|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
29-497 |
0e+00 |
|
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: 791.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 29 AAKLDELTAYFIECMEKGLNNTsvgeektvDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDGTFDMQQ 108
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLAKH--------GKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 109 LKSKIPEEYLNDkdVTSEELFSYLGRRTRAFVRKHHPELLKsTGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIE 188
Cdd:cd24088 73 EKSKIPDELKTG--VTAKDLFDYLAKSVEAFLTKHHGDSFA-AGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 189 DTVGKDVVRLYQEQLDIQGLsMINVVALTNDTVGTFLSHCYTSGsrpssagEISEPVIGCIFGTGTNGCYMEDIENIKKL 268
Cdd:cd24088 150 DAVGKDVVKLLQDELDRQGI-PVKVVALVNDTVGTLLARSYTSP-------EISGAVLGAIFGTGTNGAYLEDLEKIKKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 269 PDELRTRllhEGKTQMCINIEWGSFDNELKHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLI 348
Cdd:cd24088 222 DDSSRVG---KGKTHMVINTEWGSFDNELKVLPTTPYDNKLDQK-SSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 349 LGQYrnYDQLPHRLKTPFQLCSEVLSRIEIDDSTNLRETELSFLQSLRLPT-TFEERKAIQNLVRSITRRSAYLAAVPIA 427
Cdd:cd24088 298 LIQY--NDKSPSALNTPYGLDTAVLSAIEIDSEAELRATRKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 428 AILIKTNALNKRYHGEVEIGFDGYVIEYYPGFRSMLRHALALSPIGTEGERKIHLRLAKDGSGVGAALCA 497
Cdd:cd24088 376 AILIKTGALNKSYDGEINIGVDGSVIEFYPGFESMLREALRLLLIGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
30-497 |
0e+00 |
|
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: 524.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 30 AKLDELTAYFIECMEKGLnntsvgeeKTVDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNG-DGTFDMQQ 108
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGL--------EGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGnGGIFIIVQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 109 LKSKIPEEYlndKDVTSEELFSYLGRRTRAFVRKHHpelLKSTGEniKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIE 188
Cdd:cd24018 74 RKYKIPDEA---KTGTGEELFDFIAECIAEFLEEHN---LDLQSD--KTIPLGFTFSFPVQQTSIDSGILISWTKGFNAP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 189 DTVGKDVVRLYQEQLDIQGLSmINVVALTNDTVGTFLSHCYTSGSrpssageisePVIGCIFGTGTNGCYMEDIENIKKL 268
Cdd:cd24018 146 GVVGKDVVELLQNALDRRGVN-VKVVALVNDTVGTLVASAYFDPS----------TVIGVIFGTGTNACYWEKVSNIKKL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 269 PDELRTRllhEGKTQMCINIEWGSFDNELKHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLI 348
Cdd:cd24018 215 TSPSGSV---TKSDEMIINTEWGAFDNEREVLPLTKYDRELDDA-SPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 349 LGqyrnyDQLPHRLKTPFQLCSEVLSRIEIDDSTNLRETELSFLQSLRLP-TTFEERKAIQNLVRSITRRSAYLAAVPIA 427
Cdd:cd24018 291 FS-----GKSSELLNEPYSLDTAFLSRIEADTSPDLDAVRDILKELLAIDnTTLEDRKLIKRICELVSTRAARLSAAAIA 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 428 AILIKTNALNKRyhgEVEIGFDGYVIEYYPGFRSMLRHALALSPiGTEGERKIHLRLAKDGSGVGAALCA 497
Cdd:cd24018 366 AILLKRGSLLPE---PVTVGIDGSVYEKYPGFKDRLSEALRELF-GPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
26-497 |
7.74e-130 |
|
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: 383.82 E-value: 7.74e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 26 QVDAAKLDELTAYFIECMEKGLnntSVGEEKTVDkgLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDGTFD 105
Cdd:cd24019 1 RLSDEQLEEIMDRLLKEMEKGL---SKDTHPTAS--VKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 106 MQQLKSKIPEEYLNdkdVTSEELFSYLGRRTRAFVRKHhpellkstGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSF 185
Cdd:cd24019 76 MESEIYAIPEEIMT---GTGEQLFDYIAECLAEFLEKN--------GLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 186 KIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLSHCYtsgsrpssagEISEPVIGCIFGTGTNGCYMEDIENI 265
Cdd:cd24019 145 KCSGVEGEDVVRLLQEAIKRRGDIKVDVVAVVNDTVGTLMSCAY----------EDPNCEIGLIVGTGTNACYMEKLSNV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 266 KKLPDElrtrllHEGKTQMCINIEWGSF-DN-ELKHLsATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLH 343
Cdd:cd24019 215 EKWDGD------EGDPGQVIINTEWGAFgDNgVLDFI-RTEFDREVDEE-SLNPGKQLFEKMISGMYLGELVRLVLLKLA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 344 ARGLILGQyrnydQLPHRLKTPFQLCSEVLSRIEIDDSTNLRETElSFLQSLRL-PTTFEERKAIQNLVRSITRRSAYLA 422
Cdd:cd24019 287 KEGLLFRG-----QLSEELLTRGSFETKYVSEIESDNEGDFSNTR-EILKELGLeDASDEDCEIVRYVCEAVSTRAAQLV 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366669 423 AVPIAAILIKTNALnkryhgEVEIGFDGYVIEYYPGFRSMLRHALA-LSPIGTegerKIHLRLAKDGSGVGAALCA 497
Cdd:cd24019 361 AAGIAALLNRMNRK------EVTVGVDGSLYKYHPKFHKRMHETLKeLVPPGC----KFKLMLSEDGSGKGAALVA 426
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
30-497 |
1.64e-126 |
|
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: 375.17 E-value: 1.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 30 AKLDELTAYFIECMEKGLnntsvgeekTVDKG-LPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDGTFDMQQ 108
Cdd:cd24087 2 ERLRKITDHFISELEKGL---------SKKGGnIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 109 LKSKIPEEYlndKDVTSEELFSYLGRRTRAFVRKHHPellkstGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIE 188
