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Conserved domains on  [gi|204613|gb|AAA41333|]
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hexokinase type II [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 478-912 0e+00

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: 896.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHN 557
Cdd:cd24128   1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24128  81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITAVACRIR 912
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 30-458 0e+00

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24125:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 429  Bit Score: 865.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMEN 109
Cdd:cd24125   1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24125  81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTA 458
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
 
Name Accession Description Interval E-value
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 478-912 0e+00

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: 896.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHN 557
Cdd:cd24128   1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24128  81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITAVACRIR 912
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 30-458 0e+00

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: 865.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMEN 109
Cdd:cd24125   1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24125  81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTA 458
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
PTZ00107 PTZ00107
hexokinase; Provisional
 12-460 7.40e-119

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 370.16  E-value: 7.40e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     12 TELNQNQVQKVDQFLYHMRLSDETLLEISRRFRKEMEKGL-GATTHPTA------AVKMLPTFVRSTPDGTEHGEFLALD 84
Cdd:PTZ00107   1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     85 LGGTNFRVLRVRVTDNGlqRVEMENQIYAIPEDIMRG---------SGTQLFDHIAECLANFMDKLQIKE---KKLPLGF 152
Cdd:PTZ00107  81 FGGTNFRAVRVSLRGGG--KMERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPEdlnKPVPVGF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    153 TFSFPCHQTKLDESFLVSWTKGFKSS-----GVEGRDVVDLIRKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDQ----N 223
Cdd:PTZ00107 159 TFSFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKPkntpP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    224 CEIGLIVGTGSNACYMEemrhiDMVE--GDEGRMcINMEWGAFgdDGTLNdiRTEFDREIDMGSLNPGKQLFEKMISGMY 301
Cdd:PTZ00107 238 CQVGVIIGTGSNACYFE-----PEVSayGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAY 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    302 MGELVRLILVkmakaeLLFQGKLSPELLTTGSFETKDVSDIEEDK-DGIEKAYQILMRL-GLNPLQEDCVATHRICQIVS 379
Cdd:PTZ00107 308 LGEISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVR 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    380 TRSASLCAATLAAVLWRIKENKGeerlRSTIGVDGSVYKKHPHFAKRLHKAVRRLVPD--CDVRFLRSEDGSGKGAAMVT 457
Cdd:PTZ00107 382 GRAAQLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSILGPdaGNVVFYLADDGSGKGAAIIA 457


                 ...
gi 204613    458 AVA 460
Cdd:PTZ00107 458 AMV 460
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 673-907 3.23e-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: 328.30  E-value: 3.23e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     673 EVGLIVGTGSNACYMEEMRNVELVDG---EEGRMCVNMEWGAFGDNGCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMY 749
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGklpKSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     750 LGEIVRNILIDFTKRGLLFRGRiSERLKTRGIFETKFLSQIESD-CLALLQVRAIL-RHLGLES-TCDDSIIVKEVCTVV 826
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILeELLGIETvTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     827 ARRAAQLCGAGMAAVVDKIRENRgldnlKVTVGVDGTLYKLHPHFAKVMHETVRD-LAPKCDVSFLESEDGSGKGAALIT 905
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 204613     906 AV 907
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 462-908 4.77e-106

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 336.26  E-value: 4.77e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    462 RLADQHRARQKTLESLKLSHEQLLEVKRRMKVEMEQGLskETHAV---------APVKMLPTYVCATPDGTEKGDFLALD 532
Cdd:PTZ00107   3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGL--EAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    533 LGGTNFRVLLVRVRNGKRrgVEMHNKIYSIPQEVM---------HGTGEELFDHIVQCIADFLEYMGMK---GVSLPLGF 600
Cdd:PTZ00107  81 FGGTNFRAVRVSLRGGGK--MERTQSKFSLPKSALlgekglldkKATATDLFDHIAKSIKKMMEENGDPedlNKPVPVGF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    601 TFSFPCQQNSLDQSILLKWTKGFKAS-----GCEGEDVVTLLKEAIhRREEFDLDVVAVVNDTVGTMMTCGYED----PH 671
Cdd:PTZ00107 159 TFSFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAF-KRNNVPANVVAVLNDTVGTLISCAYQKpkntPP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    672 CEVGLIVGTGSNACYMEEMrnvELVDGEEGRMcVNMEWGAFgdngCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLG 751
Cdd:PTZ00107 238 CQVGVIIGTGSNACYFEPE---VSAYGYAGTP-INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLG 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    752 EIVRNILIdftkrgLLFRGRISERLKTRGIFETKFLSQIESDCLALLQV--RAILRHLGLESTCDDSIIVKEVCTVVARR 829
Cdd:PTZ00107 310 EISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFsrQVIKEAWDVDLTDEDLYTIRKICELVRGR 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    830 AAQLCGAGMAAVVDKIRENRGldnlKVTVGVDGTLYKLHPHFAKVMHETVRD-LAPK-CDVSFLESEDGSGKGAALITAV 907
Cdd:PTZ00107 384 AAQLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAM 459


                 .
gi 204613    908 A 908
Cdd:PTZ00107 460 V 460
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 20-460 1.03e-105

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 334.23  E-value: 1.03e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    20 QKVDQFL--YHMRLSDETLLEISRRFRKEMEKGLgatTHPTAAVKMLPTFVrSTPDG-TEHGEFLALDLGGTNFRVLRVR 96
Cdd:COG5026   4 LLVDAFLkrHGFDLSSIDLEEIAAKFQEEMEKGL---EGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    97 VTDNGlqRVEMENQIyAIPediMRGSG-----TQLFDHIAECLAnfmdklQIKEKKLPLGFTFSFPCHQTKLDESFLVSW 171
Cdd:COG5026  80 FDGEG--TFEIENFK-SFP---LPGTSseitaEEFFDFIADYIE------PLLDESYKLGFCFSFPAEQLPDKDGRLIQW 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   172 TKGFKSSGVEGRDVVDLIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNC----EIGLIVGTGSNACYMEEMRHIDM 247
Cdd:COG5026 148 TKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGK 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   248 VEGDEGRMCINMEWGAFgdDGTLndiRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKaELLFQGKLSPE 327
Cdd:COG5026 228 LPAYEGPMIINMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAA-EGLFSPGFSEV 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   328 LLTTGSFETKDVSDIEEDKDGIEKAYQILMRLGLNplqEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERlR 407
Cdd:COG5026 302 FETPYSLTTVDMSRFLADPSDEKEILSQCLEAGSE---EDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-P 377

