|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02914 |
PLN02914 |
hexokinase |
1-490 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 956.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 1 MSVAATTSPAVGTLYVSRFPwsRGMPRVTMALRSNVVSVGSILTKLQQDCATPFPVIRHVADSMTADMRAGLAVDGGSNL 80
Cdd:PLN02914 1 MFSSPVVTPAIGSFTFSSRP--RRRPRSRMAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 81 KMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIPQELMFGTSEELFDFIASTLAGFAEKE 160
Cdd:PLN02914 79 KMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 161 SEKFHLPHGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEAMERQGVDMRVSALVNDTVGTLAGA 240
Cdd:PLN02914 159 GGKFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 241 RYWDDDVLVAVILGTGTNACYVERTDCIPKLQGPKSSSGRTIINTEWGAFSDGIPLTAFDRDMDAASINPGEQIFEKTIS 320
Cdd:PLN02914 239 RYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSSGRTIINTEWGAFSDGLPLTEFDREMDAASINPGEQIFEKTIS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 321 GMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKSDDLQAVGSILHNVAGVESSLSERRIVLEVCD 400
Cdd:PLN02914 319 GMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 401 AIVKRGGRLAGAGIVGILQKMEQDSKGTIFNKRTVVAMDGGLYEHYPQYRSYLQDAVTELLGSETSKNIVIEHSKDGSGI 480
Cdd:PLN02914 399 TIVKRGGRLAGAGIVGILEKMEEDSKGMIFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGI 478
|
490
....*....|
gi 1939215936 481 GAALLAATNS 490
Cdd:PLN02914 479 GAALLAATNS 488
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
52-489 |
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: 732.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 52 TPFPVIRHVADSMTADMRAGLAVDGGSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQL 131
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 132 SIPQELMFGTSEELFDFIASTLAGFAEKESEKFHlPHGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVA 211
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 212 CLNEAMERQGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGPKSSSGRTIINTEWGAF- 290
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 291 SDGIPLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKSD 370
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 371 DLQAVGSILHNVAGVE-SSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKGTIFNKRTVVAMDGGLYEHYPQY 449
Cdd:cd24020 320 DLETVARILKDALGIDdTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1939215936 450 RSYLQDAVTELLGSETSKNIVIEHSKDGSGIGAALLAATN 489
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02405 |
PLN02405 |
hexokinase |
41-490 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 631.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 41 SILTKLQQDCATPFPVIRHVADSMTADMRAGLAVDGGSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKE 120
Cdd:PLN02405 39 EILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 121 ERVVATEFEQLSIPQELMFGTSEELFDFIASTLAGFAEKESEKFHLPHGRQREIGFTFSFPVKQTSIDSGILMKWTKGFA 200
Cdd:PLN02405 119 GRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGEDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 201 VSGTAGRDVVACLNEAMERQGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGPKSSSGR 280
Cdd:PLN02405 199 IDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 281 TIINTEWGAF-SDGIPLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTP 359
Cdd:PLN02405 279 MVINMEWGNFrSSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 360 DICAMQQDKSDDLQAVGSILHNVAGV-ESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKGTIFNKRTVVAM 438
Cdd:PLN02405 359 DMSAMHHDTSPDLKVVGSKLKDILEIpNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDTVKDGEKQKSVIAM 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1939215936 439 DGGLYEHYPQYRSYLQDAVTELLGSETSKNIVIEHSKDGSGIGAALLAATNS 490
Cdd:PLN02405 439 DGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGIGAALLAASHS 490
|
|
| PLN02362 |
PLN02362 |
hexokinase |
3-491 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 532.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 3 VAATTSPAVGTLYVSRFPWSRGMPRvtmalrsnvvSVGSILTKLQQDCATPFPVIRHVADSMTADMRAGLAVDGGSNLKM 82
Cdd:PLN02362 11 AAAVAACAVAAVMVGRRVKSRRKWR----------RVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 83 ILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIPQELMFGTSEELFDFIASTLAGFAEKESE 162
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 163 KFHLPHGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEAMERQGVDMRVSALVNDTVGTLAGARY 242
Cdd:PLN02362 161 GSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 243 WDDDVLVAVILGTGTNACYVERTDCIPKLQGPKSSSGRTIINTEWGAF-SDGIPLTAFDRDMDAASINPGEQIFEKTISG 321
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFwSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 322 MYLGEIARRALVSMAEEGSLFGmAVPNKLSTPFALRTPDICAMQQDKSDDLQAVGSILHNVAGV-ESSLSERRIVLEVCD 400
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFG-PVSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGIsEVPLKVRKLVVKICD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 401 AIVKRGGRLAGAGIVGILQKMEQDSKGTIFN----------KRTVVAMDGGLYEHYPQYRSYLQDAVTELLGSETSKNIV 470
Cdd:PLN02362 400 VVTRRAARLAAAGIVGILKKIGRDGSGGITSgrsrsdiqimRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVI 479
|
490 500
....*....|....*....|.
