|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
23-484 |
0e+00 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 833.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 23 ETLSSNPQIRLQQIVDQLTISLEDLKDVSHNFYSELMHGLKAHRRHRNLWLPNECSFKMLDSFIPNIPTGKEKGSYFALD 102
Cdd:PTZ00107 1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEAHRRHRNLWIPNECSFKMLDSCVYNLPTGKEKGVYYAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 103 FGGSNFRAVRIMIEGDGKMERNQSTFSLRYSSALGPKGLLDQKATATELFDHFAKKIEHVMKESGVDPNPSKPHKVGFTF 182
Cdd:PTZ00107 81 FGGTNFRAVRVSLRGGGKMERTQSKFSLPKSALLGEKGLLDKKATATDLFDHIAKSIKKMMEENGDPEDLNKPVPVGFTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 183 SFPCTMLSPCNAILLDWTKDFETGRATNDQVEGKDVAILMNQAFKRNNMNAEVSIVLNDTVGTLLSCAYQKPKDYPPCRV 262
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFETGRATNDPVEGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYQKPKNTPPCQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 263 GVILGTGFNICYVEDEYERFGYVGRVVNIECGNFDTELPLNPVDCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMILYL 342
Cdd:PTZ00107 241 GVIIGTGSNACYFEPEVSAYGYAGTPINMECGNFDSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 343 REQAPPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDVELPKESLIALRKISEAAFGRSAGFAAASICATARKAK 422
Cdd:PTZ00107 321 QLKAPPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKTR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71031861 423 AyVTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTRPDlVGNVVLLSSDDGSGKGAAIAAAMF 484
Cdd:PTZ00107 401 T-VQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPD-AGNVVFYLADDGSGKGAAIIAAMV 460
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
45-481 |
3.48e-113 |
|
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: 338.10 E-value: 3.48e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 45 EDLKDVSHNFYSELMHGLKAHRrhrnlwlpneCSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDGKMERN 124
Cdd:cd24000 2 EDLKEITDAFLEELEKGLAGEP----------SSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 125 QSTFSLRYssalgpkglLDQKATATELFDHFAKKIEHVMKESGVDpnpsKPHKVGFTFSFPCTMLSPCNAILLDWTKDFe 204
Cdd:cd24000 72 SKKYEIPD---------EIKTASAEEFFDFIADCIAEFLKENGLK----KPLPLGFTFSFPLEQTSLNDGKLLSWTKGF- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 205 tgraTNDQVEGKDVAILMNQAFKRNNMNAEVSIVLNDTVGTLLSCAYQkpkdYPPCRVGVILGTGFNICYVED-EYERFG 283
Cdd:cd24000 138 ----KIPGVEGKDVGELLNDALKKRGLPVKVVAVLNDTVATLLAGAYK----DPDCRIGLILGTGTNAAYLEPtSNILLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 284 YVGRVVNIECGNFDTE-LPLNPVDCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMILYLREqappkmweigtftsvdas 362
Cdd:cd24000 210 DGGMIINTEWGNFGKNsLPRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 363 eilndnsedlviskqvakrswdvelpkesliALRKISEAAFGRSAGFAAASICATARKAKAYVTSKTTVAIDGSLYVKNE 442
Cdd:cd24000 272 -------------------------------ILRKICELVAERSARLAAAAIAALLRKTGDSPEKKITIAVDGSLFEKYP 320
|
410 420 430
....*....|....*....|....*....|....*....
gi 71031861 443 WYRNKLQYYIDNVTRPDLvgNVVLLSSDDGSGKGAAIAA 481
Cdd:cd24000 321 GYRERLEEYLKELLGRGI--RIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
44-481 |
1.51e-101 |
|
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: 310.72 E-value: 1.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 44 LEDLKDVSHNFYSELMHGLKAHRRhrnlwlpnecSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRImiegdgKMER 123
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGG----------SLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLV------TLDG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 124 NQSTFSLRYSSALGPKGLLDqkATATELFDHFAKKIEHVMKESGVDPNPSKPHKVGFTFSFPCTMLSPCNAILLDWTKDF 203
Cdd:cd24018 65 NGGIFIIVQRKYKIPDEAKT--GTGEELFDFIAECIAEFLEEHNLDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 204 ETGratndQVEGKDVAILMNQAFKRNNMNAEVSIVLNDTVGTLLSCAYqkpkDYPPCRVGVILGTGFNICYVED-----E 278
Cdd:cd24018 143 NAP-----GVVGKDVVELLQNALDRRGVNVKVVALVNDTVGTLVASAY----FDPSTVIGVIFGTGTNACYWEKvsnikK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 279 YERF-GYVGR----VVNIECGNFDTE---LPLNPVDCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI------LYLRE 344
Cdd:cd24018 214 LTSPsGSVTKsdemIINTEWGAFDNErevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLdlidrgLLFSG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 345 QAPPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDVELPK-ESLIALRKISEAAFGRSAGFAAASICATARKAKA 423
Cdd:cd24018 294 KSSELLNEPYSLDTAFLSRIEADTSPDLDAVRDILKELLAIDNTTlEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71031861 424 YVTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTRPDLVGNVVLLSSDDGSGKGAAIAA 481
Cdd:cd24018 374 LLPEPVTVGIDGSVYEKYPGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
42-482 |
3.04e-97 |
|