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 204613   408 STIGVDGSVYKKHPHFAKRLHKAVRR-LVPDCD--VRFLRSEDGSGKGAAMVTAVA 460
Cdd:COG5026 378 HCIAIDGSTYEKMPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALN 433
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 225-459 2.67e-103

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: 320.59  E-value: 2.67e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     225 EIGLIVGTGSNACYMEEMRHIDMVEGD---EGRMCINMEWGAFGDDGTLNDIRTEFDREIDMGSLNPGKQLFEKMISGMY 301
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     302 MGELVRLILVKMAKAELLFQGKlSPELLTTGSFETKDVSDIEEDK-DGIEKAYQILMR-LGLNPL-QEDCVATHRICQIV 378
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIETVtEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     379 STRSASLCAATLAAVLWRIKENKgeerlRSTIGVDGSVYKKHPHFAKRLHKAVRRLV-PDCDVRFLRSEDGSGKGAAMVT 457
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 204613     458 AV 459
Cdd:pfam03727 235 AV 236
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 479-909 7.25e-98

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 313.82  E-value: 7.25e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   479 LSHEQLLEVKRRMKVEMEQGLSketHAVAPVKMLPTYVcATPDG-TEKGDFLALDLGGTNFRVLLVRVrNGKRRGVEMHN 557
Cdd:COG5026  17 LSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF-DGEGTFEIENF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIP---QEVmhgTGEELFDHIVQCIADFLEYmgmkgvSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVV 634
Cdd:COG5026  92 KSFPLPgtsSEI---TAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   635 TLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDP----HCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWG 710
Cdd:COG5026 163 ELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESG 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   711 AFgdNGClddLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGlLFRGRISERLKTRGIFETKFLSQI 790
Cdd:COG5026 243 NF--NKL---PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRF 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   791 ---ESDclALLQVRAILRhlglESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNlKVTVGVDGTLYKL 867
Cdd:COG5026 317 ladPSD--EKEILSQCLE----AGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-PHCIAIDGSTYEK 389

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 204613   868 HPHFAKVMHETVRD-LAPKCD--VSFLESEDGSGKGAALITAVAC 909
Cdd:COG5026 390 MPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
 
Name Accession Description Interval E-value
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 478-912 0e+00

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: 896.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHN 557
Cdd:cd24128   1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24128  81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITAVACRIR 912
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 478-910 0e+00

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: 892.67  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHN 557
Cdd:cd24091   1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24091  81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                       410       420       430
                ....*....|....*....|....*....|...
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITAVACR 910
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 30-458 0e+00

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: 865.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMEN 109
Cdd:cd24125   1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24125  81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTA 458
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 30-458 0e+00

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: 844.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMEN 109
Cdd:cd24089   1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24089  81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTA 458
Cdd:cd24089 401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 478-911 0e+00

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: 823.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHN 557
Cdd:cd24127   1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24127  81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400

                       410       420       430
                ....*....|....*....|....*....|....
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITAVACRI 911
Cdd:cd24127 401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 2-474 0e+00

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: 795.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     2 IASHMIACLFTELNQNQVQKVDQFLYHMRLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFL 81
Cdd:cd24124   1 IAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    82 ALDLGGTNFRVLRVRVTDNGLQRVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQT 161
Cdd:cd24124  81 ALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   162 KLDESFLVSWTKGFKSSGVEGRDVVDLIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEE 241
Cdd:cd24124 161 KIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   242 MRHIDMVEGDEGRMCINMEWGAFGDDGTLNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQ 321
Cdd:cd24124 241 LRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFE 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   322 GKLSPELLTTGSFETKDVSDIEEDKDGIEKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENK 401
Cdd:cd24124 321 GRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNK 400

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 204613   402 GEERLRSTIGVDGSVYKKHPHFAKRLHKAVRRLVPDCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTL 474
Cdd:cd24124 401 GTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 478-911 0e+00

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: 768.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGkRRGVEMHN 557
Cdd:cd24130   1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSG-RRSVRMYN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24130  80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399

                       410       420       430
                ....*....|....*....|....*....|....
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITAVACRI 911
Cdd:cd24130 400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 30-458 0e+00

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: 755.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMEN 109
Cdd:cd24126   1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24126  81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTA 458
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 30-458 0e+00

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: 735.50  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNglQRVEMEN 109
Cdd:cd24019   1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGG--SQVKMES 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24019  79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHI---DMVEGDEGRMCINMEWGAFGD 266
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVekwDGDEGDPGQVIINTEWGAFGD 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   267 DGTLNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDK 346
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   347 -DGIEKAYQILMRLGLNPLQ-EDCVATHRICQIVSTRSASLCAATLAAVLWRIkenkgeERLRSTIGVDGSVYKKHPHFA 424
Cdd:cd24019 319 eGDFSNTREILKELGLEDASdEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRM------NRKEVTVGVDGSLYKYHPKFH 392

                       410       420       430
                ....*....|....*....|....*....|....*
gi 204613   425 KRLHKAVRRLVP-DCDVRFLRSEDGSGKGAAMVTA 458
Cdd:cd24019 393 KRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 478-906 0e+00

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: 734.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRrgVEMHN 557
Cdd:cd24019   1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQ--VKMES 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24019  79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVEL---VDGEEGRMCVNMEWGAFGD 714
Cdd:cd24019 159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   715 NGCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDC 794
Cdd:cd24019 239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   795 L-ALLQVRAILRHLGLES-TCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRenrgldNLKVTVGVDGTLYKLHPHFA 872
Cdd:cd24019 319 EgDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKFH 392

                       410       420       430
                ....*....|....*....|....*....|....*
gi 204613   873 KVMHETVRDLAPK-CDVSFLESEDGSGKGAALITA 906
Cdd:cd24019 393 KRMHETLKELVPPgCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 478-910 0e+00

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: 720.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrngKRRGVEMHN 557
Cdd:cd24129   1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV---GTAGVQITS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24129  78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397

                       410       420       430
                ....*....|....*....|....*....|...
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITAVACR 910
Cdd:cd24129 398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 478-906 0e+00

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: 668.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHN 557
Cdd:cd24089   1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24089  81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITA 906
Cdd:cd24089 401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 30-462 0e+00

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: 629.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMEN 109
Cdd:cd24091   1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24091  81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                       410       420       430
                ....*....|....*....|....*....|...
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTAVAYR 462
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 478-906 0e+00

