|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
38-471 |
0e+00 |
|
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: 845.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 38 SEKMRSIVKHFISELDKGLSKKGGNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHDFDTTQNKYRLPDH 117
Cdd:cd24087 1 TERLRKITDHFISELEKGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYRLPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 118 LRTGTSEQLWSFIAKCLKEFVDEWYPDGVSEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPMLQEQIEK 197
Cdd:cd24087 81 LKTGTGEELWDFIADCLKKFVEEHFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 198 LNIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEgllPEDIGPDSPMAINCEYGSFDNEHL 277
Cdd:cd24087 161 RNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLE---HDDIPPDSPMAINCEYGAFDNEHL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 278 VLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSKIEDDPFENL 357
Cdd:cd24087 238 VLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFENL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 358 EDTDDLFKTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDKRGYKTAHIAADGSVFNRYPGYKEKAAQALKDI 437
Cdd:cd24087 318 EDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCHVAADGSVYNKYPGFKERAAQALKDI 397
|
410 420 430
....*....|....*....|....*....|....
3O4W_A 438 YNWDVekmEDHPIQLVAAEDGSGVGAAIIACLTQ 471
Cdd:cd24087 398 FGWDG---EDDPIKTVPAEDGSGVGAAIIAALTK 428
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
39-467 |
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: 591.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 39 EKMRSIVKHFISELDKGLSKKGGNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGN-HDFDTTQNKYRLPDH 117
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNgGIFIIVQRKYKIPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 118 LRTGTSEQLWSFIAKCLKEFVDEwYPDGVS--EPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPMLQEQI 195
Cdd:cd24018 82 AKTGTGEELFDFIAECIAEFLEE-HNLDLQsdKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 196 EKLNIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGLLpEDIGPDSPMAINCEYGSFDNE 275
Cdd:cd24018 161 DRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPS-GSVTKSDEMIINTEWGAFDNE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 276 HLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSKIEDDPFE 355
Cdd:cd24018 240 REVLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 356 NLEDTDDLFKTNLNIE-TTVVERKLIRKLAELVGTRAARLTVCGVSAICDKRG---YKTAHIAADGSVFNRYPGYKEKAA 431
Cdd:cd24018 320 DLDAVRDILKELLAIDnTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGsllPEPVTVGIDGSVYEKYPGFKDRLS 399
|
410 420 430
....*....|....*....|....*....|....*.
3O4W_A 432 QALKDIYNWDVekmeDHPIQLVAAEDGSGVGAAIIA 467
Cdd:cd24018 400 EALRELFGPEV----KANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
36-468 |
1.62e-152 |
|
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: 440.83 E-value: 1.62e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSK---KGGNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHDFDTTQNKY 112
Cdd:cd24019 2 LSDEQLEEIMDRLLKEMEKGLSKdthPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQVKMESEIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 113 RLPDHLRTGTSEQLWSFIAKCLKEFVDEWYPDGvsEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPMLQ 192
Cdd:cd24019 82 AIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKD--KKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 193 EQIEKLNIP-INVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGLLPEdigPDSpMAINCEYGS 271
Cdd:cd24019 160 EAIKRRGDIkVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGD---PGQ-VIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 272 F-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSKIE 350
Cdd:cd24019 236 FgDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 351 DDPFENLEDTDDLFKTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDKRGYKTAHIAADGSVFNRYPGYKEKA 430
Cdd:cd24019 316 SDNEGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKEVTVGVDGSLYKYHPKFHKRM 395
|
410 420 430
....*....|....*....|....*....|....*...