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: 299.84 E-value: 3.04e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 42 ISLEDLKDVSHNFYSELMHGLKAHrrhrnlwlPNECSF-KMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDGK 120
Cdd:cd24019 2 LSDEQLEEIMDRLLKEMEKGLSKD--------THPTASvKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 121 MERNQSTFSLryssalgPKGLLdqKATATELFDHFAKKIEHVMKESGVDpnpSKPHKVGFTFSFPCTMLSPCNAILLDWT 200
Cdd:cd24019 74 VKMESEIYAI-------PEEIM--TGTGEQLFDYIAECLAEFLEKNGLK---DKKLPLGFTFSFPCKQTGLDSATLVRWT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 201 KDFE-TGratndqVEGKDVAILMNQAFKRNN-MNAEVSIVLNDTVGTLLSCAYqkpkDYPPCRVGVILGTGFNICYVE-- 276
Cdd:cd24019 142 KGFKcSG------VEGEDVVRLLQEAIKRRGdIKVDVVAVVNDTVGTLMSCAY----EDPNCEIGLIVGTGTNACYMEkl 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 277 DEYERFGYVGR-----VVNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRfMILYLRE--- 344
Cdd:cd24019 212 SNVEKWDGDEGdpgqvIINTEWGAFGDNGVLDFIrtefDREVDEESLNPGKQLFEKMISGMYLGELVRL-VLLKLAKegl 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 345 ----QAPPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDVELPKESLIALRKISEAAFGRSAGFAAASICATARK 420
Cdd:cd24019 291 lfrgQLSEELLTRGSFETKYVSEIESDNEGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNR 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71031861 421 AKayvTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTRPDLvgNVVLLSSDDGSGKGAAIAAA 482
Cdd:cd24019 371 MN---RKEVTVGVDGSLYKYHPKFHKRMHETLKELVPPGC--KFKLMLSEDGSGKGAALVAA 427
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
28-483 |
3.13e-94 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 292.25 E-value: 3.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 28 NPQIRLQQIVDQLTISLEDLKDVSHNFYSELMHGLKAhrrhrnlwlpNECSFKMLDSFIpNIPTG-KEKGSYFALDFGGS 106
Cdd:COG5026 3 KLLVDAFLKRHGFDLSSIDLEEIAAKFQEEMEKGLEG----------KKSSLKMLPSYL-GLPTGvKETGPVIALDAGGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 107 NFRAVRIMIEGDGKME-RNQSTFSLRyssalgpkgLLDQKATATELFDHFAKKIEHVMKESgvdpnpskpHKVGFTFSFP 185
Cdd:COG5026 72 NFRVALVRFDGEGTFEiENFKSFPLP---------GTSSEITAEEFFDFIADYIEPLLDES---------YKLGFCFSFP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 186 CTMLSPCNAILLDWTKDFETgratnDQVEGKDVAILMNQAFKRNNM-NAEVSIVLNDTVGTLLSCAYQKPKDYPPCRVGV 264
Cdd:COG5026 134 AEQLPDKDGRLIQWTKEIKT-----PGVEGKNIGELLEAALARKGLdNVKPVAILNDTVATLLAGAYADPDDGYSGYIGS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 265 ILGTGFNICYVEdEYERFGYVGR-----VVNIECGNFDtELPLNPVDCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI 339
Cdd:COG5026 209 ILGTGHNTCYLE-PNAPIGKLPAyegpmIINMESGNFN-KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 340 LYLRE-----QAPPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDvelpkESLIALRKISEAAFGRSAGFAAASI 414
Cdd:COG5026 287 EAAAEglfspGFSEVFETPYSLTTVDMSRFLADPSDEKEILSQCLEAGSE-----EDREILREIADAIVERAARLVAATL 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71031861 415 CATARKAKAY--VTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTRPDLVGNVVLLSSDDGSGKGAAIAAAM 483
Cdd:COG5026 362 AGILLHLGPGktPLKPHCIAIDGSTYEKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
73-482 |
3.24e-83 |
|
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: 263.75 E-value: 3.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 73 LPNEC--SFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDGKMERNQStfslrYSSALGPKGLLDqkATATE 150
Cdd:cd24020 21 LASEGgsKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQE-----YEEVPIPPELMV--GTSEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 151 LFDHFAKKIEHVMKESGVDPNPS-KPHKVGFTFSFPCTMLSPCNAILLDWTKDFetgraTNDQVEGKDVAILMNQAFKRN 229
Cdd:cd24020 94 LFDFIAGELAKFVATEGEGFHPEgEKRELGFTFSFPVKQTSIDSGTLIKWTKGF-----TISDTVGKDVVELLEEALERQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 230 NMNAEVSIVLNDTVGTLLSCAYQKPKdyppCRVGVILGTGFNICYVedeyERFGYVGR-----------VVNIECGNFDT 298
Cdd:cd24020 169 GLDMRVAALVNDTVGTLAGGRYVDQD----TMAAVILGTGTNAAYV----ERADAIPKwsgglprsgemVINTEWGNFRS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 299 -ELPLNPVDCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRfMILYLREQA-------PPKMWEIGTFTSVDASEILNDNSE 370
Cdd:cd24020 241 sHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRR-VLLRMAEEAalfgdtvPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 371 DLVISKQVAKRSWDVE-LPKESLIALRKISEAAFGRSAGFAAASICATARKA-----KAYVTSKTTVAIDGSLYVKNEWY 444
Cdd:cd24020 320 DLETVARILKDALGIDdTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLgrdggGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 71031861 445 RNKLQYYIDNVTRPDLVGNVVLLSSDDGSGKGAAIAAA 482
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAA 437
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
42-482 |
1.70e-72 |
|
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: 235.82 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 42 ISLEDLKDVSHNFYSELMHGLKAHRRHRnlwlpneCSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRA--VRIMIEGDG 119