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: 618.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHN 557
Cdd:cd24125   1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24125  81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITA 906
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 30-463 0e+00

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: 605.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMEN 109
Cdd:cd24128   1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24128  81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                       410       420       430
                ....*....|....*....|....*....|....
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTAVAYRL 463
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 478-906 0e+00

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: 602.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHN 557
Cdd:cd24126   1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24126  81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGC 717
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   718 LDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 797
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   798 LQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHE 877
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 204613   878 TVRDLAPKCDVSFLESEDGSGKGAALITA 906
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 465-913 0e+00

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: 599.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   465 DQHRARQKTLESLKLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVR 544
Cdd:cd24124  16 DQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   545 VRNGKRRGVEMHNKIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFK 624
Cdd:cd24124  96 VNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFK 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   625 ASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMC 704
Cdd:cd24124 176 ASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMC 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   705 VNMEWGAFGDNGCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFET 784
Cdd:cd24124 256 INTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNT 335

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   785 KFLSQIESDCLALLQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTL 864
Cdd:cd24124 336 SDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSL 415

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 204613   865 YKLHPHFAKVMHETVRDLAPKCDVSFLESEDGSGKGAALITAVACRIRE 913
Cdd:cd24124 416 YKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAE 464
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 30-463 0e+00

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: 598.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMEN 109
Cdd:cd24127   1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24127  81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24127 161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24127 241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24127 321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400

                       410       420       430
                ....*....|....*....|....*....|....
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTAVAYRL 463
Cdd:cd24127 401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 30-463 0e+00

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: 581.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTdNGLQRVEMEN 109
Cdd:cd24130   1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIR-SGRRSVRMYN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24130  80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24130 160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24130 320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399

                       410       420       430
                ....*....|....*....|....*....|....
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTAVAYRL 463
Cdd:cd24130 400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 471-910 0e+00

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: 578.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   471 QKTLESLKLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKR 550
Cdd:cd24092   3 EQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   551 RG--VEMHNKIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGC 628
Cdd:cd24092  83 GQwsVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   629 EGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNME 708
Cdd:cd24092 163 EGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTE 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   709 WGAFGDNGCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLS 788
Cdd:cd24092 243 WGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVS 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   789 QIESDCLALLQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLH 868
Cdd:cd24092 323 QVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLH 402

                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 204613   869 PHFAKVMHETVRDLAPKCDVSFLESEDGSGKGAALITAVACR 910
Cdd:cd24092 403 PSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 21-462 0e+00

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: 577.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    21 KVDQFLYHMRLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDN 100
Cdd:cd24092   1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   101 --GLQRVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSS 178
Cdd:cd24092  81 eeGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   179 GVEGRDVVDLIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCIN 258
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   259 MEWGAFGDDGTLNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKD 338
Cdd:cd24092 241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   339 VSDIEEDKDGIEKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYK 418
Cdd:cd24092 321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 204613   419 KHPHFAKRLHKAVRRLVPDCDVRFLRSEDGSGKGAAMVTAVAYR 462
Cdd:cd24092 401 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 30-462 0e+00

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: 568.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    30 RLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQrveMEN 109
Cdd:cd24129   1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQ---ITS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   110 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24129  78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGT 269
Cdd:cd24129 158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   270 LNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGI 349
Cdd:cd24129 238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   350 EKAYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 429
Cdd:cd24129 318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397

                       410       420       430
                ....*....|....*....|....*....|...
gi 204613   430 AVRRLVPDCDVRFLRSEDGSGKGAAMVTAVAYR 462
Cdd:cd24129 398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 34-458 4.37e-171

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: 504.07  E-value: 4.37e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    34 ETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLG--GTNFRVLRVRVTDNGLQRVEMENQI 111
Cdd:cd24090   5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   112 YAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLIRK 191
Cdd:cd24090  85 FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRD 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   192 AIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGTLN 271
Cdd:cd24090 165 AIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALG 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   272 DIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDGIEK 351
Cdd:cd24090 245 PVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAAR 324

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   352 AYQILMRLGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHKAV 431
Cdd:cd24090 325 VRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTV 404

                       410       420
                ....*....|....*....|....*..
gi 204613   432 RRLVPDCDVRFLRSEDGSGKGAAMVTA 458
Cdd:cd24090 405 MLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 478-906 9.30e-163

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: 482.50  E-value: 9.30e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   478 KLSHEQLLEVKRRMKVEMEQGLSKETHAVAPVKMLPTYVCATPDGTEKGDFLALDLG--GTNFRVLLVRVRNGKRRGVEM 555
Cdd:cd24090   1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   556 HNKIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVT 635
Cdd:cd24090  81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   636 LLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDN 715
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   716 GCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCL 795
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   796 ALLQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVM 875
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                       410       420       430
                ....*....|....*....|....*....|.
gi 204613   876 HETVRDLAPKCDVSFLESEDGSGKGAALITA 906
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 33-456 2.75e-161

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: 478.67  E-value: 2.75e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    33 DETLLEISRRFRKEMEKGLgatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRvEMENQIY 112
Cdd:cd24018   1 VSKLEEIVKHFLSEMEKGL---EGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIF-IIVQRKY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   113 AIPEDIMRGSGTQLFDHIAECLANFMDK---LQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24018  77 KIPDEAKTGTGEELFDFIAECIAEFLEEhnlDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHI---DMVEG---DEGRMCINMEWGA 263
Cdd:cd24018 157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGsvtKSDEMIINTEWGA 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   264 FgdDGTLNDI-RTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDI 342
Cdd:cd24018 236 F--DNEREVLpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   343 EEDKDG-IEKAYQILMRLG--LNPLQEDCVATHRICQIVSTRSASLCAATLAAVL-WRIKENKGeerlRSTIGVDGSVYK 418
Cdd:cd24018 314 EADTSPdLDAVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILlKRGSLLPE----PVTVGIDGSVYE 389

                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 204613   419 KHPHFAKRLHKAVRRLVPDC---DVRFLRSEDGSGKGAAMV 456
Cdd:cd24018 390 KYPGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 482-904 8.70e-160

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: 474.82  E-value: 8.70e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   482 EQLLEVKRRMKVEMEQGLSKEThavAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKiYS 561
Cdd:cd24018   2 SKLEEIVKHFLSEMEKGLEGDG---GSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-YK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   562 IPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVS---LPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLLK 638
Cdd:cd24018  78 IPDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQ 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   639 EAIHRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEG------RMCVNMEWGAF 712
Cdd:cd24018 158 NALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPSGsvtksdEMIINTEWGAF 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   713 GDNGCLddL-RTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIE 791
Cdd:cd24018 237 DNEREV--LpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIE 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   792 SDCLALLQ-VRAILRHLG--LESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIreNRGLDNlKVTVGVDGTLYKLH 868
Cdd:cd24018 315 ADTSPDLDaVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKR--GSLLPE-PVTVGIDGSVYEKY 391

