|
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: 797.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 38 SETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLPHD 117
Cdd:cd24087 1 TERLRKITDHFISELEKGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYRLPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 118 MRTtKHQEELWSFIADSLKDFMVEQELLNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQNEIS 197
Cdd:cd24087 81 LKT-GTGEELWDFIADCLKKFVEEHFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 198 KRELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEgklADDIPSNSPMAINCEYGSFDNEH 277
Cdd:cd24087 160 KRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLE---HDDIPPDSPMAINCEYGAFDNEH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 278 LVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIEDDPFEN 357
Cdd:cd24087 237 LVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 358 LEDTDDIFQKDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTGHIAADGSVYNKYPGFKEAAAKGLRD 437
Cdd:cd24087 317 LEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCHVAADGSVYNKYPGFKERAAQALKD 396
|
410 420 430
....*....|....*....|....*....|....
gi 768525192 438 IYGWTGDasNDPITIVPAEDGSGAGAAVIAALSE 471
Cdd:cd24087 397 IFGWDGE--DDPIKTVPAEDGSGVGAAIIAALTK 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: 601.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGN-HTFDTTQSKYKLPHD 117
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNgGIFIIVQRKYKIPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 118 MRTtKHQEELWSFIADSLKDFMVEQEL-LNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQNEI 196
Cdd:cd24018 82 AKT-GTGEELFDFIAECIAEFLEEHNLdLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 197 SKRELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEgKLADDIPSNSPMAINCEYGSFDNE 276
Cdd:cd24018 161 DRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLT-SPSGSVTKSDEMIINTEWGAFDNE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 277 HLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIEDDPFE 356
Cdd:cd24018 240 REVLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 357 NLEDTDDIFQKDFGVK-TTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRG---YKTGHIAADGSVYNKYPGFKEAAA 432
Cdd:cd24018 320 DLDAVRDILKELLAIDnTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGsllPEPVTVGIDGSVYEKYPGFKDRLS 399
|
410 420 430
....*....|....*....|....*....|....*
gi 768525192 433 KGLRDIYGWTgdaSNDPITIVPAEDGSGAGAAVIA 467
Cdd:cd24018 400 EALRELFGPE---VKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
38-467 |
4.35e-139 |
|
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: 407.55 E-value: 4.35e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 38 SETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLPHD 117
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQEKSKIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 118 MRTTKHQEELWSFIADSLKDFMVE---QELLNTKDT--LPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLL 192
Cdd:cd24088 81 LKTGVTAKDLFDYLAKSVEAFLTKhhgDSFAAGKDDdrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 193 QNEISKRELPIEIVALINDTVGTLVASYYTDPE---TKMGVIFGTGVNGAFYDVVSDIEKLEGKLADDiPSNSPMAINCE 269
Cdd:cd24088 161 QDELDRQGIPVKVVALVNDTVGTLLARSYTSPEisgAVLGAIFGTGTNGAYLEDLEKIKKLDDSSRVG-KGKTHMVINTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 270 YGSFDNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLML---KDQDLSKLKQPYIMDTSY 346
Cdd:cd24088 240 WGSFDNELKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLiqyNDKSPSALNTPYGLDTAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 347 PARIEDDPFENLEDTDDIFQKDFGVKT-TLPERKLIRRLCELIGTRAARLAVCGIAAICQKRG-----YKTG-HIAADGS 419
Cdd:cd24088 320 LSAIEIDSEAELRATRKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGalnksYDGEiNIGVDGS 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 768525192 420 VYNKYPGFKEAAAKGLRDI-YGWTGDASndpITIVPAEDGSGAGAAVIA 467
Cdd:cd24088 400 VIEFYPGFESMLREALRLLlIGAEGEKR---IKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
39-468 |
9.77e-136 |
|
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: 398.07 E-value: 9.77e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGL---TKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLP 115
Cdd:cd24019 5 EQLEEIMDRLLKEMEKGLskdTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQVKMESEIYAIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 116 HD-MRTTkhQEELWSFIADSLKDFMVEQELlnTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQN 194
Cdd:cd24019 85 EEiMTGT--GEQLFDYIAECLAEFLEKNGL--KDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 195 EISKRELP-IEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLADdiPSNspMAINCEYGSF 273
