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Conserved domains on  [gi|194097330|ref|NP_002106|]
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hexokinase-3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 41-471 0e+00

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: 824.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24090    1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24090   81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24090  161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24090  241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24090  321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24090  401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 491-916 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: 820.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24091    1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrgVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24091   81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGS 723
Cdd:cd24091  161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLAL 803
Cdd:cd24091  241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 804 RQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAA 883
Cdd:cd24091  321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                        410       420       430
                 ....*....|....*....|....*....|...
gi 194097330 884 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 916
Cdd:cd24091  401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
 
Name Accession Description Interval E-value
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 41-471 0e+00

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: 824.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24090    1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24090   81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24090  161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24090  241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24090  321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24090  401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 491-916 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: 820.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24091    1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrgVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24091   81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGS 723
Cdd:cd24091  161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLAL 803
Cdd:cd24091  241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 804 RQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAA 883
Cdd:cd24091  321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                        410       420       430
                 ....*....|....*....|....*....|...
gi 194097330 884 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 916
Cdd:cd24091  401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 679-913 2.31e-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: 320.98  E-value: 2.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  679 EIGLIVGTGTNACYMEELRNVAGVPGD---SGRMCINMEWGAFGDDGSLAMLSTRFDASVDQASINPGKQRFEKMISGMY 755
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  756 LGEIVRHILLHLTSLGVLFRGqQIQRLQTRDIFKTKFLSEIESD-SLALRQVRAILED-LGLP-LTSDDALMVLEVCQAV 832
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIESDpSEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  833 SQRAAQLCGAGVAAVVEKIRENRGleelaVSVGVDGTLYKLHPRFSSLVAATVRELAPRCV-VTFLQSEDGSGKGAALVT 911
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDKK-----VTVGVDGSVYEKYPGFRERLQEALRELLGPGDkVVLVLAEDGSGVGAALIA 234


                  ..
gi 194097330  912 AV 913
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 480-914 2.92e-98

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 315.85  E-value: 2.92e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 480 RRLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRG----------EASSLRMLPTFVRATPDGSERGDFLALDLGGTNFR 549
Cdd:PTZ00107   8 RVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEAhrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 550 VLLVRVTTG--VQITSEIYSIPETVAQG---------SGQQLFDHIVDCIVDFQQKQGL---SGQSLPLGFTFSFPCRQL 615
Cdd:PTZ00107  88 AVRVSLRGGgkMERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPVGFTFSFPCTQL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 616 GLDQGILLNWTKGF---KASD--CEGQDVVSLLREAItRRQAVELNVVAIVNDTVGTMMSCGYEDPR----CEIGLIVGT 686
Cdd:PTZ00107 168 SVNNAILIDWTKGFetgRATNdpVEGKDVGELLNDAF-KRNNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVIIGT 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 687 GTNACYME---ELRNVAGVPgdsgrmcINMEWGAFgdDGSLAMlsTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHI 763
Cdd:PTZ00107 247 GSNACYFEpevSAYGYAGTP-------INMECGNF--DSKLPI--TPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 764 LLHLTSLGVLFRGQQIqrlqtrDIFKTKFLSEIESD-SLALRQVRAILEDL-GLPLTSDDALMVLEVCQAVSQRAAQLCG 841
Cdd:PTZ00107 316 IVHLLQLKAPPKMWQS------GSFESEDASMILNDqSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAA 389

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194097330 842 AGVAAVVEKIRENRGLeelaVSVGVDGTLYKLHPRFSSLVAATV-RELAPR-CVVTFLQSEDGSGKGAALVTAVA 914
Cdd:PTZ00107 390 AFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYInSILGPDaGNVVFYLADDGSGKGAAIIAAMV 460
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 490-915 5.52e-98

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 314.20  E-value: 5.52e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 490 FRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVrATPDGS-ERGDFLALDLGGTNFRVLLVRVT-TGVQITSEI-- 565
Cdd:COG5026   15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFDgEGTFEIENFks 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 566 YSIPETVAQGSGQQLFDHIVDCIVDfqqkqgLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLRE 645
Cdd:COG5026   94 FPLPGTSSEITAEEFFDFIADYIEP------LLDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 646 AITRRQAVELNVVAIVNDTVGTMMSCGYEDP----RCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFgdD 721
Cdd:COG5026  168 ALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNF--N 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 722 GSLAmlsTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGvLFRGQQIQRLQTRDIFKTKFLSE-IESDS 800
Cdd:COG5026  246 KLPR---TKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRfLADPS 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 801 LALRQVRAILEdlglPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGlEELAVSVGVDGTLYKLHPRFSSL 880
Cdd:COG5026  322 DEKEILSQCLE----AGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKT-PLKPHCIAIDGSTYEKMPGLAEK 396

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 194097330 881 VAATVRE-LAPRC--VVTFLQSEDGSGKGAALVTAVAC 915
Cdd:COG5026  397 IEYALQEyLLGEKgrYVEFVLVENASLLGAAIAAALNE 434
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 33-230 1.52e-77

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: 250.88  E-value: 1.52e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330   33 VQECLQQFKVTRAQLQQIQASLLGSMEQALrgQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTG 112
Cdd:pfam00349   2 LEELLKQFALSDEKLKEIVDRFVEEMEKGL--AKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGT--NFRVCLVELGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  113 ieGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQG---LQLGFSFSFPCHQTGLDRSTLISWTKGFR 189
Cdd:pfam00349  78 --DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEekeLPLGFTFSFPVEQTSLDSGTLIRWTKGFD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 194097330  190 CSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVNDTVGTMMGC 230
Cdd:pfam00349 156 IPGVVGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAG 195
PLN02914 PLN02914
hexokinase
 72-471 1.10e-68

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 237.09  E-value: 1.10e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  72 VRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFL 151
Cdd:PLN02914  78 LKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 152 DAQ------PVNKQgLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVNDTVG 225
Cdd:PLN02914 156 AKEggkfhlPEGRK-REIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 226 TMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDR---GRVCVSVEWGSFSDdgalGPVLTTFDHTLDHESLNPG 302
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD----GLPLTEFDREMDAASINPG 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 303 AQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM-EDPSTGAARVHAILQD-LGLSPGASD 380
Cdd:PLN02914 310 EQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMqQDNSDDLQAVGSILYDvLGVEASLSA 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 381 VELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTL--QVAVATGGRVCERHPRFCSVLQGTVM-LLAPEC--DVSL 455
Cdd:PLN02914 390 RRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTeLLGLELskNIAI 469

                        410
                 ....*....|....*.
gi 194097330 456 IPSVDGGGRGVAMVTA 471
Cdd:PLN02914 470 EHTKDGSGIGAALLAA 485
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 38-394 3.07e-64