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 204613   869 PHFAKVMHETVRDLAP---KCDVSFLESEDGSGKGAALI 904
Cdd:cd24018 392 PGFKDRLSEALRELFGpevKANISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 33-457 1.55e-141

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: 424.77  E-value: 1.55e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    33 DETLLEISRRFRKEMEKGLGATTHPtaaVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQrvEMENQIY 112
Cdd:cd24000   1 DEDLKEITDAFLEELEKGLAGEPSS---LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIE--VTISKKY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   113 AIPEDIMRGSGTQLFDHIAECLANFMDKLQIKeKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLIRKA 192
Cdd:cd24000  76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   193 IQRRGDfDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDmveGDEGRMCINMEWGAFGDDgtlND 272
Cdd:cd24000 155 LKKRGL-PVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL---LGDGGMIINTEWGNFGKN---SL 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   273 IRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELlfqgklspellttgsfetkdvsdieedkdgieka 352
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADEIL---------------------------------- 273

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   353 yqilmrlglnplqedcvatHRICQIVSTRSASLCAATLAAVLWRIKENKGEerlRSTIGVDGSVYKKHPHFAKRLHKAVR 432
Cdd:cd24000 274 -------------------RKICELVAERSARLAAAAIAALLRKTGDSPEK---KITIAVDGSLFEKYPGYRERLEEYLK 331

                       410       420
                ....*....|....*....|....*.
gi 204613   433 RLV-PDCDVRFLRSEDGSGKGAAMVT 457
Cdd:cd24000 332 ELLgRGIRIELVLVEDGSLIGAALAA 357
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 481-905 2.08e-137

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: 414.37  E-value: 2.08e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   481 HEQLLEVKRRMKVEMEQGLSKEThavAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrNGKRRgVEMHNKIY 560
Cdd:cd24000   1 DEDLKEITDAFLEELEKGLAGEP---SSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSL-DGKGI-EVTISKKY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   561 SIPQEVMHGTGEELFDHIVQCIADFLEYMGMKgVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLLKEA 640
Cdd:cd24000  76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   641 IHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNvelVDGEEGRMCVNMEWGAFGDNgclDD 720
Cdd:cd24000 155 LKKR-GLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN---SL 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   721 LRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRgllfrgriserlktrgifetkflsqiesdclallqv 800
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   801 railrhlglestcddsiIVKEVCTVVARRAAQLCGAGMAAVVDKIRENrglDNLKVTVGVDGTLYKLHPHFAKVMHETVR 880
Cdd:cd24000 272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLK 331

                       410       420
                ....*....|....*....|....*.
gi 204613   881 DLAPK-CDVSFLESEDGSGKGAALIT 905
Cdd:cd24000 332 ELLGRgIRIELVLVEDGSLIGAALAA 357
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 482-908 1.16e-123

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: 381.62  E-value: 1.16e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   482 EQLLEVKRRMKVEMEQGLSKETHAvaPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKIYS 561
Cdd:cd24020   4 SRLRQVADAMVVEMEAGLASEGGS--KLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   562 IPQEVMHGTGEELFDHIVQCIADFLEYMG----MKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLL 637
Cdd:cd24020  82 IPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   638 KEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDG---EEGRMCVNMEWGAFgD 714
Cdd:cd24020 162 EEALERQ-GLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGglpRSGEMVINTEWGNF-R 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   715 NGCLDdlRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDC 794
Cdd:cd24020 240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDD 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   795 LA-LLQVRAIL-RHLGLE-STCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKI--RENRGLDNLKVTVGVDGTLYKLHP 869
Cdd:cd24020 318 SPdLETVARILkDALGIDdTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLgrDGGGSSPAQRTVVAVDGGLYEHYP 397

                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 204613   870 HFAKVMHETVRDLAPKC---DVSFLESEDGSGKGAALITAVA 908
Cdd:cd24020 398 KFREYMQQALVELLGDEaadSVELELSNDGSGIGAALLAAAH 439
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 482-908 2.80e-120

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: 372.48  E-value: 2.80e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   482 EQLLEVKRRMKVEMEQGLSKETHAVApvkMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVR-NGKrrgVEMHNKIY 560
Cdd:cd24087   2 ERLRKITDHFISELEKGLSKKGGNIP---MIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGgNGK---FDITQSKY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   561 SIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVS--LPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLLK 638
Cdd:cd24087  76 RLPEELKTGTGEELWDFIADCLKKFVEEHFPGGKSepLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQ 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   639 EAIHRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVD----GEEGRMCVNMEWGAFgD 714
Cdd:cd24087 156 KALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-D 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   715 NGCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDC 794
Cdd:cd24087 234 NEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDP 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   795 LA-LLQVRAILRH-LGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKirenRGLDnlKVTVGVDGTLYKLHPHFA 872
Cdd:cd24087 314 FEnLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYK--TCHVAADGSVYNKYPGFK 387

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 204613   873 KVMHETVRDL----APKCDVSFLESEDGSGKGAALITAVA 908
Cdd:cd24087 388 ERAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 34-460 6.08e-119

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: 369.30  E-value: 6.08e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    34 ETLLEISRRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMENQIYA 113
Cdd:cd24020   4 SRLRQVADAMVVEMEAGLASEGG--SKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   114 IPEDIMRGSGTQLFDHIAECLANFMDK----LQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLI 189
Cdd:cd24020  82 IPPELMVGTSEELFDFIAGELAKFVATegegFHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   190 RKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGD---EGRMCINMEWGAFgD 266
Cdd:cd24020 162 EEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-R 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   267 DGTLNdiRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEED- 345
Cdd:cd24020 240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDd 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   346 ----KDGIEKAYQILMRLGLNPlqEDCVATHRICQIVSTRSASLCAATLAAVLWRI--KENKGEERLRSTIGVDGSVYKK 419
Cdd:cd24020 318 spdlETVARILKDALGIDDTSL--EARKVVVEVCDLVAERGARLAAAGIVGILKKLgrDGGGSSPAQRTVVAVDGGLYEH 395