3O4W_A 431 AQALKDIYNWDVEkmedhpIQLVAAEDGSGVGAAIIAC 468
Cdd:cd24019 396 HETLKELVPPGCK------FKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
38-467 |
2.94e-147 |
|
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: 428.35 E-value: 2.94e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 38 SEKMRSIVKHFISELDKGLSKKGGNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHDFDTTQNKYRLPDH 117
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQEKSKIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 118 LRTG-TSEQLWSFIAKCLKEFVDEWYPDGVS-----EPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPML 191
Cdd:cd24088 81 LKTGvTAKDLFDYLAKSVEAFLTKHHGDSFAagkddDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 192 QEQIEKLNIPINVVALINDTTGTLVASLYTDPQ---TKMGIIIGTGVNGAYYDVVSGIEKLEGLLPEDIGPdSPMAINCE 268
Cdd:cd24088 161 QDELDRQGIPVKVVALVNDTVGTLLARSYTSPEisgAVLGAIFGTGTNGAYLEDLEKIKKLDDSSRVGKGK-THMVINTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 269 YGSFDNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFI---FKDQDISKLKEAYVMDTSY 345
Cdd:cd24088 240 WGSFDNELKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNTPYGLDTAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 346 PSKIEDDPFENLEDTDDLFKTNLNIET-TVVERKLIRKLAELVGTRAARLTVCGVSAICDKRG------YKTAHIAADGS 418
Cdd:cd24088 320 LSAIEIDSEAELRATRKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGalnksyDGEINIGVDGS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
3O4W_A 419 VFNRYPGYKEKAAQALKDI-YNWDVEKMedhpIQLVAAEDGSGVGAAIIA 467
Cdd:cd24088 400 VIEFYPGFESMLREALRLLlIGAEGEKR----IKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
39-467 |
4.48e-132 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 386.25 E-value: 4.48e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 39 EKMRSIVKHFISELDKGLSKKGGNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHDFDTTQNKYRLPDHL 118
Cdd:cd24000 2 EDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISKKYEIPDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 119 RTGTSEQLWSFIAKCLKEFVDEwypDGVSEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPMLQEQIEKL 198
Cdd:cd24000 82 KTASAEEFFDFIADCIAEFLKE---NGLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALKKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 199 NIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEklegllpediGPDSPMAINCEYGSFDNEhlV 278
Cdd:cd24000 159 GLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL----------LGDGGMIINTEWGNFGKN--S 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 279 LPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDsgfifkdqdisklkeayvmdtsypskieddpfenle 358
Cdd:cd24000 227 LPRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLAD------------------------------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 359 dtddlfktnlniettvverKLIRKLAELVGTRAARLTVCGVSAICDKRGYKTA---HIAADGSVFNRYPGYKEKAAQALK 435
Cdd:cd24000 271 -------------------EILRKICELVAERSARLAAAAIAALLRKTGDSPEkkiTIAVDGSLFEKYPGYRERLEEYLK 331
|
410 420 430
....*....|....*....|....*....|..
3O4W_A 436 DIYNwdvekmEDHPIQLVAAEDGSGVGAAIIA 467
Cdd:cd24000 332 ELLG------RGIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
39-467 |
6.86e-125 |
|
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth.
Pssm-ID: 466870 [Multi-domain] Cd Length: 439 Bit Score: 370.84 E-value: 6.86e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 39 EKMRSIVKHFISELDKGLSKKGGN-IPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHD--FDTTQNKYRLP 115
Cdd:cd24020 4 SRLRQVADAMVVEMEAGLASEGGSkLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGrvDKQEYEEVPIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 116 DHLRTGTSEQLWSFIAKCLKEFVDEWYPDGVS--EPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPMLQE 193
Cdd:cd24020 84 PELMVGTSEELFDFIAGELAKFVATEGEGFHPegEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELLEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 194 QIEKLNIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGLLPedigPDSPMAINCEYGSFD 273
Cdd:cd24020 164 ALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLP----RSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 274 NEHlvLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSKIEDDP 353
Cdd:cd24020 240 SSH--LPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 354 FENLEDTDDLFKTNLNIETTVVE-RKLIRKLAELVGTRAARLTVCGVSAICDKRGYKTAH--------IAADGSVFNRYP 424
Cdd:cd24020 318 SPDLETVARILKDALGIDDTSLEaRKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGsspaqrtvVAVDGGLYEHYP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
3O4W_A 425 GYKEKAAQALKDIYNwdvEKMEDHpIQLVAAEDGSGVGAAIIA 467
Cdd:cd24020 398 KFREYMQQALVELLG---DEAADS-VELELSNDGSGIGAALLA 436
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
30-470 |
4.78e-108 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 328.94 E-value: 4.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 30 LETLFTVSSEKMRSIVKHFISELDKGL----SKKGGNIP------MIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKL 99