Cdd:cd24087 73 SKYRLPEEL---KTGTGEELWDFIADCLKKFVEEHFP------GGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 189 DTVGKDVVRLYQEQLDIQGLSmINVVALTNDTVGTFLSHCYTSgsrPSSAgeisepvIGCIFGTGTNGCYMEDIENIKKL 268
Cdd:cd24087 144 NVEGHDVVPMLQKALKKRNVP-IELVALINDTTGTLIASNYTD---PETK-------IGVIFGTGCNAAYMEVVSNIPKL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 269 ------PDELrtrllhegktqMCINIEWGSFDNELKHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDL 342
Cdd:cd24087 213 ehddipPDSP-----------MAINCEYGAFDNEHLVLPRTKYDVIIDEE-SPRPGQQAFEKMIAGYYLGEILRLVLLDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 343 HARGLILgqyrnYDQLPHRLKTPFQLCSEVLSRIEIDDSTNLRETELSFLQSLRLPTTFEERKAIQNLVRSITRRSAYLA 422
Cdd:cd24087 281 YDEGFLF-----KGQDTSKLEKPYVMDTSFLSRIEEDPFENLEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLS 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366669 423 AVPIAAILIKtnalnKRYHGeVEIGFDGYVIEYYPGFRSmlRHALALSPI--GTEGERKIHLRLAKDGSGVGAALCA 497
Cdd:cd24087 356 ACGIAAICKK-----RGYKT-CHVAADGSVYNKYPGFKE--RAAQALKDIfgWDGEDDPIKTVPAEDGSGVGAAIIA 424
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
29-497 |
8.63e-115 |
|
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: 345.80 E-value: 8.63e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 29 AAKLDELTAYFIECMEKGLnntsvgeEKTVDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNG--DGTFDM 106
Cdd:cd24020 3 VSRLRQVADAMVVEMEAGL-------ASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGkeGRVDKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 107 QQLKSKIPEEYLNdkdVTSEELFSYLGRRTRAFVRKHHPellKSTGENIKPLkMGFTFSYPVDQTSLSSGTLIRWTKSFK 186
Cdd:cd24020 76 EYEEVPIPPELMV---GTSEELFDFIAGELAKFVATEGE---GFHPEGEKRE-LGFTFSFPVKQTSIDSGTLIKWTKGFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 187 IEDTVGKDVVRLYQEQLDIQGLSMiNVVALTNDTVGTFLSHCYTSgsrpssageiSEPVIGCIFGTGTNGCYMEDIENIK 266
Cdd:cd24020 149 ISDTVGKDVVELLEEALERQGLDM-RVAALVNDTVGTLAGGRYVD----------QDTMAAVILGTGTNAAYVERADAIP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 267 KLPDELRTrllhegKTQMCINIEWGSFDNElkHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARG 346
Cdd:cd24020 218 KWSGGLPR------SGEMVINTEWGNFRSS--HLPRTEEDRELDAE-SLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 347 LILGqyrnyDQLPHRLKTPFQLCSEVLSRIEIDDSTNLRETELSFLQSLRLP-TTFEERKAIQNLVRSITRRSAYLAAVP 425
Cdd:cd24020 289 ALFG-----DTVPSKLEIPFILRTPDMSAMHEDDSPDLETVARILKDALGIDdTSLEARKVVVEVCDLVAERGARLAAAG 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366669 426 IAAILIKTNALNKRYHGE--VEIGFDGYVIEYYPGFRSMLRHALAlSPIGTEGERKIHLRLAKDGSGVGAALCA 497
Cdd:cd24020 364 IVGILKKLGRDGGGSSPAqrTVVAVDGGLYEHYPKFREYMQQALV-ELLGDEAADSVELELSNDGSGIGAALLA 436
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
32-495 |
1.31e-107 |
|
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: 324.23 E-value: 1.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 32 LDELTAYFIECMEKGLNNTsvgeektvDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDGTFDMQQLKS 111
Cdd:cd24000 4 LKEITDAFLEELEKGLAGE--------PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISKKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 112 KIPEEylnDKDVTSEELFSYLGRRTRAFVRKHHpellkstgeNIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIEDTV 191
Cdd:cd24000 76 EIPDE---IKTASAEEFFDFIADCIAEFLKENG---------LKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 192 GKDVVRLYQEQLDIQGLSmINVVALTNDTVGTFLSHCYTSGSrpssageisePVIGCIFGTGTNGCYMEDIENIKklpde 271
Cdd:cd24000 144 GKDVGELLNDALKKRGLP-VKVVAVLNDTVATLLAGAYKDPD----------CRIGLILGTGTNAAYLEPTSNIL----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 272 lrtrllhEGKTQMCINIEWGSFDNElkHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHarglilgq 351
Cdd:cd24000 208 -------LGDGGMIINTEWGNFGKN--SLPRTEYDREVDKA-SENPGFQPLEKMVSGKYLGELVRLILKDLA-------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 352 yrnydqlphrlktpfqlcsevlsrieiddstnlretelsflqslrlpttfeeRKAIQNLVRSITRRSAYLAAVPIAAILI 431
Cdd:cd24000 270 ----------------------------------------------------DEILRKICELVAERSARLAAAAIAALLR 297
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366669 432 KTNALNKRYhgeVEIGFDGYVIEYYPGFRSMLRHAL-ALSPIGTEgerkIHLRLAKDGSGVGAAL 495
Cdd:cd24000 298 KTGDSPEKK---ITIAVDGSLFEKYPGYRERLEEYLkELLGRGIR----IELVLVEDGSLIGAAL 355
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
245-499 |
6.51e-99 |
|
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: 297.48 E-value: 6.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 245 VIGCIFGTGTNGCYMEDIENIKKLPDELrtrllhEGKTQMCINIEWGSFDNELK-HLSATKYDIDIDQKfSPNPGYHLFE 323
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKL------PKSGEMIINTEWGAFGDNGLlPLPRTEYDKELDAE-SPNPGFQPFE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 324 KRISGMYLGELLRNILVDLHARGLILGQYrnydqlPHRLKTPFQLCSEVLSRIEIDDSTNLRETELSFLQSLRLPT-TFE 402
Cdd:pfam03727 74 KMISGMYLGELVRLVLLDLAEEGLLFKGQ------SEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETvTEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 403 ERKAIQNLVRSITRRSAYLAAVPIAAILIKTNALNKryhgeVEIGFDGYVIEYYPGFRSMLRHALALSpigTEGERKIHL 482
Cdd:pfam03727 148 DRKIVRRICEAVSTRAARLVAAGIAAILKKIGRDKK-----VTVGVDGSVYEKYPGFRERLQEALREL---LGPGDKVVL 219
|
250
....*....|....*..