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 204613   420 HPHFAKRLHKAVRRLVPDC---DVRFLRSEDGSGKGAAMVTAVA 460
Cdd:cd24020 396 YPKFREYMQQALVELLGDEaadSVELELSNDGSGIGAALLAAAH 439
PTZ00107 PTZ00107
hexokinase; Provisional
 12-460 7.40e-119

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 370.16  E-value: 7.40e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     12 TELNQNQVQKVDQFLYHMRLSDETLLEISRRFRKEMEKGL-GATTHPTA------AVKMLPTFVRSTPDGTEHGEFLALD 84
Cdd:PTZ00107   1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     85 LGGTNFRVLRVRVTDNGlqRVEMENQIYAIPEDIMRG---------SGTQLFDHIAECLANFMDKLQIKE---KKLPLGF 152
Cdd:PTZ00107  81 FGGTNFRAVRVSLRGGG--KMERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPEdlnKPVPVGF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    153 TFSFPCHQTKLDESFLVSWTKGFKSS-----GVEGRDVVDLIRKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDQ----N 223
Cdd:PTZ00107 159 TFSFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKPkntpP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    224 CEIGLIVGTGSNACYMEemrhiDMVE--GDEGRMcINMEWGAFgdDGTLNdiRTEFDREIDMGSLNPGKQLFEKMISGMY 301
Cdd:PTZ00107 238 CQVGVIIGTGSNACYFE-----PEVSayGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAY 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    302 MGELVRLILVkmakaeLLFQGKLSPELLTTGSFETKDVSDIEEDK-DGIEKAYQILMRL-GLNPLQEDCVATHRICQIVS 379
Cdd:PTZ00107 308 LGEISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVR 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    380 TRSASLCAATLAAVLWRIKENKGeerlRSTIGVDGSVYKKHPHFAKRLHKAVRRLVPD--CDVRFLRSEDGSGKGAAMVT 457
Cdd:PTZ00107 382 GRAAQLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSILGPdaGNVVFYLADDGSGKGAAIIA 457


                 ...
gi 204613    458 AVA 460
Cdd:PTZ00107 458 AMV 460
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 482-904 7.52e-112

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: 350.93  E-value: 7.52e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   482 EQLLEVKRRMKVEMEQGLSKETHavaPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrNGKRRgVEMHNKIYS 561
Cdd:cd24088   2 EKLDKLTAEFQRQMEKGLAKHGK---GMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL-HGDGT-FSLRQEKSK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   562 IPQEVMHG-TGEELFDHIVQCIADFL-EYMGMKGVS------LPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDV 633
Cdd:cd24088  77 IPDELKTGvTAKDLFDYLAKSVEAFLtKHHGDSFAAgkdddrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   634 VTLLKEAIHRREeFDLDVVAVVNDTVGTMMTCGYEDPHCE---VGLIVGTGSNACYMEEMRNVELVDGEE------GRMC 704
Cdd:cd24088 157 VKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIKKLDDSSrvgkgkTHMV 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   705 VNMEWGAFgDNgcldDLR----TVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLL---FRGRISERLK 777
Cdd:cd24088 236 INTEWGSF-DN----ELKvlptTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALN 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   778 TRGIFETKFLSQIESDCLALLQV--RAILRHLGLES-TCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNL 854
Cdd:cd24088 311 TPYGLDTAVLSAIEIDSEAELRAtrKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDG 390

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 204613   855 KVTVGVDGTLYKLHPHFAKVMHETVRDLAP----KCDVSFLESEDGSGKGAALI 904
Cdd:cd24088 391 EINIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 34-460 5.73e-111

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: 348.21  E-value: 5.73e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    34 ETLLEISRRFRKEMEKGLgatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGlqRVEMENQIYA 113
Cdd:cd24087   2 ERLRKITDHFISELEKGL---SKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNG--KFDITQSKYR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   114 IPEDIMRGSGTQLFDHIAECLANFMDK--LQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLIRK 191
Cdd:cd24087  77 LPEELKTGTGEELWDFIADCLKKFVEEhfPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   192 AIQRRGdFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVE----GDEGRMCINMEWGAFgDD 267
Cdd:cd24087 157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DN 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   268 GTLNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKD 347
Cdd:cd24087 235 EHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPF 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   348 GIEKAYQILMR--LGLNPLQEDCVATHRICQIVSTRSASLCAATLAAvlwrIKENKGEERLRstIGVDGSVYKKHPHFAK 425
Cdd:cd24087 315 ENLEDTDDLFQhfFGLETTVPERKFIRRLAELIGTRAARLSACGIAA----ICKKRGYKTCH--VAADGSVYNKYPGFKE 388

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 204613   426 RLHKAVRRL----VPDCDVRFLRSEDGSGKGAAMVTAVA 460
Cdd:cd24087 389 RAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 33-456 1.48e-109

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: 344.76  E-value: 1.48e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    33 DETLLEISRRFRKEMEKGLgatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVtdNGLQRVEMENQIY 112
Cdd:cd24088   1 DEKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL--HGDGTFSLRQEKS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   113 AIPEDIMRG-SGTQLFDHIAECLANFMDK-------LQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRD 184
Cdd:cd24088  76 KIPDELKTGvTAKDLFDYLAKSVEAFLTKhhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   185 VVDLIRKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDQNCE---IGLIVGTGSNACYMEEMRHI---DMVEGDE---GRM 255
Cdd:cd24088 156 VVKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklDDSSRVGkgkTHM 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   256 CINMEWGAFgdDGTLNDI-RTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKL--SPELLTTG 332
Cdd:cd24088 235 VINTEWGSF--DNELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNdkSPSALNTP 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   333 -SFETKDVSDIEEDKD-GIEKAYQILMR-LGLN-PLQEDCVATHRICQIVSTRSASLCAATLAAVLwrIKENK--GEERL 406
Cdd:cd24088 313 yGLDTAVLSAIEIDSEaELRATRKVLLDdLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAIL--IKTGAlnKSYDG 390

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 204613   407 RSTIGVDGSVYKKHPHFAKRLHKAVRRLVP----DCDVRFLRSEDGSGKGAAMV 456
Cdd:cd24088 391 EINIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 673-907 3.23e-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: 328.30  E-value: 3.23e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     673 EVGLIVGTGSNACYMEEMRNVELVDG---EEGRMCVNMEWGAFGDNGCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMY 749
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGklpKSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     750 LGEIVRNILIDFTKRGLLFRGRiSERLKTRGIFETKFLSQIESD-CLALLQVRAIL-RHLGLES-TCDDSIIVKEVCTVV 826
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILeELLGIETvTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     827 ARRAAQLCGAGMAAVVDKIRENRgldnlKVTVGVDGTLYKLHPHFAKVMHETVRD-LAPKCDVSFLESEDGSGKGAALIT 905
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 204613     906 AV 907
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 462-908 4.77e-106

