|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02914 |
PLN02914 |
hexokinase |
4-493 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 947.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 4 MFSSPVVTPALGSFTFSSRPRSNYIVMSAVRSNSASTCPILTKFQKDCATPTPYLRNVANAIADDMRDGLAVEGGGDLEM 83
Cdd:PLN02914 1 MFSSPVVTPAIGSFTFSSRPRRRPRSRMAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 84 ILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQISISQKLMIGTSEELFGFIASKLANFVAKEKp 163
Cdd:PLN02914 81 ILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 164 GRFLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACLNEAMEAHGLDMRVSALVNDGVGTLAGAR 243
Cdd:PLN02914 160 GKFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 244 YWDEDVMVGVILGTGTNACYVEQKHAIPKLRS-KSSSGTTIINTEWGGFSKILPQTIFDLEMDETSLNPGEHLYEKMISG 322
Cdd:PLN02914 240 YWDDDVMVAVILGTGTNACYVERTDAIPKLQGqKSSSGRTIINTEWGAFSDGLPLTEFDREMDAASINPGEQIFEKTISG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 323 MYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQEDNTDDLRDVGSILYDFLDVEANMNARRRVVEVCDT 402
Cdd:PLN02914 320 MYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 403 VVKRGGRLAGAGIVAILEKIEKDTKRMGSGKRTVVAMDGALYEKYPQYRQYMQDALVELLGHKLASHVAIKHTKDVSGLG 482
Cdd:PLN02914 400 IVKRGGRLAGAGIVGILEKMEEDSKGMIFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIG 479
|
490
....*....|.
gi 330730814 483 AALLAATNSIY 493
Cdd:PLN02914 480 AALLAATNSKY 490
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
53-490 |
0e+00 |
|
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: 736.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 53 TPTPYLRNVANAIADDMRDGLAVEGGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQI 132
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 133 SISQKLMIGTSEELFGFIASKLANFVAKEKPGRFllEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVV 212
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH--PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 213 ACLNEAMEAHGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLRSK-SSSGTTIINTEWGGF 291
Cdd:cd24020 159 ELLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlPRSGEMVINTEWGNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 292 -SKILPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQEDNT 370
Cdd:cd24020 239 rSSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 371 DDLRDVGSILYDFLDVE-ANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDTKRMGSGKRTVVAMDGALYEKYPQ 449
Cdd:cd24020 319 PDLETVARILKDALGIDdTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPK 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 330730814 450 YRQYMQDALVELLGHKLASHVAIKHTKDVSGLGAALLAATN 490
Cdd:cd24020 399 FREYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02405 |
PLN02405 |
hexokinase |
43-493 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 532.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 43 ILTKFQKDCATPTPYLRNVANAIADDMRDGLAVEGGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKE 122
Cdd:PLN02405 40 ILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 123 RVLATESEQISISQKLMIGTSEELFGFIASKLANFVAKEKPGrFLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFK 202
Cdd:PLN02405 120 RVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGED-FHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 203 VSGMEGKNVVACLNEAMEAHGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLRSK-SSSGT 281
Cdd:PLN02405 199 IDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlPKSGE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 282 TIINTEWGGF-SKILPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTE 360
Cdd:PLN02405 279 MVINMEWGNFrSSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 361 HLCKMQEDNTDDLRDVGSILYDFLDV-EANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDTKRMGSGKRTVVAM 439
Cdd:PLN02405 359 DMSAMHHDTSPDLKVVGSKLKDILEIpNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDTVKDGEKQKSVIAM 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 330730814 440 DGALYEKYPQYRQYMQDALVELLGHKLASHVAIKHTKDVSGLGAALLAATNSIY 493
Cdd:PLN02405 439 DGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGIGAALLAASHSLY 492
|
|
| PLN02362 |
PLN02362 |
hexokinase |
43-493 |
7.97e-169 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 485.93 E-value: 7.97e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 43 ILTKFQKDCATPTPYLRNVANAIADDMRDGLAVEGGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKE 122
Cdd:PLN02362 40 VLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 123 RVLATESEQISISQKLMIGTSEELFGFIASKLANFVAKEKPGrFLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFK 202
Cdd:PLN02362 120 SILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEENG-SEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 203 VSGMEGKNVVACLNEAMEAHGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLRS-KSSSGT 281
Cdd:PLN02362 199 ISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlLTTSGS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 282 TIINTEWGGF-SKILPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPaKLSTPLALRTE 360
Cdd:PLN02362 279 MVVNMEWGNFwSSHLPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGPVSS-RLSTPFVLRTP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 361 HLCKMQEDNTDDLRDVGSILYDFLDV-EANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDtkrmGSG------- 432
Cdd:PLN02362 358 SVAAMHEDDSPELQEVARILKETLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGRD----GSGgitsgrs 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330730814 433 -------KRTVVAMDGALYEKYPQYRQYMQDALVELLGHKLASHVAIKHTKDVSGLGAALLAATNSIY 493
Cdd:PLN02362 434 rsdiqimRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVILKATEDGSGIGSALLAASYSSY 501