Cdd:PTZ00107 14 LVNQFTMSKEKLKELVDYFLYELVEGLeahrRHRNLWIPnecsfkMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 100 GGNHDFDTTQNKYRLPD---------HLRTGTSEQLWSFIAKCLKEFVDEW-YPDGVSEPLPLGFTFSYPASQKKINSGV 169
Cdd:PTZ00107 94 RGGGKMERTQSKFSLPKsallgekglLDKKATATDLFDHIAKSIKKMMEENgDPEDLNKPVPVGFTFSFPCTQLSVNNAI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 170 LQRWTKGFD-----IEGVEGHDVVPMLQEQIEKLNIPINVVALINDTTGTLVASLYTD----PQTKMGIIIGTGVNGAYY 240
Cdd:PTZ00107 174 LIDWTKGFEtgratNDPVEGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYQKpkntPPCQVGVIIGTGSNACYF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 241 DVVSGIEKLEGLLpedigpdspmaINCEYGSFDNEhlvLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDL 320
Cdd:PTZ00107 254 EPEVSAYGYAGTP-----------INMECGNFDSK---LPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 321 ydsgfiFKDQDISKLKEAYVMDTSYPSKIEDDPFENLEDTDDLFKTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVS 400
Cdd:PTZ00107 320 ------LQLKAPPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3O4W_A 401 AICDKRGYKT--AHIAADGSVFNRYPGYKEKAAQALKDIYNWDVEKmedhpIQLVAAEDGSGVGAAIIACLT 470
Cdd:PTZ00107 394 APAKKTRTVQgkATVAIDGSVYVKNPWFRRLLQEYINSILGPDAGN-----VVFYLADDGSGKGAAIIAAMV 460
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
226-469 |
1.52e-106 |
|
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: 316.74 E-value: 1.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 226 KMGIIIGTGVNGAYYDVVSGIEKLEGLLPedigPDSPMAINCEYGSFDNEH-LVLPRTKYDVIIDEESPRPGQQAFEKMT 304
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLP----KSGEMIINTEWGAFGDNGlLPLPRTEYDKELDAESPNPGFQPFEKMI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 305 SGYYLGEIMRLVLLDLYDSGFIFKDQdISKLKEAYVMDTSYPSKIEDDPFENLEDTDDLFKTNLNIET-TVVERKLIRKL 383
Cdd:pfam03727 77 SGMYLGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETvTEEDRKIVRRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 384 AELVGTRAARLTVCGVSAICDKRG-YKTAHIAADGSVFNRYPGYKEKAAQALKDIYNwdvekmEDHPIQLVAAEDGSGVG 462
Cdd:pfam03727 156 CEAVSTRAARLVAAGIAAILKKIGrDKKVTVGVDGSVYEKYPGFRERLQEALRELLG------PGDKVVLVLAEDGSGVG 229
|
....*..
3O4W_A 463 AAIIACL 469
Cdd:pfam03727 230 AALIAAV 236
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
26-220 |
1.31e-104 |
|
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: 310.20 E-value: 1.31e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 26 QIHGLETLFTVSSEKMRSIVKHFISELDKGLSKKG-GNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHD 104
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGsSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 105 FDTTQNKYRLPDHLRTGTSEQLWSFIAKCLKEFVDEWYPDGVSE-PLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVE 183
Cdd:pfam00349 81 FEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEEkELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGVV 160
|
170 180 190
....*....|....*....|....*....|....*..
3O4W_A 184 GHDVVPMLQEQIEKLNIPINVVALINDTTGTLVASLY 220
Cdd:pfam00349 161 GKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
16-471 |
6.06e-104 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 317.28 E-value: 6.06e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 16 MADVPANLMEQIHGletlFTVSSEKMRSIVKHFISELDKGLSKKGGNIPMIPGWVvEYPTG-KETGDFLALDLGGTNLRV 94
Cdd:COG5026 1 MKKLLVDAFLKRHG----FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 95 VLVKLGGNHDFDTTQ-NKYRLPDHLRTGTSEQLWSFIAKCLKEFVDEWYPdgvseplpLGFTFSYPASQKKINSGVLQRW 173
Cdd:COG5026 76 ALVRFDGEGTFEIENfKSFPLPGTSSEITAEEFFDFIADYIEPLLDESYK--------LGFCFSFPAEQLPDKDGRLIQW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 174 TKGFDIEGVEGHDVVPMLQEQIEKLNIpINV--VALINDTTGTLVASLYTDPQTK----MGIIIGTGVNGAYYDVVSGIE 247
Cdd:COG5026 148 TKEIKTPGVEGKNIGELLEAALARKGL-DNVkpVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 248 KLEGllpedigPDSPMAINCEYGSFDnehlVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGfIF 327
Cdd:COG5026 227 KLPA-------YEGPMIINMESGNFN----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 328 KDQDISKLKEAYVMDTSYPSKIEDDPFENLEDTDDLFKTNlNIEttvvERKLIRKLAELVGTRAARLTVCGVSAIC---- 403
Cdd:COG5026 295 SPGFSEVFETPYSLTTVDMSRFLADPSDEKEILSQCLEAG-SEE----DREILREIADAIVERAARLVAATLAGILlhlg 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3O4W_A 404 -DKRGYKTAHIAADGSVFNRYPGYKEKAAQALKDIynwdVEKMEDHPIQLVAAEDGSGVGAAIIACLTQ 471
Cdd:COG5026 370 pGKTPLKPHCIAIDGSTYEKMPGLAEKIEYALQEY----LLGEKGRYVEFVLVENASLLGAAIAAALNE 434
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
36-472 |
3.66e-99 |
|
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: 304.85 E-value: 3.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSKKGGN---IPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKL--GGNHDFDTTQN 110
Cdd:cd24091 2 LSHDQLLEVKARMRAEMERGLRKETHAsapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVrsGKWRGVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 111 KYRLPDHLRTGTSEQLWSFIAKCLKEFVDEWYPDGVSepLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPM 190