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 336.26  E-value: 4.77e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    462 RLADQHRARQKTLESLKLSHEQLLEVKRRMKVEMEQGLskETHAV---------APVKMLPTYVCATPDGTEKGDFLALD 532
Cdd:PTZ00107   3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGL--EAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    533 LGGTNFRVLLVRVRNGKRrgVEMHNKIYSIPQEVM---------HGTGEELFDHIVQCIADFLEYMGMK---GVSLPLGF 600
Cdd:PTZ00107  81 FGGTNFRAVRVSLRGGGK--MERTQSKFSLPKSALlgekglldkKATATDLFDHIAKSIKKMMEENGDPedlNKPVPVGF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    601 TFSFPCQQNSLDQSILLKWTKGFKAS-----GCEGEDVVTLLKEAIhRREEFDLDVVAVVNDTVGTMMTCGYED----PH 671
Cdd:PTZ00107 159 TFSFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAF-KRNNVPANVVAVLNDTVGTLISCAYQKpkntPP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    672 CEVGLIVGTGSNACYMEEMrnvELVDGEEGRMcVNMEWGAFgdngCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLG 751
Cdd:PTZ00107 238 CQVGVIIGTGSNACYFEPE---VSAYGYAGTP-INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLG 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    752 EIVRNILIdftkrgLLFRGRISERLKTRGIFETKFLSQIESDCLALLQV--RAILRHLGLESTCDDSIIVKEVCTVVARR 829
Cdd:PTZ00107 310 EISRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFsrQVIKEAWDVDLTDEDLYTIRKICELVRGR 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    830 AAQLCGAGMAAVVDKIRENRGldnlKVTVGVDGTLYKLHPHFAKVMHETVRD-LAPK-CDVSFLESEDGSGKGAALITAV 907
Cdd:PTZ00107 384 AAQLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAM 459


                 .
gi 204613    908 A 908
Cdd:PTZ00107 460 V 460
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 20-460 1.03e-105

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 334.23  E-value: 1.03e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    20 QKVDQFL--YHMRLSDETLLEISRRFRKEMEKGLgatTHPTAAVKMLPTFVrSTPDG-TEHGEFLALDLGGTNFRVLRVR 96
Cdd:COG5026   4 LLVDAFLkrHGFDLSSIDLEEIAAKFQEEMEKGL---EGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    97 VTDNGlqRVEMENQIyAIPediMRGSG-----TQLFDHIAECLAnfmdklQIKEKKLPLGFTFSFPCHQTKLDESFLVSW 171
Cdd:COG5026  80 FDGEG--TFEIENFK-SFP---LPGTSseitaEEFFDFIADYIE------PLLDESYKLGFCFSFPAEQLPDKDGRLIQW 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   172 TKGFKSSGVEGRDVVDLIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNC----EIGLIVGTGSNACYMEEMRHIDM 247
Cdd:COG5026 148 TKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGK 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   248 VEGDEGRMCINMEWGAFgdDGTLndiRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKaELLFQGKLSPE 327
Cdd:COG5026 228 LPAYEGPMIINMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAA-EGLFSPGFSEV 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   328 LLTTGSFETKDVSDIEEDKDGIEKAYQILMRLGLNplqEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERlR 407
Cdd:COG5026 302 FETPYSLTTVDMSRFLADPSDEKEILSQCLEAGSE---EDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-P 377

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 204613   408 STIGVDGSVYKKHPHFAKRLHKAVRR-LVPDCD--VRFLRSEDGSGKGAAMVTAVA 460
Cdd:COG5026 378 HCIAIDGSTYEKMPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALN 433
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 225-459 2.67e-103

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: 320.59  E-value: 2.67e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     225 EIGLIVGTGSNACYMEEMRHIDMVEGD---EGRMCINMEWGAFGDDGTLNDIRTEFDREIDMGSLNPGKQLFEKMISGMY 301
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     302 MGELVRLILVKMAKAELLFQGKlSPELLTTGSFETKDVSDIEEDK-DGIEKAYQILMR-LGLNPL-QEDCVATHRICQIV 378
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIETVtEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     379 STRSASLCAATLAAVLWRIKENKgeerlRSTIGVDGSVYKKHPHFAKRLHKAVRRLV-PDCDVRFLRSEDGSGKGAAMVT 457
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 204613     458 AV 459
Cdd:pfam03727 235 AV 236
PLN02914 PLN02914
hexokinase
 484-906 6.35e-100

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 321.06  E-value: 6.35e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    484 LLEVKRRMKVEMEQGLSKEthAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKIYSIP 563
Cdd:PLN02914  55 LRHVADAMAADMRAGLAVD--GGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    564 QEVMHGTGEELFDHIVQCIADFLEYMGMK-----GVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLLK 638
Cdd:PLN02914 133 QELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLN 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    639 EAIhRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDG---EEGRMCVNMEWGAFGDN 715
Cdd:PLN02914 213 EAM-ERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGqksSSGRTIINTEWGAFSDG 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    716 GCLddlrTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCL 795
Cdd:PLN02914 292 LPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNS 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    796 ALLQ-VRAILRH-LGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIREN-RGLDNLKVT-VGVDGTLYKLHPHF 871
Cdd:PLN02914 368 DDLQaVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDsKGMIFGKRTvVAMDGGLYEKYPQY 447

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 204613    872 AKVMHETVRD-LAPKC--DVSFLESEDGSGKGAALITA 906
Cdd:PLN02914 448 RRYMQDAVTElLGLELskNIAIEHTKDGSGIGAALLAA 485
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 479-909 7.25e-98

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 313.82  E-value: 7.25e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   479 LSHEQLLEVKRRMKVEMEQGLSketHAVAPVKMLPTYVcATPDG-TEKGDFLALDLGGTNFRVLLVRVrNGKRRGVEMHN 557
Cdd:COG5026  17 LSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF-DGEGTFEIENF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   558 KIYSIP---QEVmhgTGEELFDHIVQCIADFLEYmgmkgvSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVV 634
Cdd:COG5026  92 KSFPLPgtsSEI---TAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   635 TLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDP----HCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWG 710
Cdd:COG5026 163 ELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESG 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   711 AFgdNGClddLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGlLFRGRISERLKTRGIFETKFLSQI 790
Cdd:COG5026 243 NF--NKL---PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRF 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   791 ---ESDclALLQVRAILRhlglESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNlKVTVGVDGTLYKL 867
Cdd:COG5026 317 ladPSD--EKEILSQCLE----AGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-PHCIAIDGSTYEK 389