Cdd:cd24089 2 LSDETLLDISRRFRKEMEKGLGKDTHPT-------ATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVlwVQVNDEKNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 120 KMERNQSTFSLryssalgPKGLLdqKATATELFDHFAKKIEHVMKESGVDpnpSKPHKVGFTFSFPCTMLSPCNAILLDW 199
Cdd:cd24089 75 KVEMESQVYAI-------PEEIM--HGSGTQLFDHVAECLADFMDKQKIK---DKKLPLGFTFSFPCRQTKIDESILISW 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 200 TKDFETgratnDQVEGKDVAILMNQAFKRN-NMNAEVSIVLNDTVGTLLSCAYQKPKdyppCRVGVILGTGFNICYVED- 277
Cdd:cd24089 143 TKGFKA-----SGVEGKDVVKLLRKAIRRRgDYDIDIVAVVNDTVGTMMTCGYDDQN----CEVGLIIGTGTNACYMEEm 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 278 -EYERF-GYVGRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMILYLRE------ 344
Cdd:cd24089 214 rNIDLVeGDEGRMcINTEWGAFGDDGSLEDIrtefDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEgllfgg 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 345 QAPPKMWEIGTFTSVDASEIlNDNSEDLVISKQVAKRsWDVELPKESLIALRKISEAAFGRSAGFAAASICATA---RKA 421
Cdd:cd24089 294 KISPELLTRGKFETKDVSAI-EKEKEGLANAKEILTR-LGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILtrlREN 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71031861 422 KAYVTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTrPDLvgNVVLLSSDDGSGKGAAIAAA 482
Cdd:cd24089 372 KGLERLRTTVGVDGSVYKKHPQFSKRLHKAVRRLV-PDC--DVRFLLSEDGSGKGAAMVTA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
33-251 |
1.26e-69 |
|
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: 220.45 E-value: 1.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 33 LQQIVDQLTISLEDLKDVSHNFYSELMHGLKAHRRhrnlwlpneCSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVR 112
Cdd:pfam00349 2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGS---------SSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 113 IMIEGDGKMERNQSTFSLryssalgPKGLLdqKATATELFDHFAKKIEHVMKESGVDPNPSKPHKVGFTFSFPCTMLSPC 192
Cdd:pfam00349 73 VELGGDGKFEITQEKYKI-------PEELM--TGTGEELFDFIADCIAEFLKEHGLEDFEEKELPLGFTFSFPVEQTSLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 71031861 193 NAILLDWTKDFETgratnDQVEGKDVAILMNQAFKRNNMNAEVSIVLNDTVGTLLSCAY 251
Cdd:pfam00349 144 SGTLIRWTKGFDI-----PGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
45-481 |
7.44e-69 |
|
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: 226.51 E-value: 7.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 45 EDLKDVSHNFYSELMHGLKahrrhrnlwlPNECSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDGkmern 124
Cdd:cd24088 2 EKLDKLTAEFQRQMEKGLA----------KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDG----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 125 qsTFSLRYSSALGPKGLLDQKaTATELFDHFAKKIEHVMKESGVDPNPS----KPHKVGFTFSFPCTMLSPCNAILLDWT 200
Cdd:cd24088 67 --TFSLRQEKSKIPDELKTGV-TAKDLFDYLAKSVEAFLTKHHGDSFAAgkddDRLKLGFTFSFPVDQTAINSGTLIRWT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 201 KDFETGRATndqveGKDVAILMNQAFKRNNMNAEVSIVLNDTVGTLLSCAYQKPKDYPPCrVGVILGTGFNICYVED--- 277
Cdd:cd24088 144 KGFDIADAV-----GKDVVKLLQDELDRQGIPVKVVALVNDTVGTLLARSYTSPEISGAV-LGAIFGTGTNGAYLEDlek 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 278 -------EYERFGYVGRVVNIECGNFDTE---LPLNPVDCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI-------- 339
Cdd:cd24088 218 ikklddsSRVGKGKTHMVINTEWGSFDNElkvLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVdlhkqglf 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 340 -LYLREQAPPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDVELPK-ESLIALRKISEAAFGRSAGFAAASICAT 417
Cdd:cd24088 298 lIQYNDKSPSALNTPYGLDTAVLSAIEIDSEAELRATRKVLLDDLGLPAPSlEDAEAVRKISRAIGRRAARLSAVAIAAI 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71031861 418 ARKAKAYVTSKTT---VAIDGSLYvknEWYrNKLQYYIDNVTRPDLVG-----NVVLLSSDDGSGKGAAIAA 481
Cdd:cd24088 378 LIKTGALNKSYDGeinIGVDGSVI---EFY-PGFESMLREALRLLLIGaegekRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
40-483 |
8.45e-68 |
|
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: 224.88 E-value: 8.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 40 LTISLEDLKDVSHNFYSELMHGLKahrRHRNlwlPNeCSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEgdg 119
Cdd:cd24124 28 MRLSDETLIDIMTRFRKEMKNGLS---RDFN---PT-ATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVN--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 120 kMERNQsTFSLRYSSALGPKGLLdqKATATELFDHFAKKIEHVMKESGVDpnpSKPHKVGFTFSFPCTMLSPCNAILLDW 199
Cdd:cd24124 98 -HEKNQ-NVHMESEVYDTPENIV--HGSGSQLFDHVAECLGDFMEKRKIK---DKKLPVGFTFSFPCQQSKIDEAILITW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 200 TKDFETgratnDQVEGKDVAILMNQAF-KRNNMNAEVSIVLNDTVGTLLSCAYqkpkDYPPCRVGVILGTGFNICYVE-- 276
Cdd:cd24124 171 TKRFKA-----SGVEGADVVKLLNKAIkKRGDYDANIVAVVNDTVGTMMTCGY----DDQHCEVGLIIGTGTNACYMEel 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 277 ---DEYErfGYVGRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMILYLRE---- 344