Cdd:cd24091 82 IYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVS--LPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 191 LQEQIEKLN-IPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGllpeDIGPdspMAINCEY 269
Cdd:cd24091 160 LREAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG----EEGR---MCINMEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 270 GSF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSK 348
Cdd:cd24091 233 GAFgDNGCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 349 IEDDPFENLEDTDDLfkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDK----RGYKTAHIA--ADGSVFNR 422
Cdd:cd24091 313 IESDRLALLQVRAIL--QQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKirenRGLDHLNVTvgVDGTLYKL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
3O4W_A 423 YPGYKEKAAQALKDIYNWDVekmedhpIQLVAAEDGSGVGAAIIACLTQK 472
Cdd:cd24091 391 HPHFSRVMHETVKELAPKCD-------VTFLQSEDGSGKGAALITAVACR 433
|
|
| PLN02405 |
PLN02405 |
hexokinase |
21-467 |
7.63e-93 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 290.58 E-value: 7.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 21 ANLMEQIHGLETLFTVSSEKMRSIVKHFISELDKGLSKKGGN-IPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKL 99
Cdd:PLN02405 35 ARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 100 GGNHDFDTTQN--KYRLPDHLRTGTSEQLWSFIAKCLKEFVDEWYPDgvSEPLP-----LGFTFSYPASQKKINSGVLQR 172
Cdd:PLN02405 115 GGKDGRVVKQEfeEVSIPPHLMTGSSDALFDFIAAALAKFVATEGED--FHLPPgrqreLGFTFSFPVKQTSISSGTLIK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 173 WTKGFDIEGVEGHDVVPMLQEQIEKLNIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGL 252
Cdd:PLN02405 193 WTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 253 LPEdigpDSPMAINCEYGSFDNEHlvLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDI 332
Cdd:PLN02405 273 LPK----SGEMVINMEWGNFRSSH--LPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 333 SKLKEAYVMDTSYPSKIEDDPFENLEDTDDLFKTNLNIETTVVE-RKLIRKLAELVGTRAARLTVCGVSAICDKRGYKTA 411
Cdd:PLN02405 347 PKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSLKmRKVVVELCNIVATRGARLSAAGIYGILKKLGRDTV 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
3O4W_A 412 H--------IAADGSVFNRYPGYKEKAAQALKDIYNWDVEKmedhPIQLVAAEDGSGVGAAIIA 467
Cdd:PLN02405 427 KdgekqksvIAMDGGLFEHYTEFSKCMESTLKELLGEEVSE----SIEVEHSNDGSGIGAALLA 486
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
36-468 |
1.14e-92 |
|
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: 288.34 E-value: 1.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSKKGGN---IPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKL-GGNHDFDTTQNK 111
Cdd:cd24128 2 LSHDQLLEVKRRMKVEMERGLSKETHAsapVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVrNGKWRGVEMHNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 112 -YRLPDHLRTGTSEQLWSFIAKCLKEFVDEWYPDGVSepLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPM 190
Cdd:cd24128 82 iYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVS--LPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 191 LQEQIEKL-NIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGllpedigPDSPMAINCEY 269
Cdd:cd24128 160 LKEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG-------EEGRMCVNMEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 270 GSF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSK 348
Cdd:cd24128 233 GAFgDNGCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 349 IEDDPFENLEDTDDLfkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDK----RGYKTAHI--AADGSVFNR 422
Cdd:cd24128 313 IESDRLALLQVRAIL--QHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKirenRGLDALKVtvGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
3O4W_A 423 YPGYKEKAAQALKDIynwdVEKMEdhpIQLVAAEDGSGVGAAII---AC 468
Cdd:cd24128 391 HPHFAKVMHETVKDL----APKCD---VSFLQSEDGSGKGAALItavAC 432
|
|
| PLN02362 |
PLN02362 |
hexokinase |
40-467 |
5.24e-92 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 289.09 E-value: 5.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 40 KMRSIVKHFISELDKGLSKKGGN-IPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHDFDTTQNKYR--LPD 116
Cdd:PLN02362 54 RLRQVVDAMAVEMHAGLASEGGSkLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERhpIPQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 117 HLRTGTSEQLWSFIAKCLKEFVDEWYPDgvSEPLP-----LGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPML 191
Cdd:PLN02362 134 HLMNSTSEVLFDFIASSLKQFVEKEENG--SEFSQvrrreLGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 192 QEQIEKLNIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGLLPEDIGpdspMAINCEYGS 271
Cdd:PLN02362 212 QGALNRRGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGS----MVVNMEWGN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 272 FDNEHlvLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDiSKLKEAYVMDTSYPSKIED 351