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 204613   868 HPHFAKVMHETVRD-LAPKCD--VSFLESEDGSGKGAALITAVAC 909
Cdd:COG5026 390 MPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 21-219 6.19e-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: 297.11  E-value: 6.19e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613      21 KVDQFLYHMRLSDETLLEISRRFRKEMEKGLGAttHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDN 100
Cdd:pfam00349   1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAK--EGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     101 GlqRVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDK---LQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKS 177
Cdd:pfam00349  79 G--KFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEhglEDFEEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 204613     178 SGVEGRDVVDLIRKAIQRRGDfDIDIVAVVNDTVGTMMTCGY 219
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 471-667 7.22e-93

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: 291.33  E-value: 7.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     471 QKTLESLKLSHEQLLEVKRRMKVEMEQGLSKETHAVapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrnGKR 550
Cdd:pfam00349   3 EELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSS--LKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVEL--GGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     551 RGVEMHNKIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMK---GVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASG 627
Cdd:pfam00349  79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 204613     628 CEGEDVVTLLKEAIHRREEfDLDVVAVVNDTVGTMMTCGY 667
Cdd:pfam00349 159 VVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
PLN02914 PLN02914
hexokinase
 26-458 1.43e-89

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 293.72  E-value: 1.43e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     26 LYHMRLSDETLLEISRRFRKEMEKGL--GATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQ 103
Cdd:PLN02914  41 LTKLQKDCATPLPVLRHVADAMAADMraGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDER 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    104 RVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFM----DKLQIKE-KKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSS 178
Cdd:PLN02914 121 VIATEFEQVSIPQELMFGTSEELFDFIASGLANFVakegGKFHLPEgRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVS 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    179 GVEGRDVVDLIRKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDE---GRM 255
Cdd:PLN02914 201 GTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRT 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    256 CINMEWGAFGDDGTLndirTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFqGKLSPELLTTG-SF 334
Cdd:PLN02914 280 IINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLF-GHFVPEKLSTPfAL 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    335 ETKDVSDIEED-KDGIEKAYQILMR-LGLNPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKgeERL----RS 408
Cdd:PLN02914 355 RTPHLCAMQQDnSDDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDS--KGMifgkRT 432

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 204613    409 TIGVDGSVYKKHPHFAKRLHKAVRRLVPD---CDVRFLRSEDGSGKGAAMVTA 458
Cdd:PLN02914 433 VVAMDGGLYEKYPQYRRYMQDAVTELLGLelsKNIAIEHTKDGSGIGAALLAA 485
PLN02362 PLN02362
hexokinase
 483-906 3.12e-82

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 274.45  E-value: 3.12e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    483 QLLEVKRRMKVEMEQGLSKEthAVAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLlvRVRNGKRRG------VEMH 556
Cdd:PLN02362  54 RLRQVVDAMAVEMHAGLASE--GGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVL--RVQLGGQRSsilsqdVERH 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    557 nkiySIPQEVMHGTGEELFDHIVQCIADFLEYMG-----MKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGE 631
Cdd:PLN02362 130 ----PIPQHLMNSTSEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGK 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    632 DVVTLLKEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDG---EEGRMCVNME 708
Cdd:PLN02362 206 DVAECLQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNME 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    709 WGAFGDNGClddLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFrGRISERLKTRGIFETKFLS 788
Cdd:PLN02362 285 WGNFWSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVA 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    789 QI-ESDCLALLQVRAILRH-LGL-ESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKI-----------RENRGLDNL 854
Cdd:PLN02362 361 AMhEDDSPELQEVARILKEtLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgrdgsggitsgRSRSDIQIM 440

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 204613    855 KVT-VGVDGTLYKLHPHFAKVMHETVRDLAPKcDVS----FLESEDGSGKGAALITA 906
Cdd:PLN02362 441 RRTvVAVEGGLYTNYTMFREYLHEALNEILGE-DVAqhviLKATEDGSGIGSALLAA 496
PLN02405 PLN02405
hexokinase
 452-906 3.04e-78

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 263.23  E-value: 3.04e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    452 GAAMVTAVAYRLAdQHRARQ-----KTLESLKLSHE-------QLLEVKRRMKVEMEQGLSKEthAVAPVKMLPTYVCAT 519
Cdd:PLN02405  12 CAAAVCAAAALVV-RRRMKSsgkwaRAMEILKEFEEdcatpigKLRQVADAMTVEMHAGLASE--GGSKLKMLISYVDNL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    520 PDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGmKGVSLP-- 597
Cdd:PLN02405  89 PSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEG-EDFHLPpg 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    598 ----LGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLLKEAIhRREEFDLDVVAVVNDTVGTMMTCGYEDPHCE 673
Cdd:PLN02405 168 rqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAM-ERVGLDMRVSALVNDTIGTLAGGRYYNPDVV 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    674 VGLIVGTGSNACYMEEMRNVELVDG---EEGRMCVNMEWGAFGDNGClddLRTVFDVAVDELSLNPGKQRFEKMISGMYL 750
Cdd:PLN02405 247 AAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFRSSHL---PLTEYDHALDVESLNPGEQIFEKIISGMYL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    751 GEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQVRAILRHLGLE---STCDDSIIVKEVCTVVA 827
Cdd:PLN02405 324 GEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEipnTSLKMRKVVVELCNIVA 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    828 RRAAQLCGAGMAAVVDKIREN--RGLDNLKVTVGVDGTLYKLHPHFAKVMHETVRDLAPK---CDVSFLESEDGSGKGAA 902
Cdd:PLN02405 404 TRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEevsESIEVEHSNDGSGIGAA 483


                 ....
gi 204613    903 LITA 906
Cdd:PLN02405 484 LLAA 487
PLN02405 PLN02405
hexokinase
 46-458 8.98e-78

