17864242 414 AYMRQTLQKLVKADKEWDIMLSEDGSGRGAALVA 447
Cdd:cd24000 324 ERLEEYLKELLGRGIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
19-450 |
1.08e-120 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.
Pssm-ID: 466937 [Multi-domain] Cd Length: 428 Bit Score: 358.61 E-value: 1.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 19 QVQEVYSRFCLEVARGLkrsTHPQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVDSQIYAVPK 98
Cdd:cd24087 3 RLRKITDHFISELEKGL---SKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYRLPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 99 DLMVGPGVDLFDHIAGCLAKFVEKH--DMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHEAIQ 176
Cdd:cd24087 80 ELKTGTGEELWDFIADCLKKFVEEHfpGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 177 RRGdADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADFKKTKRSVIVNAEWGAFgEGGQL 256
Cdd:cd24087 160 KRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDDIPPDSPMAINCEYGAF-DNEHL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 257 DFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFK-QSSRRPEFASvlqrneeVFETRYISEIE 335
Cdd:cd24087 238 VLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKgQDTSKLEKPY-------VMDTSFLSRIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 336 DDSFPEFASTRKIVKNLFGLEkASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSNRRVIVGMDGSVYRYHPKFDAY 415
Cdd:cd24087 311 EDPFENLEDTDDLFQHFFGLE-TTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCHVAADGSVYNKYPGFKER 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 17864242 416 MRQTLQKLVKADKEWD---IMLSEDGSGRGAALVAAVA 450
Cdd:cd24087 390 AAQALKDIFGWDGEDDpikTVPAEDGSGVGAAIIAALT 427
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
19-450 |
2.31e-117 |
|
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: 350.42 E-value: 2.31e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 19 QVQEVYSRFCLEVARGLKRSTHPQanVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVDSQI--YAV 96
Cdd:cd24020 5 RLRQVADAMVVEMEAGLASEGGSK--LKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYeeVPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 97 PKDLMVGPGVDLFDHIAGCLAKFVEKH----DMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLH 172
Cdd:cd24020 83 PPELMVGTSEELFDFIAGELAKFVATEgegfHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 173 EAIQRRGdADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADFKKTkRSVIVNAEWGAFgE 252
Cdd:cd24020 163 EALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRS-GEMVINTEWGNF-R 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 253 GGQLDfvRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVrlvllraleRKLIFKQSSRRPEF---ASVLQRNEEVFETR 329
Cdd:cd24020 240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIV---------RRVLLRMAEEAALFgdtVPSKLEIPFILRTP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 330 YISEIEDDSFPEFASTRKIVKNLFGLEKASVEDCQTLRYICECVAKRAATLVAIGVSGLVNR--------TSNRRVIVGM 401
Cdd:cd24020 309 DMSAMHEDDSPDLETVARILKDALGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKlgrdgggsSPAQRTVVAV 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 17864242 402 DGSVYRYHPKFDAYMRQTLQKLV--KADKEWDIMLSEDGSGRGAALVAAVA 450
Cdd:cd24020 389 DGGLYEHYPKFREYMQQALVELLgdEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
13-454 |
8.92e-104 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 316.62 E-value: 8.92e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 13 FVLSDYQVQEVYSRFCLEVARGLK-RSTHPQAN------VKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHH 85
Cdd:PTZ00107 18 FTMSKEKLKELVDYFLYELVEGLEaHRRHRNLWipnecsFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 86 DATVDSQIYAVPKDLMVGP---------GVDLFDHIAGCLAKFVEK---HDMKTAYLPLGFTFSFPCVQLGLKEGILVRW 153
Cdd:PTZ00107 98 KMERTQSKFSLPKSALLGEkglldkkatATDLFDHIAKSIKKMMEEngdPEDLNKPVPVGFTFSFPCTQLSVNNAILIDW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 154 TKGFDCA-----GVEGEDVGRMLHEAIQRRGdADIAVVAILNDTTGTLMSCAHR----NADCRVGVIVGTGCNACYVEDv 224
Cdd:PTZ00107 178 TKGFETGratndPVEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQkpknTPPCQVGVIIGTGSNACYFEP- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 225 envdllraDFKKTKRS-VIVNAEWGAFGEggqlDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVrlvllraleRK 303
Cdd:PTZ00107 256 --------EVSAYGYAgTPINMECGNFDS----KLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEIS---------RR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 304 LI--FKQSSRRPEFasvLQRNeeVFETRYISEIEDDSFPEFASTRKIVKNLFGLEKASvEDCQTLRYICECVAKRAATLV 381