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 222.91  E-value: 3.07e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  38 QQFKVTRAQLQQIQASLLGSMEQALRGQASpapAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGIEGHR 117
Cdd:COG5026   13 HGFDLSSIDLEEIAAKFQEEMEKGLEGKKS---SLKMLPSYLGLPTGVKETGPVIALDAGGT--NFRVALVRFDGEGTFE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 118 VEpRSQEFVIP---QEVmlgAGQQLFDFAAHCLSEFLDaqpvnkQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVE 194
Cdd:COG5026   88 IE-NFKSFPLPgtsSEI---TAEEFFDFIADYIEPLLD------ESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 195 GQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMG---CEP-GVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCV 270
Cdd:COG5026  158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAgayADPdDGYSGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 271 SVEWGSFSddgalGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGvLFGGCTSPALLSQGSILLE 350
Cdd:COG5026  238 NMESGNFN-----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 194097330 351 HVAE-MEDPSTGAARVHAILQdlglSPGASDVELVQHVCAAVCTR 394
Cdd:COG5026  312 DMSRfLADPSDEKEILSQCLE----AGSEEDREILREIADAIVER 352
 
Name Accession Description Interval E-value
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 41-471 0e+00

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: 824.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24090    1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24090   81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24090  161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24090  241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24090  321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24090  401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 491-916 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: 820.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24091    1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrgVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24091   81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGS 723
Cdd:cd24091  161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLAL 803
Cdd:cd24091  241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 804 RQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAA 883
Cdd:cd24091  321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                        410       420       430
                 ....*....|....*....|....*....|...
gi 194097330 884 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 916
Cdd:cd24091  401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 491-916 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: 811.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTT-GVQITSEIY 566
Cdd:cd24129    1 QLSHDQLAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTaGVQITSEIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 567 SIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREA 646
Cdd:cd24129   81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 647 ITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGSLAM 726
Cdd:cd24129  161 ATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCLAM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 727 LSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLALRQV 806
Cdd:cd24129  241 ISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALRQV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 807 RAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAATVR 886
Cdd:cd24129  321 RAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQATVR 400

                        410       420       430
                 ....*....|....*....|....*....|
gi 194097330 887 ELAPRCVVTFLQSEDGSGKGAALVTAVACR 916
Cdd:cd24129  401 ELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 491-912 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: 671.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG--VQITSEI 565
Cdd:cd24019    1 RLSDEQLEEIMDRLLKEMEKGLSKDthpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGsqVKMESEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 566 YSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLRE 645
Cdd:cd24019   81 YAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 646 AITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV---AGVPGDSGRMCINMEWGAFGDDG 722
Cdd:cd24019  161 AIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVekwDGDEGDPGQVIINTEWGAFGDNG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 723 SLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSL- 801
Cdd:cd24019  241 VLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDNEg 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 802 ALRQVRAILEDLGL-PLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRgleelaVSVGVDGTLYKLHPRFSSL 880
Cdd:cd24019  321 DFSNTREILKELGLeDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKE------VTVGVDGSLYKYHPKFHKR 394

                        410       420       430
                 ....*....|....*....|....*....|...
gi 194097330 881 VAATVRELAP-RCVVTFLQSEDGSGKGAALVTA 912
Cdd:cd24019  395 MHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 491-917 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: 665.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24128    1 QLSHDQLLEVKRRMKVEMERGLSKEthaSAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGkwrgVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24128   81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGS 723
Cdd:cd24128  161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLAL 803
Cdd:cd24128  241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 804 RQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAA 883
Cdd:cd24128  321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 194097330 884 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACRL 917
Cdd:cd24128  401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 491-917 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: 651.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRG---EASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24127    1 HLTKDMLLEVKKRMRAEMELGLRKqthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGkkrtVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24127   81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGS 723
Cdd:cd24127  161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLAL 803
Cdd:cd24127  241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 804 RQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAA 883
Cdd:cd24127  321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 194097330 884 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACRL 917
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 ...
 491-917 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: 633.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG---VQITSE 564
Cdd:cd24130    1 QLTRDQLQEVKQKMRTELEYGLKKEThptASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGrrsVRMYNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 565 IYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLR 644
Cdd:cd24130   81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 645 EAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGSL 724
Cdd:cd24130  161 EAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGCI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 725 AMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLALR 804
Cdd:cd24130  241 DDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 805 QVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAAT 884
Cdd:cd24130  321 QVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQET 400

                        410       420       430
                 ....*....|....*....|....*....|...
gi 194097330 885 VRELAPRCVVTFLQSEDGSGKGAALVTAVACRL 917
Cdd:cd24130  401 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 491-912 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: 609.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24089    1 RLSDETLLDISRRFRKEMEKGLGKDThptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEknqkVEMES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24089   81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGS 723
Cdd:cd24089  161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLAL 803
Cdd:cd24089  241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 804 RQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAA 883
Cdd:cd24089  321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400

                        410       420
                 ....*....|....*....|....*....
gi 194097330 884 TVRELAPRCVVTFLQSEDGSGKGAALVTA 912
Cdd:cd24089  401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 41-471 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: 586.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGieGHRVEP 120
Cdd:cd24019    1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLG--GTNFRVLLVTLNG--GSQVKM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24019   77 ESEIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDR---GRVCVSVEWGSF 277
Cdd:cd24019  157 LLQEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEgdpGQVIINTEWGAF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 278 SDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEME- 356
Cdd:cd24019  237 GDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIEs 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 357 DPSTGAARVHAILQDLGLSP-GASDVELVQHVCAAVCTRAAQLCAAALAAVLsclqhsREQQTLQVAVATGGRVCERHPR 435
Cdd:cd24019  317 DNEGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALL------NRMNRKEVTVGVDGSLYKYHPK 390

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 194097330 436 FCSVLQGTVMLLAP-ECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24019  391 FHKRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 491-912 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: 559.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGEASS---LRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTT----GVQITS 563
Cdd:cd24126    1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPtaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEdgkqKVQMES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24126   81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGS 723
Cdd:cd24126  161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLAL 803
Cdd:cd24126  241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 804 RQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAA 883
Cdd:cd24126  321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400

