|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02914 |
PLN02914 |
hexokinase |
1-490 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 949.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 1 MSVATTTSPAVGSFCVSRSRRRLSPMRMAVRSNVVSVAPILTKLQKECATPLPVLRQVADAMTADMRAGLEADGASDLKM 80
Cdd:PLN02914 1 MFSSPVVTPAIGSFTFSSRPRRRPRSRMAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 81 ILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIPQELMFGTSEELFDFIASGLANFAQKEGG 160
Cdd:PLN02914 81 ILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 161 KFHLPHGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLNEAMKRRGLDMRVSALVNDTVGTLAGARY 240
Cdd:PLN02914 161 KFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 241 WDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSSSRRTIVNTEWGAFSTGIPLTEFDREMDAASINPGEQIFEKTISGM 320
Cdd:PLN02914 241 WDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSSGRTIINTEWGAFSDGLPLTEFDREMDAASINPGEQIFEKTISGM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 321 YLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNSDDLQSVGSILCNVLGAESSSSARKIVVEVCDTI 400
Cdd:PLN02914 321 YLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 401 VKRGGRLAGAGIVGILQKMEEDSKGLIFGKRTVVAMDGGLYEHYPQYRRYLQEAVTEILGLEISKNIVIEHSKDGSGIGA 480
Cdd:PLN02914 401 VKRGGRLAGAGIVGILEKMEEDSKGMIFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGA 480
|
490
....*....|
gi 643728993 481 ALLAATNSKY 490
Cdd:PLN02914 481 ALLAATNSKY 490
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
50-487 |
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: 749.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 50 TPLPVLRQVADAMTADMRAGLEADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQV 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 130 SIPQELMFGTSEELFDFIASGLANFAQKEGGKFHlPHGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVA 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 210 CLNEAMKRRGLDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSSSRRTIVNTEWGAF- 288
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 289 STGIPLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNSD 368
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 369 DLQSVGSILCNVLGAESSS-SARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDSKGLIFGKRTVVAMDGGLYEHYPQY 447
Cdd:cd24020 320 DLETVARILKDALGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 643728993 448 RRYLQEAVTEILGLEISKNIVIEHSKDGSGIGAALLAATN 487
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02405 |
PLN02405 |
hexokinase |
1-490 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 625.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 1 MSVATTTSPAVGSFCVSRSRRRLSPMRMAVRsnvvsVAPILTKLQKECATPLPVLRQVADAMTADMRAGLEADGASDLKM 80
Cdd:PLN02405 6 VGAAVVCAAAVCAAAALVVRRRMKSSGKWAR-----AMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 81 ILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIPQELMFGTSEELFDFIASGLANFAQKEGG 160
Cdd:PLN02405 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 161 KFHLPHGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLNEAMKRRGLDMRVSALVNDTVGTLAGARY 240
Cdd:PLN02405 161 DFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 241 WDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSSSRRTIVNTEWGAF-STGIPLTEFDREMDAASINPGEQIFEKTISG 319
Cdd:PLN02405 241 YNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFrSSHLPLTEYDHALDVESLNPGEQIFEKIISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 320 MYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNSDDLQSVGSILCNVLGAESSS-SARKIVVEVCD 398
Cdd:PLN02405 321 MYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSlKMRKVVVELCN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 399 TIVKRGGRLAGAGIVGILQKMEEDSKGLIFGKRTVVAMDGGLYEHYPQYRRYLQEAVTEILGLEISKNIVIEHSKDGSGI 478
Cdd:PLN02405 401 IVATRGARLSAAGIYGILKKLGRDTVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGI 480
|
490
....*....|..