gi 1939215936 471 IEHSKDGSGIGAALLAATNSN 491
Cdd:PLN02362 480 LKATEDGSGIGSALLAASYSS 500
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
57-486 |
1.21e-167 |
|
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: 488.68 E-value: 1.21e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLAVDGGSnLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEfEQLSIPQE 136
Cdd:cd24018 4 LEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQ-RKYKIPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 137 LMFGTSEELFDFIASTLAGFAEKESEKFHLPHGRqrEIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEA 216
Cdd:cd24018 82 AKTGTGEELFDFIAECIAEFLEEHNLDLQSDKTI--PLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 217 MERQGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGPKSSSGRT---IINTEWGAF-SD 292
Cdd:cd24018 160 LDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPSGSVTKSdemIINTEWGAFdNE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 293 G--IPLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKSD 370
Cdd:cd24018 240 RevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 371 DLQAVGSILHNVAGVE-SSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMeqdskGTIFNKRTVVAMDGGLYEHYPQY 449
Cdd:cd24018 320 DLDAVRDILKELLAIDnTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKR-----GSLLPEPVTVGIDGSVYEKYPGF 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 1939215936 450 RSYLQDAVTELLGSETSKNIVIEHSKDGSGIGAALLA 486
Cdd:cd24018 395 KDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
57-487 |
1.18e-161 |
|
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: 473.18 E-value: 1.18e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLAVDG--GSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLggKEERVVATEFEQLSIP 134
Cdd:cd24019 7 LEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTL--NGGSQVKMESEIYAIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 135 QELMFGTSEELFDFIASTLAGFAEKES-EKFHLPhgrqreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACL 213
Cdd:cd24019 85 EEIMTGTGEQLFDYIAECLAEFLEKNGlKDKKLP------LGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 214 NEAMERQG-VDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGPKSSSGRTIINTEWGAFSD 292
Cdd:cd24019 159 QEAIKRRGdIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 293 GIPL----TAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDK 368
Cdd:cd24019 239 NGVLdfirTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 369 SDDLQAVGSILHNVAGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEqdskgtifNKRTVVAMDGGLYEHYPQ 448
Cdd:cd24019 319 EGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN--------RKEVTVGVDGSLYKYHPK 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 1939215936 449 YRSYLQDAVTELLGSETskNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24019 391 FHKRMHETLKELVPPGC--KFKLMLSEDGSGKGAALVAA 427
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
42-492 |
3.64e-160 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 471.67 E-value: 3.64e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 42 ILTKLQQDCATPFPVIRHVADSMTADMRAGLAVDGGSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEE 121
Cdd:PLN02596 41 ILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 122 RVVATEFEQLSIPQELMFGTSEELFDFIASTLAGF-AEKESEKFHLPHgRQREIGFTFSFPVKQTSIDSGILMKWtKGFA 200
Cdd:PLN02596 121 PISDLYREEISIPSNVLNGTSQELFDYIALELAKFvAEHPGDEADTPE-RVKKLGFTVSYPVDQAAASSGSAIKW-KSFS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 201 VSGTAGRDVVACLNEAMERQGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGPKSSSGR 280
Cdd:PLN02596 199 ADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPESQE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 281 TIINTEWGAF-SDGIPLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTP 359
Cdd:PLN02596 279 IVISTEWGNFnSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 360 DICAMQQDKSDDLQAVGSILHNVAGV-ESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMeqdskGTIFNKRTVVAM 438
Cdd:PLN02596 359 DMAAMHQDTSEDHEVVNEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKL-----GRIENKKSVVTV 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1939215936 439 DGGLYEHYPQYRSYLQDAVTELLGSETSKNIVIEHSKDGSGIGAALLAATNSNN 492
Cdd:PLN02596 434 EGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAACQTGE 487
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
56-486 |
9.73e-123 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 370.45 E-value: 9.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 56 VIRHVADSMTADMRAGLAvDGGSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKeeRVVATEFEQLSIPQ 135
Cdd:cd24000 3 DLKEITDAFLEELEKGLA-GEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGK--GIEVTISKKYEIPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 136 ELMFGTSEELFDFIASTLAGFAEKESEKFHLPhgrqreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNE 215
Cdd:cd24000 80 EIKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLND 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 216 AMERQGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIpklqgpKSSSGRTIINTEWGAFSD-GI 294
Cdd:cd24000 154 ALKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKnSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 295 PLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEgslfgmavpnklstpfalrtpdicamqqdksddlqa 374
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 375 vgsilhnvagvesslserrIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKGTIfnkrtVVAMDGGLYEHYPQYRSYLQ 454
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTGDSPEKKI-----TIAVDGSLFEKYPGYRERLE 327
|
410 420 430
....*....|....*....|....*....|..