                        410       420
                 ....*....|....*....|....*....
gi 194097330 884 TVRELAPRCVVTFLQSEDGSGKGAALVTA 912
Cdd:cd24126  401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 491-912 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: 542.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24125    1 RLSDETLLEISKRFRKEMEKGLGATThptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNglqkVEMEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24125   81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGS 723
Cdd:cd24125  161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLAL 803
Cdd:cd24125  241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 804 RQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAA 883
Cdd:cd24125  321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                        410       420
                 ....*....|....*....|....*....
gi 194097330 884 TVRELAPRCVVTFLQSEDGSGKGAALVTA 912
Cdd:cd24125  401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 483-916 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: 530.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 483 LEETLAPFRLNHDQLAAVQAQMRKAMAKGLR---GEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG- 558
Cdd:cd24092    2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRletHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGe 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 559 -----VQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASD 633
Cdd:cd24092   82 egqwsVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 634 CEGQDVVSLLREAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINM 713
Cdd:cd24092  162 AEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 714 EWGAFGDDGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFL 793
Cdd:cd24092  242 EWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 794 SEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKL 873
Cdd:cd24092  322 SQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 401

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 194097330 874 HPRFSSLVAATVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 916
Cdd:cd24092  402 HPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 483-922 3.98e-180

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: 529.19  E-value: 3.98e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 483 LEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVT--- 556
Cdd:cd24124   21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNhek 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 557 -TGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCE 635
Cdd:cd24124  101 nQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 636 GQDVVSLLREAITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEW 715
Cdd:cd24124  181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 716 GAFGDDGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSE 795
Cdd:cd24124  261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 796 IESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHP 875
Cdd:cd24124  341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 194097330 876 RFSSLVAATVRELAPRCVVTFLQSEDGSGKGAALVTAVACRLAQLTR 922
Cdd:cd24124  421 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHR 467
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 41-471 2.62e-172

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: 507.39  E-value: 2.62e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24089    1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLG--GSNFRVLWVQVNDEKNQKVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24089   79 ESQVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24089  159 LLRKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24089  239 GSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKE 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24089  319 GLANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRL 398

                        410       420       430
                 ....*....|....*....|....*....|.
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24089  399 HKAVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 495-910 2.49e-168

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: 497.16  E-value: 2.49e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 495 DQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRV---TTGVQITSEIYSIPET 571
Cdd:cd24018    2 SKLEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLdgnGGIFIIVQRKYKIPDE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 572 VAQGSGQQLFDHIVDCIVDFQQKQGLSGQS---LPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAIT 648
Cdd:cd24018   82 AKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNALD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 649 RRQaVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV------AGVPGDSGRMCINMEWGAFgdDG 722
Cdd:cd24018  162 RRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWGAF--DN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 723 SLAML-STRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSL 801
Cdd:cd24018  239 EREVLpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTS 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 802 A-LRQVRAILEDLG--LPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIREnrgLEELAVSVGVDGTLYKLHPRFS 878
Cdd:cd24018  319 PdLDAVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS---LLPEPVTVGIDGSVYEKYPGFK 395

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 194097330 879 SLVAATVRELAPRCV---VTFLQSEDGSGKGAALV 910
Cdd:cd24018  396 DRLSEALRELFGPEVkanISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 496-912 6.91e-153

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: 457.46  E-value: 6.91e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 496 QLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLG--GTNFRVLLVRVTT----GVQITSEIY 566
Cdd:cd24090    6 QLQQIQASLLGSMEQALRGQaspAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGieghRVEPRSQEF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 567 SIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREA 646
Cdd:cd24090   86 VIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRDA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 647 ITRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDDGSLAM 726
Cdd:cd24090  166 IQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALGP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 727 LSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLALRQV 806
Cdd:cd24090  246 VLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAARV 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 807 RAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAATVR 886
Cdd:cd24090  326 RAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTVM 405

                        410       420
                 ....*....|....*....|....*.
gi 194097330 887 ELAPRCVVTFLQSEDGSGKGAALVTA 912
Cdd:cd24090  406 LLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 46-471 1.28e-145

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: 438.51  E-value: 1.28e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  46 QLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQEF 125
Cdd:cd24126    6 TLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLG--GSKFRVLRVKVSEDGKQKVQMESQFY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 126 VIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDA 205
Cdd:cd24126   84 PTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLRKA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 206 IRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALGP 285
Cdd:cd24126  164 IRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGSLED 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 286 VLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPSTGAARV 365
Cdd:cd24126  244 IRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGLYNT 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 366 HAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVLQGTVM 445
Cdd:cd24126  324 REILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHKVVR 403

                        410       420
                 ....*....|....*....|....*.
gi 194097330 446 LLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24126  404 RLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 41-471 3.69e-145

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: 437.40  E-value: 3.69e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24125    1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLG--GTNFRVLWVKVSDNGLQKVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24125   79 ENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24125  159 LLRKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24125  239 GSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24125  319 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRL 398

                        410       420       430
                 ....*....|....*....|....*....|.
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24125  399 HKTVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 41-475 4.91e-143

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: 431.97  E-value: 4.91e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24091    1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLG--GTNFRVLLVKVRSGKWRGVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24091   79 HNKIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24091  159 LLREAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24091  239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24091  319 ALLQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVM 398

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAAR 475
Cdd:cd24091  399 HETVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 28-487 8.19e-140

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: 425.19  E-value: 8.19e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  28 DSSELVQECLQQFKVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLW 107
Cdd:cd24124   16 DQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 108 VTLTGIEGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKG 187
Cdd:cd24124   94 VQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 188 FRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGR 267
Cdd:cd24124  174 FKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGR 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 268 VCVSVEWGSFSDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSI 347
Cdd:cd24124  254 MCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKF 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 348 LLEHVAEMEDPSTGAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGG 427
Cdd:cd24124  334 NTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDG 413

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 428 RVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHRRLLEETL 487
Cdd:cd24124  414 SLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 41-475 1.37e-136

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: 415.05  E-value: 1.37e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLtGIEGHRVEp 120
Cdd:cd24129    1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLG--GTNFRVLLVHV-GTAGVQIT- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 rSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24129   77 -SEIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24129  156 LLREAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDN 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24129  236 GCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24129  316 ALRQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLV 395

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAAR 475
Cdd:cd24129  396 QATVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 41-476 5.82e-131

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: 400.81  E-value: 5.82e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24128    1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLG--GTNFRVLLVRVRNGKWRGVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24128   79 HNKIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24128  159 LLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24128  239 GCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24128  319 ALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVM 398

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARL 476
Cdd:cd24128  399 HETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 494-911 2.27e-130