Cdd:PLN02362 288 FWSSH--LPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGPVS-SRLSTPFVLRTPSVAAMHE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 352 DPFENLEDTDDLFKTNLNI-ETTVVERKLIRKLAELVGTRAARLTVCGVSAICDKRG------------------YKTAH 412
Cdd:PLN02362 365 DDSPELQEVARILKETLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGrdgsggitsgrsrsdiqiMRRTV 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
3O4W_A 413 IAADGSVFNRYPGYKEKAAQALKDIYNWDVEKmedHPIqLVAAEDGSGVGAAIIA 467
Cdd:PLN02362 445 VAVEGGLYTNYTMFREYLHEALNEILGEDVAQ---HVI-LKATEDGSGIGSALLA 495
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
36-466 |
3.49e-90 |
|
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: 281.66 E-value: 3.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSKKGGN---IPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLG--GNHDFDTTQN 110
Cdd:cd24089 2 LSDETLLDISRRFRKEMEKGLGKDTHPtatVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNdeKNQKVEMESQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 111 KYRLPDHLRTGTSEQLWSFIAKCLKEFVDEwyPDGVSEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPM 190
Cdd:cd24089 82 VYAIPEEIMHGSGTQLFDHVAECLADFMDK--QKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 191 LQEQIEKL-NIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEgllpediGPDSPMAINCEY 269
Cdd:cd24089 160 LRKAIRRRgDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVE-------GDEGRMCINTEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 270 GSF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSK 348
Cdd:cd24089 233 GAFgDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 349 IEDDPfENLEDTDDLFkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDK-RGYKTAH-----IAADGSVFNR 422
Cdd:cd24089 313 IEKEK-EGLANAKEIL-TRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRlRENKGLErlrttVGVDGSVYKK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
3O4W_A 423 YPGYKEKAAQALKDIynwdvekMEDHPIQLVAAEDGSGVGAAII 466
Cdd:cd24089 391 HPQFSKRLHKAVRRL-------VPDCDVRFLLSEDGSGKGAAMV 427
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
34-472 |
5.52e-90 |
|
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: 281.77 E-value: 5.52e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 34 FTVSSEKMRSIVKHFISELDKGL---SKKGGNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLG----GNHDFD 106
Cdd:cd24092 9 FQLQEEDLKKVMRRMQKEMDRGLrleTHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGegeeGQWSVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 107 TTQNKYRLPDHLRTGTSEQLWSFIAKCLKEFVDEwyPDGVSEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHD 186
Cdd:cd24092 89 TKHQMYSIPEDAMTGTAEMLFDYISECISDFLDK--HQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 187 VVPMLQEQIEKL-NIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGllpedigPDSPMAI 265
Cdd:cd24092 167 VVGLLRDAIKRRgDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG-------DEGRMCV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 266 NCEYGSF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTS 344
Cdd:cd24092 240 NTEWGAFgDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 345 YPSKIEDDPFENLEDTDDLfkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAI----CDKRGYKTAHIAA--DGS 418
Cdd:cd24092 320 FVSQVESDTGDRKQIYNIL--STLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVinrmRESRSEDVMRITVgvDGS 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
3O4W_A 419 VFNRYPGYKEKaaqalkdiYNWDVEKMEDH-PIQLVAAEDGSGVGAAIIACLTQK 472
Cdd:cd24092 398 VYKLHPSFKER--------FHASVRRLTPScEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
36-472 |
5.78e-89 |
|
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: 278.74 E-value: 5.78e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSKKG---GNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHDFDTTQNK- 111
Cdd:cd24130 2 LTRDQLQEVKQKMRTELEYGLKKEThptASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRSVRMYNKi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 112 YRLPDHLRTGTSEQLWSFIAKCLKEFVDEWYPDGVSepLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPML 191
Cdd:cd24130 82 FAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGAR--LPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 192 QEQIEKLN-IPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGllpedigPDSPMAINCEYG 270
Cdd:cd24130 160 REAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG-------DEGRMCINTEWG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 271 SF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSKI 349
Cdd:cd24130 233 GFgDNGCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 350 EDDPFENLEDTDDLfkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDK----RGYKTAHI--AADGSVFNRY 423
Cdd:cd24130 313 ESDRLALLQVRRIL--QQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKirenQGLDRLDItvGVDGTLYKLH 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
3O4W_A 424 PGYKEKAAQALKDIY-NWDVEKMedhpiqlvAAEDGSGVGAAIIACLTQK 472
Cdd:cd24130 391 PHFSRILQETVKELApQCDVTFM--------LSEDGSGKGAALITAVAKR 432
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