gi 1939215936 455 DAVTELLGSEtsKNIVIEHSKDGSGIGAALLA 486
Cdd:cd24000 328 EYLKELLGRG--IRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
68-486 |
3.79e-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: 359.40 E-value: 3.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 68 MRAGLAVDGGSnLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKeeRVVATEFEQLSIPQELMFG-TSEELF 146
Cdd:cd24088 15 MEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGD--GTFSLRQEKSKIPDELKTGvTAKDLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 147 DFIASTLAGFAEKESEKfHLPHGRQREI---GFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEAMERQGVD 223
Cdd:cd24088 92 DYLAKSVEAFLTKHHGD-SFAAGKDDDRlklGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDRQGIP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 224 MRVSALVNDTVGTLAGARYWDDDV---LVAVILGTGTNACYVERTDCIPKL---QGPKSSSGRTIINTEWGAFSDG---I 294
Cdd:cd24088 171 VKVVALVNDTVGTLLARSYTSPEIsgaVLGAIFGTGTNGAYLEDLEKIKKLddsSRVGKGKTHMVINTEWGSFDNElkvL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 295 PLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEG---SLFGMAVPNKLSTPFALRTPDICAMQQDKSDD 371
Cdd:cd24088 251 PTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGlflIQYNDKSPSALNTPYGLDTAVLSAIEIDSEAE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 372 LQAVGSILHNVAGVES-SLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKM--EQDSKGTIFNkrtvVAMDGGLYEHYPQ 448
Cdd:cd24088 331 LRATRKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTgaLNKSYDGEIN----IGVDGSVIEFYPG 406
|
410 420 430
....*....|....*....|....*....|....*....
gi 1939215936 449 YRSYLQDAVTELL-GSETSKNIVIEHSKDGSGIGAALLA 486
Cdd:cd24088 407 FESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
57-487 |
3.15e-115 |
|
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: 353.69 E-value: 3.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLAVDGG--SNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIP 134
Cdd:cd24089 7 LLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 135 QELMFGTSEELFDFIASTLAGFAEKESEKfhlphGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLN 214
Cdd:cd24089 87 EEIMHGSGTQLFDHVAECLADFMDKQKIK-----DKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 215 EAMERQG-VDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSDG 293
Cdd:cd24089 162 KAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 294 IPL----TAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKs 369
Cdd:cd24089 239 GSLedirTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEK- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 370 DDLQAVGSILhNVAGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMeQDSKGTiFNKRTVVAMDGGLYEHYPQY 449
Cdd:cd24089 318 EGLANAKEIL-TRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRL-RENKGL-ERLRTTVGVDGSVYKKHPQF 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 1939215936 450 RSYLQDAVTELLGSETSKNIViehSKDGSGIGAALLAA 487
Cdd:cd24089 395 SKRLHKAVRRLVPDCDVRFLL---SEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
57-487 |
5.04e-112 |
|
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: 345.51 E-value: 5.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLAVDGGsNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGkeervvATEFE----QLS 132
Cdd:cd24087 4 LRKITDHFISELEKGLSKKGG-NIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGG------NGKFDitqsKYR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 133 IPQELMFGTSEELFDFIASTLAGFAEkesEKFHLPHGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVAC 212
Cdd:cd24087 77 LPEELKTGTGEELWDFIADCLKKFVE---EHFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 213 LNEAMERQGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQG---PKSSSgrTIINTEWGA 289
Cdd:cd24087 154 LQKALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHddiPPDSP--MAINCEYGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 290 FSDG---IPLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQ 366
Cdd:cd24087 232 FDNEhlvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 367 DKSDDLQAVGSILHNVAGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKGtifnkrtvVAMDGGLYEHY 446
Cdd:cd24087 312 DPFENLEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCH--------VAADGSVYNKY 383
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1939215936 447 PQYRSYLQDAVTELLGSE-TSKNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24087 384 PGFKERAAQALKDIFGWDgEDDPIKTVPAEDGSGVGAAIIAA 425
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
78-493 |
2.32e-110 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 342.43 E-value: 2.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 78 SNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQL--GGKEERVvateFEQLSIPQELMFG---------TSEELF 146
Cdd:PTZ00107 55 CSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLrgGGKMERT----QSKFSLPKSALLGekglldkkaTATDLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 147 DFIASTLAGFAEkESeKFHLPHGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVS-----GTAGRDVVACLNEAMERQG 221
Cdd:PTZ00107 131 DHIAKSIKKMME-EN-GDPEDLNKPVPVGFTFSFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFKRNN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 222 VDMRVSALVNDTVGTLAGARYWDD----DVLVAVILGTGTNACYVErtdcipklqgPKSS---SGRTIINTEWGAFSDGI 294
Cdd:PTZ00107 209 VPANVVAVLNDTVGTLISCAYQKPkntpPCQVGVIIGTGSNACYFE----------PEVSaygYAGTPINMECGNFDSKL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 295 PLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNklstpfALRTPDICAMQQDKSDDLQA 374
Cdd:PTZ00107 279 PITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKAPPKMWQSG------SFESEDASMILNDQSPDLQF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 375 VGSILHNVAGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEqdskgtIFNKRTVVAMDGGLYEHYPQYRSYLQ 454
Cdd:PTZ00107 353 SRQVIKEAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKTR------TVQGKATVAIDGSVYVKNPWFRRLLQ 426
|
410 420 430
....*....|....*....|....*....|....*....