gi 643728993 479 GAALLAATNSKY 490
Cdd:PLN02405 481 GAALLAASHSLY 492
|
|
| PLN02362 |
PLN02362 |
hexokinase |
27-493 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 537.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 27 RMAVRSNVVSVAPILTKLQKECATPLPVLRQVADAMTADMRAGLEADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTN 106
Cdd:PLN02362 27 RVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 107 FRVLRVQLGGKEERVVATEFEQVSIPQELMFGTSEELFDFIASGLANFAQKEGGKFHLPHGREREIGFTFSFPVKQTSVD 186
Cdd:PLN02362 107 FRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEENGSEFSQVRRRELGFTFSFPVKQTSIS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 187 SGILIKWTKGFAVSGTAGRDVVACLNEAMKRRGLDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAI 266
Cdd:PLN02362 187 SGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 267 PKLQGPKSSSRRTIVNTEWGAF-STGIPLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKfVP 345
Cdd:PLN02362 267 IKCQGLLTTSGSMVVNMEWGNFwSSHLPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGP-VS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 346 EKLSTPFALCTPDLCAMQQDNSDDLQSVGSILCNVLG-AESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDSK 424
Cdd:PLN02362 346 SRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGiSEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGRDGS 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 643728993 425 GLIFG----------KRTVVAMDGGLYEHYPQYRRYLQEAVTEILGLEISKNIVIEHSKDGSGIGAALLAATNSKYDHD 493
Cdd:PLN02362 426 GGITSgrsrsdiqimRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVILKATEDGSGIGSALLAASYSSYSVD 504
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
55-484 |
1.42e-169 |
|
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: 484.83 E-value: 1.42e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGLEADGASdLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEfEQVSIPQE 134
Cdd:cd24018 4 LEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQ-RKYKIPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 135 LMFGTSEELFDFIASGLANFAQKEGGKFHLPhgREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLNEA 214
Cdd:cd24018 82 AKTGTGEELFDFIAECIAEFLEEHNLDLQSD--KTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 215 MKRRGLDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSSSRRT---IVNTEWGAF--- 288
Cdd:cd24018 160 LDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPSGSVTKSdemIINTEWGAFdne 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 289 STGIPLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNSD 368
Cdd:cd24018 240 REVLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 369 DLQSVGSILCNVLGAESSSSA-RKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDSKglifgKRTVVAMDGGLYEHYPQY 447
Cdd:cd24018 320 DLDAVRDILKELLAIDNTTLEdRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLP-----EPVTVGIDGSVYEKYPGF 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 643728993 448 RRYLQEAVTEILGLEISKNIVIEHSKDGSGIGAALLA 484
Cdd:cd24018 395 KDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
55-485 |
2.12e-167 |
|
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: 479.35 E-value: 2.12e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGLEADG--ASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLggKEERVVATEFEQVSIP 132
Cdd:cd24019 7 LEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTL--NGGSQVKMESEIYAIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGGKFH-LPhgrereIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACL 211
Cdd:cd24019 85 EEIMTGTGEQLFDYIAECLAEFLEKNGLKDKkLP------LGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 212 NEAMKRRGL-DMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSSSRRTIVNTEWGAFST 290
Cdd:cd24019 159 QEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 291 GIPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDN 366
Cdd:cd24019 239 NGVLdfirTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 367 SDDLQSVGSILCNVLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEdskglifgKRTVVAMDGGLYEHYPQ 446
Cdd:cd24019 319 EGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR--------KEVTVGVDGSLYKYHPK 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 643728993 447 YRRYLQEAVTEILGLEIskNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24019 391 FHKRMHETLKELVPPGC--KFKLMLSEDGSGKGAALVAA 427
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
2-485 |
4.67e-165 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 475.91 E-value: 4.67e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 2 SVATTTSPAVGSFCVSRSRRRLSPMRMAVRSnvvsvapILTKLQKECATPLPVLRQVADAMTADMRAGLEADGASDLKMI 81
Cdd:PLN02596 10 ATVATVAAVAAAVLMGRWKRRKERQWKHTQR-------ILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 82 LSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIPQELMFGTSEELFDFIASGLANFAQKEGGK 161
Cdd:PLN02596 83 VSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 162 FHLPHGREREIGFTFSFPVKQTSVDSGILIKWtKGFAVSGTAGRDVVACLNEAMKRRGLDMRVSALVNDTVGTLAGARYW 241
Cdd:PLN02596 163 EADTPERVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 242 DNDVMVAVILGTGTNACYVERIDAIPKLQGPKSSSRRTIVNTEWGAF-STGIPLTEFDREMDAASINPGEQIFEKTISGM 320
Cdd:PLN02596 242 NKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPESQEIVISTEWGNFnSCHLPITEFDASLDAESSNPGSRIFEKLTSGM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 321 YLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNSDDLQSVGSILCNVLG-AESSSSARKIVVEVCDT 399
Cdd:PLN02596 322 YLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGiTDSTPMAREVVAEVCDI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 400 IVKRGGRLAGAGIVGILQKMeedskGLIFGKRTVVAMDGGLYEHYPQYRRYLQEAVTEILGLEISKNIVIEHSKDGSGIG 479
Cdd:PLN02596 402 VAERGARLAGAGIVGIIKKL-----GRIENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAG 476
|
....*.