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: 396.26  E-value: 2.27e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 494 HDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG--VQITSEIYSIPET 571
Cdd:cd24000    1 DEDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKgiEVTISKKYEIPDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 572 VAQGSGQQLFDHIVDCIVDFQQKQGLSgQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAItRRQ 651
Cdd:cd24000   81 IKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDAL-KKR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 652 AVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNvagVPGDSGRMCINMEWGAFGDDGSLAmlsTRF 731
Cdd:cd24000  159 GLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKNSLPR---TEY 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 732 DASVDQASINPGKQRFEKMISGMYLGEIVRHILLhltslgvlfrgqqiqrlqtrdifktkflseiesdSLALRQVRAIle 811
Cdd:cd24000  233 DREVDKASENPGFQPLEKMVSGKYLGELVRLILK----------------------------------DLADEILRKI-- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 812 dlglpltsddalmvlevCQAVSQRAAQLCGAGVAAVVEKIRENrglEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPR 891
Cdd:cd24000  277 -----------------CELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLKELLGR 336

                        410       420
                 ....*....|....*....|.
gi 194097330 892 CV-VTFLQSEDGSGKGAALVT 911
Cdd:cd24000  337 GIrIELVLVEDGSLIGAALAA 357
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 41-476 5.76e-129

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: 395.44  E-value: 5.76e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24127    1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLG--GTNFRVLLVKIRSGKKRTVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24127   79 HNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24127  159 LLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24127  239 GCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24127  319 ALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIM 398

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARL 476
Cdd:cd24127  399 HQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 41-476 1.50e-125

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: 386.60  E-value: 1.50e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEgHRVEP 120
Cdd:cd24130    1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLG--GTNFRVLLVKIRSGR-RSVRM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24130   78 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24130  158 MLREAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24130  238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24130  318 ALLQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRIL 397

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 194097330 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARL 476
Cdd:cd24130  398 QETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 33-475 1.78e-123

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: 381.54  E-value: 1.78e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  33 VQECLQQFKVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTL-T 111
Cdd:cd24092    2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLG--GTNFRVMLVKVgE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 112 GIEGH-RVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRC 190
Cdd:cd24092   80 GEEGQwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 191 SGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCV 270
Cdd:cd24092  160 SGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 271 SVEWGSFSDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLE 350
Cdd:cd24092  240 NTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 351 HVAEMEDPSTGAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVC 430
Cdd:cd24092  320 FVSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVY 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 194097330 431 ERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAAR 475
Cdd:cd24092  400 KLHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 495-914 2.36e-122

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: 378.54  E-value: 2.36e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 495 DQLAAVQAQMRKAMAKGLRGEA-SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLlvRVTTG-----VQIT-SEIYS 567
Cdd:cd24020    4 SRLRQVADAMVVEMEAGLASEGgSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVL--RVQLGgkegrVDKQeYEEVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 568 IPETVAQGSGQQLFDHIVDCIVDFQQKQG----LSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:cd24020   82 IPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAITRrQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV---AGVPGDSGRMCINMEWGAFGd 720
Cdd:cd24020  162 EEALER-QGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIpkwSGGLPRSGEMVINTEWGNFR- 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 721 dgSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEI-ESD 799
Cdd:cd24020  240 --SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDD 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 800 SLALRQVRAILED-LGLPLTS-DDALMVLEVCQAVSQRAAQLCGAGVAAVVEKI-RENRGLEELAVS-VGVDGTLYKLHP 875
Cdd:cd24020  318 SPDLETVARILKDaLGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGSSPAQRTvVAVDGGLYEHYP 397

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 194097330 876 RFSSLVAATVRELAPRCV---VTFLQSEDGSGKGAALVTAVA 914
Cdd:cd24020  398 KFREYMQQALVELLGDEAadsVELELSNDGSGIGAALLAAAH 439
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 45-469 5.13e-115

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: 358.87  E-value: 5.13e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  45 AQLQQIQASLLGSMEQALRGQASpapAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGiEGHRVEPRSQE 124
Cdd:cd24018    2 SKLEEIVKHFLSEMEKGLEGDGG---SLPMLPSFVTERPTGKETGTYLALDLGGT--NLRVCLVTLDG-NGGIFIIVQRK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 125 FVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPV---NKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQL 201
Cdd:cd24018   76 YKIPDEAKTGTGEELFDFIAECIAEFLEEHNLdlqSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVEL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 202 LRDAIRRQGaYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD------EDRGRVCVSVEWG 275
Cdd:cd24018  156 LQNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsgsvTKSDEMIINTEWG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 276 SFSDDGALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM 355
Cdd:cd24018  235 AFDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 356 E-DPSTGAARVHAILQDLGLSPGAS--DVELVQHVCAAVCTRaaqLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCER 432
Cdd:cd24018  314 EaDTSPDLDAVRDILKELLAIDNTTleDRKLIKRICELVSTR---AARLSAAAIAAILLKRGSLLPEPVTVGIDGSVYEK 390

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 194097330 433 HPRFCSVLQGTV-MLLAPEC--DVSLIPSVDGGGRGVAMV 469
Cdd:cd24018  391 YPGFKDRLSEALrELFGPEVkaNISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 510-914 2.35e-114

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: 357.07  E-value: 2.35e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 510 KGLRGEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG--VQITSEIYSIPETVAQGSGQQLFDHIVDC 587
Cdd:cd24087   17 KGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNgkFDITQSKYRLPEELKTGTGEELWDFIADC 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 588 IVDF---QQKQGLSGQsLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQaVELNVVAIVNDT 664
Cdd:cd24087   97 LKKFveeHFPGGKSEP-LPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKKRN-VPIELVALINDT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 665 VGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVA-----GVPGDSgRMCINMEWGAFgDDGSLAMLSTRFDASVDQAS 739
Cdd:cd24087  175 TGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPklehdDIPPDS-PMAINCEYGAF-DNEHLVLPRTKYDVIIDEES 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 740 INPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLA--LRQVRAILEDLGLPL 817
Cdd:cd24087  253 PRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEnlEDTDDLFQHFFGLET 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 818 TSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKirenRGLEElaVSVGVDGTLYKLHPRFSSLVAATVREL-----APRC 892
Cdd:cd24087  333 TVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYKT--CHVAADGSVYNKYPGFKERAAQALKDIfgwdgEDDP 406

                        410       420
                 ....*....|....*....|..
gi 194097330 893 VVTFlQSEDGSGKGAALVTAVA 914
Cdd:cd24087  407 IKTV-PAEDGSGVGAAIIAALT 427
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 496-910 5.61e-113