Cdd:PTZ00107 315 LIvhLLQLKAPPKM---WQSG--SFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTD-EDLYTIRKICELVRGRAAQLA 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864242 382 AIGVSGLVNRTSNR--RVIVGMDGSVYRYHPKFDAYMRQTLqKLVKADKEWDI--MLSEDGSGRGAALVAAVASKTK 454
Cdd:PTZ00107 389 AAFIAAPAKKTRTVqgKATVAIDGSVYVKNPWFRRLLQEYI-NSILGPDAGNVvfYLADDGSGKGAAIIAAMVANDK 464
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
17-447 |
9.32e-104 |
|
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: 315.87 E-value: 9.32e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 17 DYQVQEVYSRFCLEVARGLKRSTHPQANVkcfPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVDSQIYAV 96
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLAKHGKGMAMI---PTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQEKSKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 97 PKDLMVG-PGVDLFDHIAGCLAKFVEKH-------DMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVG 168
Cdd:cd24088 78 PDELKTGvTAKDLFDYLAKSVEAFLTKHhgdsfaaGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 169 RMLHEAIQRRGdADIAVVAILNDTTGTLMS---CAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADF--KKTKRSVIV 243
Cdd:cd24088 158 KLLQDELDRQG-IPVKVVALVNDTVGTLLArsyTSPEISGAVLGAIFGTGTNGAYLEDLEKIKKLDDSSrvGKGKTHMVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 244 NAEWGAFgeggqlDFVR-----TEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFKQSSrrpEFASV 318
Cdd:cd24088 237 NTEWGSF------DNELkvlptTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYN---DKSPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 319 LQRNEEVFETRYISEIEDDSFPEFASTRKIVKNLFGLEKASVEDCQTLRYICECVAKRAATLVAIGV------SGLVNRT 392
Cdd:cd24088 308 ALNTPYGLDTAVLSAIEIDSEAELRATRKVLLDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIaailikTGALNKS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 17864242 393 SNRRVIVGMDGSVYRYHPKFDAYMRQTLQKLV---KADKEWDIMLSEDGSGRGAALVA 447
Cdd:cd24088 388 YDGEINIGVDGSVIEFYPGFESMLREALRLLLigaEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
19-448 |
2.51e-101 |
|
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: 309.16 E-value: 2.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 19 QVQEVYSRFCLEVARGLKRSTHPQANVKCFPTYVQDLPTGDEMGKYLALDLG--GTNFRVLLVSLKG--HHDATVDSQIY 94
Cdd:cd24090 6 QLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGieGHRVEPRSQEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 95 AVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHEA 174
Cdd:cd24090 86 VIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 175 IQRRGDADIAVVAILNDTTGTLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLradfKKTKRSVIVNAEWGAFGEGG 254
Cdd:cd24090 166 IQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVL----DEDRGRVCVSVEWGSFSDDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 255 QLDFVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIFKQSSrrpefASVLqRNEEVFETRYISEI 334
Cdd:cd24090 242 ALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGST-----SPAL-RSQGSILLEHVAEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 335 EDDSfPEFASTRKIVKNLfGLeKASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSNRR------VIVGMDGSVYRY 408
Cdd:cd24090 316 EDPS-AGAARVRAILQDL-GL-SPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSReqqtlqVAVATGGRVCER 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 17864242 409 HPKFDAYMRQTLQKLVkadKEWDIML--SEDGSGRGAALVAA 448
Cdd:cd24090 393 HPRFCSILQGTVMLLA---PECDVSFipSVDGGGRGVAMVTA 431
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
207-449 |
5.87e-97 |
|
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: 290.93 E-value: 5.87e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 207 RVGVIVGTGCNACYVEDVENVDLLRADFKKTKRsVIVNAEWGAFGEGGQLDFVRTEYDREVDEKSLNRSEQLFEKMTAGM 286
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGE-MIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 287 YLGNLVRLVLLRALERKLIFKQSSRRpefasvlQRNEEVFETRYISEIEDDSFPEFASTRKIVKNLFGLEKASVEDCQTL 366
Cdd:pfam03727 80 YLGELVRLVLLDLAEEGLLFKGQSEK-------LKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEDRKIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 367 RYICECVAKRAATLVAIGVSGLVNRTSN-RRVIVGMDGSVYRYHPKFDAYMRQTLQKLVKADKEWDIMLSEDGSGRGAAL 445
Cdd:pfam03727 153 RRICEAVSTRAARLVAAGIAAILKKIGRdKKVTVGVDGSVYEKYPGFRERLQEALRELLGPGDKVVLVLAEDGSGVGAAL 232
|
....