Cdd:cd24019 161 AIKRRGDIkVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGD--PGQ--VIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 274 -DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIED 352
Cdd:cd24019 237 gDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIES 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 353 DPFENLEDTDDIFQKDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTGHIAADGSVYNKYPGFKEAAA 432
Cdd:cd24019 317 DNEGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKEVTVGVDGSLYKYHPKFHKRMH 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 768525192 433 KGLRDIYGWTGDasndpITIVPAEDGSGAGAAVIAA 468
Cdd:cd24019 397 ETLKELVPPGCK-----FKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
39-467 |
5.83e-126 |
|
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: 370.84 E-value: 5.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLPHDM 118
Cdd:cd24000 2 EDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISKKYEIPDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 119 RTTKhQEELWSFIADSLKDFMVEqelLNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQNEISK 198
Cdd:cd24000 82 KTAS-AEEFFDFIADCIAEFLKE---NGLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 199 RELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKladdipsnspMAINCEYGSFDNEhl 278
Cdd:cd24000 158 RGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNILLGDGG----------MIINTEWGNFGKN-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 279 VLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYlgellrlvllelneKGLMLKdqdlsklkqpYIMdtsyparieddpfenL 358
Cdd:cd24000 226 SLPRTEYDREVDKASENPGFQPLEKMVSGKY--------------LGELVR----------LIL---------------K 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 359 EDTDDIfqkdfgvkttlperklIRRLCELIGTRAARLAVCGIAAICQKRGYKTG---HIAADGSVYNKYPGFKEAAAKGL 435
Cdd:cd24000 267 DLADEI----------------LRKICELVAERSARLAAAAIAALLRKTGDSPEkkiTIAVDGSLFEKYPGYRERLEEYL 330
|
410 420 430
....*....|....*....|....*....|..
gi 768525192 436 RDIYGwtgdaSNDPITIVPAEDGSGAGAAVIA 467
Cdd:cd24000 331 KELLG-----RGIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
39-468 |
1.31e-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: 347.34 E-value: 1.31e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGLTKKGGN-IPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLP-- 115
Cdd:cd24020 4 SRLRQVADAMVVEMEAGLASEGGSkLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVPip 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 116 -HDMRTTKhqEELWSFIADSLKDFmVEQELLNTKDTL---PLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPL 191
Cdd:cd24020 84 pELMVGTS--EELFDFIAGELAKF-VATEGEGFHPEGekrELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 192 LQNEISKRELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLaddiPSNSPMAINCEYG 271
Cdd:cd24020 161 LEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGL----PRSGEMVINTEWG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 272 SFDNEHlvLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIE 351
Cdd:cd24020 237 NFRSSH--LPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 352 DDPFENLEDTDDIFQKDFGV-KTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTGH--------IAADGSVYN 422
Cdd:cd24020 315 EDDSPDLETVARILKDALGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGsspaqrtvVAVDGGLYE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 768525192 423 KYPGFKEAAAKGLRDIygwTGDASNDPITIVPAEDGSGAGAAVIAA 468
Cdd:cd24020 395 HYPKFREYMQQALVEL---LGDEAADSVELELSNDGSGIGAALLAA 437
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
22-469 |
1.09e-104 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 320.08 E-value: 1.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 22 ELMDEIHQLEDMFTVDSETLRKVVKHFIDELNKGL----TKKGGNIP------MIPGWVMEFPTGKESGNYLAIDLGGTN 91
Cdd:PTZ00107 6 KQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeahrRHRNLWIPnecsfkMLDSCVYNLPTGKEKGVYYAIDFGGTN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 92 LRVVLVKLSGNHTFDTTQSKYKLPH--------DMRTTKHQEELWSFIADSLKDFMVE-QELLNTKDTLPLGFTFSYPAS 162
Cdd:PTZ00107 86 FRAVRVSLRGGGKMERTQSKFSLPKsallgekgLLDKKATATDLFDHIAKSIKKMMEEnGDPEDLNKPVPVGFTFSFPCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 163 QNKINEGILQRWTKGFDIP-----NVEGHDVVPLLQNEISKRELPIEIVALINDTVGTLVASYYTD----PETKMGVIFG 233
Cdd:PTZ00107 166 QLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYQKpkntPPCQVGVIIG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 234 TGVNGAFYDVVSDIEKLEGKLaddipsnspmaINCEYGSFDNEhlvLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGEL 313
Cdd:PTZ00107 246 TGSNACYFEPEVSAYGYAGTP-----------INMECGNFDSK---LPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 314 LRLVLLelnekgLMLKDQDLSKLKQPYIMDTSYPARIEDDPFENLEDTDDIFQKDFGVKTTLPERKLIRRLCELIGTRAA 393