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
55-487 |
2.51e-156 |
|
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: 451.32 E-value: 2.51e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 55 TPYLRNVANAIADDMRDGLAVEGGGdLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLaTESEQISI 134
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFI-IVQRKYKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 135 SQKLMIGTSEELFGFIASKLANFVAKEKPGrflLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVAC 214
Cdd:cd24018 79 PDEAKTGTGEELFDFIAECIAEFLEEHNLD---LQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 215 LNEAMEAHGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLRSKSSSGTT----IINTEWGG 290
Cdd:cd24018 156 LQNALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPSGSVTKsdemIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 291 F---SKILPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQE 367
Cdd:cd24018 236 FdneREVLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 368 DNTDDLRDVGSILYDFLDVEANMNARRRVV-EVCDTVVKRGGRLAGAGIVAILEKIEKDTKrmgsgKRTVVAMDGALYEK 446
Cdd:cd24018 316 DTSPDLDAVRDILKELLAIDNTTLEDRKLIkRICELVSTRAARLSAAAIAAILLKRGSLLP-----EPVTVGIDGSVYEK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 330730814 447 YPQYRQYMQDALVELLGHKLASHVAIKHTKDVSGLGAALLA 487
Cdd:cd24018 391 YPGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
58-488 |
2.71e-146 |
|
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: 425.42 E-value: 2.71e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVEG--GGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGkkERVLATESEQISIS 135
Cdd:cd24019 7 LEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNG--GSQVKMESEIYAIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVAKEKPgrflleEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24019 85 EEIMTGTGEQLFDYIAECLAEFLEKNGL------KDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEAMEAHGL-DMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLRS-KSSSGTTIINTEWGGFSK 293
Cdd:cd24019 159 QEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGdEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 294 ------ILpqTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQE 367
Cdd:cd24019 239 ngvldfIR--TEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIES 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 368 DNTDDLRDVGSILYDFLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKdtkrmgsgKRTVVAMDGALYEKY 447
Cdd:cd24019 317 DNEGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR--------KEVTVGVDGSLYKYH 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 330730814 448 PQYRQYMQDALVELLghKLASHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24019 389 PKFHKRMHETLKELV--PPGCKFKLMLSEDGSGKGAALVAA 427
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
43-488 |
7.23e-132 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 391.16 E-value: 7.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 43 ILTKFQKDCATPTPYLRNVANAIADDMRDGLAVEGGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKE 122
Cdd:PLN02596 41 ILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 123 RVLATESEQISISQKLMIGTSEELFGFIASKLANFVAkEKPGRFLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWtKGFK 202
Cdd:PLN02596 121 PISDLYREEISIPSNVLNGTSQELFDYIALELAKFVA-EHPGDEADTPERVKKLGFTVSYPVDQAAASSGSAIKW-KSFS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 203 VSGMEGKNVVACLNEAMEAHGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLRSKS-SSGT 281
Cdd:PLN02596 199 ADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSpESQE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 282 TIINTEWGGFSKI-LPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTE 360
Cdd:PLN02596 279 IVISTEWGNFNSChLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 361 HLCKMQEDNTDDLRDVGSILYDFLDV-EANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDTKrmgsgKRTVVAM 439
Cdd:PLN02596 359 DMAAMHQDTSEDHEVVNEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRIEN-----KKSVVTV 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 330730814 440 DGALYEKYPQYRQYMQDALVELLGHKLASHVAIKHTKDVSGLGAALLAA 488
Cdd:PLN02596 434 EGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAA 482
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
58-487 |
6.19e-122 |
|
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: 360.82 E-value: 6.19e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAvEGGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVlaTESEQISISQK 137
Cdd:cd24000 4 LKEITDAFLEELEKGLA-GEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEV--TISKKYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 138 LMIGTSEELFGFIASKLANFVAKekpgrflLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACLNE 217
Cdd:cd24000 81 IKTASAEEFFDFIADCIAEFLKE-------NGLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLND 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 218 AMEAHGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIpklrsKSSSGTTIINTEWGGFSK-ILP 296
Cdd:cd24000 154 ALKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI-----LLGDGGMIINTEWGNFGKnSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 297 QTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCetsdlfghfapaklstplalrtehlckmqedntDDLrdv 376
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLA---------------------------------DEI--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 377 gsilydfldveanmnarrrVVEVCDTVVKRGGRLAGAGIVAILEKIEKDTKrmgsgKRTVVAMDGALYEKYPQYRQYMQD 456
Cdd:cd24000 273 -------------------LRKICELVAERSARLAAAAIAALLRKTGDSPE-----KKITIAVDGSLFEKYPGYRERLEE 328
|
410 420 430
....*....|....*....|....*....|.