gi 643728993 480 AALLAA 485
Cdd:PLN02596 477 ALFLAA 482
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
54-484 |
6.99e-132 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 386.25 E-value: 6.99e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 54 VLRQVADAMTADMRAGLEADGASdLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKeeRVVATEFEQVSIPQ 133
Cdd:cd24000 3 DLKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGK--GIEVTISKKYEIPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 134 ELMFGTSEELFDFIASGLANFAQKEGGKFHLPhgrereIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLNE 213
Cdd:cd24000 80 EIKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLND 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 214 AMKRRGLDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIpklqgpKSSSRRTIVNTEWGAF-STGI 292
Cdd:cd24000 154 ALKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFgKNSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 293 PLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEEsalfgkfvpeklstpfalctpdlcamqqdnsddlqs 372
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 373 vgsilcnvlgaessssarkIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDSKglifgKRTVVAMDGGLYEHYPQYRRYLQ 452
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTGDSPE-----KKITIAVDGSLFEKYPGYRERLE 327
|
410 420 430
....*....|....*....|....*....|..
gi 643728993 453 EAVTEILGLEIskNIVIEHSKDGSGIGAALLA 484
Cdd:cd24000 328 EYLKELLGRGI--RIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
66-484 |
1.10e-118 |
|
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: 355.55 E-value: 1.10e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 66 MRAGLEADGAsDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKeeRVVATEFEQVSIPQELMFG-TSEELF 144
Cdd:cd24088 15 MEKGLAKHGK-GMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGD--GTFSLRQEKSKIPDELKTGvTAKDLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 145 DFIASGLANFAQKEGGKfHLPHGREREI---GFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLNEAMKRRGLD 221
Cdd:cd24088 92 DYLAKSVEAFLTKHHGD-SFAAGKDDDRlklGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDRQGIP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 222 MRVSALVNDTVGTLAGARYWDNDVMVAV---ILGTGTNACYVERIDAIPKL---QGPKSSSRRTIVNTEWGAFSTG---I 292
Cdd:cd24088 171 VKVVALVNDTVGTLLARSYTSPEISGAVlgaIFGTGTNGAYLEDLEKIKKLddsSRVGKGKTHMVINTEWGSFDNElkvL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 293 PLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFV---PEKLSTPFALCTPDLCAMQQDNSDD 369
Cdd:cd24088 251 PTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNdksPSALNTPYGLDTAVLSAIEIDSEAE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 370 LQSVGSILCNVLGAESSS-SARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDSKGliFGKRTVVAMDGGLYEHYPQYR 448
Cdd:cd24088 331 LRATRKVLLDDLGLPAPSlEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKS--YDGEINIGVDGSVIEFYPGFE 408
|
410 420 430
....*....|....*....|....*....|....*..