Cdd:PTZ00107 312 SRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAA 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768525192 394 RLAVCGIAAICQKRGYKTGH--IAADGSVYNKYPGFKEAAAKGLRDIygwTGDASNDpITIVPAEDGSGAGAAVIAAL 469
Cdd:PTZ00107 386 QLAAAFIAAPAKKTRTVQGKatVAIDGSVYVKNPWFRRLLQEYINSI---LGPDAGN-VVFYLADDGSGKGAAIIAAM 459
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
26-221 |
2.43e-101 |
|
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: 301.73 E-value: 2.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 26 EIHQLEDMFTVDSETLRKVVKHFIDELNKGLTKKG-GNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHT 104
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGsSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 105 FDTTQSKYKLPHDMRTTKHqEELWSFIADSLKDFMVEQEL-LNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNV 183
Cdd:pfam00349 81 FEITQEKYKIPEELMTGTG-EELFDFIADCIAEFLKEHGLeDFEEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 768525192 184 EGHDVVPLLQNEISKRELPIEIVALINDTVGTLVASYY 221
Cdd:pfam00349 160 VGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
227-469 |
2.40e-97 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.
Pssm-ID: 461028 Cd Length: 236 Bit Score: 293.24 E-value: 2.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 227 KMGVIFGTGVNGAFYDVVSDIEKLEGKLADDipsnSPMAINCEYGSFDNEH-LVLPRTKYDVAVDEQSPRPGQQAFEKMT 305
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKS----GEMIINTEWGAFGDNGlLPLPRTEYDKELDAESPNPGFQPFEKMI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 306 SGYYLgellrlvllelnekG----LMLKD---------QDLSKLKQPYIMDTSYPARIEDDPFENLEDTDDIFQKDFGVK 372
Cdd:pfam03727 77 SGMYL--------------GelvrLVLLDlaeegllfkGQSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 373 T-TLPERKLIRRLCELIGTRAARLAVCGIAAICQKRG-YKTGHIAADGSVYNKYPGFKEAAAKGLRDIYGwtgdaSNDPI 450
Cdd:pfam03727 143 TvTEEDRKIVRRICEAVSTRAARLVAAGIAAILKKIGrDKKVTVGVDGSVYEKYPGFRERLQEALRELLG-----PGDKV 217
|
250
....*....|....*....
gi 768525192 451 TIVPAEDGSGAGAAVIAAL 469
Cdd:pfam03727 218 VLVLAEDGSGVGAALIAAV 236
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
21-471 |
1.20e-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: 1.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 21 KELMDEIHQLEDMFTVDSETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVmEFPTG-KESGNYLAIDLGGTNLRVVLVKL 99
Cdd:COG5026 2 KKLLVDAFLKRHGFDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 100 SGNHTFDTtqsKYKLPHDMRTTKHQ---EELWSFIADSLKDFmveqellnTKDTLPLGFTFSYPASQNKINEGILQRWTK 176
Cdd:COG5026 81 DGEGTFEI---ENFKSFPLPGTSSEitaEEFFDFIADYIEPL--------LDESYKLGFCFSFPAEQLPDKDGRLIQWTK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 177 GFDIPNVEGHDVVPLLQNEISKREL-PIEIVALINDTVGTLVASYYTDPETK----MGVIFGTGVNGAFYDVVSDIEKLE 251
Cdd:COG5026 150 EIKTPGVEGKNIGELLEAALARKGLdNVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 252 GKLAddipsnsPMAINCEYGSFDnehlVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQ 331
Cdd:COG5026 230 AYEG-------PMIINMESGNFN----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPGF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 332 DlSKLKQPYIMDTSYPARIEDDPFENLEDTDDIFQkdfgvKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRG-YK 410
Cdd:COG5026 299 S-EVFETPYSLTTVDMSRFLADPSDEKEILSQCLE-----AGSEEDREILREIADAIVERAARLVAATLAGILLHLGpGK 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768525192 411 TGH----IAADGSVYNKYPGFKEAAAKGLRDIYgwTGDASnDPITIVPAEDGSGAGAAVIAALSE 471
Cdd:COG5026 373 TPLkphcIAIDGSTYEKMPGLAEKIEYALQEYL--LGEKG-RYVEFVLVENASLLGAAIAAALNE 434
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
39-472 |
2.39e-90 |
|
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: 282.13 E-value: 2.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGLTKKGGN---IPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKL-SGNH-TFDTTQSKYK 113
Cdd:cd24091 5 DQLLEVKARMRAEMERGLRKETHAsapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVrSGKWrGVEMHNKIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 114 LPHD-MRTTKhqEELWSFIADSLKDFMVEQELLNTKdtLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLL 192
Cdd:cd24091 85 IPQEiMQGTG--EELFDHIVQCIADFLEYMGLKGVS--LPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 193 QNEISKR-ELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKladdipsNSPMAINCEYG 271
Cdd:cd24091 161 REAIKRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGE-------EGRMCINMEWG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 272 SF-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARI 350
Cdd:cd24091 234 AFgDNGCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 351 EDDPFENLEdTDDIFQkDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTG------HIAADGSVYNKY 424