gi 17864242 446 VAAV 449
Cdd:pfam03727 233 IAAV 236
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
5-201 |
6.66e-94 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.
Pssm-ID: 459774 [Multi-domain] Cd Length: 197 Bit Score: 281.70 E-value: 6.66e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 5 EVRELMQPFVLSDYQVQEVYSRFCLEVARGLKRSThpQANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGH 84
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 85 HDATVDSQIYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKTA---YLPLGFTFSFPCVQLGLKEGILVRWTKGFDCAG 161
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFeekELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17864242 162 VEGEDVGRMLHEAIQRRGDaDIAVVAILNDTTGTLMSCAH 201
Cdd:pfam00349 159 VVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
|
|
| PLN02914 |
PLN02914 |
hexokinase |
43-452 |
6.87e-90 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 281.77 E-value: 6.87e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 43 ANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVDSQI--YAVPKDLMVGPGVDLFDHIAGCLAKFV 120
Cdd:PLN02914 76 GDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFeqVSIPQELMFGTSEELFDFIASGLANFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 121 EKHDMKTaYLP------LGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHEAIQRRGdADIAVVAILNDTTG 194
Cdd:PLN02914 156 AKEGGKF-HLPegrkreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 195 TLMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADFKKTKRSvIVNAEWGAFGEGGQLdfvrTEYDREVDEKSLNR 274
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSSGRT-IINTEWGAFSDGLPL----TEFDREMDAASINP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 275 SEQLFEKMTAGMYLGNLVRLVLLRALERKLIFKQssrrpeFASVLQRNEEVFETRYISEIEDDSFPEFASTRKIVKNLFG 354
Cdd:PLN02914 309 GEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGH------FVPEKLSTPFALRTPHLCAMQQDNSDDLQAVGSILYDVLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 355 LEkASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRT--------SNRRVIVGMDGSVYRYHPKFDAYMRQTLQKLVKA 426
Cdd:PLN02914 383 VE-ASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMeedskgmiFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGL 461
|
410 420
....*....|....*....|....*...
gi 17864242 427 DKEWDIML--SEDGSGRGAALVAAVASK 452
Cdd:PLN02914 462 ELSKNIAIehTKDGSGIGAALLAATNSK 489
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
1-450 |
7.89e-87 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 272.22 E-value: 7.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 1 MLDAEVRELMQPFVLSDYQVQEVYSRFCLEVARGLKrstHPQANVKCFPTYVQdLPTG-DEMGKYLALDLGGTNFRVLLV 79
Cdd:COG5026 3 KLLVDAFLKRHGFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYLG-LPTGvKETGPVIALDAGGTNFRVALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 80 SLKGHHDATVDSQIyavpKDLMVGPG-----VDLFDHIAGCLAKFVEKHDmktaylPLGFTFSFPCVQLGLKEGILVRWT 154
Cdd:COG5026 79 RFDGEGTFEIENFK----SFPLPGTSseitaEEFFDFIADYIEPLLDESY------KLGFCFSFPAEQLPDKDGRLIQWT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 155 KGFDCAGVEGEDVGRMLHEAIQRRGDADIAVVAILNDTTGTLMSCAHRNADC----RVGVIVGTGCNACYVEDVENVDLL 230
Cdd:COG5026 149 KEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 231 RAdfkkTKRSVIVNAEWGAFGEGgqldfVRTEYDREVDEKSLNRSEQLFEKMTAGMYLGNLVRLVLLRALERKLIfkqSS 310
Cdd:COG5026 229 PA----YEGPMIINMESGNFNKL-----PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLF---SP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 311 RRPEFASVLQRneevFETRYISEIEDDSFPEfastrkivKNLFG--LEKASVEDCQTLRYICECVAKRAATLVAIGVSGL 388