gi 643728993 449 RYLQEAVTEIL-GLEISKNIVIEHSKDGSGIGAALLA 484
Cdd:cd24088 409 SMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
55-485 |
4.51e-117 |
|
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: 351.00 E-value: 4.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGLEADGASD--LKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIP 132
Cdd:cd24089 7 LLDISRRFRKEMEKGLGKDTHPTatVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGgkfhlPHGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLN 212
Cdd:cd24089 87 EEIMHGSGTQLFDHVAECLADFMDKQK-----IKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 213 EAMKRRG-LDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSssrRTIVNTEWGAFSTG 291
Cdd:cd24089 162 KAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEG---RMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 292 IPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMqQDNS 367
Cdd:cd24089 239 GSLedirTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAI-EKEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 368 DDLQSVGSILcNVLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDSKglIFGKRTVVAMDGGLYEHYPQY 447
Cdd:cd24089 318 EGLANAKEIL-TRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKG--LERLRTTVGVDGSVYKKHPQF 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 643728993 448 RRYLQEAVTEilgLEISKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24089 395 SKRLHKAVRR---LVPDCDVRFLLSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
55-485 |
1.33e-116 |
|
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: 349.75 E-value: 1.33e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGLEADGAsDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGkeervvATEFE----QVS 130
Cdd:cd24087 4 LRKITDHFISELEKGLSKKGG-NIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGG------NGKFDitqsKYR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 131 IPQELMFGTSEELFDFIASGLANFAqkeggKFHLPHGRER--EIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVV 208
Cdd:cd24087 77 LPEELKTGTGEELWDFIADCLKKFV-----EEHFPGGKSEplPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 209 ACLNEAMKRRGLDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQG---PKSSSrrTIVNTEW 285
Cdd:cd24087 152 PMLQKALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHddiPPDSP--MAINCEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 286 GAFSTG---IPLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAM 362
Cdd:cd24087 230 GAFDNEhlvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 363 QQDNSDDLQSVGSILCNVLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMeedskglifGKRTV-VAMDGGLY 441
Cdd:cd24087 310 EEDPFENLEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKR---------GYKTChVAADGSVY 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 643728993 442 EHYPQYRRYLQEAVTEILGLEIS-KNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24087 381 NKYPGFKERAAQALKDIFGWDGEdDPIKTVPAEDGSGVGAAIIAA 425
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
54-488 |
2.25e-116 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 350.52 E-value: 2.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 54 VLRQVADAMTADMRAGLEA---------DGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQL--GGKEERVv 122
Cdd:PTZ00107 24 KLKELVDYFLYELVEGLEAhrrhrnlwiPNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLrgGGKMERT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 123 ateFEQVSIPQELMFG---------TSEELFDFIASGLANFAQKEGGkfHLPHGREREIGFTFSFPVKQTSVDSGILIKW 193
Cdd:PTZ00107 103 ---QSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGD--PEDLNKPVPVGFTFSFPCTQLSVNNAILIDW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 194 TKGFAVS-----GTAGRDVVACLNEAMKRRGLDMRVSALVNDTVGTLAGARYWDN----DVMVAVILGTGTNACYVErid 264
Cdd:PTZ00107 178 TKGFETGratndPVEGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYQKPkntpPCQVGVIIGTGSNACYFE--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 265 aipklqgPKSSSRR---TIVNTEWGAFSTGIPLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESAlfg 341
Cdd:PTZ00107 255 -------PEVSAYGyagTPINMECGNFDSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKA--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 342 kfvPEKLSTPFALCTPDLCAMQQDNSDDLQSVGSILCNVLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEe 421
Cdd:PTZ00107 325 ---PPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKTR- 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 643728993 422 dskglIFGKRTVVAMDGGLYEHYPQYRRYLQEAVTEILGlEISKNIVIEHSKDGSGIGAALLAATNS 488