Cdd:cd24124 242 rhiDLVE--GDEGRMcINTEWGAFGDDGSLEDIrtefDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEgllf 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 345 --QAPPKMWEIGTFTSVDASEIlNDNSEDLVISKQVAKRsWDVELPKESLIALRKISEAAFGRSAGFAAASICAT---AR 419
Cdd:cd24124 320 egRITPELLTRGKFNTSDVSAI-EKNKEGLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAIlnrLR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71031861 420 KAKAYVTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTrPDlvGNVVLLSSDDGSGKGAAIAAAM 483
Cdd:cd24124 398 DNKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLV-PD--SDVRFLLSESGSGKGAAMVTAV 458
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
42-482 |
5.69e-66 |
|
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: 218.61 E-value: 5.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 42 ISLEDLKDVSHNFYSELMHGLKAHRRhrnlwlPNECsFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDG-- 119
Cdd:cd24125 2 LSDETLLEISKRFRKEMEKGLGATTH------PTAA-VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGlq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 120 KMERNQSTFSLryssalgPKGLLdqKATATELFDHFAKKIEHVMKESGVDpnpSKPHKVGFTFSFPCTMLSPCNAILLDW 199
Cdd:cd24125 75 KVEMENQIYAI-------PEDIM--RGSGTQLFDHIAECLANFMDKLQIK---DKKLPLGFTFSFPCHQTKLDESFLVSW 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 200 TKDFETGratndQVEGKDVAILMNQAF-KRNNMNAEVSIVLNDTVGTLLSCAYqkpkDYPPCRVGVILGTGFNICYVEdE 278
Cdd:cd24125 143 TKGFKSS-----GVEGRDVVALLRKAIqKRGDFDIDIVAVVNDTVGTMMTCGY----DDHNCEIGLIVGTGTNACYME-E 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 279 YERFGYV----GRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMILYLRE----- 344
Cdd:cd24125 213 MRHIDLVegdeGRMcINMEWGAFGDDGSLDDIrtefDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEellfg 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 345 -QAPPKMWEIGTFTSVDASEILNDnSEDLVISKQVAKRsWDVELPKESLIALRKISEAAFGRSAGFAAASICATARKA-- 421
Cdd:cd24125 293 gKLSPELLNTGHFETKDVSDIEGE-KDGIRKAREVLMR-LGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIke 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71031861 422 -KAYVTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTrPDLvgNVVLLSSDDGSGKGAAIAAA 482
Cdd:cd24125 371 nKGEERLRSTIGVDGSVYKKHPHFARRLHKTVRRLV-PGC--DVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
45-483 |
2.02e-63 |
|
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: 211.85 E-value: 2.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 45 EDLKDVSHNFYSELMHGLKAhrrhrnlwlpNECSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDGKMERN 124
Cdd:cd24087 2 ERLRKITDHFISELEKGLSK----------KGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 125 QSTFSLryssalgPKgllDQK-ATATELFDHFAKKIEHVMKESGVDpNPSKPHKVGFTFSFPCTMLSPCNAILLDWTKDF 203
Cdd:cd24087 72 QSKYRL-------PE---ELKtGTGEELWDFIADCLKKFVEEHFPG-GKSEPLPLGFTFSYPASQDKINHGILQRWTKGF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 204 EtgratNDQVEGKDVAILMNQAFKRNNMNAEVSIVLNDTVGTLLSCAYQKPKdyppCRVGVILGTGFNICYvedeYERFG 283
Cdd:cd24087 141 D-----IPNVEGHDVVPMLQKALKKRNVPIELVALINDTTGTLIASNYTDPE----TKIGVIFGTGCNAAY----MEVVS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 284 YVGRV------------VNIECGNFDTE---LPLNPVDCEIDfYTSNR-GRGKLEKLVAGAYLGEIIRRFMI-LY----- 341
Cdd:cd24087 208 NIPKLehddippdspmaINCEYGAFDNEhlvLPRTKYDVIID-EESPRpGQQAFEKMIAGYYLGEILRLVLLdLYdegfl 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 342 LREQAPPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDVELPKESLIALRKISEAAFGRSAGFAAASICATARKa 421
Cdd:cd24087 287 FKGQDTSKLEKPYVMDTSFLSRIEEDPFENLEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK- 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71031861 422 KAYVTSKttVAIDGSLYVKNEWYRNKL-QYYIDNVTRPDLVGNVVLLSSDDGSGKGAAIAAAM 483
Cdd:cd24087 366 RGYKTCH--VAADGSVYNKYPGFKERAaQALKDIFGWDGEDDPIKTVPAEDGSGVGAAIIAAL 426
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
42-483 |
3.93e-60 |
|
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: 203.55 E-value: 3.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 42 ISLEDLKDVSHNFYSELMHGLKAHRRhrnlwlpNECSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRA--VRIMIEGDG 119
Cdd:cd24091 2 LSHDQLLEVKARMRAEMERGLRKETH-------ASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVllVKVRSGKWR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 120 KMERNQSTFSLRYSSALGpkglldqkaTATELFDHFAKKIEHVMKESGVDpNPSKPhkVGFTFSFPCTMLSPCNAILLDW 199
Cdd:cd24091 75 GVEMHNKIYAIPQEIMQG---------TGEELFDHIVQCIADFLEYMGLK-GVSLP--LGFTFSFPCQQTSLDEGILLKW 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 200 TKDFetgRATNdqVEGKDVAILMNQAFKRNN-MNAEVSIVLNDTVGTLLSCAYQKPKdyppCRVGVILGTGFNICYVED- 277