gi 330730814 457 ALVELLGHklASHVAIKHTKDVSGLGAALLA 487
Cdd:cd24000 329 YLKELLGR--GIRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
67-487 |
2.45e-117 |
|
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: 352.08 E-value: 2.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 67 DDMRDGLAvEGGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKkeRVLATESEQISISQKLMIG-TSEE 145
Cdd:cd24088 13 RQMEKGLA-KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGD--GTFSLRQEKSKIPDELKTGvTAKD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 146 LFGFIASKLANFVAKEKPGRFLLEEGRKR-ELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACLNEAMEAHGL 224
Cdd:cd24088 90 LFDYLAKSVEAFLTKHHGDSFAAGKDDDRlKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDRQGI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 225 DMRVSALVNDGVGTLAGARYWDEDV---MVGVILGTGTNACYVEQKHAIPKL----RSKSSSGTTIINTEWGGFS---KI 294
Cdd:cd24088 170 PVKVVALVNDTVGTLLARSYTSPEIsgaVLGAIFGTGTNGAYLEDLEKIKKLddssRVGKGKTHMVINTEWGSFDnelKV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 295 LPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFA---PAKLSTPLALRTEHLCKMQEDNTD 371
Cdd:cd24088 250 LPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNdksPSALNTPYGLDTAVLSAIEIDSEA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 372 DLRDVGSILYDFLDVEANMNARRRVVE-VCDTVVKRGGRLAGAGIVAILEKIEKDTKRmgSGKRTVVAMDGALYEKYPQY 450
Cdd:cd24088 330 ELRATRKVLLDDLGLPAPSLEDAEAVRkISRAIGRRAARLSAVAIAAILIKTGALNKS--YDGEINIGVDGSVIEFYPGF 407
|
410 420 430
....*....|....*....|....*....|....*...
gi 330730814 451 RQYMQDALVELL-GHKLASHVAIKHTKDVSGLGAALLA 487
Cdd:cd24088 408 ESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
58-488 |
7.01e-113 |
|
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: 340.12 E-value: 7.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAvEGGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKErvLATESEQISISQK 137
Cdd:cd24087 4 LRKITDHFISELEKGLS-KKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGK--FDITQSKYRLPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 138 LMIGTSEELFGFIASKLANFVAKEKPGrfllEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACLNE 217
Cdd:cd24087 81 LKTGTGEELWDFIADCLKKFVEEHFPG----GKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 218 AMEAHGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLRSKS--SSGTTIINTEWGGFS--- 292
Cdd:cd24087 157 ALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDDipPDSPMAINCEYGAFDneh 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 293 KILPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQEDNTDD 372
Cdd:cd24087 237 LVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 373 LRDVGSILYDFLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKieKDTKRMGsgkrtvVAMDGALYEKYPQYRQ 452
Cdd:cd24087 317 LEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK--RGYKTCH------VAADGSVYNKYPGFKE 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 330730814 453 YMQDALVELLGHKLASH-VAIKHTKDVSGLGAALLAA 488
Cdd:cd24087 389 RAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAA 425
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
58-490 |
2.77e-107 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 326.14 E-value: 2.77e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAvEGGGDLEMILTFVdALPSG-NEEGLFYALDLGGTNFRVRSVQLGGKKErvlateSEQISISQ 136
Cdd:COG5026 22 LEEIAAKFQEEMEKGLE-GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGT------FEIENFKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 137 KLMIGTS-----EELFGFIASKLANFVAKEKPgrflleegrkreLGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNV 211
Cdd:COG5026 94 FPLPGTSseitaEEFFDFIADYIEPLLDESYK------------LGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 212 VACLNEAMEAHGLD-MRVSALVNDGVGTLAGARYWDEDVM----VGVILGTGTNACYVEQKHAIPKLRSKSSSgtTIINT 286
Cdd:COG5026 162 GELLEAALARKGLDnVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKLPAYEGP--MIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 287 EWGGFSKiLPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCEtSDLFGHFAPAKLSTPLALRTEHLCKMQ 366
Cdd:COG5026 240 ESGNFNK-LPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAA-EGLFSPGFSEVFETPYSLTTVDMSRFL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 367 EDNTDDLRDVGSILydfldvEANMNARRRVV-EVCDTVVKRGGRLAGAGIVAILEKIEKDtkrMGSGKRTVVAMDGALYE 445