gi 398366669 483 RLAKDGSGVGAALCALV 499
Cdd:pfam03727 220 VLAEDGSGVGAALIAAV 236
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
25-500 |
1.80e-95 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 295.71 E-value: 1.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 25 LQVDAAKLDELTAYFIECMEKGLNntsvGEEKTvdkgLPMIPTYVTsLPNG-TERGVLLAADLGGTHFRVCSVTLNGDGT 103
Cdd:COG5026 15 FDLSSIDLEEIAAKFQEEMEKGLE----GKKSS----LKMLPSYLG-LPTGvKETGPVIALDAGGTNFRVALVRFDGEGT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 104 FDMQQLKSK-IPeeyLNDKDVTSEELFSYLGrrtrafvrkhhpellkstgENIKPL-----KMGFTFSYPVDQTSLSSGT 177
Cdd:COG5026 86 FEIENFKSFpLP---GTSSEITAEEFFDFIA-------------------DYIEPLldesyKLGFCFSFPAEQLPDKDGR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 178 LIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLSHCYTSGSRPSSAgeisepVIGCIFGTGTNGC 257
Cdd:COG5026 144 LIQWTKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDGYSG------YIGSILGTGHNTC 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 258 YMEDIENIKKLPDElrtrllhegKTQMCINIEWGSFDNelkhLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRN 337
Cdd:COG5026 218 YLEPNAPIGKLPAY---------EGPMIINMESGNFNK----LPRTKIDEILDQQ-SEKPGEQLLEKMVSGRYLGELCRL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 338 ILVDLHARGLILGqyrnydQLPHRLKTPFQLCSEVLSRIEIDDStnlreTELSFLQSLRLPTTFEERKAIQNLVRSITRR 417
Cdd:COG5026 284 TLREAAAEGLFSP------GFSEVFETPYSLTTVDMSRFLADPS-----DEKEILSQCLEAGSEEDREILREIADAIVER 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 418 SAYLAAVPIAAILIKTNAlNKRYHGEVEIGFDGYVIEYYPGFRSMLRHALALSPIGTEGeRKIHLRLAKDGSGVGAALCA 497
Cdd:COG5026 353 AARLVAATLAGILLHLGP-GKTPLKPHCIAIDGSTYEKMPGLAEKIEYALQEYLLGEKG-RYVEFVLVENASLLGAAIAA 430
|
...
gi 398366669 498 LVA 500
Cdd:COG5026 431 ALN 433
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
17-229 |
3.04e-93 |
|
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: 3.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 17 AVVEICSSLQVDAAKLDELTAYFIECMEKGLnntsvgeEKTVDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSV 96
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGL-------AKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 97 TLNGDGTFDMQQLKSKIPEEYLNDkdvTSEELFSYLGRRTRAFVRKHHPELLKStgeniKPLKMGFTFSYPVDQTSLSSG 176
Cdd:pfam00349 74 ELGGDGKFEITQEKYKIPEELMTG---TGEELFDFIADCIAEFLKEHGLEDFEE-----KELPLGFTFSFPVEQTSLDSG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398366669 177 TLIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSmINVVALTNDTVGTFLSHCY 229
Cdd:pfam00349 146 TLIRWTKGFDIPGVVGKDVVQLLQEALERRGLP-VKVVALVNDTVGTLMAGAY 197
|
|
| PLN02914 |
PLN02914 |
hexokinase |
58-497 |
2.30e-87 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 276.77 E-value: 2.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 58 VDKG--LPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNG--DGTFDMQQLKSKIPEEYLNDkdvTSEELFSYLG 133
Cdd:PLN02914 72 VDGGgdLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGkdERVIATEFEQVSIPQELMFG---TSEELFDFIA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 134 RRTRAFVRKHHPELLKSTGeniKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSMiNV 213
Cdd:PLN02914 149 SGLANFVAKEGGKFHLPEG---RKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDM-RV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 214 VALTNDTVGTFlshcytSGSRPSSageiSEPVIGCIFGTGTNGCYMEDIENIKKlpdeLRTRLLHEGKTqmCINIEWGSF 293
Cdd:PLN02914 225 SALVNDTVGTL------AGARYWD----DDVMVAVILGTGTNACYVERTDAIPK----LQGQKSSSGRT--IINTEWGAF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 294 DNElkhLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLILGQYrnydqLPHRLKTPFQLCSEVL 373
Cdd:PLN02914 289 SDG---LPLTEFDREMDAA-SINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHF-----VPEKLSTPFALRTPHL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 374 SRIEIDDSTNLRETELSFLQSLRLPTTFEERKAIQNLVRSITRRSAYLAAVPIAAILIKTNALNKR--YHGEVEIGFDGY 451
Cdd:PLN02914 360 CAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGmiFGKRTVVAMDGG 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 398366669 452 VIEYYPGFRSMLRHALAlSPIGTEGERKIHLRLAKDGSGVGAALCA 497
Cdd:PLN02914 440 LYEKYPQYRRYMQDAVT-ELLGLELSKNIAIEHTKDGSGIGAALLA 484
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
43-500 |
5.00e-85 |
|
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: 269.03 E-value: 5.00e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 43 MEKGLNNTSVGeektvDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNgDGTFDMQQLKSKI---PEEYLN 119