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: 354.01  E-value: 5.61e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 496 QLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVT--TGVQITSEIYSIPETVA 573
Cdd:cd24088    3 KLDKLTAEFQRQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHgdGTFSLRQEKSKIPDELK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 574 QG-SGQQLFDHIVDCIVDFQQK-------QGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLRE 645
Cdd:cd24088   83 TGvTAKDLFDYLAKSVEAFLTKhhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 646 AITrRQAVELNVVAIVNDTVGTMMSCGYEDPRCE---IGLIVGTGTNACYMEELRNV------AGVPGDSGRMCINMEWG 716
Cdd:cd24088  163 ELD-RQGIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKTHMVINTEWG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 717 AFgdDGSLAML-STRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ---RLQTRDIFKTKF 792
Cdd:cd24088  242 SF--DNELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNDKspsALNTPYGLDTAV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 793 LSEIESDSLA-LRQVRAIL-EDLGLP-LTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGLEELAVSVGVDGT 869
Cdd:cd24088  320 LSAIEIDSEAeLRATRKVLlDDLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEINIGVDGS 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 194097330 870 LYKLHPRFSSLVAATVRELAP----RCVVTFLQSEDGSGKGAALV 910
Cdd:cd24088  400 VIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 679-913 2.31e-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: 320.98  E-value: 2.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  679 EIGLIVGTGTNACYMEELRNVAGVPGD---SGRMCINMEWGAFGDDGSLAMLSTRFDASVDQASINPGKQRFEKMISGMY 755
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  756 LGEIVRHILLHLTSLGVLFRGqQIQRLQTRDIFKTKFLSEIESD-SLALRQVRAILED-LGLP-LTSDDALMVLEVCQAV 832
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIESDpSEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  833 SQRAAQLCGAGVAAVVEKIRENRGleelaVSVGVDGTLYKLHPRFSSLVAATVRELAPRCV-VTFLQSEDGSGKGAALVT 911
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDKK-----VTVGVDGSVYEKYPGFRERLQEALRELLGPGDkVVLVLAEDGSGVGAALIA 234


                  ..
gi 194097330  912 AV 913
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 480-914 2.92e-98

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 315.85  E-value: 2.92e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 480 RRLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRG----------EASSLRMLPTFVRATPDGSERGDFLALDLGGTNFR 549
Cdd:PTZ00107   8 RVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEAhrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 550 VLLVRVTTG--VQITSEIYSIPETVAQG---------SGQQLFDHIVDCIVDFQQKQGL---SGQSLPLGFTFSFPCRQL 615
Cdd:PTZ00107  88 AVRVSLRGGgkMERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPVGFTFSFPCTQL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 616 GLDQGILLNWTKGF---KASD--CEGQDVVSLLREAItRRQAVELNVVAIVNDTVGTMMSCGYEDPR----CEIGLIVGT 686
Cdd:PTZ00107 168 SVNNAILIDWTKGFetgRATNdpVEGKDVGELLNDAF-KRNNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVIIGT 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 687 GTNACYME---ELRNVAGVPgdsgrmcINMEWGAFgdDGSLAMlsTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHI 763
Cdd:PTZ00107 247 GSNACYFEpevSAYGYAGTP-------INMECGNF--DSKLPI--TPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 764 LLHLTSLGVLFRGQQIqrlqtrDIFKTKFLSEIESD-SLALRQVRAILEDL-GLPLTSDDALMVLEVCQAVSQRAAQLCG 841
Cdd:PTZ00107 316 IVHLLQLKAPPKMWQS------GSFESEDASMILNDqSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAA 389

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194097330 842 AGVAAVVEKIRENRGLeelaVSVGVDGTLYKLHPRFSSLVAATV-RELAPR-CVVTFLQSEDGSGKGAALVTAVA 914
Cdd:PTZ00107 390 AFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYInSILGPDaGNVVFYLADDGSGKGAAIIAAMV 460
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 490-915 5.52e-98

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 314.20  E-value: 5.52e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 490 FRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVrATPDGS-ERGDFLALDLGGTNFRVLLVRVT-TGVQITSEI-- 565
Cdd:COG5026   15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFDgEGTFEIENFks 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 566 YSIPETVAQGSGQQLFDHIVDCIVDfqqkqgLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLRE 645
Cdd:COG5026   94 FPLPGTSSEITAEEFFDFIADYIEP------LLDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 646 AITRRQAVELNVVAIVNDTVGTMMSCGYEDP----RCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFgdD 721
Cdd:COG5026  168 ALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNF--N 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 722 GSLAmlsTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGvLFRGQQIQRLQTRDIFKTKFLSE-IESDS 800
Cdd:COG5026  246 KLPR---TKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRfLADPS 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 801 LALRQVRAILEdlglPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIRENRGlEELAVSVGVDGTLYKLHPRFSSL 880
Cdd:COG5026  322 DEKEILSQCLE----AGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKT-PLKPHCIAIDGSTYEKMPGLAEK 396

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 194097330 881 VAATVRE-LAPRC--VVTFLQSEDGSGKGAALVTAVAC 915
Cdd:COG5026  397 IEYALQEyLLGEKgrYVEFVLVENASLLGAAIAAALNE 434
PLN02914 PLN02914
hexokinase
 497-912 7.02e-92

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 299.88  E-value: 7.02e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 497 LAAVQAQMRKAMAKGLRGE-ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLlvRVTTG------VQITSEIYSIP 569
Cdd:PLN02914  55 LRHVADAMAADMRAGLAVDgGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVL--RVQLGgkdervIATEFEQVSIP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 570 ETVAQGSGQQLFDHIVDCIVDFQQKQG-----LSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLR 644
Cdd:PLN02914 133 QELMFGTSEELFDFIASGLANFVAKEGgkfhlPEGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLN 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 645 EAItRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEE---LRNVAGVPGDSGRMCINMEWGAFGDD 721
Cdd:PLN02914 213 EAM-ERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERtdaIPKLQGQKSSSGRTIINTEWGAFSDG 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 722 GSLamlsTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESD-S 800
Cdd:PLN02914 292 LPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDnS 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 801 LALRQVRAILED-LGLPLTSDDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIREN--RGLEELAVSVGVDGTLYKLHPRF 877
Cdd:PLN02914 368 DDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDskGMIFGKRTVVAMDGGLYEKYPQY 447

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 194097330 878 SSLVAATVREL-----APRCVVTflQSEDGSGKGAALVTA 912
Cdd:PLN02914 448 RRYMQDAVTELlglelSKNIAIE--HTKDGSGIGAALLAA 485
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 483-673 5.64e-89

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: 281.31  E-value: 5.64e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  483 LEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGE-ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVT--TGV 559
Cdd:pfam00349   2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEgSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGgdGKF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  560 QITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLS---GQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEG 636
Cdd:pfam00349  82 EITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGVVG 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 194097330  637 QDVVSLLREAITRRQaVELNVVAIVNDTVGTMMSCGY 673
Cdd:pfam00349 162 KDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAGAY 197
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 45-478 5.68e-89