Cdd:COG5026 318 ADPSDEKEILSQCL------EAGSEEDREILrEIADAIVERAARLVAATLAGILLHLGPG---KTPLKPHCIAIDGSTYE 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 330730814 446 KYPQYRQYMQDALVELLGHKLASHVAIKHTKDVSGLGAALLAATN 490
Cdd:COG5026 389 KMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAALN 433
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
58-488 |
2.52e-106 |
|
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: 323.26 E-value: 2.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVEGGGD--LEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQISIS 135
Cdd:cd24089 7 LLDISRRFRKEMEKGLGKDTHPTatVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVAKEKPgrflleEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24089 87 EEIMHGSGTQLFDHVAECLADFMDKQKI------KDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEAMEAHG-LDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPklRSKSSSGTTIINTEWGGF--- 291
Cdd:cd24089 161 RKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNID--LVEGDEGRMCINTEWGAFgdd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 292 ---SKIlpQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMqED 368
Cdd:cd24089 239 gslEDI--RTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAI-EK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 369 NTDDLRDVGSILYDfLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDtkRMGSGKRTVVAMDGALYEKYP 448
Cdd:cd24089 316 EKEGLANAKEILTR-LGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLREN--KGLERLRTTVGVDGSVYKKHP 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 330730814 449 QYRQYMQDALvellgHKLASHVAIKH--TKDVSGLGAALLAA 488
Cdd:cd24089 393 QFSKRLHKAV-----RRLVPDCDVRFllSEDGSGKGAAMVTA 429
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
81-491 |
2.67e-101 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 311.61 E-value: 2.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 81 LEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQL--GGKKERV--------LATESEQISISQKlmiGTSEELFGFI 150
Cdd:PTZ00107 57 FKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLrgGGKMERTqskfslpkSALLGEKGLLDKK---ATATDLFDHI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 151 ASKLANFVAKEKPgrfLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVS-----GMEGKNVVACLNEAMEAHGLD 225
Cdd:PTZ00107 134 AKSIKKMMEENGD---PEDLNKPVPVGFTFSFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFKRNNVP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 226 MRVSALVNDGVGTLAGARYWDE----DVMVGVILGTGTNACYVEqkhaiPKLRSKSSSGTtIINTEWGGFSKILPQTIFD 301
Cdd:PTZ00107 211 ANVVAVLNDTVGTLISCAYQKPkntpPCQVGVIIGTGSNACYFE-----PEVSAYGYAGT-PINMECGNFDSKLPITPYD 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 302 LEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHmcetsdLFGHFAPAKLSTPLALRTEHLCKMQEDNTDDLRDVGSILY 381
Cdd:PTZ00107 285 LEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVH------LLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFSRQVIK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 382 DFLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDTkrmgsgKRTVVAMDGALYEKYPQYRQYMQDALVEL 461
Cdd:PTZ00107 359 EAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKTRTVQ------GKATVAIDGSVYVKNPWFRRLLQEYINSI 432
|
410 420 430
....*....|....*....|....*....|
gi 330730814 462 LGHKlASHVAIKHTKDVSGLGAALLAATNS 491
Cdd:PTZ00107 433 LGPD-AGNVVFYLADDGSGKGAAIIAAMVA 461
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
250-489 |
5.06e-95 |
|
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: 287.47 E-value: 5.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 250 MVGVILGTGTNACYVEQKHAIPKLRSK-SSSGTTIINTEWGGF----SKILPQTIFDLEMDETSLNPGEHLYEKMISGMY 324
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKlPKSGEMIINTEWGAFgdngLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 325 LGEIVRRVLLHMCETSDLFGHfAPAKLSTPLALRTEHLCKMQEDNTDDLRDVGSILYDFLDVE-ANMNARRRVVEVCDTV 403
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIEtVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 404 VKRGGRLAGAGIVAILekiekdtKRMGSGKRTVVAMDGALYEKYPQYRQYMQDALVELLGhkLASHVAIKHTKDVSGLGA 483
Cdd:pfam03727 160 STRAARLVAAGIAAIL-------KKIGRDKKVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVLAEDGSGVGA 230
|
....*.