35-466 |
9.98e-89 |
|
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: 277.95 E-value: 9.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 35 TVSSEKMRSIVKHFISELDKGLSKKGGN---IPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKL-GGNHDFDTTQN 110
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIrSGKKRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 111 K-YRLPDHLRTGTSEQLWSFIAKCLKEFVDEWypdGVSEP-LPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVV 188
Cdd:cd24127 81 KiYAIPIEIMQGTGEELFDHIVSCISDFLDYM---GIKGPrMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 189 PMLQEQIEKLN-IPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGllpedigPDSPMAINC 267
Cdd:cd24127 158 TLLRDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG-------DQGQMCINM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 268 EYGSF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYP 346
Cdd:cd24127 231 EWGAFgDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 347 SKIEDDPFENLEDTDDLFKTNLNieTTVVERKLIRKLAELVGTRAARLTVCGVSAICDK----RGYKTAHI--AADGSVF 420
Cdd:cd24127 311 SQIESDRLALLQVRAILQQLGLN--STCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKirenRGLDHLNVtvGVDGTLY 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
3O4W_A 421 NRYPGYKEKAAQALKDIynwdvekMEDHPIQLVAAEDGSGVGAAII 466
Cdd:cd24127 389 KLHPHFSRIMHQTVKEL-------SPKCNVSFLLSEDGSGKGAALI 427
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
36-467 |
1.03e-87 |
|
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: 275.22 E-value: 1.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSKK---GGNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGgNHDFDTTQNKY 112
Cdd:cd24129 2 LSHDQLAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVG-TAGVQITSEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 113 RLPDHLRTGTSEQLWSFIAKCLKEFVDEwyPDGVSEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPMLQ 192
Cdd:cd24129 81 SIPETVAQGTGQQLFDHIVDCIVDFQQK--QGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 193 EQIE-KLNIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGllpeDIGPdspMAINCEYGS 271
Cdd:cd24129 159 EAATrKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPG----DSGR---MCINMEWGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 272 F-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSKIE 350
Cdd:cd24129 232 FgDNGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 351 DDPFENLEDTDDLfkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDK----RGYK--TAHIAADGSVFNRYP 424
Cdd:cd24129 312 SDSLALRQVRAIL--EDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKmrenRGLDelAVTVGVDGTLYKLHP 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
3O4W_A 425 GYKEKAAQALKDIY-NWDVEKMEdhpiqlvaAEDGSGVGAAIIA 467
Cdd:cd24129 390 RFSSLVQATVRELApRCVVTFLQ--------SEDGSGKGAALVT 425
|
|
| PLN02914 |
PLN02914 |
hexokinase |
41-472 |
2.66e-85 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 270.99 E-value: 2.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 41 MRSIVKHFISELDKGLSKKGG-NIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHD--FDTTQNKYRLPDH 117
Cdd:PLN02914 55 LRHVADAMAADMRAGLAVDGGgDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDErvIATEFEQVSIPQE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 118 LRTGTSEQLWSFIAKCLKEFVDEwypDGVSEPLP------LGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPML 191
Cdd:PLN02914 135 LMFGTSEELFDFIASGLANFVAK---EGGKFHLPegrkreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 192 QEQIEKLNIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGLLPEdigpDSPMAINCEYGS 271
Cdd:PLN02914 212 NEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSS----SGRTIINTEWGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 272 FDNehlVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSKIED 351
Cdd:PLN02914 288 FSD---GLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 352 DPFENLEDTDDLFKTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDK-----RGY---KTAHIAADGSVFNRY 423
Cdd:PLN02914 365 DNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKmeedsKGMifgKRTVVAMDGGLYEKY 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
3O4W_A 424 PGYKEKAAQALKDIYNwdvEKMEDHpIQLVAAEDGSGVGAAIIACLTQK 472
Cdd:PLN02914 445 PQYRRYMQDAVTELLG---LELSKN-IAIEHTKDGSGIGAALLAATNSK 489
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
36-466 |
5.33e-83 |
|
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: 262.91 E-value: 5.33e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSKKG---GNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGN--HDFDTTQN 110
Cdd:cd24125 2 LSDETLLEISKRFRKEMEKGLGATThptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNglQKVEMENQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 111 KYRLPDHLRTGTSEQLWSFIAKCLKEFVDEWypdGVSEP-LPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVP 189