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: 290.33  E-value: 5.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  45 AQLQQIQASLLGSMEQALRgqASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 124
Cdd:cd24020    4 SRLRQVADAMVVEMEAGLA--SEGGSKLKMLPSYVDNLPSGDEKGLFYALDLG--GTNFRVLRVQLGGKEGRVDKQEYEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 125 FVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQG----LQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24020   80 VPIPPELMVGTSEELFDFIAGELAKFVATEGEGFHPegekRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGaYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGR---VCVSVEWGSF 277
Cdd:cd24020  160 LLEEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRsgeMVINTEWGNF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 278 sdDGALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM-E 356
Cdd:cd24020  239 --RSSHLP-RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhE 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 357 DPSTGAARVHAILQDLGLSPGAS--DVELVQHVCAAVCTRAAQLCAAALAAVLSCLQH--SREQQTLQVAVATGGRVCER 432
Cdd:cd24020  316 DDSPDLETVARILKDALGIDDTSleARKVVVEVCDLVAERGARLAAAGIVGILKKLGRdgGGSSPAQRTVVAVDGGLYEH 395

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 194097330 433 HPRFCSVLQGTVM-LLAPEC--DVSLIPSVDGGGRGvamvtavAARLAA 478
Cdd:cd24020  396 YPKFREYMQQALVeLLGDEAadSVELELSNDGSGIG-------AALLAA 437
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 44-470 1.14e-88

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: 286.48  E-value: 1.14e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  44 RAQLQQIQASLLGSMEQALRGQASPapaVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGieGHRVEPRSQ 123
Cdd:cd24000    1 DEDLKEITDAFLEELEKGLAGEPSS---LKMLPSYVSPLPTGLESGEFLAIDLG--GTNLRVALVSLDG--KGIEVTISK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 124 EFVIPQEVMLGAGQQLFDFAAHCLSEFLDaQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLR 203
Cdd:cd24000   74 KYEIPDEIKTASAEEFFDFIADCIAEFLK-ENGLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 204 DAIRRQGaYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVavlDEDRGRVCVSVEWGSFSDDGAl 283
Cdd:cd24000  153 DALKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI---LLGDGGMIINTEWGNFGKNSL- 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 284 gpVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARcgvlfggctspallsqgsILLEHVAEMedPSTGAA 363
Cdd:cd24000  228 --PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLAD------------------EILRKICEL--VAERSA 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 364 RVHAILqdlglspgasdvelvqhvCAAVCtraaqlcaaalaavlsclQHSREQQTLQVAVATGGRVCERHPRFCSVLQGT 443
Cdd:cd24000  286 RLAAAA------------------IAALL------------------RKTGDSPEKKITIAVDGSLFEKYPGYRERLEEY 329

                        410       420
                 ....*....|....*....|....*...
gi 194097330 444 V-MLLAPECDVSLIPSVDGGGRGVAMVT 470
Cdd:cd24000  330 LkELLGRGIRIELVLVEDGSLIGAALAA 357
PLN02405 PLN02405
hexokinase
 496-912 4.18e-80

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 268.62  E-value: 4.18e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 496 QLAAVQAQMRKAMAKGLRGEA-SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLlvRVTTG------VQITSEIYSI 568
Cdd:PLN02405  54 KLRQVADAMTVEMHAGLASEGgSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVL--RVLLGgkdgrvVKQEFEEVSI 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 569 PETVAQGSGQQLFDHIVDCIVDFQQKQG-----LSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLL 643
Cdd:PLN02405 132 PPHLMTGSSDALFDFIAAALAKFVATEGedfhlPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGEL 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 644 REAItRRQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGD---SGRMCINMEWGAFGd 720
Cdd:PLN02405 212 TKAM-ERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR- 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 721 dgSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESD- 799
Cdd:PLN02405 290 --SSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDt 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 800 SLALRQVRAILED-LGLPLTS-DDALMVLEVCQAVSQRAAQLCGAGVAAVVEKIREN--RGLEELAVSVGVDGTLYKLHP 875
Cdd:PLN02405 368 SPDLKVVGSKLKDiLEIPNTSlKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHYT 447

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 194097330 876 RFSSLVAATVRELAPRCV---VTFLQSEDGSGKGAALVTA 912
Cdd:PLN02405 448 EFSKCMESTLKELLGEEVsesIEVEHSNDGSGIGAALLAA 487
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 33-230 1.52e-77

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: 250.88  E-value: 1.52e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330   33 VQECLQQFKVTRAQLQQIQASLLGSMEQALrgQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTG 112
Cdd:pfam00349   2 LEELLKQFALSDEKLKEIVDRFVEEMEKGL--AKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGT--NFRVCLVELGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  113 ieGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQG---LQLGFSFSFPCHQTGLDRSTLISWTKGFR 189
Cdd:pfam00349  78 --DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEekeLPLGFTFSFPVEQTSLDSGTLIRWTKGFD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 194097330  190 CSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVNDTVGTMMGC 230
Cdd:pfam00349 156 IPGVVGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAG 195
PLN02362 PLN02362
hexokinase
 503-912 8.01e-77

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 259.81  E-value: 8.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 503 QMRKAMA----KGLRGEA-SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLlvRVTTGVQITS------EIYSIPET 571
Cdd:PLN02362  57 QVVDAMAvemhAGLASEGgSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVL--RVQLGGQRSSilsqdvERHPIPQH 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 572 VAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLP-----LGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREA 646
Cdd:PLN02362 135 LMNSTSEVLFDFIASSLKQFVEKEENGSEFSQvrrreLGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGA 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 647 ITRRqAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV---AGVPGDSGRMCINMEWGAFgddGS 723
Cdd:PLN02362 215 LNRR-GLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIikcQGLLTTSGSMVVNMEWGNF---WS 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 724 LAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFrGQQIQRLQTRDIFKTKFLSEI-ESDSLA 802
Cdd:PLN02362 291 SHLPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPE 369

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 803 LRQVRAIL-EDLGLPLTSDDAL-MVLEVCQAVSQRAAQLCGAGVAAVVEKI-------------RENRGLEELAVsVGVD 867
Cdd:PLN02362 370 LQEVARILkETLGISEVPLKVRkLVVKICDVVTRRAARLAAAGIVGILKKIgrdgsggitsgrsRSDIQIMRRTV-VAVE 448

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 194097330 868 GTLYKLHPRFSSLVAATVRELAPRCV---VTFLQSEDGSGKGAALVTA 912
Cdd:PLN02362 449 GGLYTNYTMFREYLHEALNEILGEDVaqhVILKATEDGSGIGSALLAA 496
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 45-469 2.19e-76