Cdd:cd24091 143 TKGF---KATD--CEGEDVVTLLREAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPH----CEIGLIVGTGSNACYMEEm 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 278 -EYERF-GYVGRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI------LYLRE 344
Cdd:cd24091 214 rNVEMVeGEEGRMcINMEWGAFGDNGCLDDIrtryDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIdltkrgLLFRG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 345 QAPPKMWEIGTFTSVDASEILNDNSEDLviskQVAKRSWDVELPK--ESLIALRKISEAAFGRSAGFAAASICATA---R 419
Cdd:cd24091 294 QISERLKTRGIFETKFLSQIESDRLALL----QVRAILQQLGLDStcDDSIIVKEVCGVVSRRAAQLCGAGMAAVVdkiR 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71031861 420 KAKAYVTSKTTVAIDGSLYvknewyrnKLQYYIDNV---TRPDLVG--NVVLLSSDDGSGKGAAIAAAM 483
Cdd:cd24091 370 ENRGLDHLNVTVGVDGTLY--------KLHPHFSRVmheTVKELAPkcDVTFLQSEDGSGKGAALITAV 430
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
42-482 |
3.97e-60 |
|
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: 203.16 E-value: 3.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 42 ISLEDLKDVSHNFYSELMHGLKahrRHRNlwlpNECSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDGKM 121
Cdd:cd24126 2 LSDDTLLDIMTRFRAEMEKGLA---KDTN----PTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 122 ernqstfSLRYSSALGPKGLLDQKATATELFDHFAKKIEHVMKESGVDpnpSKPHKVGFTFSFPCTMLSPCNAILLDWTK 201
Cdd:cd24126 75 -------KVQMESQFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIK---HKKLPLGFTFSFPCRQTKLDEGVLISWTK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 202 DFetgRATNdqVEGKDVAILMNQAF-KRNNMNAEVSIVLNDTVGTLLSCAYqkpkDYPPCRVGVILGTGFNICYVE---- 276
Cdd:cd24126 145 NF---KARG--VQGTDVVSSLRKAIrKHKDVDVDVLALVNDTVGTMMTCGY----DDQYCEVGVIIGTGTNACYMEemsh 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 277 -DEYErfGYVGRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI------LYLRE 344
Cdd:cd24126 216 iDLVE--GDEGRMcINTEWGAFGDDGSLEDIrtefDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLkmakkgLLFKG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 345 QAPPKMWEIGTFTSVDASEIlNDNSEDLVISKQVAKrSWDVELPKESLIALRKISEAAFGRSAGFAAASICAT---ARKA 421
Cdd:cd24126 294 QISPALRTKGKIETKHVAAI-EKYKEGLYNTREILS-DLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAIltrLREN 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71031861 422 KAYVTSKTTVAIDGSLYVKNEWYRNKLQyyidNVTRpDLVGN--VVLLSSDDGSGKGAAIAAA 482
Cdd:cd24126 372 KKLERLRTTVGMDGTVYKTHPQYAKRLH----KVVR-RLVPScdVRFLLSESGSGKGAAMVTA 429
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
261-483 |
7.09e-60 |
|
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: 196.56 E-value: 7.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 261 RVGVILGTGFNICYVED---------EYERFGYVgrVVNIECGNFDTE----LPLNPVDCEIDFYTSNRGRGKLEKLVAG 327
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKvsnipklegKLPKSGEM--IINTEWGAFGDNgllpLPRTEYDKELDAESPNPGFQPFEKMISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 328 AYLGEIIRRFMILYLREQA-----PPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDVELPKES-LIALRKISEA 401
Cdd:pfam03727 79 MYLGELVRLVLLDLAEEGLlfkgqSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEdRKIVRRICEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 402 AFGRSAGFAAASICATARKAKAYvtSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTRPDLvgNVVLLSSDDGSGKGAAIAA 481
Cdd:pfam03727 159 VSTRAARLVAAGIAAILKKIGRD--KKVTVGVDGSVYEKYPGFRERLQEALRELLGPGD--KVVLVLAEDGSGVGAALIA 234
|
..
gi 71031861 482 AM 483
Cdd:pfam03727 235 AV 236
|
|
| PLN02914 |
PLN02914 |
hexokinase |
80-482 |
7.45e-59 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 201.65 E-value: 7.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 80 KMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIegDGKMERNQSTFSLRYSSalgPKGLLdqKATATELFDHFAKKI 159
Cdd:PLN02914 79 KMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQL--GGKDERVIATEFEQVSI---PQELM--FGTSEELFDFIASGL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 160 EH-VMKESGVDPNPS-KPHKVGFTFSFPCTMLSPCNAILLDWTKDFETgratnDQVEGKDVAILMNQAFKRNNMNAEVSI 237
Cdd:PLN02914 152 ANfVAKEGGKFHLPEgRKREIGFTFSFPVKQTSIDSGILMKWTKGFAV-----SGTAGKDVVACLNEAMERQGLDMRVSA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 238 VLNDTVGTLLSCAYQKPKdyppCRVGVILGTGFNICYVEDEY------ERFGYVGR-VVNIECGNFDTELPLNPVDCEID 310
Cdd:PLN02914 227 LVNDTVGTLAGARYWDDD----VMVAVILGTGTNACYVERTDaipklqGQKSSSGRtIINTEWGAFSDGLPLTEFDREMD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 311 FYTSNRGRGKLEKLVAGAYLGEIIRRFMILYLREQA------PPKMWEIGTFTSVDASEILNDNSEDLvisKQVAKRSWD 384
Cdd:PLN02914 303 AASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDlfghfvPEKLSTPFALRTPHLCAMQQDNSDDL---QAVGSILYD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 385 VELPKESLIALR---KISEAAFGRSAGFAAASICATARK----AKAYVTSK-TTVAIDGSLYVKNEWYRNKLQYYIDNVT 456
Cdd:PLN02914 380 VLGVEASLSARRrvvEVCDTIVKRGGRLAGAGIVGILEKmeedSKGMIFGKrTVVAMDGGLYEKYPQYRRYMQDAVTELL 459
|
410 420
....*....|....*....|....*.