gi 1939215936 455 DAVTELLGsETSKNIVIEHSKDGSGIGAALLAATNSNNR 493
Cdd:PTZ00107 427 EYINSILG-PDAGNVVFYLADDGSGKGAAIIAAMVANDK 464
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
57-489 |
6.32e-108 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 335.00 E-value: 6.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLAvDGGSNLKMILSYVdSLPSG-NEKGLFYALDLGGTNFRALRVQLGGKEErvvateFEQLSIPQ 135
Cdd:COG5026 22 LEEIAAKFQEEMEKGLE-GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGT------FEIENFKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 136 ELMFGTS-----EELFDFIASTLAGFAeKESEKfhlphgrqreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVV 210
Cdd:COG5026 94 FPLPGTSseitaEEFFDFIADYIEPLL-DESYK----------LGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 211 ACLNEAMERQG-VDMRVSALVNDTVGTLAGARYWDDDVL----VAVILGTGTNACYVERTDCIPKLQGPKSSsgrTIINT 285
Cdd:COG5026 163 ELLEAALARKGlDNVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKLPAYEGP---MIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 286 EWGAFsDGIPLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGsLFGMAVPNKLSTPFALRTPDICAMQ 365
Cdd:COG5026 240 ESGNF-NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRFL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 366 QDKSDDLQAVGSILHnvagvESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKGtifNKRTVVAMDGGLYEH 445
Cdd:COG5026 318 ADPSDEKEILSQCLE-----AGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTP---LKPHCIAIDGSTYEK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1939215936 446 YPQYRSYLQDAVTELLGSETSKNIVIEHSKDGSGIGAALLAATN 489
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 ... |
60-487 |
1.70e-106 |
|
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: 331.04 E-value: 1.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 60 VADSMTADMRAGLAVDGGSN--LKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIPQEL 137
Cdd:cd24126 10 IMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 138 MFGTSEELFDFIASTLAGFAEKEsekfHLPHGRqREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEAM 217
Cdd:cd24126 90 IHGTGTELFDYVAECLADFMKKK----GIKHKK-LPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLRKAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 218 ERQG-VDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSDGIPL 296
Cdd:cd24126 165 RKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAFGDDGSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 297 ----TAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKSdDL 372
Cdd:cd24126 242 edirTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKE-GL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 373 QAVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKgtIFNKRTVVAMDGGLYEHYPQYRSY 452
Cdd:cd24126 321 YNTREILSDL-GLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKK--LERLRTTVGMDGTVYKTHPQYAKR 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1939215936 453 LQDAVTELLGSETSKNIViehSKDGSGIGAALLAA 487
Cdd:cd24126 398 LHKVVRRLVPSCDVRFLL---SESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
57-487 |
6.03e-105 |
|
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: 327.19 E-value: 6.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLAVDGGSN--LKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIP 134
Cdd:cd24091 7 LLEVKARMRAEMERGLRKETHASapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 135 QELMFGTSEELFDFIASTLAGFAEKESEKfhlphGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLN 214
Cdd:cd24091 87 QEIMQGTGEELFDHIVQCIADFLEYMGLK-----GVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 215 EAME-RQGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSDG 293
Cdd:cd24091 162 EAIKrREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAFGDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 294 IPL----TAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKS 369
Cdd:cd24091 239 GCLddirTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 370 DDLQaVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDsKGtIFNKRTVVAMDGGLYEHYPQY 449
Cdd:cd24091 319 ALLQ-VRAILQQL-GLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIREN-RG-LDHLNVTVGVDGTLYKLHPHF 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 1939215936 450 RSYLQDAVTELlgsETSKNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24091 395 SRVMHETVKEL---APKCDVTFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
66-487 |
1.00e-100 |
|
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: 317.71 E-value: 1.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 66 ADMRAGLAVDGG--SNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIPQELMFGTSE 143
Cdd:cd24124 44 KEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 144 ELFDFIASTLAGFAEKESEKfhlphGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEAMERQG-V 222
Cdd:cd24124 124 QLFDHVAECLGDFMEKRKIK-----DKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGdY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 223 DMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSDGIPL----TA 298
Cdd:cd24124 199 DANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGDDGSLedirTE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 299 FDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKsDDLQAVGSI 378
Cdd:cd24124 276 FDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNK-EGLHNAKEI 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 379 LHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMeQDSKGTIfNKRTVVAMDGGLYEHYPQYRSYLQDAVT 458
Cdd:cd24124 355 LTRL-GVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRL-RDNKGTP-RLRTTVGVDGSLYKTHPQYSRRFHKTLR 431
|
410 420
....*....|....*....|....*....