Cdd:PTZ00107 401 -----TVQGKATVAIDGSVYVKNPWFRRLLQEYINSILG-PDAGNVVFYLADDGSGKGAAIIAAMVA 461
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
55-485 |
6.55e-112 |
|
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: 337.98 E-value: 6.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGL--EADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIP 132
Cdd:cd24091 7 LLEVKARMRAEMERGLrkETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGGKfhlphGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLN 212
Cdd:cd24091 87 QEIMQGTGEELFDHIVQCIADFLEYMGLK-----GVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 213 EAMKRRG-LDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGpksSSRRTIVNTEWGAFSTG 291
Cdd:cd24091 162 EAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 292 IPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNS 367
Cdd:cd24091 239 GCLddirTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 368 DDLQsVGSILCNvLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDsKGLIFGKRTvVAMDGGLYEHYPQY 447
Cdd:cd24091 319 ALLQ-VRAILQQ-LGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIREN-RGLDHLNVT-VGVDGTLYKLHPHF 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 643728993 448 RRYLQEAVTEilgLEISKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24091 395 SRVMHETVKE---LAPKCDVTFLQSEDGSGKGAALITA 429
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
55-487 |
3.04e-111 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 336.16 E-value: 3.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGLEaDGASDLKMILSYVdSLPSG-NEKGLFYALDLGGTNFRVLRVQLGGKEERVVateFEQVSIPq 133
Cdd:COG5026 22 LEEIAAKFQEEMEKGLE-GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFEI---ENFKSFP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 134 elMFGTS-----EELFDFIASGLANFAQKEggkfhlphgreREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVV 208
Cdd:COG5026 96 --LPGTSseitaEEFFDFIADYIEPLLDES-----------YKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 209 ACLNEAMKRRGLD-MRVSALVNDTVGTLAGARYWDNDVM----VAVILGTGTNACYVERIDAIPKLQGPKSSsrrTIVNT 283
Cdd:COG5026 163 ELLEAALARKGLDnVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKLPAYEGP---MIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 284 EWGAFStGIPLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEEsALFGKFVPEKLSTPFALCTPDLCAMQ 363
Cdd:COG5026 240 ESGNFN-KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAE-GLFSPGFSEVFETPYSLTTVDMSRFL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 364 QDNSDDLQSVGSILcnvlgAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEedsKGLIFGKRTVVAMDGGLYEH 443
Cdd:COG5026 318 ADPSDEKEILSQCL-----EAGSEEDREILREIADAIVERAARLVAATLAGILLHLG---PGKTPLKPHCIAIDGSTYEK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 643728993 444 YPQYRRYLQEAVTEILGLEISKNIVIEHSKDGSGIGAALLAATN 487
Cdd:COG5026 390 MPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAALN 433
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
54-485 |
1.20e-107 |
|
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: 326.81 E-value: 1.20e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 54 VLRQVADAMTADMRAGLEADG--ASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSI 131
Cdd:cd24126 6 TLLDIMTRFRAEMEKGLAKDTnpTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 132 PQELMFGTSEELFDFIASGLANFAQKEggkfHLPHGReREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACL 211
Cdd:cd24126 86 PEEIIHGTGTELFDYVAECLADFMKKK----GIKHKK-LPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 212 NEAMKRRG-LDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSssrRTIVNTEWGAFST 290
Cdd:cd24126 161 RKAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEG---RMCINTEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 291 GIPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDN 366
Cdd:cd24126 238 DGSLedirTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 367 SdDLQSVGSILCNvLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDSKglIFGKRTVVAMDGGLYEHYPQ 446
Cdd:cd24126 318 E-GLYNTREILSD-LGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKK--LERLRTTVGMDGTVYKTHPQ 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 643728993 447 YRRYLQEAVTEilgLEISKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24126 394 YAKRLHKVVRR---LVPSCDVRFLLSESGSGKGAAMVTA 429
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
246-486 |
3.21e-106 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.