gi 330730814 484 ALLAAT 489
Cdd:pfam03727 231 ALIAAV 236
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
58-488 |
6.35e-95 |
|
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: 294.45 E-value: 6.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVEGGGD--LEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQISIS 135
Cdd:cd24091 7 LLEVKARMRAEMERGLRKETHASapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVakEKPGRflleEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24091 87 QEIMQGTGEELFDHIVQCIADFL--EYMGL----KGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEAMEA-HGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGF--- 291
Cdd:cd24091 161 REAIKRrEEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMV--EGEEGRMCINMEWGAFgdn 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 292 -SKILPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQEDNT 370
Cdd:cd24091 239 gCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 371 dDLRDVGSILYDfLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDtkRMGSGKRTVVAMDGALYEKYPQY 450
Cdd:cd24091 319 -ALLQVRAILQQ-LGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKLHPHF 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 330730814 451 RQYMQDALVELLGHklaSHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24091 395 SRVMHETVKELAPK---CDVTFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
58-488 |
4.10e-92 |
|
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: 286.75 E-value: 4.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVEGG--GDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQISIS 135
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNptAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVAKEKPgrflleEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24126 87 EEIIHGTGTELFDYVAECLADFMKKKGI------KHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEAMEAHG-LDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGFSK- 293
Cdd:cd24126 161 RKAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLV--EGDEGRMCINTEWGAFGDd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 294 -ILP--QTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMqEDNT 370
Cdd:cd24126 239 gSLEdiRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAI-EKYK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 371 DDLRDVGSILYDfLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDTK--RMgsgkRTVVAMDGALYEKYP 448
Cdd:cd24126 318 EGLYNTREILSD-LGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKleRL----RTTVGMDGTVYKTHP 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 330730814 449 QYRQYMQDALVELLGhklASHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24126 393 QYAKRLHKVVRRLVP---SCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
58-488 |
3.72e-89 |
|
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: 279.46 E-value: 3.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVE--GGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLateSEQISIS 135
Cdd:cd24129 7 LAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQIT---SEIYSIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVAKEKPgrflleEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24129 84 ETVAQGTGQQLFDHIVDCIVDFQQKQGL------SGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEA-MEAHGLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGF--- 291
Cdd:cd24129 158 REAaTRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGV--PGDSGRMCINMEWGAFgdn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 292 -SKILPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQEDnT 370
Cdd:cd24129 236 gCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESD-S 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 371 DDLRDVGSILYDfLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDtkRMGSGKRTVVAMDGALYEKYPQY 450
Cdd:cd24129 315 LALRQVRAILED-LGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMREN--RGLDELAVTVGVDGTLYKLHPRF 391
|
410 420 430
....*....|....*....|....*....|....*...