gi 1939215936 459 ELLGSETSKNIViehSKDGSGIGAALLAA 487
Cdd:cd24124 432 RLVPDSDVRFLL---SESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
57-487 |
1.44e-100 |
|
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: 315.67 E-value: 1.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLAVD--GGSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVAtefEQLSIP 134
Cdd:cd24129 7 LAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITS---EIYSIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 135 QELMFGTSEELFDFIASTLAGFAEKESEKfhlphGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLN 214
Cdd:cd24129 84 ETVAQGTGQQLFDHIVDCIVDFQQKQGLS-----GQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 215 EAMER-QGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSD- 292
Cdd:cd24129 159 EAATRkQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPG---DSGRMCINMEWGAFGDn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 293 ---GIPLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDkS 369
Cdd:cd24129 236 gclAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESD-S 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 370 DDLQAVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDsKGtiFNKRTV-VAMDGGLYEHYPQ 448
Cdd:cd24129 315 LALRQVRAILEDL-GLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMREN-RG--LDELAVtVGVDGTLYKLHPR 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 1939215936 449 YRSYLQDAVTELlgsETSKNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24129 391 FSSLVQATVREL---APRCVVTFLQSEDGSGKGAALVTA 426
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
249-488 |
2.57e-100 |
|
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: 307.88 E-value: 2.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 249 VAVILGTGTNACYVERTDCIPKLQGPKSSSGRTIINTEWGAFSDG----IPLTAFDRDMDAASINPGEQIFEKTISGMYL 324
Cdd:pfam03727 2 IGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNgllpLPRTEYDKELDAESPNPGFQPFEKMISGMYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 325 GEIARRALVSMAEEGSLFGMAVPnKLSTPFALRTPDICAMQQDKSDDLQAVGSILHNVAGVES-SLSERRIVLEVCDAIV 403
Cdd:pfam03727 82 GELVRLVLLDLAEEGLLFKGQSE-KLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETvTEEDRKIVRRICEAVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 404 KRGGRLAGAGIVGILQKMEQDskgtifnKRTVVAMDGGLYEHYPQYRSYLQDAVTELLGSEtsKNIVIEHSKDGSGIGAA 483
Cdd:pfam03727 161 TRAARLVAAGIAAILKKIGRD-------KKVTVGVDGSVYEKYPGFRERLQEALRELLGPG--DKVVLVLAEDGSGVGAA 231
|
....*
gi 1939215936 484 LLAAT 488
Cdd:pfam03727 232 LIAAV 236
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
60-487 |
2.56e-98 |
|
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: 310.29 E-value: 2.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 60 VADSMTADMRAGLAVDGGSN--LKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIPQEL 137
Cdd:cd24128 10 VKRRMKVEMERGLSKETHASapVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNKIYAIPQEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 138 MFGTSEELFDFIASTLAGFAEKESEKfhlphGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEAM 217
Cdd:cd24128 90 MHGTGEELFDHIVHCIADFLEYMGMK-----GVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLKEAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 218 ER-QGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSDGIPL 296
Cdd:cd24128 165 HRrEEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 297 ----TAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKSDDL 372
Cdd:cd24128 242 ddfrTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 373 QaVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKgtIFNKRTVVAMDGGLYEHYPQYRSY 452
Cdd:cd24128 322 Q-VRAILQHL-GLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRG--LDALKVTVGVDGTLYKLHPHFAKV 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1939215936 453 LQDAVTELlgsETSKNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24128 398 MHETVKDL---APKCDVSFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
60-487 |
5.36e-96 |
|
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: 303.74 E-value: 5.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 60 VADSMTADMRAGLAVDGG--SNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIPQEL 137
Cdd:cd24125 10 ISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIPEDI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 138 MFGTSEELFDFIASTLAGFAEKESEKfhlphGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEAM 217
Cdd:cd24125 90 MRGSGTQLFDHIAECLANFMDKLQIK-----DKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLRKAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 218 ERQG-VDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSDGIPL 296
Cdd:cd24125 165 QKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFGDDGSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 297 ----TAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKsDDL 372
Cdd:cd24125 242 ddirTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEK-DGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 373 QAVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMeQDSKGTIfNKRTVVAMDGGLYEHYPQYRSY 452
Cdd:cd24125 321 RKAREVLMRL-GLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRI-KENKGEE-RLRSTIGVDGSVYKKHPHFARR 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1939215936 453 LQDAVTELLgseTSKNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24125 398 LHKTVRRLV---PGCDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
57-487 |
2.19e-93 |
|
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: 297.23 E-value: 2.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLA--VDGGSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEeRVVATEFEQLSIP 134
Cdd:cd24130 7 LQEVKQKMRTELEYGLKkeTHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYNKIFAIP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 135 QELMFGTSEELFDFIASTLAGFAEKESEKfhlphGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLN 214