Cdd:cd24091 314 ESDRLALLQ-VRAILQ-QLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGldhlnvTVGVDGTLYKLH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 768525192 425 PGFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAALSEK 472
Cdd:cd24091 392 PHFSRVMHETVKEL------APKCDVTFLQSEDGSGKGAALITAVACR 433
|
|
| PLN02362 |
PLN02362 |
hexokinase |
27-468 |
2.99e-85 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 271.37 E-value: 2.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 27 IHQLEDMFTVDSETLRKVVKHFIDELNKGLTKKGGN-IPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTF 105
Cdd:PLN02362 41 LKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSkLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 106 DTTQSKYKLP---HDMRTTkhQEELWSFIADSLKDFmVEQELLNTKDTLP----LGFTFSYPASQNKINEGILQRWTKGF 178
Cdd:PLN02362 121 ILSQDVERHPipqHLMNST--SEVLFDFIASSLKQF-VEKEENGSEFSQVrrreLGFTFSFPVKQTSISSGILIKWTKGF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 179 DIPNVEGHDVVPLLQNEISKRELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLAddi 258
Cdd:PLN02362 198 AISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLT--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 259 pSNSPMAINCEYGSFDNEHlvLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLElnekglMLKDQDL----- 333
Cdd:PLN02362 275 -TSGSMVVNMEWGNFWSSH--LPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILR------MSQESDIfgpvs 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 334 SKLKQPYIMDTSYPARIEDDPFENLEDTDDIFQKDFGV-KTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRG---- 408
Cdd:PLN02362 346 SRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGrdgs 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768525192 409 --------------YKTGHIAADGSVYNKYPGFKEAAAKGLRDIYGwtGDASNDPITIVpAEDGSGAGAAVIAA 468
Cdd:PLN02362 426 ggitsgrsrsdiqiMRRTVVAVEGGLYTNYTMFREYLHEALNEILG--EDVAQHVILKA-TEDGSGIGSALLAA 496
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
39-470 |
5.04e-84 |
|
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: 265.99 E-value: 5.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGLTKKGGN---IPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKL-SGNHTFDTTQSK-YK 113
Cdd:cd24128 5 DQLLEVKRRMKVEMERGLSKETHAsapVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVrNGKWRGVEMHNKiYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 114 LPHD-MRTTKhqEELWSFIADSLKDFMveqELLNTKD-TLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPL 191
Cdd:cd24128 85 IPQEvMHGTG--EELFDHIVHCIADFL---EYMGMKGvSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 192 LQNEISKRE-LPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKladdipsNSPMAINCEY 270
Cdd:cd24128 160 LKEAIHRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGE-------EGRMCVNMEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 271 GSF-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPAR 349
Cdd:cd24128 233 GAFgDNGCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 350 IEDDPFENLEdTDDIFQKdFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQK----RGYKTGHI--AADGSVYNK 423
Cdd:cd24128 313 IESDRLALLQ-VRAILQH-LGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKirenRGLDALKVtvGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 768525192 424 YPGFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAALS 470
Cdd:cd24128 391 HPHFAKVMHETVKDL------APKCDVSFLQSEDGSGKGAALITAVA 431
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
39-468 |
1.84e-82 |
|
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: 261.63 E-value: 1.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGLTKKGGN---IPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKL--SGNHTFDTTQSKYK 113
Cdd:cd24089 5 ETLLDISRRFRKEMEKGLGKDTHPtatVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVndEKNQKVEMESQVYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 114 LPHD-MRTTKhqEELWSFIADSLKDFMVEQELLNTKdtLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLL 192
Cdd:cd24089 85 IPEEiMHGSG--TQLFDHVAECLADFMDKQKIKDKK--LPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 193 QNEISKR-ELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGklaDDipsnSPMAINCEYG 271
Cdd:cd24089 161 RKAIRRRgDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DE----GRMCINTEWG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 272 SF-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARI 350
Cdd:cd24089 234 AFgDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 351 EDDPfENLEDTDDIFqKDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQK-RGYKTGH-----IAADGSVYNKY 424