Cdd:cd24125 82 IYAIPEDIMRGSGTQLFDHIAECLANFMDKL---QIKDKkLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 190 MLQEQIEKL-NIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEgllpediGPDSPMAINCE 268
Cdd:cd24125 159 LLRKAIQKRgDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVE-------GDEGRMCINME 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 269 YGSF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPS 347
Cdd:cd24125 232 WGAFgDDGSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 348 KIEDDPfENLEDTDDLFkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSA----ICDKRGYK--TAHIAADGSVFN 421
Cdd:cd24125 312 DIEGEK-DGIRKAREVL-MRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAvlqrIKENKGEErlRSTIGVDGSVYK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
3O4W_A 422 RYPGYKEKAAQALKDIynwdvekMEDHPIQLVAAEDGSGVGAAII 466
Cdd:cd24125 390 KHPHFARRLHKTVRRL-------VPGCDVRFLRSEDGSGKGAAMV 427
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
36-466 |
1.35e-80 |
|
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: 256.70 E-value: 1.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSKKG---GNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLG--GNHDFDTTQN 110
Cdd:cd24126 2 LSDDTLLDIMTRFRAEMEKGLAKDTnptAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSedGKQKVQMESQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 111 KYRLPDHLRTGTSEQLWSFIAKCLKEFVDEwyPDGVSEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVVPM 190
Cdd:cd24126 82 FYPTPEEIIHGTGTELFDYVAECLADFMKK--KGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 191 LQEQIEKL-NIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGllpeDIGpdsPMAINCEY 269
Cdd:cd24126 160 LRKAIRKHkDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG----DEG---RMCINTEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 270 GSF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSK 348
Cdd:cd24126 233 GAFgDDGSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 349 IEdDPFENLEDTDDLFkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAICDK-------RGYKTAhIAADGSVFN 421
Cdd:cd24126 313 IE-KYKEGLYNTREIL-SDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRlrenkklERLRTT-VGMDGTVYK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
3O4W_A 422 RYPGYKEKAAQALKDIynwdvekMEDHPIQLVAAEDGSGVGAAII 466
Cdd:cd24126 390 THPQYAKRLHKVVRRL-------VPSCDVRFLLSESGSGKGAAMV 427
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
36-475 |
8.05e-77 |
|
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: 248.38 E-value: 8.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 36 VSSEKMRSIVKHFISELDKGLSKK---GGNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLggNHDFDTT---- 108
Cdd:cd24124 30 LSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV--NHEKNQNvhme 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 109 QNKYRLPDHLRTGTSEQLWSFIAKCLKEFVDEWYPDgvSEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDVV 188
Cdd:cd24124 108 SEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIK--DKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 189 PMLQEQIEKL-NIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEgllpediGPDSPMAINC 267
Cdd:cd24124 186 KLLNKAIKKRgDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVE-------GDEGRMCINT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 268 EYGSF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYP 346
Cdd:cd24124 259 EWGAFgDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 347 SKIEDDPfENLEDTDDLFkTNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAIC----DKRGYKTAH--IAADGSVF 420
Cdd:cd24124 339 SAIEKNK-EGLHNAKEIL-TRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILnrlrDNKGTPRLRttVGVDGSLY 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
3O4W_A 421 NRYPGYKEKAAQALKDIynwdvekMEDHPIQLVAAEDGSGVGAAIIACLTQkRLA 475
Cdd:cd24124 417 KTHPQYSRRFHKTLRRL-------VPDSDVRFLLSESGSGKGAAMVTAVAY-RLA 463
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
35-466 |
2.76e-67 |
|
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: 222.11 E-value: 2.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 35 TVSSEKMRSIVKHFISELDKGLSKKGGNIP---MIPGWVVEYPTGKETGDFLALDLG--GTNLRVVLVKLGG--NHDFDT 107
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQASPAPavrMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGieGHRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 108 TQNKYRLPDHLRTGTSEQLWSFIAKCLKEFVDEWypDGVSEPLPLGFTFSYPASQKKINSGVLQRWTKGFDIEGVEGHDV 187
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQ--PVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 188 VPMLQEQIEKLNI-PINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEgllpEDIGpdsPMAIN 266
Cdd:cd24090 159 VQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD----EDRG---RVCVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 267 CEYGSFDNEHLVLP-RTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSY 345
Cdd:cd24090 232 VEWGSFSDDGALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 346 PSKIEdDPFENLEDTDDLFKtNLNIETTVVERKLIRKLAELVGTRAARLTVCGVSAIC----DKRGYKTAHI--AADGSV 419