Cdd:cd24091 18 MERGLRKETHA-----SAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVR-SGKWRGVEMHNKIyaiPQEIMQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 120 DkdvTSEELFSYLGRRTRAFvrkhhpelLKSTGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIEDTVGKDVVRLY 199
Cdd:cd24091 92 G---TGEELFDHIVQCIADF--------LEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 200 QEQLDIQGLSMINVVALTNDTVGTFLSHCYtsgsrpssagEISEPVIGCIFGTGTNGCYMEDIENIKKLPDElrtrllhE 279
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGY----------EDPHCEIGLIVGTGSNACYMEEMRNVEMVEGE-------E 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 280 GKtqMCINIEWGSF--DNELKHLSaTKYDIDIDQkFSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLIlgqYRNydQ 357
Cdd:cd24091 224 GR--MCINMEWGAFgdNGCLDDIR-TRYDVEVDE-LSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLL---FRG--Q 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 358 LPHRLKTPFQLCSEVLSRIEiDDSTNLRETElSFLQSLRLPTTFEERKAIQNLVRSITRRSAYLAAVPIAAILIKTNALN 437
Cdd:cd24091 295 ISERLKTRGIFETKFLSQIE-SDRLALLQVR-AILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENR 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366669 438 KRYHGEVEIGFDGYVIEYYPGFRSMLRHAL-ALSPigtegERKIHLRLAKDGSGVGAALCALVA 500
Cdd:cd24091 373 GLDHLNVTVGVDGTLYKLHPHFSRVMHETVkELAP-----KCDVTFLQSEDGSGKGAALITAVA 431
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
30-495 |
1.85e-83 |
|
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: 264.71 E-value: 1.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 30 AKLDELTAYFIECMEKGLnntsvGEEKTVDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDGT--FDMQ 107
Cdd:cd24089 5 ETLLDISRRFRKEMEKGL-----GKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNqkVEME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 108 QLKSKIPEEYLNDkdvTSEELFSYLGRRTRAFVRKHHpelLKStgeniKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKI 187
Cdd:cd24089 80 SQVYAIPEEIMHG---SGTQLFDHVAECLADFMDKQK---IKD-----KKLPLGFTFSFPCRQTKIDESILISWTKGFKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 188 EDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLSHCYTSgsrPSSAgeisepvIGCIFGTGTNGCYMEDIENIKK 267
Cdd:cd24089 149 SGVEGKDVVKLLRKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDD---QNCE-------VGLIIGTGTNACYMEEMRNIDL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 268 LPDElrtrllhEGKtqMCINIEWGSF--DNELKHLSaTKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHAR 345
Cdd:cd24089 219 VEGD-------EGR--MCINTEWGAFgdDGSLEDIR-TEFDREIDRG-SLNPGKQLFEKMISGMYLGELVRLILVKMAKE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 346 GLILGqyrnyDQLPHRLKTPFQLCSEVLSRIEiDDSTNLRETElSFLQSLRLPTTFEERKAIQNLVRSITRRSAYLAAVP 425
Cdd:cd24089 288 GLLFG-----GKISPELLTRGKFETKDVSAIE-KEKEGLANAK-EILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAAT 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366669 426 IAAIL--IKTNALNKRYhgEVEIGFDGYVIEYYPGFRSMLRHALA-LSPigtegERKIHLRLAKDGSGVGAAL 495
Cdd:cd24089 361 LAAILtrLRENKGLERL--RTTVGVDGSVYKKHPQFSKRLHKAVRrLVP-----DCDVRFLLSEDGSGKGAAM 426
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
30-500 |
2.22e-83 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 265.77 E-value: 2.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 30 AKLDELTAYFIECMEKGL------NNTSVGEEKTVDkglpMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDGT 103
Cdd:PTZ00107 23 EKLKELVDYFLYELVEGLeahrrhRNLWIPNECSFK----MLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGGK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 104 FDMQQLKSKIP------EEYLNDKDVTSEELFSYLGRRTRAFV-RKHHPEllkstgENIKPLKMGFTFSYPVDQTSLSSG 176
Cdd:PTZ00107 99 MERTQSKFSLPksallgEKGLLDKKATATDLFDHIAKSIKKMMeENGDPE------DLNKPVPVGFTFSFPCTQLSVNNA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 177 TLIRWTKSFK----IEDTV-GKDVVRLYQEQLDIQGLSmINVVALTNDTVGTFLSHCYTSGSrpssagEISEPVIGCIFG 251
Cdd:PTZ00107 173 ILIDWTKGFEtgraTNDPVeGKDVGELLNDAFKRNNVP-ANVVAVLNDTVGTLISCAYQKPK------NTPPCQVGVIIG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 252 TGTNGCYMEDienikklpdelrtRLLHEGKTQMCINIEWGSFDNElkhLSATKYDIDIDQkFSPNPGYHLFEKRISGMYL 331
Cdd:PTZ00107 246 TGSNACYFEP-------------EVSAYGYAGTPINMECGNFDSK---LPITPYDLEMDW-YTPNRGRQQFEKMISGAYL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 332 GELLRNILVdlharglilgqyrNYDQLpHRLKTPFQ---LCSEVLSRIEIDDSTNLRETELSFLQSLRLPTTFEERKAIQ 408
Cdd:PTZ00107 309 GEISRRLIV-------------HLLQL-KAPPKMWQsgsFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTDEDLYTIR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 409 NLVRSITRRSAYLAAVPIAAILIKTnalnKRYHGEVEIGFDGYVIEYYPGFRSMLRHALALspIGTEGERKIHLRLAKDG 488
Cdd:PTZ00107 375 KICELVRGRAAQLAAAFIAAPAKKT----RTVQGKATVAIDGSVYVKNPWFRRLLQEYINS--ILGPDAGNVVFYLADDG 448
|
490
....*....|...