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: 256.55  E-value: 2.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  45 AQLQQIQASLLGSMEQALrgqASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGieGHRVEPRSQE 124
Cdd:cd24088    2 EKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGT--NFRVCSVELHG--DGTFSLRQEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 125 FVIPQEVMLGA-GQQLFDFAAHCLSEFL-----DAQPVNKQG--LQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQ 196
Cdd:cd24088   75 SKIPDELKTGVtAKDLFDYLAKSVEAFLtkhhgDSFAAGKDDdrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 197 DVVQLLRDAIRRQGAyNIDVVAVVNDTVGTMMG---CEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD------EDRGR 267
Cdd:cd24088  155 DVVKLLQDELDRQGI-PVKVVALVNDTVGTLLArsyTSPEISGAVLGAIFGTGTNGAYLEDLEKIKKLDdssrvgKGKTH 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 268 VCVSVEWGSFSDDGALGPVlTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCT--SPALLSQG 345
Cdd:cd24088  234 MVINTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNdkSPSALNTP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 346 SIL----LEHVAEMEDPSTGAARvHAILQDLGL-SPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ 420
Cdd:cd24088  313 YGLdtavLSAIEIDSEAELRATR-KVLLDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGE 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194097330 421 VAVATGGRVCERHPRFCSVLQGTVMLLAP----ECDVSLIPSVDGGGRGVAMV 469
Cdd:cd24088  392 INIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
PLN02914 PLN02914
hexokinase
 72-471 1.10e-68

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 237.09  E-value: 1.10e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  72 VRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFL 151
Cdd:PLN02914  78 LKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 152 DAQ------PVNKQgLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVNDTVG 225
Cdd:PLN02914 156 AKEggkfhlPEGRK-REIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 226 TMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDR---GRVCVSVEWGSFSDdgalGPVLTTFDHTLDHESLNPG 302
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD----GLPLTEFDREMDAASINPG 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 303 AQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM-EDPSTGAARVHAILQD-LGLSPGASD 380
Cdd:PLN02914 310 EQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMqQDNSDDLQAVGSILYDvLGVEASLSA 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 381 VELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTL--QVAVATGGRVCERHPRFCSVLQGTVM-LLAPEC--DVSL 455
Cdd:PLN02914 390 RRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTeLLGLELskNIAI 469

                        410
                 ....*....|....*.
gi 194097330 456 IPSVDGGGRGVAMVTA 471
Cdd:PLN02914 470 EHTKDGSGIGAALLAA 485
PTZ00107 PTZ00107
hexokinase; Provisional
 39-474 2.58e-67

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 232.26  E-value: 2.58e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  39 QFKVTRAQLQQIQASLLGSMEQALRGQASPAPA-------VRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLt 111
Cdd:PTZ00107  17 QFTMSKEKLKELVDYFLYELVEGLEAHRRHRNLwipnecsFKMLDSCVYNLPTGKEKGVYYAIDFG--GTNFRAVRVSL- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 112 giEGHRVEPRSQE-FVIPQEVMLGA---------GQQLFDFAAHCLSEFLD--AQPVN-KQGLQLGFSFSFPCHQTGLDR 178
Cdd:PTZ00107  94 --RGGGKMERTQSkFSLPKSALLGEkglldkkatATDLFDHIAKSIKKMMEenGDPEDlNKPVPVGFTFSFPCTQLSVNN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 179 STLISWTKGFRCS-----GVEGQDVVQLLRDAIRRQGAyNIDVVAVVNDTVGTMMGC----EPGVRPCEVGLVVDTGTNA 249
Cdd:PTZ00107 172 AILIDWTKGFETGratndPVEGKDVGELLNDAFKRNNV-PANVVAVLNDTVGTLISCayqkPKNTPPCQVGVIIGTGSNA 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 250 CYME-EARHvavldedRGR--VCVSVEWGSFSDDgaLgPVlTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHL 326
Cdd:PTZ00107 251 CYFEpEVSA-------YGYagTPINMECGNFDSK--L-PI-TPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 327 ARCGvlfggcTSPALLSQGSILLEHVAEM-EDPSTGAARVHAILQDL-GLSPGASDVELVQHVCAAVCTRAAQLCAAALA 404
Cdd:PTZ00107 320 LQLK------APPKMWQSGSFESEDASMIlNDQSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIA 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194097330 405 AVLSCLQHSREQQTlqvaVATGGRVCERHPRFCSVLQGTV-MLLAPE-CDVSLIPSVDGGGRGVAMVTAVAA 474
Cdd:PTZ00107 394 APAKKTRTVQGKAT----VAIDGSVYVKNPWFRRLLQEYInSILGPDaGNVVFYLADDGSGKGAAIIAAMVA 461
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 38-394 3.07e-64

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 222.91  E-value: 3.07e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  38 QQFKVTRAQLQQIQASLLGSMEQALRGQASpapAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGIEGHR 117
Cdd:COG5026   13 HGFDLSSIDLEEIAAKFQEEMEKGLEGKKS---SLKMLPSYLGLPTGVKETGPVIALDAGGT--NFRVALVRFDGEGTFE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 118 VEpRSQEFVIP---QEVmlgAGQQLFDFAAHCLSEFLDaqpvnkQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVE 194
Cdd:COG5026   88 IE-NFKSFPLPgtsSEI---TAEEFFDFIADYIEPLLD------ESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 195 GQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMG---CEP-GVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCV 270
Cdd:COG5026  158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAgayADPdDGYSGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 271 SVEWGSFSddgalGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGvLFGGCTSPALLSQGSILLE 350
Cdd:COG5026  238 NMESGNFN-----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 194097330 351 HVAE-MEDPSTGAARVHAILQdlglSPGASDVELVQHVCAAVCTR 394
Cdd:COG5026  312 DMSRfLADPSDEKEILSQCLE----AGSEEDREILREIADAIVER 352
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 45-335 4.09e-64

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: 222.64  E-value: 4.09e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  45 AQLQQIQASLLGSMEQAL--RGQASPapavrMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGieGHRVEPRS 122
Cdd:cd24087    2 ERLRKITDHFISELEKGLskKGGNIP-----MIPTWVMGFPTGKETGDYLALDLGGT--NLRVCLVKLGG--NGKFDITQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 123 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVN--KQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24087   73 SKYRLPEELKTGTGEELWDFIADCLKKFVEEHFPGgkSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAyNIDVVAVVNDTVGTMMG---CEPGVrpcEVGLVVDTGTNACYMEEARHVAVLDED----RGRVCVSVE 273
Cdd:cd24087  153 MLQKALKKRNV-PIELVALINDTTGTLIAsnyTDPET---KIGVIFGTGCNAAYMEVVSNIPKLEHDdippDSPMAINCE 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194097330 274 WGSFsDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGG 335
Cdd:cd24087  229 YGAF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKG 289
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 238-472 9.59e-61