Cdd:cd24090 312 VAEME-DPSAGAARVRAILQ-DLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLshlqHSREQQTLQVavATGGRV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
3O4W_A 420 FNRYPGYKEkaaqALKDIYNWDVEKMEdhpIQLVAAEDGSGVGAAII 466
Cdd:cd24090 390 CERHPRFCS----ILQGTVMLLAPECD---VSFIPSVDGGGRGVAMV 429
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
40-472 |
1.90e-49 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 176.22 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 40 KMRSIVKHFISELDKGLSKKG-GNIPMIPGWVVEYPTGKETGDFLALDLGGTNLRVVLVKLGGNHD--FDTTQNKYRLPD 116
Cdd:PLN02596 55 KLWEVADALVSDMTASLTAEEtTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEpiSDLYREEISIPS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 117 HLRTGTSEQLWSFIAKCLKEFVDEWYPD---GVSEPLPLGFTFSYPASQKKINSGVLQRWtKGFDIEGVEGHDVVPMLQE 193
Cdd:PLN02596 135 NVLNGTSQELFDYIALELAKFVAEHPGDeadTPERVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 194 QIEKLNIPINVVALINDTTGTLVASLYTDPQTKMGIIIGTGVNGAYYDVVSGIEKLEGLLPEDigpdSPMAINCEYGSFD 273
Cdd:PLN02596 214 ALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPES----QEIVISTEWGNFN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 274 NEHLvlPRTKYDVIIDEESPRPGQQAFEKMTSGYYLGEIMRLVLLDLYDSGFIFKDQDISKLKEAYVMDTSYPSKIEDDP 353
Cdd:PLN02596 290 SCHL--PITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 354 FENLEDTDDLFKTNLNI-ETTVVERKLIRKLAELVGTRAARLTVCGVSAICDKRGY---KTAHIAADGSVFNRYPGYKEK 429
Cdd:PLN02596 368 SEDHEVVNEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRienKKSVVTVEGGLYEHYRVFRNY 447
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
3O4W_A 430 AAQALkdiynWDV--EKMEDHPIqLVAAEDGSGVGAAII-ACLTQK 472
Cdd:PLN02596 448 LHSSV-----WEMlgSELSDNVV-IEHSHGGSGAGALFLaACQTGE 487
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
82-238 |
9.31e-05 |
|
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: 44.50 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 82 FLALDLGGTNLRVVLVKLGGNhdfdtTQNKYRLPDHLRTGTsEQLWSFIAKCLKEFVDEWYPDGvSEPLPLGFTFSYPAS 161
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGE-----VLARERIPTPAGAGP-EAVLEAIAELIEELLAEAGISR-GRILGIGIGVPGPVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 162 QKK---INSGVLQRWtkgfdiegvEGHDVVPMLQeqiEKLNIPinvVALINDTTGTLVASLY----TDPQTKMGIIIGTG 234
Cdd:COG1940 80 PETgvvLNAPNLPGW---------RGVPLAELLE---ERLGLP---VFVENDANAAALAEAWfgagRGADNVVYLTLGTG 144
|
....
3O4W_A 235 VNGA 238
Cdd:COG1940 145 IGGG 148
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
82-240 |
1.27e-04 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 43.82 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 82 FLALDLGGTNLRVVLVKLGGN-HDFDttqnKYRLPDHLRTGTSEQLWSFIAKCLKEFVDEwyPDGVSeplpLGFtfsyPA 160
Cdd:PRK09698 6 VLGIDMGGTHIRFCLVDAEGEiLHCE----KKRTAEVIAPDLVSGLGEMIDEYLRRFNAR--CHGIV----MGF----PA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 161 SQKKINSGVLQrwTKGFDIEGVEGHDVVPMLQeqiEKLNIPinvVALINDTTGTL---VASLYTDPQTKMGIIIGTG--- 234
Cdd:PRK09698 72 LVSKDRRTVIS--TPNLPLTALDLYDLADKLE---NTLNCP---VFFSRDVNLQLlwdVKENNLTQQLVLGAYLGTGmgf 143
|
....*....
3O4W_A 235 ---VNGAYY 240
Cdd:PRK09698 144 avwMNGAPW 152
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
83-238 |
1.89e-03 |
|
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This subfamily is composed of uncharacterized proteins belonging to the the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466988 [Multi-domain] Cd Length: 286 Bit Score: 40.24 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 83 LALDLGGTNLRVVLVklggNHDFDTTqNKYRLPDHLrtGTSEQLWSFIAKCLKEFVDEwyPDGVSeplplgftFSYP--- 159
Cdd:cd24152 3 LVFDIGGTFIKYALV----DENGNII-KKGKIPTPK--DSLEEFLDYIKKIIKRYDEE--IDGIA--------ISAPgvi 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 160 -ASQKKINSGVLQRWTKGFDiegveghdvvpMLQEQIEKLNIPinvVALINDTTGTLVASLY----TDPQTKMGIIIGTG 234
Cdd:cd24152 66 dPETGIIYGGGALPYLKGFN-----------LKEELEERCNLP---VSIENDAKCAALAELWlgslKGIKNGAVIVLGTG 131
|
....
3O4W_A 235 VNGA 238
Cdd:cd24152 132 IGGA 135
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
82-240 |
2.66e-03 |
|
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1.55), also called allokinase, catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. It has also low level glucokinase activity in vitro. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466920 [Multi-domain] Cd Length: 293 Bit Score: 39.84 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 82 FLALDLGGTNLRVVLVKLGGN-HDFD--TTQNKYRLPDHLrtgtseqlwSFIAKCLKEFVDEWY--PDGVSeplpLGFtf 156
Cdd:cd24070 3 VLGIDIGGTNIRIGLVDEDGKlLDFEkvPSKDLLRAGDPV---------EVLADLIREYIEEAGlkPAAIV----IGV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3O4W_A 157 syPASQKKINSGVLQrwtkGFDIEGVEGHDVVPMLQeqiEKLNIPinvVALINDTT----GTLVASLYTDPQTKMGIIIG 232
Cdd:cd24070 68 --PGTVDKDRRTVIS----TPNIPGLDGVNLADILE---NKLGIP---VILERDVNllllYDMRAGNLDDEGVVLGFYIG 135
|
....*...
3O4W_A 233 TGVNGAYY 240
Cdd:cd24070 136 TGIGNAIL 143
|
|
| |