Cdd:COG5026 297 GFSEVFETPYS----LTTVDMSRFLADPSDE--------KEILSqcLEAGSEEDREILREIADAIVERAARLVAATLAGI 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17864242 389 V-----NRTSNRRVIVGMDGSVYRYHPKFDAYMRQTLQKLV--KADKEWDIMLSEDGSGRGAALVAAVA 450
Cdd:COG5026 365 LlhlgpGKTPLKPHCIAIDGSTYEKMPGLAEKIEYALQEYLlgEKGRYVEFVLVENASLLGAAIAAALN 433
|
|
| PLN02362 |
PLN02362 |
hexokinase |
43-451 |
1.23e-79 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 255.58 E-value: 1.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 43 ANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATV--DSQIYAVPKDLMVGPGVDLFDHIAGCLAKFV 120
Cdd:PLN02362 76 SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILsqDVERHPIPQHLMNSTSEVLFDFIASSLKQFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 121 EKHDMKTAYLP-----LGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHEAIQRRGdADIAVVAILNDTTGT 195
Cdd:PLN02362 156 EKEENGSEFSQvrrreLGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LDMRVAALVNDTVGT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 196 LMSCAHRNADCRVGVIVGTGCNACYVEdvenvdllRAD-------FKKTKRSVIVNAEWGAFGEGgqlDFVRTEYDREVD 268
Cdd:PLN02362 235 LALGHYHDPDTVAAVIIGTGTNACYLE--------RTDaiikcqgLLTTSGSMVVNMEWGNFWSS---HLPRTSYDIDLD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 269 EKSLNRSEQLFEKMTAGMYLGNLVrlvllraleRKLIFKQSSRRPEFASVLQRNEEVF--ETRYISEIEDDSFPEFASTR 346
Cdd:PLN02362 304 AESPNPNDQGFEKMISGMYLGDIV---------RRVILRMSQESDIFGPVSSRLSTPFvlRTPSVAAMHEDDSPELQEVA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 347 KIVKNLFGLEKASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSN------------------RRVIVGMDGSVYRY 408
Cdd:PLN02362 375 RILKETLGISEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGRdgsggitsgrsrsdiqimRRTVVAVEGGLYTN 454
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 17864242 409 HPKFDAYMRQTLQKLVKADKEWDIML--SEDGSGRGAALVAAVAS 451
Cdd:PLN02362 455 YTMFREYLHEALNEILGEDVAQHVILkaTEDGSGIGSALLAASYS 499
|
|
| PLN02405 |
PLN02405 |
hexokinase |
43-451 |
2.78e-76 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 246.67 E-value: 2.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 43 ANVKCFPTYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVDSQIYAV--PKDLMVGPGVDLFDHIAGCLAKFV 120
Cdd:PLN02405 76 SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVsiPPHLMTGSSDALFDFIAAALAKFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 121 EKHDMKTAYLP-----LGFTFSFPCVQLGLKEGILVRWTKGFDCAGVEGEDVGRMLHEAIQRRGdADIAVVAILNDTTGT 195
Cdd:PLN02405 156 ATEGEDFHLPPgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-LDMRVSALVNDTIGT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 196 LMSCAHRNADCRVGVIVGTGCNACYVEDVENVDLLRADFKKTKRSVIvNAEWGAFgEGGQLDFvrTEYDREVDEKSLNRS 275
Cdd:PLN02405 235 LAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVI-NMEWGNF-RSSHLPL--TEYDHALDVESLNPG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 276 EQLFEKMTAGMYLGNLVrlvllraleRKLIFKQSSRRPEFASVLQRNEEV---FETRYISEIEDDSFPEFASTRKIVKNL 352
Cdd:PLN02405 311 EQIFEKIISGMYLGEIL---------RRVLLKMAEEAAFFGDTVPPKLKIpfiLRTPDMSAMHHDTSPDLKVVGSKLKDI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 353 FGLEKASVEDCQTLRYICECVAKRAATLVAIGVSGLVNRTSN--------RRVIVGMDGSVYRYHPKFDAYMRQTLQKLV 424
Cdd:PLN02405 382 LEIPNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRdtvkdgekQKSVIAMDGGLFEHYTEFSKCMESTLKELL 461
|
410 420
....*....|....*....|....*....