Cdd:cd24130 86 LEIMQGTGEELFDHIVQCIADFLDYMGLK-----GARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 215 EAMERQG-VDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSDG 293
Cdd:cd24130 161 EAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 294 IPL----TAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKS 369
Cdd:cd24130 238 GCIddirTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 370 DDLQaVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKGTIFnkRTVVAMDGGLYEHYPQY 449
Cdd:cd24130 318 ALLQ-VRRILQQL-GLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRL--DITVGVDGTLYKLHPHF 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 1939215936 450 RSYLQDAVTELlgsETSKNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24130 394 SRILQETVKEL---APQCDVTFMLSEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
57-487 |
1.12e-92 |
|
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: 295.64 E-value: 1.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 57 IRHVADSMTADMRAGLAVDG--GSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEER--VVATEFEQLS 132
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGqwSVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 133 IPQELMFGTSEELFDFIASTLAGFAEKESEKFhlphgRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVAC 212
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFLDKHQMKH-----KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 213 LNEAMERQG-VDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFS 291
Cdd:cd24092 171 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 292 DGIPLTAF----DRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQD 367
Cdd:cd24092 248 DSGELDEFlleyDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 368 KSDDLQaVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKGTIFnkRTVVAMDGGLYEHYP 447
Cdd:cd24092 328 TGDRKQ-IYNILSTL-GLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVM--RITVGVDGSVYKLHP 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1939215936 448 QYRSYLQDAVTELlgsETSKNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24092 404 SFKERFHASVRRL---TPSCEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
60-487 |
1.30e-92 |
|
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: 295.28 E-value: 1.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 60 VADSMTADMRAGL--AVDGGSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGKEERVVATEFEQLSIPQEL 137
Cdd:cd24127 10 VKKRMRAEMELGLrkQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIPIEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 138 MFGTSEELFDFIASTLAGFAEKESEKfhlphGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGRDVVACLNEAM 217
Cdd:cd24127 90 MQGTGEELFDHIVSCISDFLDYMGIK-----GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLRDAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 218 E-RQGVDMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQGpksSSGRTIINTEWGAFSDGIPL 296
Cdd:cd24127 165 KrREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFGDNGCL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 297 ----TAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDICAMQQDKSDDL 372
Cdd:cd24127 242 ddirTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 373 QaVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMEQDSKGTIFNkrTVVAMDGGLYEHYPQYRSY 452
Cdd:cd24127 322 Q-VRAILQQL-GLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLN--VTVGVDGTLYKLHPHFSRI 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1939215936 453 LQDAVTELlgsETSKNIVIEHSKDGSGIGAALLAA 487
Cdd:cd24127 398 MHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
42-242 |
1.55e-87 |
|
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: 273.23 E-value: 1.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 42 ILTKLQQDCATPFPVIRHVADSMTADMRAGLAVDGGSNLKMILSYVDSLPSGNEKGLFYALDLGGTNFRALRVQLGGkeE 121
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGG--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 122 RVVATEFEQLSIPQELMFGTSEELFDFIASTLAGFAEKESEKFHlpHGRQREIGFTFSFPVKQTSIDSGILMKWTKGFAV 201
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF--EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1939215936 202 SGTAGRDVVACLNEAMERQGVDMRVSALVNDTVGTLAGARY 242
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 ... |
53-487 |
1.53e-83 |
|
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: 271.41 E-value: 1.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 53 PFPVIRHVADSMTADMRAGLA--VDGGSNLKMILSYVDSLPSGNEKGLFYALDLG--GTNFRALRVQLGGKEERVVATEF 128
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRgqASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 129 EQLSIPQELMFGTSEELFDFIASTLAGFAE-KESEKFHLPhgrqreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGR 207
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDgQPVPKQGLQ------LGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 208 DVVACLNEAMERQGV-DMRVSALVNDTVGTLAGARYWDDDVLVAVILGTGTNACYVERTDCIPKLQgpkSSSGRTIINTE 286
Cdd:cd24090 157 DVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD---EDRGRVCVSVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 287 WGAFSD----GIPLTAFDRDMDAASINPGEQIFEKTISGMYLGEIARRALVSMAEEGSLFGMAVPNKLSTPFALRTPDIC 362
Cdd:cd24090 234 WGSFSDdgalGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 363 AMqQDKSDDLQAVGSILHNVaGVESSLSERRIVLEVCDAIVKRGGRLAGAGIVGILQKMeQDSKGtIFNKRTVVAMDGGL 442
Cdd:cd24090 314 EM-EDPSAGAARVRAILQDL-GLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHL-QHSRE-QQTLQVAVATGGRV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1939215936 443 YEHYPQYRSYLQdAVTELLGSETSKNIVieHSKDGSGIGAALLAA 487
Cdd:cd24090 390 CERHPRFCSILQ-GTVMLLAPECDVSFI--PSVDGGGRGVAMVTA 431
|
|
| AP2_sigma |
cd14833 |
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ... |
497-629 |
9.78e-78 |
|
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.