gi 398366669 489 SGVGAA-LCALVA 500
Cdd:PTZ00107 449 SGKGAAiIAAMVA 461
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
26-500 |
8.38e-83 |
|
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: 262.90 E-value: 8.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 26 QVDAAKLDELTAYFIECMEKGLnntsvGEEKTVDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDGTfd 105
Cdd:cd24129 1 QLSHDQLAAVQAQMRKEMAKGL-----RGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 106 mqQLKSK---IPEEYLNDkdvTSEELFSYLGRRTRAFVRKHhpellkstGENIKPLKMGFTFSYPVDQTSLSSGTLIRWT 182
Cdd:cd24129 74 --QITSEiysIPETVAQG---TGQQLFDHIVDCIVDFQQKQ--------GLSGQSLPLGFTFSFPCRQLGLDQGILLNWT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 183 KSFKIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLSHCYTSgsrPSSAgeisepvIGCIFGTGTNGCYMEDI 262
Cdd:cd24129 141 KGFKASGCVGQDVVSLLREAATRKQAVELNVVAIVNDTVGTMMSCGYED---PRCE-------IGLIVGTGTNACYMEEL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 263 ENIKKLPDElrtrllhEGktQMCINIEWGSF--DNELKHLSaTKYDIDIDQkFSPNPGYHLFEKRISGMYLGELLRNILV 340
Cdd:cd24129 211 RNVAGVPGD-------SG--RMCINMEWGAFgdNGCLAMIS-TRFDASVDQ-ASINPGKQRFEKMISGMYLGEIVRHILL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 341 DLHARGLILGqyrnyDQLPHRLKTPFQLCSEVLSRIEIdDSTNLRETElSFLQSLRLPTTFEERKAIQNLVRSITRRSAY 420
Cdd:cd24129 280 HLTSLGVLFR-----GKQIQRLQTRDIFKTKFLSEIES-DSLALRQVR-AILEDLGLPLTSDDALLVLEVCQTVSQRAAQ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 421 LAAVPIAAILIKTNALNKRYHGEVEIGFDGYVIEYYPGFRSMLRHAL-ALSPigtegERKIHLRLAKDGSGVGAALCALV 499
Cdd:cd24129 353 LCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQATVrELAP-----RCVVTFLQSEDGSGKGAALVTAV 427
|
.
gi 398366669 500 A 500
Cdd:cd24129 428 A 428
|
|
| PLN02405 |
PLN02405 |
hexokinase |
62-497 |
6.17e-78 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 252.44 E-value: 6.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 62 LPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNG-DGTFDMQQLKS-KIPEEYLNDkdvTSEELFSYLGRRTRAF 139
Cdd:PLN02405 78 LKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGkDGRVVKQEFEEvSIPPHLMTG---SSDALFDFIAAALAKF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 140 VRKHHPELLKSTGeniKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSMiNVVALTND 219
Cdd:PLN02405 155 VATEGEDFHLPPG---RQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDM-RVSALVND 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 220 TVGTFLSHCYTSgsrpssageiSEPVIGCIFGTGTNGCYMEDIENIKK----LPdelrtrllHEGktQMCINIEWGSFDN 295
Cdd:PLN02405 231 TIGTLAGGRYYN----------PDVVAAVILGTGTNAAYVERAQAIPKwhglLP--------KSG--EMVINMEWGNFRS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 296 ElkHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLILGqyrnyDQLPHRLKTPFQLCSEVLSR 375
Cdd:PLN02405 291 S--HLPLTEYDHALDVE-SLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFG-----DTVPPKLKIPFILRTPDMSA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 376 IEIDDSTNLRETELSFLQSLRLPTT-FEERKAIQNLVRSITRRSAYLAAVPIAAILIKT--NALNKRYHGEVEIGFDGYV 452
Cdd:PLN02405 363 MHHDTSPDLKVVGSKLKDILEIPNTsLKMRKVVVELCNIVATRGARLSAAGIYGILKKLgrDTVKDGEKQKSVIAMDGGL 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 398366669 453 IEYYPGFRSMLRHALAlSPIGTEGERKIHLRLAKDGSGVGAALCA 497
Cdd:PLN02405 443 FEHYTEFSKCMESTLK-ELLGEEVSESIEVEHSNDGSGIGAALLA 486
|
|
| PLN02362 |
PLN02362 |
hexokinase |
62-497 |
4.70e-77 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 250.57 E-value: 4.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 62 LPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGD-GTFDMQQLKSK-IPEEYLNDkdvTSEELFSYLGRRTRAF 139
Cdd:PLN02362 78 LKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQrSSILSQDVERHpIPQHLMNS---TSEVLFDFIASSLKQF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 140 VRKhhpELLKSTGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSMiNVVALTND 219
Cdd:PLN02362 155 VEK---EENGSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDM-RVAALVND 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 220 TVGTFlshcytsgsrpsSAGEISEP--VIGCIFGTGTNGCYMEDIENIKKLPDELRTrllhegKTQMCINIEWGSFDNEl 297
Cdd:PLN02362 231 TVGTL------------ALGHYHDPdtVAAVIIGTGTNACYLERTDAIIKCQGLLTT------SGSMVVNMEWGNFWSS- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 298 kHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLILGqyrnydQLPHRLKTPFQLCSEVLSRIE 377
Cdd:PLN02362 292 -HLPRTSYDIDLDAE-SPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFG------PVSSRLSTPFVLRTPSVAAMH 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 378 IDDSTNLRETELSFLQSLRLP-TTFEERKAIQNLVRSITRRSAYLAAVPIAAILIKT------NALNKRYHGEVE----- 445
Cdd:PLN02362 364 EDDSPELQEVARILKETLGISeVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgrdgsgGITSGRSRSDIQimrrt 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 398366669 446 -IGFDGYVIEYYPGFRSMLRHALAlSPIGTEGERKIHLRLAKDGSGVGAALCA 497
Cdd:PLN02362 444 vVAVEGGLYTNYTMFREYLHEALN-EILGEDVAQHVILKATEDGSGIGSALLA 495