Cdd:cd24089 314 EKEK-EGLANAKEIL-TRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRlRENKGLErlrttVGVDGSVYKKH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 768525192 425 PGFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAA 468
Cdd:cd24089 392 PQFSKRLHKAVRRL------VPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
38-472 |
2.98e-82 |
|
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: 261.41 E-value: 2.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 38 SETLRKVVKHFIDELNKGLTKKG---GNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKL-SGNHTFDTTQSKYK 113
Cdd:cd24130 4 RDQLQEVKQKMRTELEYGLKKEThptASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIrSGRRSVRMYNKIFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 114 LPHD-MRTTKhqEELWSFIADSLKDFMVEQELLNTKdtLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLL 192
Cdd:cd24130 84 IPLEiMQGTG--EELFDHIVQCIADFLDYMGLKGAR--LPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 193 QNEISKR-ELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGkladdipSNSPMAINCEYG 271
Cdd:cd24130 160 REAIKRRnEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG-------DEGRMCINTEWG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 272 SF-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARI 350
Cdd:cd24130 233 GFgDNGCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 351 EDDPFENLEdTDDIFQKdFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTG------HIAADGSVYNKY 424
Cdd:cd24130 313 ESDRLALLQ-VRRILQQ-LGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGldrldiTVGVDGTLYKLH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 768525192 425 PGFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAALSEK 472
Cdd:cd24130 391 PHFSRILQETVKEL------APQCDVTFMLSEDGSGKGAALITAVAKR 432
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
26-472 |
5.92e-80 |
|
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: 255.58 E-value: 5.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 26 EIHQLEDMFTVDSETLRKVVKHFIDELNKGL---TKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKL--- 99
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLrleTHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 100 -SGNHTFDTTQSKYKLPHDMrTTKHQEELWSFIADSLKDFMVEQELLNTKdtLPLGFTFSYPASQNKINEGILQRWTKGF 178
Cdd:cd24092 81 eEGQWSVKTKHQMYSIPEDA-MTGTAEMLFDYISECISDFLDKHQMKHKK--LPLGFTFSFPVRHEDIDKGILLNWTKGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 179 DIPNVEGHDVVPLLQNEISKR-ELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKladd 257
Cdd:cd24092 158 KASGAEGNNVVGLLRDAIKRRgDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGD---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 258 ipsNSPMAINCEYGSF-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKL 336
Cdd:cd24092 234 ---EGRMCVNTEWGAFgDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 337 KQPYIMDTSYPARIEDDPfENLEDTDDIFQKdFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAI----CQKRGYKTG 412
Cdd:cd24092 311 RTRGAFETRFVSQVESDT-GDRKQIYNILST-LGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVinrmRESRSEDVM 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768525192 413 HIAA--DGSVYNKYPGFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAALSEK 472
Cdd:cd24092 389 RITVgvDGSVYKLHPSFKERFHASVRRL------TPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
51-470 |
1.00e-79 |
|
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: 254.42 E-value: 1.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 51 ELNKGL---TKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLsGNHTFDTTQSKYKLPHDMrTTKHQEEL 127
Cdd:cd24129 17 EMAKGLrgeTHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV-GTAGVQITSEIYSIPETV-AQGTGQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 128 WSFIADSLKDFMVEQELLNTKdtLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQNEISKRE-LPIEIV 206
Cdd:cd24129 95 FDHIVDCIVDFQQKQGLSGQS--LPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREAATRKQaVELNVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 207 ALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKladdipsNSPMAINCEYGSF-DNEHLVLPRTKY 285
Cdd:cd24129 173 AIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGD-------SGRMCINMEWGAFgDNGCLAMISTRF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 286 DVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIEDDPFeNLEDTDDIF 365
Cdd:cd24129 246 DASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL-ALRQVRAIL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 366 QkDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTG------HIAADGSVYNKYPGFKEAAAKGLRDIy 439
Cdd:cd24129 325 E-DLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGldelavTVGVDGTLYKLHPRFSSLVQATVREL- 402
|
410 420 430
....*....|....*....|....*....|.