Pssm-ID: 341437 Cd Length: 141 Bit Score: 245.56 E-value: 9.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 497 MIRFILLQNRQGKTRLAKYYVPLEDSEKHKVEY-----------------EFRTHKVIYRRYAGLFFALCVDITDNELAY 559
Cdd:cd14833 1 MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEevhrlvtsrdkkhtnfvEFRNYKLVYRRYAGLFFCICVDVNDNELAY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 560 LECIHLFVEILDHFFSNVCELDLVFNFHklclisvssKVYLILDEFILAGELQETSKRAIIERMGELEKL 629
Cdd:cd14833 81 LEAIHLFVEVLDEYFGNVCELDLVFNFY---------KVYAILDEMFLAGEIQETSKKVILERLKELDKL 141
|
|
| AP1_sigma |
cd14831 |
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ... |
499-620 |
8.69e-51 |
|
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.
Pssm-ID: 341435 Cd Length: 143 Bit Score: 173.51 E-value: 8.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 499 RFILLQNRQGKTRLAKYYVPLEDSEKHKVE-----------------YEFRTHKVIYRRYAGLFFALCVDITDNELAYLE 561
Cdd:cd14831 1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITrevstlvlarkpkmcnfLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939215936 562 CIHLFVEILDHFFSNVCELDLVFNFHklclisvssKVYLILDEFILAGELQETSKRAII 620
Cdd:cd14831 81 IIHRYVEILDKYFGNVCELDIIFNFH---------KAYFILDELLLGGELQETSKKNVL 130
|
|
| APS2 |
COG5030 |
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion]; |
497-630 |
6.80e-48 |
|
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
Pssm-ID: 227363 Cd Length: 152 Bit Score: 166.05 E-value: 6.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 497 MIRFILLQNRQGKTRLAKYYVPLEDSEKHKVE-----------------YEFRTHKVIYRRYAGLFFALCVDITDNELAY 559
Cdd:COG5030 1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIadiyelisarkpkesnfIEGKNEKIVYRRYATLYFVFGVDNDDNELII 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939215936 560 LECIHLFVEILDHFFSNVCELDLVFNFhklclisvsSKVYLILDEFILAGELQETSKRAIIERMGELEKLD 630
Cdd:COG5030 81 LELIHNFVEILDRFFGNVCELDLIFNF---------QKVYAILDEMILGGEIIESSKNEVLEHVYALDAES 142
|
|
| Clat_adaptor_s |
pfam01217 |
Clathrin adaptor complex small chain; |
497-630 |
8.54e-45 |
|
Clathrin adaptor complex small chain;
Pssm-ID: 460115 Cd Length: 142 Bit Score: 157.13 E-value: 8.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 497 MIRFILLQNRQGKTRLAKYYVPLEDSEKHK-VE----------------YEFRTHKVIYRRYAGLFFALCVDITDNELAY 559
Cdd:pfam01217 1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKlIEqiyalisarkpkmsnfIEFNDLKVIYKRYATLYFVVIVDDQDNELII 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939215936 560 LECIHLFVEILDHFFSNVCELDLVFNFhklclisvsSKVYLILDEFILAGELQETSKRAIIERMGELEKLD 630
Cdd:pfam01217 81 LELIHRFVESLDRYFGNVCELDLIFNF---------EKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
|
|
| AP_sigma |
cd14827 |
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ... |
499-628 |
3.40e-44 |
|
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.
Pssm-ID: 341431 Cd Length: 138 Bit Score: 155.29 E-value: 3.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 499 RFILLQNRQGKTRLAKYYVPLEDSEKHKVE-----------------YEFRTHKVIYRRYAGLFFALCVDITDNELAYLE 561
Cdd:cd14827 1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIeeivqvvlsrdakhcnfVEFRNYKLIYRRYASLYFCICVDSNDNELAILE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939215936 562 CIHLFVEILDHFFSNVCELDLVFNFHklclisvssKVYLILDEFILAGELQETSKRAIIERMGELEK 628
Cdd:cd14827 81 AIHNFVETLDKYFENVCELDLIFNFE---------KVYFIVDEMVLGGEIRETSQTKILKQIEMLDK 138
|
|
| AP4_sigma |
cd14832 |
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ... |
499-628 |
7.85e-38 |
|
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.