Pssm-ID: 461028 Cd Length: 236 Bit Score: 315.97 E-value: 3.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 246 MVAVILGTGTNACYVERIDAIPKLQGPKSSSRRTIVNTEWGAFSTG----IPLTEFDREMDAASINPGEQIFEKTISGMY 321
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNgllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 322 LGEIARRVLLKMAEESALFgKFVPEKLSTPFALCTPDLCAMQQDNSDDLQSVGSILCNVLGAESSSSA-RKIVVEVCDTI 400
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLF-KGQSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEdRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 401 VKRGGRLAGAGIVGILQKMEEDskglifgKRTVVAMDGGLYEHYPQYRRYLQEAVTEILGLEisKNIVIEHSKDGSGIGA 480
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRD-------KKVTVGVDGSVYEKYPGFRERLQEALRELLGPG--DKVVLVLAEDGSGVGA 230
|
....*.
gi 643728993 481 ALLAAT 486
Cdd:pfam03727 231 ALIAAV 236
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
55-485 |
7.44e-105 |
|
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: 321.18 E-value: 7.44e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGLEAD--GASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIP 132
Cdd:cd24124 35 LIDIMTRFRKEMKNGLSRDfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGGKfhlphGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLN 212
Cdd:cd24124 115 ENIVHGSGSQLFDHVAECLGDFMEKRKIK-----DKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 213 EAMKRRG-LDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSssrRTIVNTEWGAFSTG 291
Cdd:cd24124 190 KAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEG---RMCINTEWGAFGDD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 292 IPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALF-GKFVPEkLSTPFALCTPDLCAMQQdN 366
Cdd:cd24124 267 GSLedirTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFeGRITPE-LLTRGKFNTSDVSAIEK-N 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 367 SDDLQSVGSILCNvLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMeEDSKGlIFGKRTVVAMDGGLYEHYPQ 446
Cdd:cd24124 345 KEGLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRL-RDNKG-TPRLRTTVGVDGSLYKTHPQ 421
|
410 420 430
....*....|....*....|....*....|....*....
gi 643728993 447 YRRYLQEAVTEILGleiSKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24124 422 YSRRFHKTLRRLVP---DSDVRFLLSESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
55-485 |
5.57e-103 |
|
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: 314.90 E-value: 5.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGL--EADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVAtefEQVSIP 132
Cdd:cd24129 7 LAAVQAQMRKEMAKGLrgETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITS---EIYSIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGGKfhlphGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLN 212
Cdd:cd24129 84 ETVAQGTGQQLFDHIVDCIVDFQQKQGLS-----GQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 213 EAMKRR-GLDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGpksSSRRTIVNTEWGAF--- 288
Cdd:cd24129 159 EAATRKqAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPG---DSGRMCINMEWGAFgdn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 289 -STGIPLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDnS 367
Cdd:cd24129 236 gCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESD-S 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 368 DDLQSVGSILCNvLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDsKGLIFGKRTvVAMDGGLYEHYPQY 447
Cdd:cd24129 315 LALRQVRAILED-LGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMREN-RGLDELAVT-VGVDGTLYKLHPRF 391
|
410 420 430
....*....|....*....|....*....|....*...