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: 206.57  E-value: 9.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  238 EVGLVVDTGTNACYMEEARHVAVLDEDR---GRVCVSVEWGSFSDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLY 314
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKLpksGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  315 LGELVRLVLAHLARCGVLFGGcTSPALLSQGSILLEHVAEME-DPSTGAARVHAILQD-LGLSPGAS-DVELVQHVCAAV 391
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIEsDPSEDLETTREILEElLGIETVTEeDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  392 CTRaaqlcaaalaavlsclqhS-------------REQQTLQVAVATGGRVCERHPRFCSVLQGTV-MLLAPECDVSLIP 457
Cdd:pfam03727 160 STR------------------AarlvaagiaailkKIGRDKKVTVGVDGSVYEKYPGFRERLQEALrELLGPGDKVVLVL 221

                         250
                  ....*....|....*
gi 194097330  458 SVDGGGRGVAMVTAV 472
Cdd:pfam03727 222 AEDGSGVGAALIAAV 236
PLN02405 PLN02405
hexokinase
 45-471 9.17e-54

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 195.44  E-value: 9.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  45 AQLQQIQASLLGSMEQALRGQAspAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 124
Cdd:PLN02405  53 GKLRQVADAMTVEMHAGLASEG--GSKLKMLISYVDNLPSGDEKGLFYALDLG--GTNFRVLRVLLGGKDGRVVKQEFEE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 125 FVIPQEVMLGAGQQLFDFAAHCLSEFL-----DAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVV 199
Cdd:PLN02405 129 VSIPPHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVV 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 200 QLLRDAIRRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVEWGS 276
Cdd:PLN02405 209 GELTKAMERVGL-DMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKwhgLLPKSGEMVINMEWGN 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 277 FSDDGAlgpVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM- 355
Cdd:PLN02405 288 FRSSHL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMh 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 356 EDPSTGAARVHAILQDLGLSPGAS--DVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHS--REQQTLQVAVATGGRVCE 431
Cdd:PLN02405 365 HDTSPDLKVVGSKLKDILEIPNTSlkMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFE 444

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 194097330 432 RHPRFCSVLQGTVM-LLAPEC--DVSLIPSVDGGGRGVAMVTA 471
Cdd:PLN02405 445 HYTEFSKCMESTLKeLLGEEVseSIEVEHSNDGSGIGAALLAA 487
PLN02596 PLN02596
hexokinase-like
 515-912 1.79e-51

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 188.55  E-value: 1.79e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 515 EASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTGVQITSEIY----SIPETVAQGSGQQLFDHIVDCIVD 590
Cdd:PLN02596  75 ETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYreeiSIPSNVLNGTSQELFDYIALELAK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 591 FQQKQGLSGQSLP-----LGFTFSFPCRQLGLDQGILLNWtKGFKASDCEGQDVVSLLREAItRRQAVELNVVAIVNDTV 665
Cdd:PLN02596 155 FVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRAL-EKHGLKIRVFALVDDTI 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 666 GTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVA---GVPGDSGRMCINMEWGAFGddgSLAMLSTRFDASVDQASINP 742
Cdd:PLN02596 233 GNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPkwqSPSPESQEIVISTEWGNFN---SCHLPITEFDASLDAESSNP 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 743 GKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQRLQTRDIFKTKFLSEIESDSLALRQV--RAILEDLGLpltSD 820
Cdd:PLN02596 310 GSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTSEDHEVvnEKLKEIFGI---TD 386

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 821 DALM----VLEVCQAVSQRAAQLCGAGVAAVVEKIREnrgLEELAVSVGVDGTLYKLHPRFSSLVAATV-----RELAPR 891
Cdd:PLN02596 387 STPMarevVAEVCDIVAERGARLAGAGIVGIIKKLGR---IENKKSVVTVEGGLYEHYRVFRNYLHSSVwemlgSELSDN 463

                        410       420
                 ....*....|....*....|.
gi 194097330 892 CVVTflQSEDGSGKGAALVTA 912
Cdd:PLN02596 464 VVIE--HSHGGSGAGALFLAA 482
PLN02362 PLN02362
hexokinase
 72-394 5.71e-45

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 170.06  E-value: 5.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  72 VRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTG----IEGHRVEPRSqefvIPQEVMLGAGQQLFDFAAHCL 147
Cdd:PLN02362  78 LKMLLTFVDDLPTGSEIGTYYALDLG--GTNFRVLRVQLGGqrssILSQDVERHP----IPQHLMNSTSEVLFDFIASSL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 148 SEFL-----DAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVND 222
Cdd:PLN02362 152 KQFVekeenGSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LDMRVAALVND 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 223 TVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVEWGSFSDDGAlgpVLTTFDHTLDHESL 299
Cdd:PLN02362 231 TVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKcqgLLTTSGSMVVNMEWGNFWSSHL---PRTSYDIDLDAESP 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 300 NPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTS----PALLSQGSILLEHvaemEDPSTGAARVHAILQD-LGL 374
Cdd:PLN02362 308 NPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGPVSSrlstPFVLRTPSVAAMH----EDDSPELQEVARILKEtLGI 383

                        330       340
                 ....*....|....*....|.
gi 194097330 375 SPGASDV-ELVQHVCAAVCTR 394
Cdd:PLN02362 384 SEVPLKVrKLVVKICDVVTRR 404
PLN02596 PLN02596
hexokinase-like
 46-394 6.81e-37

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 145.79  E-value: 6.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330  46 QLQQIQASLLGSMEQALRGQASPApaVRMLPTYVGSTPHGTEQGDFVVLELgaTGASLRVLWVTLTGIEGHRVEPRSQEF 125
Cdd:PLN02596  55 KLWEVADALVSDMTASLTAEETTT--LNMLVSYVASLPSGDEKGLYYGLNL--RGSNFLLLRARLGGKNEPISDLYREEI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 126 VIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNK-----QGLQLGFSFSFPCHQTGLDRSTLISWtKGFRCSGVEGQDVVQ 200
Cdd:PLN02596 131 SIPSNVLNGTSQELFDYIALELAKFVAEHPGDEadtpeRVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVN 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 201 LLRDAIRRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDE---DRGRVCVSVEWGSF 277
Cdd:PLN02596 210 DINRALEKHGL-KIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097330 278 SddgALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM-E 356
Cdd:PLN02596 289 N---SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMhQ 365

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 194097330 357 DPSTGAARVHAILQD-LGL---SPGASdvELVQHVCAAVCTR 394
Cdd:PLN02596 366 DTSEDHEVVNEKLKEiFGItdsTPMAR--EVVAEVCDIVAER 405
 
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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