gi 768525192 440 gwtgdASNDPITIVPAEDGSGAGAAVIAALS 470
Cdd:cd24129 403 -----APRCVVTFLQSEDGSGKGAALVTAVA 428
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
35-470 |
3.16e-79 |
|
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: 253.30 E-value: 3.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 35 TVDSETLRKVVKHFIDELNKGLTKKGGN---IPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKL-SGN-HTFDTTQ 109
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIrSGKkRTVEMHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 110 SKYKLPHD-MRTTKhqEELWSFIADSLKDFMVEQELLNTKdtLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDV 188
Cdd:cd24127 81 KIYAIPIEiMQGTG--EELFDHIVSCISDFLDYMGIKGPR--MPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 189 VPLLQNEISKR-ELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKladdipsNSPMAIN 267
Cdd:cd24127 157 VTLLRDAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGD-------QGQMCIN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 268 CEYGSF-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSY 346
Cdd:cd24127 230 MEWGAFgDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 347 PARIEDDPFENLEdTDDIFQKdFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQK----RGYKTGHI--AADGSV 420
Cdd:cd24127 310 LSQIESDRLALLQ-VRAILQQ-LGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKirenRGLDHLNVtvGVDGTL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768525192 421 YNKYPGFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAALS 470
Cdd:cd24127 388 YKLHPHFSRIMHQTVKEL------SPKCNVSFLLSEDGSGKGAALITAVG 431
|
|
| PLN02914 |
PLN02914 |
hexokinase |
41-472 |
4.69e-77 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 249.42 E-value: 4.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 41 LRKVVKHFIDELNKGLTKKGG-NIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGN--HTFDTTQSKYKLPHD 117
Cdd:PLN02914 55 LRHVADAMAADMRAGLAVDGGgDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKdeRVIATEFEQVSIPQE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 118 -MRTTkhQEELWSFIADSLKDFmVEQEllNTKDTLP------LGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVP 190
Cdd:PLN02914 135 lMFGT--SEELFDFIASGLANF-VAKE--GGKFHLPegrkreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 191 LLQNEISKRELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLAddipSNSPMAINCEY 270
Cdd:PLN02914 210 CLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKS----SSGRTIINTEW 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 271 GSFDNehlVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARI 350
Cdd:PLN02914 286 GAFSD---GLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 351 EDDPFENLEDTDDIFQKDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQK-----RGYKTGH---IAADGSVYN 422
Cdd:PLN02914 363 QQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKmeedsKGMIFGKrtvVAMDGGLYE 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768525192 423 KYPGFKEAAAKGLRDIYgwtGDASNDPITIVPAEDGSGAGAAVIAALSEK 472
Cdd:PLN02914 443 KYPQYRRYMQDAVTELL---GLELSKNIAIEHTKDGSGIGAALLAATNSK 489
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
39-468 |
5.47e-77 |
|
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: 247.50 E-value: 5.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGL---TKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGN--HTFDTTQSKYK 113
Cdd:cd24125 5 ETLLEISKRFRKEMEKGLgatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNglQKVEMENQIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 114 LPHD-MRTTKhqEELWSFIADSLKDFMveqELLNTKDT-LPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPL 191
Cdd:cd24125 85 IPEDiMRGSG--TQLFDHIAECLANFM---DKLQIKDKkLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 192 LQNEISKR-ELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGkladdipSNSPMAINCEY 270
Cdd:cd24125 160 LRKAIQKRgDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG-------DEGRMCINMEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 271 GSF-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPAR 349
Cdd:cd24125 233 GAFgDDGSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 350 IEDDPfENLEDTDDIFQKdFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTG------HIAADGSVYNK 423
Cdd:cd24125 313 IEGEK-DGIRKAREVLMR-LGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGeerlrsTIGVDGSVYKK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 768525192 424 YPGFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAA 468