gi 643728993 448 RRYLQEAVTEilgLEISKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24129 392 SSLVQATVRE---LAPRCVVTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
55-485 |
3.10e-102 |
|
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: 313.37 E-value: 3.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGL--EADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIP 132
Cdd:cd24128 7 LLEVKRRMKVEMERGLskETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNKIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGGKfhlphGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLN 212
Cdd:cd24128 87 QEVMHGTGEELFDHIVHCIADFLEYMGMK-----GVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 213 EAMKRR-GLDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSssrRTIVNTEWGAFSTG 291
Cdd:cd24128 162 EAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEG---RMCVNMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 292 IPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNS 367
Cdd:cd24128 239 GCLddfrTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 368 DDLQsVGSILCNvLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDsKGLIFGKRTvVAMDGGLYEHYPQY 447
Cdd:cd24128 319 ALLQ-VRAILQH-LGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIREN-RGLDALKVT-VGVDGTLYKLHPHF 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 643728993 448 RRYLQEAVTEilgLEISKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24128 395 AKVMHETVKD---LAPKCDVSFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
55-489 |
2.95e-100 |
|
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: 308.35 E-value: 2.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGL--EADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEER--VVATEFEQVS 130
Cdd:cd24092 16 LKKVMRRMQKEMDRGLrlETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGqwSVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 131 IPQELMFGTSEELFDFIASGLANFAQKEGGKFH-LPhgrereIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVA 209
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFLDKHQMKHKkLP------LGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 210 CLNEAMKRRG-LDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSssrRTIVNTEWGAF 288
Cdd:cd24092 170 LLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEG---RMCVNTEWGAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 289 STGIPLTEF----DREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQ 364
Cdd:cd24092 247 GDSGELDEFlleyDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVES 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 365 DNSDDLQSVGSILCnvLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDSKGLIFgkRTVVAMDGGLYEHY 444
Cdd:cd24092 327 DTGDRKQIYNILST--LGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVM--RITVGVDGSVYKLH 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 643728993 445 PQYRRYLQEAVTEilgLEISKNIVIEHSKDGSGIGAALLAATNSK 489
Cdd:cd24092 403 PSFKERFHASVRR---LTPSCEITFIESEEGSGRGAALVSAVACK 444
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
55-485 |
1.10e-99 |
|
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: 306.44 E-value: 1.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGLEADG--ASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIP 132
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATThpTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGGKfhlphGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLN 212
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDKLQIK-----DKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 213 EAMKRRG-LDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSssrRTIVNTEWGAFSTG 291
Cdd:cd24125 162 KAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEG---RMCINMEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 292 IPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALF-GKFVPEKLSTPFaLCTPDLCAMQQDn 366
Cdd:cd24125 239 GSLddirTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFgGKLSPELLNTGH-FETKDVSDIEGE- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 367 SDDLQSVGSILCNvLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDsKGLIfGKRTVVAMDGGLYEHYPQ 446
Cdd:cd24125 317 KDGIRKAREVLMR-LGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKEN-KGEE-RLRSTIGVDGSVYKKHPH 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 643728993 447 YRRYLQEAVTEILGleiSKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24125 394 FARRLHKTVRRLVP---GCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
55-485 |
1.63e-98 |
|
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: 303.39 E-value: 1.63e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGL--EADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEeRVVATEFEQVSIP 132
Cdd:cd24130 7 LQEVKQKMRTELEYGLkkETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYNKIFAIP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGGKfhlphGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLN 212
Cdd:cd24130 86 LEIMQGTGEELFDHIVQCIADFLDYMGLK-----GARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 213 EAMKRRG-LDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSssrRTIVNTEWGAFSTG 291