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 262.07  E-value: 8.98e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     46 EMEKGLGatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMENQIYAIPEDIMRGSGTQ 125
Cdd:PLN02405  65 EMHAGLA--SEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    126 LFDHIAECLANFMDKlQIKEKKLP------LGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLIRKAIQRRGdF 199
Cdd:PLN02405 143 LFDFIAAALAKFVAT-EGEDFHLPpgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG-L 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    200 DIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGD---EGRMCINMEWGAFGDDgtlNDIRTE 276
Cdd:PLN02405 221 DMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFRSS---HLPLTE 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    277 FDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEEDKDG----IEKA 352
Cdd:PLN02405 298 YDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPdlkvVGSK 377

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    353 YQILMRLGLNPLQEDCVAThRICQIVSTRSASLCAATLAAVLWRIKEN--KGEERLRSTIGVDGSVYKKHPHFAKRLHKA 430
Cdd:PLN02405 378 LKDILEIPNTSLKMRKVVV-ELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHYTEFSKCMEST 456

                        410       420       430
                 ....*....|....*....|....*....|.
gi 204613    431 VRRLVPD---CDVRFLRSEDGSGKGAAMVTA 458
Cdd:PLN02405 457 LKELLGEevsESIEVEHSNDGSGIGAALLAA 487
PLN02362 PLN02362
hexokinase
 46-458 4.29e-73

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 249.80  E-value: 4.29e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     46 EMEKGLgaTTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVtdnGLQRVEMENQ---IYAIPEDIMRGS 122
Cdd:PLN02362  65 EMHAGL--ASEGGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQL---GGQRSSILSQdveRHPIPQHLMNST 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    123 GTQLFDHIAECLANFMDKLQ-----IKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLIRKAIQRRG 197
Cdd:PLN02362 140 SEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    198 dFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEG---DEGRMCINMEWGAFGDDgtlNDIR 274
Cdd:PLN02362 220 -LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFWSS---HLPR 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    275 TEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFqGKLSPELLTTGSFETKDVSDIEEDK--DGIEKA 352
Cdd:PLN02362 296 TSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMHEDDspELQEVA 374

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    353 YQILMRLGLN--PLQEDCVAThRICQIVSTRSASLCAATLAAVLWRIKE----------NKGEERL--RSTIGVDGSVYK 418
Cdd:PLN02362 375 RILKETLGISevPLKVRKLVV-KICDVVTRRAARLAAAGIVGILKKIGRdgsggitsgrSRSDIQImrRTVVAVEGGLYT 453

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 204613    419 KHPHFAKRLHKAVRRLVPDCDVRFL---RSEDGSGKGAAMVTA 458
Cdd:PLN02362 454 NYTMFREYLHEALNEILGEDVAQHVilkATEDGSGIGSALLAA 496
PLN02596 PLN02596
hexokinase-like
 36-458 1.67e-53

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 194.32  E-value: 1.67e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613     36 LLEISRRFRKEMEKGLgaTTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMENQIYAIP 115
Cdd:PLN02596  56 LWEVADALVSDMTASL--TAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    116 EDIMRGSGTQLFDHIAECLANFM-----DKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWtKGFKSSGVEGRDVVDLIR 190
Cdd:PLN02596 134 SNVLNGTSQELFDYIALELAKFVaehpgDEADTPERVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDIN 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    191 KAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEG---DEGRMCINMEWGAFGdd 267
Cdd:PLN02596 213 RALEKHG-LKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN-- 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    268 gTLNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVS----DIE 343
Cdd:PLN02596 290 -SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAamhqDTS 368

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    344 EDKDGI-EKAYQILMRLGLNPLQEDCVAthRICQIVSTRSASLCAATLAAV---LWRIkENKgeerlRSTIGVDGSVYKK 419
Cdd:PLN02596 369 EDHEVVnEKLKEIFGITDSTPMAREVVA--EVCDIVAERGARLAGAGIVGIikkLGRI-ENK-----KSVVTVEGGLYEH 440

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 204613    420 HPHFAKRLHKAVRRLVPD---CDVRFLRSEDGSGKGAAMVTA 458
Cdd:PLN02596 441 YRVFRNYLHSSVWEMLGSelsDNVVIEHSHGGSGAGALFLAA 482
PLN02596 PLN02596
hexokinase-like
 453-906 2.33e-51

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 188.16  E-value: 2.33e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    453 AAMVTAVAYRLADQHRARQKTLESLKLSHE------QLLEVKRRMKVEMEQGLSKETHAVapVKMLPTYVCATPDGTEKG 526
Cdd:PLN02596  19 AAAVLMGRWKRRKERQWKHTQRILRKFAREcatpvsKLWEVADALVSDMTASLTAEETTT--LNMLVSYVASLPSGDEKG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    527 DFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLP-----LGFT 601
Cdd:PLN02596  97 LYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFT 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    602 FSFPCQQNSLDQSILLKWtKGFKASGCEGEDVVTLLKEAIHRrEEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTG 681
Cdd:PLN02596 177 VSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMG 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    682 SNACYMEEMRNVELVDG---EEGRMCVNMEWGAFGdngCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNIL 758
Cdd:PLN02596 255 TNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN---SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVL 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613    759 IDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQV--RAILRHLGL-ESTCDDSIIVKEVCTVVARRAAQLCG 835
Cdd:PLN02596 332 LKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVvnEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAG 411

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204613    836 AGMAAVVDKIREnrgLDNLKVTVGVDGTLYKLHPHFAKVMHETV-----RDLAPkcDVSFLESEDGSGKGAALITA 906
Cdd:PLN02596 412 AGIVGIIKKLGR---IENKKSVVTVEGGLYEHYRVFRNYLHSSVwemlgSELSD--NVVIEHSHGGSGAGALFLAA 482
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
 607-683 4.60e-04

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. Members in this family are mainly from metazoa.


Pssm-ID: 466928 [Multi-domain]  Cd Length: 314  Bit Score: 43.34  E-value: 4.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   607 QQNSLDQSILLKwTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCgyedphCEVG---LIVGTGSN 683
Cdd:cd24078  55 KKAGLDPDTPLK-SLGLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATA------FENGgivLISGTGSN 127
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
 178-268 4.93e-03

BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 39.86  E-value: 4.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204613   178 SGVEGRDVVDLIRKAIQRRGDFDIdiVAVVNDTVGTMMtCGYDDQNCeIGLIVGTGSNACYMEEMRHIDMVEGdegrmci 257
Cdd:COG2971  72 AGAGTPEDAEALEAALRELFPFAR--VVVVNDALAALA-GALGGEDG-IVVIAGTGSIAAGRDGDGRTARVGG------- 140

                        90
                ....*....|..
gi 204613   258 nmeWG-AFGDDG 268
Cdd:COG2971 141 ---WGyLLGDEG 149
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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