Cdd:cd24125 391 HPHFARRLHKTVRRL------VPGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| PLN02405 |
PLN02405 |
hexokinase |
41-468 |
2.95e-75 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 245.13 E-value: 2.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 41 LRKVVKHFIDELNKGLTKKGGN-IPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKL---PH 116
Cdd:PLN02405 55 LRQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVsipPH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 117 DMrtTKHQEELWSFIADSLKDFMV---EQELLNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQ 193
Cdd:PLN02405 135 LM--TGSSDALFDFIAAALAKFVAtegEDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 194 NEISKRELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLaddiPSNSPMAINCEYGSF 273
Cdd:PLN02405 213 KAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLL----PKSGEMVINMEWGNF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 274 DNEHlvLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIEDD 353
Cdd:PLN02405 289 RSSH--LPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 354 PFENLEDTDDIFQKDFGVKTT-LPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTGH--------IAADGSVYNKY 424
Cdd:PLN02405 367 TSPDLKVVGSKLKDILEIPNTsLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDTVKdgekqksvIAMDGGLFEHY 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 768525192 425 PGFKEAAAKGLRDIygwTGDASNDPITIVPAEDGSGAGAAVIAA 468
Cdd:PLN02405 447 TEFSKCMESTLKEL---LGEEVSESIEVEHSNDGSGIGAALLAA 487
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
39-468 |
1.17e-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: 238.98 E-value: 1.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGLTKKG---GNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLS--GNHTFDTTQSKYK 113
Cdd:cd24126 5 DTLLDIMTRFRAEMEKGLAKDTnptAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSedGKQKVQMESQFYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 114 LPHDMrTTKHQEELWSFIADSLKDFMVEQELLNTKdtLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQ 193
Cdd:cd24126 85 TPEEI-IHGTGTELFDYVAECLADFMKKKGIKHKK--LPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 194 NEISK-RELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGkladdipSNSPMAINCEYGS 272
Cdd:cd24126 162 KAIRKhKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG-------DEGRMCINTEWGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 273 F-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIE 351
Cdd:cd24126 235 FgDDGSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 352 dDPFENLEDTDDIFQkDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAIC--------QKRGYKTghIAADGSVYNK 423
Cdd:cd24126 315 -KYKEGLYNTREILS-DLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILtrlrenkkLERLRTT--VGMDGTVYKT 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 768525192 424 YPGFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAA 468
Cdd:cd24126 391 HPQYAKRLHKVVRRL------VPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
39-476 |
5.42e-70 |
|
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: 230.66 E-value: 5.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 39 ETLRKVVKHFIDELNKGLTKK---GGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLS--GNHTFDTTQSKYK 113
Cdd:cd24124 33 ETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVHMESEVYD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 114 LPHDMrTTKHQEELWSFIADSLKDFMVEQELLNTKdtLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQ 193
Cdd:cd24124 113 TPENI-VHGSGSQLFDHVAECLGDFMEKRKIKDKK--LPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 194 NEISKR-ELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGkladdipSNSPMAINCEYGS 272
Cdd:cd24124 190 KAIKKRgDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG-------DEGRMCINTEWGA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 273 F-DNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIE 351
Cdd:cd24124 263 FgDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 352 DDPfENLEDTDDIFQKdFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTG------HIAADGSVYNKYP 425
Cdd:cd24124 343 KNK-EGLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGtprlrtTVGVDGSLYKTHP 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 768525192 426 GFKEAAAKGLRDIygwtgdASNDPITIVPAEDGSGAGAAVIAALSeKRIAE 476
Cdd:cd24124 421 QYSRRFHKTLRRL------VPDSDVRFLLSESGSGKGAAMVTAVA-YRLAE 464