gi 330730814 451 RQYMQDALVELLGHklaSHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24129 392 SSLVQATVRELAPR---CVVTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
58-488 |
4.70e-89 |
|
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: 279.09 E-value: 4.70e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVE--GGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQISIS 135
Cdd:cd24128 7 LLEVKRRMKVEMERGLSKEthASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNKIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVakekpgRFLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24128 87 QEVMHGTGEELFDHIVHCIADFL------EYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEAMEAH-GLDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGFSKI 294
Cdd:cd24128 161 KEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELV--EGEEGRMCVNMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 295 LP----QTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQEDNT 370
Cdd:cd24128 239 GClddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 371 dDLRDVGSILyDFLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDtkRMGSGKRTVVAMDGALYEKYPQY 450
Cdd:cd24128 319 -ALLQVRAIL-QHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIREN--RGLDALKVTVGVDGTLYKLHPHF 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 330730814 451 RQYMQDALVELLGHklaSHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24128 395 AKVMHETVKDLAPK---CDVSFLQSEDGSGKGAALITA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
43-244 |
1.48e-86 |
|
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: 264.37 E-value: 1.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 43 ILTKFQKDCATPTPYLRNVANAIADDMRDGLAVEGGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGkkE 122
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGG--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 123 RVLATESEQISISQKLMIGTSEELFGFIASKLANFVAKEKPGRFlleEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFK 202
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF---EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 330730814 203 VSGMEGKNVVACLNEAMEAHGLDMRVSALVNDGVGTLAGARY 244
Cdd:pfam00349 156 IPGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
58-488 |
1.09e-85 |
|
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: 271.88 E-value: 1.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVEGG--GDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQISIS 135
Cdd:cd24124 35 LIDIMTRFRKEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVAKEKPgrflleEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24124 115 ENIVHGSGSQLFDHVAECLGDFMEKRKI------KDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEAMEAHG-LDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGF--- 291
Cdd:cd24124 189 NKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLV--EGDEGRMCINTEWGAFgdd 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 292 -SKILPQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLF-GHFAPaKLSTPLALRTEHLCKMqEDN 369
Cdd:cd24124 267 gSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFeGRITP-ELLTRGKFNTSDVSAI-EKN 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 370 TDDLRDVGSILYDfLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIeKDTKrmGSGK-RTVVAMDGALYEKYP 448
Cdd:cd24124 345 KEGLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRL-RDNK--GTPRlRTTVGVDGSLYKTHP 420
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 330730814 449 QYRQYMQDALVELLGHklaSHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24124 421 QYSRRFHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
58-488 |
3.77e-83 |
|
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: 263.72 E-value: 3.77e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVE--GGGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKeRVLATESEQISIS 135
Cdd:cd24130 7 LQEVKQKMRTELEYGLKKEthPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYNKIFAIP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVakekpgRFLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24130 86 LEIMQGTGEELFDHIVQCIADFL------DYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEAMEAHG-LDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGFSK- 293
Cdd:cd24130 160 REAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIV--EGDEGRMCINTEWGGFGDn 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 294 -----IlpQTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQED 368
Cdd:cd24130 238 gciddI--RTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 369 NTdDLRDVGSILYDfLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKDtkRMGSGKRTVVAMDGALYEKYP 448
Cdd:cd24130 316 RL-ALLQVRRILQQ-LGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIREN--QGLDRLDITVGVDGTLYKLHP 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 330730814 449 QYRQYMQDALVELLGHklaSHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24130 392 HFSRILQETVKELAPQ---CDVTFMLSEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
58-488 |
1.13e-82 |
|
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: 262.89 E-value: 1.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVEG--GGDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKER--VLATESEQIS 133
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGqwSVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 134 ISQKLMIGTSEELFGFIASKLANFVAKEKpgrfllEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVA 213