gi 71031861 457 RPDLVGNVVLLSSDDGSGKGAAIAAA 482
Cdd:PLN02914 460 GLELSKNIAIEHTKDGSGIGAALLAA 485
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
42-483 |
2.34e-58 |
|
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: 198.62 E-value: 2.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 42 ISLEDLKDVSHNFYSELMHGLKAHRRHrnlwlpnECSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIegdgKM 121
Cdd:cd24130 2 LTRDQLQEVKQKMRTELEYGLKKETHP-------TASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKI----RS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 122 ERNqstfSLRYSSALGPKGLLDQKATATELFDHFAKKIEHVMKESGVDpNPSKPhkVGFTFSFPCTMLSPCNAILLDWTK 201
Cdd:cd24130 71 GRR----SVRMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLK-GARLP--LGFTFSFPCRQTGIDKGTLVGWTK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 202 DFetgRATNdqVEGKDVAILMNQAFK-RNNMNAEVSIVLNDTVGTLLSCAYQKPKdyppCRVGVILGTGFNICYVED--E 278
Cdd:cd24130 144 GF---KATD--CEGEDVVDMLREAIKrRNEFDLDIVAVVNDTVGTMMTCGYEDPK----CEIGLIAGTGSNVCYMEEmrN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 279 YERF-GYVGRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI------LYLREQA 346
Cdd:cd24130 215 IEIVeGDEGRMcINTEWGGFGDNGCIDDIrtryDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIdltkqgLLFRGQI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 347 PPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDVELpkESLIALRKISEAAFGRSA---GFAAASICATARKAKA 423
Cdd:cd24130 295 SERLRTRGIFETKFLSQIESDRLALLQVRRILQQLGLDSTC--EDSIIVKEVCGAVSRRAAqlcGAGLAAIVEKIRENQG 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 424 YVTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTrPDLvgNVVLLSSDDGSGKGAAIAAAM 483
Cdd:cd24130 373 LDRLDITVGVDGTLYKLHPHFSRILQETVKELA-PQC--DVTFMLSEDGSGKGAALITAV 429
|
|
| PLN02362 |
PLN02362 |
hexokinase |
79-482 |
5.46e-57 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 197.03 E-value: 5.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 79 FKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGdgkmeRNQSTFSLRYSSALGPKGLLDqkATATELFDHFAKK 158
Cdd:PLN02362 78 LKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGG-----QRSSILSQDVERHPIPQHLMN--STSEVLFDFIASS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 159 IEHVM--KESGVDPNPSKPHKVGFTFSFPCTMLSPCNAILLDWTKDFetgrATNDQVeGKDVAILMNQAFKRNNMNAEVS 236
Cdd:PLN02362 151 LKQFVekEENGSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGF----AISDMV-GKDVAECLQGALNRRGLDMRVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 237 IVLNDTVGTLLSCAYQKPKDYppcrVGVILGTGFNICYVED-------EYERFGYVGRVVNIECGNF-DTELPLNPVDCE 308
Cdd:PLN02362 226 ALVNDTVGTLALGHYHDPDTV----AAVIIGTGTNACYLERtdaiikcQGLLTTSGSMVVNMEWGNFwSSHLPRTSYDID 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 309 IDFYTSNRGRGKLEKLVAGAYLGEIIRRfMILYLREQA------PPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRS 382
Cdd:PLN02362 302 LDAESPNPNDQGFEKMISGMYLGDIVRR-VILRMSQESdifgpvSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKET 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 383 WDV-ELPKESLIALRKISEAAFGRSAGFAAASICATARK----AKAYVTS-----------KTTVAIDGSLYVKNEWYRN 446
Cdd:PLN02362 381 LGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKigrdGSGGITSgrsrsdiqimrRTVVAVEGGLYTNYTMFRE 460
|
410 420 430
....*....|....*....|....*....|....*.
gi 71031861 447 KLQYYIDNVTRPDLVGNVVLLSSDDGSGKGAAIAAA 482
Cdd:PLN02362 461 YLHEALNEILGEDVAQHVILKATEDGSGIGSALLAA 496
|
|
| PLN02405 |
PLN02405 |
hexokinase |
80-482 |
9.80e-57 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 196.21 E-value: 9.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 80 KMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDGKMERNQstfslRYSSALGPKGLLdqKATATELFDHFAKKI 159
Cdd:PLN02405 79 KMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQ-----EFEEVSIPPHLM--TGSSDALFDFIAAAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 160 -EHVMKES-GVDPNPSKPHKVGFTFSFPCTMLSPCNAILLDWTKDFETgratnDQVEGKDVAILMNQAFKRNNMNAEVSI 237
Cdd:PLN02405 152 aKFVATEGeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSI-----DDAVGQDVVGELTKAMERVGLDMRVSA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 238 VLNDTVGTLLSCAYQkpkdYPPCRVGVILGTGFNICYVEDEYERFGYVG-------RVVNIECGNF-DTELPLNPVDCEI 309
Cdd:PLN02405 227 LVNDTIGTLAGGRYY----NPDVVAAVILGTGTNAAYVERAQAIPKWHGllpksgeMVINMEWGNFrSSHLPLTEYDHAL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 310 DFYTSNRGRGKLEKLVAGAYLGEIIRRFMILYLREQA------PPKMWEIGTFTSVDASEILNDNSEDLvisKQVAKRSW 383
Cdd:PLN02405 303 DVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAffgdtvPPKLKIPFILRTPDMSAMHHDTSPDL---KVVGSKLK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 384 DV-ELPKESLiALRKI----SEAAFGRSAGFAAASICATARK-----AKAYVTSKTTVAIDGSLYVKNEWYRNKLQYYID 453
Cdd:PLN02405 380 DIlEIPNTSL-KMRKVvvelCNIVATRGARLSAAGIYGILKKlgrdtVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLK 458
|
410 420
....*....|....*....|....*....