gi 17864242 425 KAD--KEWDIMLSEDGSGRGAALVAAVAS 451
Cdd:PLN02405 462 GEEvsESIEVEHSNDGSGIGAALLAASHS 490
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
50-448 |
3.87e-47 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 169.29 E-value: 3.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 50 TYVQDLPTGDEMGKYLALDLGGTNFRVLLVSLKGHHDATVD--SQIYAVPKDLMVGPGVDLFDHIAGCLAKFVEKHDMKT 127
Cdd:PLN02596 84 SYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDlyREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 128 AYLP-----LGFTFSFPCVQLGLKEGILVRWtKGFDCAGVEGEDVGRMLHEAIQRRGdADIAVVAILNDTTGTLMSCAHR 202
Cdd:PLN02596 164 ADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDTIGNLAGGRYY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 203 NADCRVGVIVGTGCNACYVEDVENVDLLRADFKKTKrSVIVNAEWGAFGeggQLDFVRTEYDREVDEKSLNRSEQLFEKM 282
Cdd:PLN02596 242 NKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPESQ-EIVISTEWGNFN---SCHLPITEFDASLDAESSNPGSRIFEKL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 283 TAGMYLGNLVrlvllraleRKLIFKQSSRRPEFASVLQ---RNEEVFETRYISEIEDDSFPEFASTRKIVKNLFGLEKAS 359
Cdd:PLN02596 318 TSGMYLGEIV---------RRVLLKMAEETALFGDTLPpklTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITDST 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 360 VEDCQTLRYICECVAKRAATLVAIGVSGLVN---RTSNRRVIVGMDGSVYRYHPKFDAYMRQTLQKLVKADKEWDIML-- 434
Cdd:PLN02596 389 PMAREVVAEVCDIVAERGARLAGAGIVGIIKklgRIENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIeh 468
|
410
....*....|....
gi 17864242 435 SEDGSGRGAALVAA 448
Cdd:PLN02596 469 SHGGSGAGALFLAA 482
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
60-223 |
3.42e-06 |
|
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: 48.74 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 60 EMGKYLALDLGGTNFRVLLVSLKGH--HDATVDSQIYAVPKDLMvgpgvdlfDHIAGCLAKFVEKHDMkTAYLPLGFTFS 137
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEvlARERIPTPAGAGPEAVL--------EAIAELIEELLAEAGI-SRGRILGIGIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 138 FPcvqlGL---KEGIlVRWTKGFDcaGVEGEDVGRMLHEAIQRRgdadiavVAILNDTT----GTLMSCAHRNADCRVGV 210
Cdd:COG1940 74 VP----GPvdpETGV-VLNAPNLP--GWRGVPLAELLEERLGLP-------VFVENDANaaalAEAWFGAGRGADNVVYL 139
|
170
....*....|...
gi 17864242 211 IVGTGCNACYVED 223
Cdd:COG1940 140 TLGTGIGGGIVIN 152
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
65-215 |
2.52e-04 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins 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: 466849 [Multi-domain] Cd Length: 239 Bit Score: 42.45 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 65 LALDLGGTNFRVLLVSLKGHhdaTVDSQIYAVPKDlmvGPGVDLFDHIAGCLAKFVEKHDMKTAYLPLGftFSFPCVqLG 144
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGE---ILARERVPTPAE---EGPEAVLDRIAELIEELLAEAGVRERILGIG--IGVPGP-VD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864242 145 LKEGILVR-----WTKGFdcagvegeDVGRMLHEAIQRRgdadiavVAILNDTT----GTLMSCAHRNADCRVGVIVGTG 215
Cdd:cd23763 72 PETGIVLFapnlpWWKNV--------PLRELLEERLGLP-------VVVENDANaaalGEAWFGAGRGVRNFVYITLGTG 136
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
160-221 |
6.71e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 38.32 E-value: 6.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17864242 160 AGVEGEDVGRMLHEAIQRRGDAdiAVVAILNDTTGTLMScAHRNADCrVGVIVGTGCNACYV 221
Cdd:COG2971 72 AGAGTPEDAEALEAALRELFPF--ARVVVVNDALAALAG-ALGGEDG-IVVIAGTGSIAAGR 129
|
|
| |