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
26-500 |
9.94e-77 |
|
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: 247.51 E-value: 9.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 26 QVDAAKLDELTAYFIECMEKGLNNTSvGEEKTVDkglpMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGD--GT 103
Cdd:cd24128 1 QLSHDQLLEVKRRMKVEMERGLSKET-HASAPVK----MLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGkwRG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 104 FDMQQLKSKIPEEYLNDkdvTSEELFSYLGRRTRAFvrkhhpelLKSTGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTK 183
Cdd:cd24128 76 VEMHNKIYAIPQEVMHG---TGEELFDHIVHCIADF--------LEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 184 SFKIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLSHCYtsgsrpssagEISEPVIGCIFGTGTNGCYMEDIE 263
Cdd:cd24128 145 GFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGY----------EDPHCEVGLIVGTGSNACYMEEMR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 264 NIKKLPDElrtrllhEGktQMCINIEWGSF-DNELKHLSATKYDIDIDqKFSPNPGYHLFEKRISGMYLGELLRNILVDL 342
Cdd:cd24128 215 NVELVEGE-------EG--RMCVNMEWGAFgDNGCLDDFRTEFDVAVD-ELSLNPGKQRYEKMISGMYLGEIVRNILIDF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 343 HARGLIlgqYRNydQLPHRLKTPFQLCSEVLSRIEiDDSTNLRETElSFLQSLRLPTTFEERKAIQNLVRSITRRSAYLA 422
Cdd:cd24128 285 TKRGLL---FRG--RISERLKTRGIFETKFLSQIE-SDRLALLQVR-AILQHLGLESTCDDSIIVKEVCTVVARRAAQLC 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366669 423 AVPIAAILIKTNALNKRYHGEVEIGFDGYVIEYYPGFRSMLRHALA-LSPigtegERKIHLRLAKDGSGVGAALCALVA 500
Cdd:cd24128 358 GAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKdLAP-----KCDVSFLQSEDGSGKGAALITAVA 431
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
64-500 |
2.18e-76 |
|
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: 246.38 E-value: 2.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 64 MIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTL-NGDGTFDMQQLKSKIPEEYLNDkdvTSEELFSYLGRRTRAFvrk 142
Cdd:cd24130 34 MLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIrSGRRSVRMYNKIFAIPLEIMQG---TGEELFDHIVQCIADF--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 143 hhpelLKSTGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVG 222
Cdd:cd24130 108 -----LDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLREAIKRRNEFDLDIVAVVNDTVG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 223 TFLSHCYtsgsrpssagEISEPVIGCIFGTGTNGCYMEDIENIKklpdelrtrLLHEGKTQMCINIEWGSF-DNELKHLS 301
Cdd:cd24130 183 TMMTCGY----------EDPKCEIGLIAGTGSNVCYMEEMRNIE---------IVEGDEGRMCINTEWGGFgDNGCIDDI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 302 ATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLIlgqYRNydQLPHRLKTPFQLCSEVLSRIEIDDS 381
Cdd:cd24130 244 RTRYDREVDEG-SLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLL---FRG--QISERLRTRGIFETKFLSQIESDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 382 TNLRETELsfLQSLRLPTTFEERKAIQNLVRSITRRSAYLAAVPIAAILIKTNALNKRYHGEVEIGFDGYVIEYYPGFRS 461
Cdd:cd24130 318 ALLQVRRI--LQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 398366669 462 MLRHAL-ALSPigtegERKIHLRLAKDGSGVGAALCALVA 500
Cdd:cd24130 396 ILQETVkELAP-----QCDVTFMLSEDGSGKGAALITAVA 430
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
43-500 |
5.40e-75 |
|
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: 242.90 E-value: 5.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 43 MEKGLNNtSVGEEKTVDkglpMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDG--TFDMQQLKSKIPEEYLND 120
Cdd:cd24127 18 MELGLRK-QTHNNAVVK----MLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKkrTVEMHNKIYAIPIEIMQG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 121 kdvTSEELFSYLGRRTRAFvrkhhpelLKSTGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIEDTVGKDVVRLYQ 200
Cdd:cd24127 93 ---TGEELFDHIVSCISDF--------LDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 201 EQLDIQGLSMINVVALTNDTVGTFLSHCYtsgsrpssageiSEPV--IGCIFGTGTNGCYMEDIENIKKLPDElrtrllh 278
Cdd:cd24127 162 DAIKRREEFDLDVVAVVNDTVGTMMTCAY------------EEPTceVGLIVGTGSNACYMEEMKNVEMVEGD------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 279 egKTQMCINIEWGSF-DNELKHLSATKYDIDIDQkFSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLIlgqYRNydQ 357
Cdd:cd24127 223 --QGQMCINMEWGAFgDNGCLDDIRTHYDRLVDE-YSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFL---FRG--Q 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 358 LPHRLKTPFQLCSEVLSRIEIDDSTNLRETelSFLQSLRLPTTFEERKAIQNLVRSITRRSAYLAAVPIAAILIKTNALN 437
Cdd:cd24127 295 ISETLKTRGIFETKFLSQIESDRLALLQVR--AILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENR 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366669 438 KRYHGEVEIGFDGYVIEYYPGF-RSMLRHALALSPigtegERKIHLRLAKDGSGVGAALCALVA 500
Cdd:cd24127 373 GLDHLNVTVGVDGTLYKLHPHFsRIMHQTVKELSP-----KCNVSFLLSEDGSGKGAALITAVG 431
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
28-495 |
2.38e-73 |
|