gi 71031861 454 NVTRPDLVGNVVLLSSDDGSGKGAAIAAA 482
Cdd:PLN02405 459 ELLGEEVSESIEVEHSNDGSGIGAALLAA 487
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
42-483 |
1.67e-55 |
|
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: 191.25 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 42 ISLEDLKDVSHNFYSELMHGLKAHRrHRNlwlpneCSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFR--AVRIMIEGdg 119
Cdd:cd24129 2 LSHDQLAAVQAQMRKEMAKGLRGET-HAA------ASVRMLPTYVRATPDGSERGDFLALDLGGTNFRvlLVHVGTAG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 120 kMERNQSTFSLRYSSALGpkglldqkaTATELFDHFAKKIEHVMKESGVDpnpSKPHKVGFTFSFPCTMLSPCNAILLDW 199
Cdd:cd24129 73 -VQITSEIYSIPETVAQG---------TGQQLFDHIVDCIVDFQQKQGLS---GQSLPLGFTFSFPCRQLGLDQGILLNW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 200 TKDFETgratnDQVEGKDVAILMNQA-FKRNNMNAEVSIVLNDTVGTLLSCAYQKPKdyppCRVGVILGTGFNICYVEdE 278
Cdd:cd24129 140 TKGFKA-----SGCVGQDVVSLLREAaTRKQAVELNVVAIVNDTVGTMMSCGYEDPR----CEIGLIVGTGTNACYME-E 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 279 YERFGYV----GRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI------LYLR 343
Cdd:cd24129 210 LRNVAGVpgdsGRMcINMEWGAFGDNGCLAMIstrfDASVDQASINPGKQRFEKMISGMYLGEIVRHILLhltslgVLFR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 344 EQAPPKMWEIGTFTSVDASEILNDNsedlVISKQVAKRSWDVELPK--ESLIALRKISEAAFGRSAGFAAASICATARKA 421
Cdd:cd24129 290 GKQIQRLQTRDIFKTKFLSEIESDS----LALRQVRAILEDLGLPLtsDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKM 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71031861 422 KA---YVTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTrPDLvgNVVLLSSDDGSGKGAAIAAAM 483
Cdd:cd24129 366 REnrgLDELAVTVGVDGTLYKLHPRFSSLVQATVRELA-PRC--VVTFLQSEDGSGKGAALVTAV 427
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
42-483 |
2.73e-54 |
|
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: 188.18 E-value: 2.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 42 ISLEDLKDVSHNFYSELMHGLKAHRRhrnlwlpNECSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGD--G 119
Cdd:cd24128 2 LSHDQLLEVKRRMKVEMERGLSKETH-------ASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGkwR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 120 KMERNQSTFSLRYSSALGpkglldqkaTATELFDHFAKKIEHVMKESGVDpNPSKPhkVGFTFSFPCTMLSPCNAILLDW 199
Cdd:cd24128 75 GVEMHNKIYAIPQEVMHG---------TGEELFDHIVHCIADFLEYMGMK-GVSLP--LGFTFSFPCQQNSLDEGILLKW 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 200 TKDFetgRATNdqVEGKDVAILMNQAFKR-NNMNAEVSIVLNDTVGTLLSCAYqkpkDYPPCRVGVILGTGFNICYVED- 277
Cdd:cd24128 143 TKGF---KASG--CEGEDVVTLLKEAIHRrEEFDLDVVAVVNDTVGTMMTCGY----EDPHCEVGLIVGTGSNACYMEEm 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 278 -EYERF-GYVGRV-VNIECGNFDTELPLN----PVDCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI------LYLRE 344
Cdd:cd24128 214 rNVELVeGEEGRMcVNMEWGAFGDNGCLDdfrtEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIdftkrgLLFRG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 345 QAPPKMWEIGTFTSVDASEIlndnSEDLVISKQVakRSWDVELPKESL----IALRKISEAAFGRSAGFAAASICATA-- 418
Cdd:cd24128 294 RISERLKTRGIFETKFLSQI----ESDRLALLQV--RAILQHLGLESTcddsIIVKEVCTVVARRAAQLCGAGMAAVVdk 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71031861 419 -RKAKAYVTSKTTVAIDGSLYvknewyrnKLQYYIDNV---TRPDLVGN--VVLLSSDDGSGKGAAIAAAM 483
Cdd:cd24128 368 iRENRGLDALKVTVGVDGTLY--------KLHPHFAKVmheTVKDLAPKcdVSFLQSEDGSGKGAALITAV 430
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
41-483 |
2.33e-53 |
|
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: 185.50 E-value: 2.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 41 TISLEDLKDVSHNFYSELMHGLKAHRRhrnlwlpNECSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGDGK 120
Cdd:cd24127 1 HLTKDMLLEVKKRMRAEMELGLRKQTH-------NNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 121 --MERNQSTFSLryssalgPKGLLdqKATATELFDHFAKKIEHVMKESGVDpNPSKPhkVGFTFSFPCTMLSPCNAILLD 198
Cdd:cd24127 74 rtVEMHNKIYAI-------PIEIM--QGTGEELFDHIVSCISDFLDYMGIK-GPRMP--LGFTFSFPCQQTSLDAGILIT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 199 WTKDFetgRATNdqVEGKDVAILMNQAFK-RNNMNAEVSIVLNDTVGTLLSCAYQKPKdyppCRVGVILGTGFNICYVED 277
Cdd:cd24127 142 WTKGF---KATD--CEGHDVVTLLRDAIKrREEFDLDVVAVVNDTVGTMMTCAYEEPT----CEVGLIVGTGSNACYMEE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 278 --EYERF-GYVGRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMI------LYLR 343
Cdd:cd24127 213 mkNVEMVeGDQGQMcINMEWGAFGDNGCLDDIrthyDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIdftkkgFLFR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 344 EQAPPKMWEIGTFTSVDASEILNDNSEDLVISKQVAKRSWDVELpkESLIALRKISEAAFGRSAGFAAASICATA---RK 420
Cdd:cd24127 293 GQISETLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTC--DDSILVKTVCGVVSRRAAQLCGAGMAAVVdkiRE 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71031861 421 AKAYVTSKTTVAIDGSLYvknewyrnKLQYYIDNV---TRPDLVG--NVVLLSSDDGSGKGAAIAAAM 483
Cdd:cd24127 371 NRGLDHLNVTVGVDGTLY--------KLHPHFSRImhqTVKELSPkcNVSFLLSEDGSGKGAALITAV 430
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
32-483 |
2.80e-49 |
|
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: 174.68 E-value: 2.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 32 RLQQIVDQLTISLEDLKDVSHNFYSELMHGLKahrrhrnLWLPNECSFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAV 111
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLR-------LETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 112 RIMI----EGDGKMERNQSTFSLRYSSALGpkglldqkaTATELFDHFAKKI-----EHVMKEsgvdpnpsKPHKVGFTF 182
Cdd:cd24092 74 LVKVgegeEGQWSVKTKHQMYSIPEDAMTG---------TAEMLFDYISECIsdfldKHQMKH--------KKLPLGFTF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 183 SFPCTMLSPCNAILLDWTKDFETGRAtndqvEGKDVAILMNQAFK-RNNMNAEVSIVLNDTVGTLLSCAYQKPKdyppCR 261
Cdd:cd24092 137 SFPVRHEDIDKGILLNWTKGFKASGA-----EGNNVVGLLRDAIKrRGDFEMDVVAMVNDTVATMISCYYEDHQ----CE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 262 VGVILGTGFNICYVEdEYERFGYV----GRV-VNIECGNFDTELPLNPVDCE----IDFYTSNRGRGKLEKLVAGAYLGE 332
Cdd:cd24092 208 VGMIVGTGCNACYME-EMQNVELVegdeGRMcVNTEWGAFGDSGELDEFLLEydrlVDESSANPGQQLYEKLIGGKYMGE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 333 IIRRFMILYLRE------QAPPKMWEIGTFTSVDASEILNDNSEdlviSKQVAK--RSWDVELPKESLIALRKISEAAFG 404
Cdd:cd24092 287 LVRLVLLRLVDEnllfhgEASEQLRTRGAFETRFVSQVESDTGD----RKQIYNilSTLGLRPSTTDCDIVRRACESVST 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 405 RSAGFAAASICAT---ARKAKAYVTSKTTVAIDGSLYVKNEWYRNKLQYYIDNVTrPDLvgNVVLLSSDDGSGKGAAIAA 481
Cdd:cd24092 363 RAAHMCSAGLAGVinrMRESRSEDVMRITVGVDGSVYKLHPSFKERFHASVRRLT-PSC--EITFIESEEGSGRGAALVS 439
|
..