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
35-468 |
3.01e-58 |
|
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: 198.61 E-value: 3.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 35 TVDSETLRKVVKHFIDELNKGLTKKGGNIP---MIPGWVMEFPTGKESGNYLAIDLG--GTNLRVVLVKLSG--NHTFDT 107
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQASPAPavrMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGieGHRVEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 108 TQSKYKLPHDMRTTKHQEeLWSFIADSLKDFMVEQELlnTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHD 187
Cdd:cd24090 81 RSQEFVIPQEVMLGAGQQ-LFDFAAHCLSEFLDGQPV--PKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 188 VVPLLQNEISKREL-PIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEgkladdiPSNSPMAI 266
Cdd:cd24090 158 VVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD-------EDRGRVCV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 267 NCEYGSFDNEHLVLP-RTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTS 345
Cdd:cd24090 231 SVEWGSFSDDGALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 346 YPARIEdDPFENLEDTDDIFQkDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAIC----QKRGYKTGHI--AADGS 419
Cdd:cd24090 311 HVAEME-DPSAGAARVRAILQ-DLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLshlqHSREQQTLQVavATGGR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 768525192 420 VYNKYPGFKEAaakgLRDIYGWTgdASNDPITIVPAEDGSGAGAAVIAA 468
Cdd:cd24090 389 VCERHPRFCSI----LQGTVMLL--APECDVSFIPSVDGGGRGVAMVTA 431
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
41-468 |
9.72e-45 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 163.51 E-value: 9.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 41 LRKVVKHFIDELNKGLTKKG-GNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNH--TFDTTQSKYKLPHD 117
Cdd:PLN02596 56 LWEVADALVSDMTASLTAEEtTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNepISDLYREEISIPSN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 118 MRTTKHQEeLWSFIADSLKDFMVEQELLNTKDTL---PLGFTFSYPASQNKINEGILQRWtKGFDIPNVEGHDVVPLLQN 194
Cdd:PLN02596 136 VLNGTSQE-LFDYIALELAKFVAEHPGDEADTPErvkKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 195 EISKRELPIEIVALINDTVGTLVASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKladdIPSNSPMAINCEYGSFD 274
Cdd:PLN02596 214 ALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSP----SPESQEIVISTEWGNFN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 275 NEHLvlPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIEDDP 354
Cdd:PLN02596 290 SCHL--PITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 355 FENLEDTDDIFQKDFGV-KTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGY---KTGHIAADGSVYNKYPGFKEA 430
Cdd:PLN02596 368 SEDHEVVNEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRienKKSVVTVEGGLYEHYRVFRNY 447
|
410 420 430
....*....|....*....|....*....|....*...
gi 768525192 431 AAKGlrdIYGWTGDASNDPITIVPAEDGSGAGAAVIAA 468
Cdd:PLN02596 448 LHSS---VWEMLGSELSDNVVIEHSHGGSGAGALFLAA 482
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
77-240 |
1.29e-04 |
|
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: 43.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 77 KESGNYLAIDLGGTNLRVVLVKLSGNhtfdtTQSKYKLPHDMRTTkhQEELWSFIADSLKDFMvEQELLNTKDTLPLGFT 156
Cdd:COG1940 2 PDAGYVIGIDIGGTKIKAALVDLDGE-----VLARERIPTPAGAG--PEAVLEAIAELIEELL-AEAGISRGRILGIGIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 157 FSYPASqnkINEGILQRWTKgfdIPNVEGHDVVPLLQNEISkreLPieiVALINDTVGTLVASYY----TDPETKMGVIF 232
Cdd:COG1940 74 VPGPVD---PETGVVLNAPN---LPGWRGVPLAELLEERLG---LP---VFVENDANAAALAEAWfgagRGADNVVYLTL 141
|
....*...
gi 768525192 233 GTGVNGAF 240
Cdd:COG1940 142 GTGIGGGI 149
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
81-241 |
7.84e-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: 38.30 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 81 NYLAIDLGGTNLRVVLVKLSGN-HTFDTTQSKyklphdmrTTKHQEELWSFIADSLKDFMVEQELlntkdtLPLGFTFSY 159
Cdd:cd24070 2 YVLGIDIGGTNIRIGLVDEDGKlLDFEKVPSK--------DLLRAGDPVEVLADLIREYIEEAGL------KPAAIVIGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768525192 160 PASQNKINEGILQrwtkGFDIPNVEGHDVVPLLQNEIskrELPieiVALINDTV----GTLVASYYTDPETKMGVIFGTG 235
Cdd:cd24070 68 PGTVDKDRRTVIS----TPNIPGLDGVNLADILENKL---GIP---VILERDVNllllYDMRAGNLDDEGVVLGFYIGTG 137
|
....*.
gi 768525192 236 VNGAFY 241
Cdd:cd24070 138 IGNAIL 143
|
|
| |