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: 238.60 E-value: 2.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 28 DAAKLDELTAYFIEcMEKGLNntsvgEEKTVDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTL--NGDGTFD 105
Cdd:cd24126 4 DDTLLDIMTRFRAE-MEKGLA-----KDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVseDGKQKVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 106 MQQLKSKIPEEYLNDkdvTSEELFSYLGRRTRAFVRKHHPellkstgeNIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSF 185
Cdd:cd24126 78 MESQFYPTPEEIIHG---TGTELFDYVAECLADFMKKKGI--------KHKKLPLGFTFSFPCRQTKLDEGVLISWTKNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 186 KIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLSHCYtsgsrpssagEISEPVIGCIFGTGTNGCYMEDIENI 265
Cdd:cd24126 147 KARGVQGTDVVSSLRKAIRKHKDVDVDVLALVNDTVGTMMTCGY----------DDQYCEVGVIIGTGTNACYMEEMSHI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 266 KklpdelrtrLLHEGKTQMCINIEWGSF-DNELKHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHA 344
Cdd:cd24126 217 D---------LVEGDEGRMCINTEWGAFgDDGSLEDIRTEFDREIDLG-SLNPGKQLFEKMISGLYMGELVRLILLKMAK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 345 RGLILGqyrnyDQLPHRLKTPFQLCSEVLSRIEIDDS--TNLREtelsFLQSLRLPTTFEERKAIQNLVRSITRRSAYLA 422
Cdd:cd24126 287 KGLLFK-----GQISPALRTKGKIETKHVAAIEKYKEglYNTRE----ILSDLGLEPSEEDCIAVQHVCTIVSFRSANLC 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366669 423 AVPIAAILIKTNALNKRYHGEVEIGFDGYVIEYYPGFRSMLRHAL-ALSPigtegERKIHLRLAKDGSGVGAAL 495
Cdd:cd24126 358 AAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHKVVrRLVP-----SCDVRFLLSESGSGKGAAM 426
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
32-495 |
3.05e-71 |
|
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: 232.86 E-value: 3.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 32 LDELTAYFIECMEKGLnntsvGEEKTVDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRV--CSVTLNGDGTFDMQQL 109
Cdd:cd24125 7 LLEISKRFRKEMEKGL-----GATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVlwVKVSDNGLQKVEMENQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 110 KSKIPEEYLNDkdvTSEELFSYLGRRTRAFVRKhhpellksTGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIED 189
Cdd:cd24125 82 IYAIPEDIMRG---SGTQLFDHIAECLANFMDK--------LQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 190 TVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLSHCYTSGSRPssageisepvIGCIFGTGTNGCYMEDIENIKklp 269
Cdd:cd24125 151 VEGRDVVALLRKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCE----------IGLIVGTGTNACYMEEMRHID--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 270 delrtrLLHEGKTQMCINIEWGSF--DNELKHLSaTKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARGL 347
Cdd:cd24125 218 ------LVEGDEGRMCINMEWGAFgdDGSLDDIR-TEFDREIDMG-SLNPGKQLFEKMISGMYMGELVRLILVKMAKEEL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 348 ILGQYRNYDQLPH-RLKTPFqlcsevLSRIEIDDSTNLRETELsfLQSLRLPTTFEERKAIQNLVRSITRRSAYLAAVPI 426
Cdd:cd24125 290 LFGGKLSPELLNTgHFETKD------VSDIEGEKDGIRKAREV--LMRLGLDPTQEDCVATHRICQIVSTRSASLCAATL 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366669 427 AAIL--IKTNALNKRYHGevEIGFDGYVIEYYPGFRSMLRHAL-ALSPigtegERKIHLRLAKDGSGVGAAL 495
Cdd:cd24125 362 AAVLqrIKENKGEERLRS--TIGVDGSVYKKHPHFARRLHKTVrRLVP-----GCDVRFLRSEDGSGKGAAM 426
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
26-495 |
9.91e-71 |
|
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: 231.74 E-value: 9.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 26 QVDAAKLDELTAYFIECMEKGLNNtSVGEEKTVDkglpMIPTYVTSLPNGTERGVLLAADLG--GTHFRVCSVTLNGDGT 103
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRG-QASPAPAVR----MLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 104 FDMQQLKSK--IPEEYLNDKdvtSEELFSylgrrtraFVRKHHPELLKSTGENIKPLKMGFTFSYPVDQTSLSSGTLIRW 181
Cdd:cd24090 76 HRVEPRSQEfvIPQEVMLGA---GQQLFD--------FAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 182 TKSFKIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLShCYTsGSRPSSageisepvIGCIFGTGTNGCYMED 261
Cdd:cd24090 145 TKGFRCSDVEGQDVVQLLRDAIQRQGAYNIDVVAVVNDTVGTMMG-CEP-GVRPCE--------VGLVVDTGTNACYMEE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 262 IENIKKLpDELRTRllhegktqMCINIEWGSF--DNELKHLsATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNIL 339
Cdd:cd24090 215 ARHVAVL-DEDRGR--------VCVSVEWGSFsdDGALGPV-LTTFDHTLDHE-SLNPGAQRFEKMIGGLYLGELVRLVL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 340 VDLHARGLILGQYrnydQLPHRLKTPFQLCSEVLsriEIDDSTNLRETELSFLQSLRLPTTFEERKAIQNLVRSITRRSA 419
Cdd:cd24090 284 VHLAQRGVLFGGS----TSPALRSQGSILLEHVA---EMEDPSAGAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAA 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366669 420 YLAAVPIAAILIKTNALNKRYHGEVEIGFDGYVIEYYPGFRSMLRHALA-LSPigtegERKIHLRLAKDGSGVGAAL 495
Cdd:cd24090 357 QLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTVMlLAP-----ECDVSFIPSVDGGGRGVAM 428
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
24-500 |
4.97e-63 |
|