gi 71031861 482 AM 483
Cdd:cd24092 440 AV 441
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
41-482 |
3.05e-43 |
|
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: 158.16 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 41 TISLEDLKDVSHNFYSELMHGLKAHRRhrnlwlPNECsFKMLDSFIPNIPTGKEKGSYFALDFG--GSNFRAVRIMIEGD 118
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQAS------PAPA-VRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 119 G--KMERNQSTFSLRYSSALGPkglldqkatATELFDHFAKKIEHVMKesgVDPNPSKPHKVGFTFSFPCTMLSPCNAIL 196
Cdd:cd24090 74 EghRVEPRSQEFVIPQEVMLGA---------GQQLFDFAAHCLSEFLD---GQPVPKQGLQLGFSFSFPCHQTGLDRSTL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 197 LDWTKDFETgratnDQVEGKDVAILMNQAFKRNNM-NAEVSIVLNDTVGTLLSCayqKPKDyPPCRVGVILGTGFNICYV 275
Cdd:cd24090 142 ISWTKGFRC-----SDVEGQDVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGC---EPGV-RPCEVGLVVDTGTNACYM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 276 ED-------EYERfgyvGRV-VNIECGNFDTELPLNPV----DCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMILYLR 343
Cdd:cd24090 213 EEarhvavlDEDR----GRVcVSVEWGSFSDDGALGPVlttfDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 344 EQAppkmweigTFTSVDASEILndnSEDLVISKQVAkrswDVELPKESLIALRKISEaAFGRSAGFA------------- 410
Cdd:cd24090 289 RGV--------LFGGSTSPALR---SQGSILLEHVA----EMEDPSAGAARVRAILQ-DLGLSPSASdvelvqhvcravc 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 411 --AASICATA--------RKAKAYVTSKTTVAIDGSLYVKNEWYRNKLQYYIdNVTRPDLvgNVVLLSSDDGSGKGAAIA 480
Cdd:cd24090 353 trAAQLCAAAlaavlshlQHSREQQTLQVAVATGGRVCERHPRFCSILQGTV-MLLAPEC--DVSFIPSVDGGGRGVAMV 429
|
..
gi 71031861 481 AA 482
Cdd:cd24090 430 TA 431
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
73-482 |
1.15e-35 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 138.47 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 73 LPNEC--SFKMLDSFIPNIPTGKEKGSYFALDFGGSNFRAVRIMIEGdgkmeRNQSTFSLRYSSALGPKGLLDqkATATE 150
Cdd:PLN02596 71 LTAEEttTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGG-----KNEPISDLYREEISIPSNVLN--GTSQE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 151 LFDHFAKKIEHVMKESGVDPN--PSKPHKVGFTFSFPCTMLSPCNAILLDWtKDFetgrATNDQVeGKDVAILMNQAFKR 228
Cdd:PLN02596 144 LFDYIALELAKFVAEHPGDEAdtPERVKKLGFTVSYPVDQAAASSGSAIKW-KSF----SADDTV-GKALVNDINRALEK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 229 NNMNAEVSIVLNDTVGTLLSCAYQKpKDyppCRVGVILGTGFNICYVEDEYERFGYVGR-------VVNIECGNFDT-EL 300
Cdd:PLN02596 218 HGLKIRVFALVDDTIGNLAGGRYYN-KD---TVAAVTLGMGTNAAYVEPAQAIPKWQSPspesqeiVISTEWGNFNScHL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 301 PLNPVDCEIDFYTSNRGRGKLEKLVAGAYLGEIIRRFMILYLREQA------PPKMWEIGTFTSVDASEILNDNSEDLVI 374
Cdd:PLN02596 294 PITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETAlfgdtlPPKLTTPYLLRSPDMAAMHQDTSEDHEV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71031861 375 SKQVAKRSWDVelpKESLIALR----KISEAAFGRSAGFAAASICATARKAKAYVTSKTTVAIDGSLYVKNEWYRNKLQY 450
Cdd:PLN02596 374 VNEKLKEIFGI---TDSTPMARevvaEVCDIVAERGARLAGAGIVGIIKKLGRIENKKSVVTVEGGLYEHYRVFRNYLHS 450
|
410 420 430
....*....|....*....|....*....|..
gi 71031861 451 YIDNVTRPDLVGNVVLLSSDDGSGKGAAIAAA 482
Cdd:PLN02596 451 SVWEMLGSELSDNVVIEHSHGGSGAGALFLAA 482
|
|
| |