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFLDKHQ------MKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 214 CLNEAMEAHG-LDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGFS 292
Cdd:cd24092 170 LLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELV--EGDEGRMCVNTEWGAFG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 293 KILPQTIFDLE----MDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQED 368
Cdd:cd24092 248 DSGELDEFLLEydrlVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 369 nTDDLRDVGSILYDF--LDVEANMNARRRvveVCDTVVKRGGRLAGAGIVAILEKIeKDTKRMGSGKRTvVAMDGALYEK 446
Cdd:cd24092 328 -TGDRKQIYNILSTLglRPSTTDCDIVRR---ACESVSTRAAHMCSAGLAGVINRM-RESRSEDVMRIT-VGVDGSVYKL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 330730814 447 YPQYRQYMQDALVELLGHklaSHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24092 402 HPSFKERFHASVRRLTPS---CEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
58-488 |
2.14e-81 |
|
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: 259.06 E-value: 2.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 58 LRNVANAIADDMRDGLAVEGG--GDLEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQISIS 135
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 136 QKLMIGTSEELFGFIASKLANFVAKekpgrfLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACL 215
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDK------LQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 216 NEAMEAHG-LDMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGFSK- 293
Cdd:cd24125 161 RKAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLV--EGDEGRMCINMEWGAFGDd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 294 -ILP--QTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQEDNt 370
Cdd:cd24125 239 gSLDdiRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEK- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 371 DDLRDVGSILYDfLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIE--KDTKRMgsgkRTVVAMDGALYEKYP 448
Cdd:cd24125 318 DGIRKAREVLMR-LGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKenKGEERL----RSTIGVDGSVYKKHP 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 330730814 449 QYRQYMQDALVELLGHklaSHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24125 393 HFARRLHKTVRRLVPG---CDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
81-488 |
1.93e-80 |
|
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: 256.76 E-value: 1.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 81 LEMILTFVDALPSGNEEGLFYALDLGGTNFRVRSVQLGGKKERVLATESEQISISQKLMIGTSEELFGFIASKLANFVak 160
Cdd:cd24127 32 VKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFL-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 161 ekpgRFLLEEGRKRELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEGKNVVACLNEAMEAHG-LDMRVSALVNDGVGTL 239
Cdd:cd24127 110 ----DYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLRDAIKRREeFDLDVVAVVNDTVGTM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 240 AGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTEWGGF--SKILP--QTIFDLEMDETSLNPGEHL 315
Cdd:cd24127 186 MTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMV--EGDQGQMCINMEWGAFgdNGCLDdiRTHYDRLVDEYSLNAGKQR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 316 YEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLCKMQEDNTdDLRDVGSILYDfLDVEANMNARRR 395
Cdd:cd24127 264 YEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL-ALLQVRAILQQ-LGLNSTCDDSIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 396 VVEVCDTVVKRGGRLAGAGIVAILEKIEKDtkRMGSGKRTVVAMDGALYEKYPQYRQYMQDALVELlghKLASHVAIKHT 475
Cdd:cd24127 342 VKTVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKLHPHFSRIMHQTVKEL---SPKCNVSFLLS 416
|
410
....*....|...
gi 330730814 476 KDVSGLGAALLAA 488
Cdd:cd24127 417 EDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
54-488 |
2.00e-74 |
|
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: 240.98 E-value: 2.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 54 PTPYLRNVANAIADDMRDGLAVEGGGD--LEMILTFVDALPSGNEEGLFYALDLGGTNFRVRS--VQLGGKKERVLATES 129
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASPApaVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVlwVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 130 EQISISQKLMIGTSEELFGFIASKLANFV-AKEKPGRFLleegrkrELGFTFSFPVKQTSIDSGTLSKWTKGFKVSGMEG 208
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLdGQPVPKQGL-------QLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 209 KNVVACLNEAMEAHGL-DMRVSALVNDGVGTLAGARYWDEDVMVGVILGTGTNACYVEQKHAIPKLrsKSSSGTTIINTE 287
Cdd:cd24090 156 QDVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVL--DEDRGRVCVSVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 288 WGGFS---KILP-QTIFDLEMDETSLNPGEHLYEKMISGMYLGEIVRRVLLHMCETSDLFGHFAPAKLSTPLALRTEHLC 363
Cdd:cd24090 234 WGSFSddgALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330730814 364 KMqEDNTDDLRDVGSILYDfLDVEANMNARRRVVEVCDTVVKRGGRLAGAGIVAILEKIEKdtKRMGSGKRTVVAMDGAL 443
Cdd:cd24090 314 EM-EDPSAGAARVRAILQD-LGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQH--SREQQTLQVAVATGGRV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 330730814 444 YEKYPQYRQYMQdALVELLGHKlaSHVAIKHTKDVSGLGAALLAA 488
Cdd:cd24090 390 CERHPRFCSILQ-GTVMLLAPE--CDVSFIPSVDGGGRGVAMVTA 431
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
215-264 |
2.15e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 40.25 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 330730814 215 LNEAMEAHGLDMRVsALVNDGVGTLAGArYWDEDVMVgVILGTGTNACYV 264
Cdd:COG2971 83 LEAALRELFPFARV-VVVNDALAALAGA-LGGEDGIV-VIAGTGSIAAGR 129
|
|
| |