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: 212.56 E-value: 4.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 24 SLQVDAAKLDELTAYFIECMEKGL----NNTSVgeektvdkgLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLN 99
Cdd:cd24124 27 AMRLSDETLIDIMTRFRKEMKNGLsrdfNPTAT---------VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 100 GDGTFDMQqLKSKI---PEEYLNDkdvTSEELFSYLGRRTRAFVRKHHpelLKStgeniKPLKMGFTFSYPVDQTSLSSG 176
Cdd:cd24124 98 HEKNQNVH-MESEVydtPENIVHG---SGSQLFDHVAECLGDFMEKRK---IKD-----KKLPVGFTFSFPCQQSKIDEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 177 TLIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLShCYTSGSRPSsageisepvIGCIFGTGTNG 256
Cdd:cd24124 166 ILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMT-CGYDDQHCE---------VGLIIGTGTNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 257 CYMEDIENIKKLPDElrtrllhEGKtqMCINIEWGSF--DNELKHLSaTKYDIDIDqKFSPNPGYHLFEKRISGMYLGEL 334
Cdd:cd24124 236 CYMEELRHIDLVEGD-------EGR--MCINTEWGAFgdDGSLEDIR-TEFDREID-RGSLNPGKQLFEKMVSGMYLGEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 335 LRNILVDLHARGLILgQYRNYDQLPHRLKtpFQlcSEVLSRIEIDDSTNLRETELsfLQSLRLPTTFEERKAIQNLVRSI 414
Cdd:cd24124 305 VRLILVKMAKEGLLF-EGRITPELLTRGK--FN--TSDVSAIEKNKEGLHNAKEI--LTRLGVEPSDDDCVSVQHVCTIV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 415 TRRSAYLAAVPIAAILIKTNALNKRYHGEVEIGFDGYVIEYYPGF-RSMLRHALALSPigtegERKIHLRLAKDGSGVGA 493
Cdd:cd24124 378 SFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYsRRFHKTLRRLVP-----DSDVRFLLSESGSGKGA 452
|
....*..
gi 398366669 494 ALCALVA 500
Cdd:cd24124 453 AMVTAVA 459
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
18-500 |
9.71e-61 |
|
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: 205.88 E-value: 9.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 18 VVEICSSLQVDAAKLDELTAYFIECMEKGLNnTSVGEEKTVDkglpMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVT 97
Cdd:cd24092 2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLR-LETHEEASVK----MLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 98 LnGDGTFDMQQLKSK-----IPEEYLNDkdvTSEELFSYLGRRTRAFVRKHHpelLKStgeniKPLKMGFTFSYPVDQTS 172
Cdd:cd24092 77 V-GEGEEGQWSVKTKhqmysIPEDAMTG---TAEMLFDYISECISDFLDKHQ---MKH-----KKLPLGFTFSFPVRHED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 173 LSSGTLIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLShCYTSGSRPSsageisepvIGCIFGT 252
Cdd:cd24092 145 IDKGILLNWTKGFKASGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMIS-CYYEDHQCE---------VGMIVGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 253 GTNGCYMEDIENIKKLPDElrtrllhEGKtqMCINIEWGSFDN--ELKHLSaTKYDIDIDQKfSPNPGYHLFEKRISGMY 330
Cdd:cd24092 215 GCNACYMEEMQNVELVEGD-------EGR--MCVNTEWGAFGDsgELDEFL-LEYDRLVDES-SANPGQQLYEKLIGGKY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 331 LGELLRNILVDLHARGLILGqyrnyDQLPHRLKTPFQLCSEVLSRIEiDDSTNLRETeLSFLQSLRLPTTFEERKAIQNL 410
Cdd:cd24092 284 MGELVRLVLLRLVDENLLFH-----GEASEQLRTRGAFETRFVSQVE-SDTGDRKQI-YNILSTLGLRPSTTDCDIVRRA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 411 VRSITRRSAYLAAVPIAAILIKTNALNKRYHGEVEIGFDGYVIEYYPGFRSMLrHALA--LSPiGTEgerkIHLRLAKDG 488
Cdd:cd24092 357 CESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF-HASVrrLTP-SCE----ITFIESEEG 430
|
490
....*....|..
gi 398366669 489 SGVGAALCALVA 500
Cdd:cd24092 431 SGRGAALVSAVA 442
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
49-497 |
8.76e-49 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 175.06 E-value: 8.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 49 NTSVGEEKTVDkgLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNG--DGTFDMQQLKSKIPEEYLNDkdvTSE 126
Cdd:PLN02596 68 TASLTAEETTT--LNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGknEPISDLYREEISIPSNVLNG---TSQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 127 ELFSYLGRRTRAFVRKHHPELlKSTGENIKplKMGFTFSYPVDQTSLSSGTLIRWtKSFKIEDTVGKDVVRLYQEQLDIQ 206
Cdd:PLN02596 143 ELFDYIALELAKFVAEHPGDE-ADTPERVK--KLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 207 GLSMiNVVALTNDTVGTFLSHCYTSgsrpssageiSEPVIGCIFGTGTNGCYMEDIENIKKLPDELRTrllhegKTQMCI 286
Cdd:PLN02596 219 GLKI-RVFALVDDTIGNLAGGRYYN----------KDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPE------SQEIVI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 287 NIEWGSFDNelKHLSATKYDIDIDQKfSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLILGqyrnyDQLPHRLKTPF 366
Cdd:PLN02596 282 STEWGNFNS--CHLPITEFDASLDAE-SSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFG-----DTLPPKLTTPY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366669 367 QLCSEVLSRIEIDDSTNLRETELSFLQSLRLP-TTFEERKAIQNLVRSITRRSAYLAAVPIAAILIKTNALNKRyhgEVE 445
Cdd:PLN02596 354 LLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITdSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRIENK---KSV 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 398366669 446 IGFDGYVIEYYPGFRSMLrHALALSPIGTEGERKIHLRLAKDGSGVGAALCA 497
Cdd:PLN02596 431 VTVEGGLYEHYRVFRNYL-HSSVWEMLGSELSDNVVIEHSHGGSGAGALFLA 481
|
|
| |