Pssm-ID: 341436 Cd Length: 138 Bit Score: 137.36 E-value: 7.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 499 RFILLQNRQGKTRLAKYYVPLEDSEKHKVE-----------------YEFRTHKVIYRRYAGLFFALCVDITDNELAYLE 561
Cdd:cd14832 1 KFILMVNKQGQTRLAQYYEFLSIEERVALEgeiirkclsrsekqcsfLEYRGYKLVYRRYASLYFIVGVDEDENELAILE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939215936 562 CIHLFVEILDHFFSNVCELDLVFNFhklclisvsSKVYLILDEFILAGELQETSKRAIIERMGELEK 628
Cdd:cd14832 81 FIHNLVETLDKYFENVCELDIMFNL---------EKAHFILDEMVMNGCIVETNKSNILAPILLMDK 138
|
|
| AP3_sigma |
cd14834 |
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ... |
497-628 |
1.94e-28 |
|
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.
Pssm-ID: 341438 Cd Length: 146 Bit Score: 111.17 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 497 MIRFILLQNRQGKTRLAKYYVPL-EDSEKHKVEYEFRT----------------------HKVIYRRYAGLFFALCVDIT 553
Cdd:cd14834 1 MIKAILIFNNHGKPRLSKFYQHYsEEKQQQIIRETFQLvskrddnvcnfleggsliggsdTKLIYRHYATLYFVFCVDSS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939215936 554 DNELAYLECIHLFVEILDHFFSNVCELDLVFNFhklclisvsSKVYLILDEFILAGELQETSKRAIIERMGELEK 628
Cdd:cd14834 81 ESELGILDLIQVFVETLDKCFENVCELDLIFHV---------DKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
|
|
| AP_longin-like |
cd14823 |
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ... |
500-622 |
1.50e-20 |
|
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.
Pssm-ID: 341427 Cd Length: 131 Bit Score: 87.96 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 500 FILLQNRQGKTRLAKYYVPLEDSEKHKVEY--------EFRTH--------KVIYRRYAGLFFALCVDITDNELAYLECI 563
Cdd:cd14823 2 AILVLDNDGKRLFAKYYDDTYPSVKEQKAFeknifnkkHRTDSeivlleglRVVYKSSIDLYFVVIGSKNENELLLLEVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939215936 564 HLFVEILDHFFSNVCELDLVFNFHKLclisvsskvYLILDEFILAGELQETSKRAIIER 622
Cdd:cd14823 82 NCLVDVLSEYFRKVEERAILENFEGL---------YFALDEIVDGGYIQETDPKQVVHF 131
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
198-264 |
3.21e-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: 3.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939215936 198 GFAVSGTAGRDVVACLNEAMERQGVDMRVsALVNDTVGTLAGAryWDDDVLVAVILGTGTNACYVER 264
Cdd:COG2971 68 GFGLAGAGTPEDAEALEAALRELFPFARV-VVVNDALAALAGA--LGGEDGIVVIAGTGSIAAGRDG 131
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
94-486 |
3.56e-03 |
|
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: 40.27 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 94 NEKGLFYALDLGGTNFRALRVQLGGK--EERVVATEFEQlsipqelmfgTSEELFDFIASTLAGFAEKESEKFHLPHGrq 171
Cdd:COG1940 2 PDAGYVIGIDIGGTKIKAALVDLDGEvlARERIPTPAGA----------GPEAVLEAIAELIEELLAEAGISRGRILG-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 172 reIGFTFSFPV---KQTSIDSGILMKWTkgfavsgtaGRDVVACLNEAmerqgVDMRVsALVND-TVGTLAGARYW---D 244
Cdd:COG1940 70 --IGIGVPGPVdpeTGVVLNAPNLPGWR---------GVPLAELLEER-----LGLPV-FVENDaNAAALAEAWFGagrG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 245 DDVLVAVILGTGTNACYVertdcipkLQGpKSSSGRTIINTEWGAfsdgIPLtafdrDMDAASINPGEQ-IFEKTISGmy 323
Cdd:COG1940 133 ADNVVYLTLGTGIGGGIV--------ING-KLLRGANGNAGEIGH----MPV-----DPDGPLCGCGNRgCLETYASG-- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 324 lgeiarRALVSMAEEgslfgmavpnkLSTPFALRTPDIC--AMQQDksddlqavgsilhnvagvesslserrivlEVCDA 401
Cdd:COG1940 193 ------PALLRRARE-----------LGGAEKLTAEELFaaARAGD-----------------------------PLALE 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939215936 402 IVKRGGRLAGAGIVGILqkmeqdskgTIFNKRTVVaMDGGLYEHYPQYRSYLQDAVTELLGSETSKNIVIEHSKDG--SG 479
Cdd:COG1940 227 VLDEAARYLGIGLANLI---------NLLDPEVIV-LGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGddAG 296
|
....*...
gi 1939215936 480 -IGAALLA 486
Cdd:COG1940 297 lLGAAALA 304
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