Cdd:cd24130 161 EAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEG---RMCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 292 IPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNS 367
Cdd:cd24130 238 GCIddirTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 368 DDLQsVGSILcNVLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDsKGLIFGKRTvVAMDGGLYEHYPQY 447
Cdd:cd24130 318 ALLQ-VRRIL-QQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIREN-QGLDRLDIT-VGVDGTLYKLHPHF 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 643728993 448 RRYLQEAVTEilgLEISKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24130 394 SRILQETVKE---LAPQCDVTFMLSEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
55-485 |
1.06e-97 |
|
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: 301.45 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 55 LRQVADAMTADMRAGL--EADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKEERVVATEFEQVSIP 132
Cdd:cd24127 7 LLEVKKRMRAEMELGLrkQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 133 QELMFGTSEELFDFIASGLANFAQKEGGKfhlphGREREIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGRDVVACLN 212
Cdd:cd24127 87 IEIMQGTGEELFDHIVSCISDFLDYMGIK-----GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 213 EAMKRRG-LDMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQGPKSssrRTIVNTEWGAFSTG 291
Cdd:cd24127 162 DAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQG---QMCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 292 IPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLCAMQQDNS 367
Cdd:cd24127 239 GCLddirTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 368 DDLQsVGSILcNVLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEDsKGLIFGKRTvVAMDGGLYEHYPQY 447
Cdd:cd24127 319 ALLQ-VRAIL-QQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIREN-RGLDHLNVT-VGVDGTLYKLHPHF 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 643728993 448 RRYLQEAVTEilgLEISKNIVIEHSKDGSGIGAALLAA 485
Cdd:cd24127 395 SRIMHQTVKE---LSPKCNVSFLLSEDGSGKGAALITA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
40-240 |
2.42e-95 |
|
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: 286.71 E-value: 2.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 40 ILTKLQKECATPLPVLRQVADAMTADMRAGLEADGASDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGkeE 119
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGG--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 120 RVVATEFEQVSIPQELMFGTSEELFDFIASGLANFAQKEGGKFHlpHGREREIGFTFSFPVKQTSVDSGILIKWTKGFAV 199
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF--EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 643728993 200 SGTAGRDVVACLNEAMKRRGLDMRVSALVNDTVGTLAGARY 240
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-485 |
8.08e-80 |
|
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: 255.23 E-value: 8.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 51 PLPVLRQVADAMTADMRAGL--EADGASDLKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKEERVVATEF 126
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALrgQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 127 EQVSIPQELMFGTSEELFDFIASGLANFAQKeggkfhLPHGRER-EIGFTFSFPVKQTSVDSGILIKWTKGFAVSGTAGR 205
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDG------QPVPKQGlQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 206 DVVACLNEAMKRRGL-DMRVSALVNDTVGTLAGARYWDNDVMVAVILGTGTNACYVERIDAIPKLQgpkSSSRRTIVNTE 284
Cdd:cd24090 157 DVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD---EDRGRVCVSVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 285 WGAFST----GIPLTEFDREMDAASINPGEQIFEKTISGMYLGEIARRVLLKMAEESALFGKFVPEKLSTPFALCTPDLC 360
Cdd:cd24090 234 WGSFSDdgalGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 361 AMqQDNSDDLQSVGSILcNVLGAESSSSARKIVVEVCDTIVKRGGRLAGAGIVGILQKMEEdSKGLIfGKRTVVAMDGGL 440
Cdd:cd24090 314 EM-EDPSAGAARVRAIL-QDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQH-SREQQ-TLQVAVATGGRV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 643728993 441 YEHYPQYRRYLQEaVTEILGLEISKNIVieHSKDGSGIGAALLAA 485
Cdd:cd24090 390 CERHPRFCSILQG-TVMLLAPECDVSFI--PSVDGGGRGVAMVTA 431
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
92-260 |
4.52e-04 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 42.19 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 92 NEKGLFYALDLGGTNFRVLRVQLGGKeerVVATefEQVSIPQElmfGTSEELFDFIASGLANFAQKEGGKFHLPHGrere 171
Cdd:COG1940 2 PDAGYVIGIDIGGTKIKAALVDLDGE---VLAR--ERIPTPAG---AGPEAVLEAIAELIEELLAEAGISRGRILG---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643728993 172 IGFTFSFPV---KQTSVDSGILIKWTkgfavsgtaGRDVVACLNEAmkrrgLDMRVsALVND-TVGTLAGARYW---DND 244
Cdd:COG1940 70 IGIGVPGPVdpeTGVVLNAPNLPGWR---------GVPLAELLEER-----LGLPV-FVENDaNAAALAEAWFGagrGAD 134
|
170
....*....|....*.
gi 643728993 245 VMVAVILGTGTNACYV 260
Cdd:COG1940 135 NVVYLTLGTGIGGGIV 150
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
196-262 |
2.01e-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: 2.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 643728993 196 GFAVSGTAGRDVVACLNEAMKRRGLDMRVsALVNDTVGTLAGArYWDNDVmVAVILGTGTNACYVER 262
Cdd:COG2971 68 GFGLAGAGTPEDAEALEAALRELFPFARV-VVVNDALAALAGA-LGGEDG-IVVIAGTGSIAAGRDG 131
|
|
| |
