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Conserved domains on  [gi|74150193|dbj|BAE24390|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 489-915 0e+00

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


The actual alignment was detected with superfamily member cd24091:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 433  Bit Score: 767.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIIN 562
Cdd:cd24091   1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24091  81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                       410       420       430
                ....*....|....*....|....*....|...
gi 74150193 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTAVACR 915
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 39-469 0e+00

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


The actual alignment was detected with superfamily member cd24090:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 431  Bit Score: 710.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24090   1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24090  81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                       410       420       430
                ....*....|....*....|....*....|.
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
 
Name Accession Description Interval E-value
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 489-915 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: 767.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIIN 562
Cdd:cd24091   1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24091  81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                       410       420       430
                ....*....|....*....|....*....|...
gi 74150193 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTAVACR 915
Cdd:cd24091 401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 39-469 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: 710.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24090   1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24090  81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                       410       420       430
                ....*....|....*....|....*....|.
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 678-912 1.72e-102

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: 318.67  E-value: 1.72e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   678 EMGLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMY 754
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   755 LGEIVRHILLHLTNLGVLFRGQkTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGL-TLTSDDALMVLEVCQAV 831
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEElLGIeTVTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   832 SRRAAQLCGAGVAAVVEKIRENRglqelTVSVGVDGTLYKLHPHFSKLVSATVRK-LAPQCTVTFLQSEDGSGKGAALVT 910
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 74150193   911 AV 912
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 488-913 5.20e-101

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 323.17  E-value: 5.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  488 FQLTLEQMTVVQAQMRVAMIRGLQG----------EASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGS 557
Cdd:PTZ00107  18 FTMSKEKLKELVDYFLYELVEGLEAhrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  558 VQIINQ-VYSIPECRAQG---------SGQKLFDHIVDCIVDFQKRQGL---SGQSLPLGFTFSFPCKQLGLDQGILLNW 624
Cdd:PTZ00107  98 KMERTQsKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPVGFTFSFPCTQLSVNNAILIDW 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  625 TKGF-----NASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPR----CEMGLIVGTGTNACYME-- 693
Cdd:PTZ00107 178 TKGFetgraTNDPVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVIIGTGSNACYFEpe 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  694 -ELRNVASVPgdsglmcINMEWGAFgdDGSLGTlsTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVL 772
Cdd:PTZ00107 257 vSAYGYAGTP-------INMECGNF--DSKLPI--TPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKAP 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  773 FRGQKtqclqaRDIFKTKFLSEIESD-SLALRQVRAILEDL-GLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI 850
Cdd:PTZ00107 326 PKMWQ------SGSFESEDASMILNDqSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKT 399

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74150193  851 RENRGLqeltVSVGVDGTLYKLHPHFSKLVSATVRK-LAPQ-CTVTFLQSEDGSGKGAALVTAVA 913
Cdd:PTZ00107 400 RTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 488-914 3.71e-97

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 311.89  E-value: 3.71e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 488 FQLTLEQMTVVQAQMRVAMIRGLQGEASSLRMLPTYVrATPDGS-ERGDFLALDLGGTNFRVLLVRVA-EGSVQIIN-QV 564
Cdd:COG5026  15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFDgEGTFEIENfKS 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 565 YSIPECRAQGSGQKLFDHIVDCIVDfqkrqgLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLRE 644
Cdd:COG5026  94 FPLPGTSSEITAEEFFDFIADYIEP------LLDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEA 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 645 AIRRRQAVELNVVAIVNDTVGTMMSCGYDDP----RCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGdd 720
Cdd:COG5026 168 ALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNFN-- 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 721 gslGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGvLFRGQKTQCLQARDIFKTKFLSE-IESDS 799
Cdd:COG5026 246 ---KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRfLADPS 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 800 LALRQVRAILEDlgltLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI-RENRGLQELTVSvgVDGTLYKLHPHFSK 878
Cdd:COG5026 322 DEKEILSQCLEA----GSEEDREILREIADAIVERAARLVAATLAGILLHLgPGKTPLKPHCIA--IDGSTYEKMPGLAE 395

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 74150193 879 LVSATVRK-LAPQCT--VTFLQSEDGSGKGAALVTAVAC 914
Cdd:COG5026 396 KIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 33-228 4.37e-74

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: 241.25  E-value: 4.37e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193    33 ECLQQFKVTRTQLQQIQASLLCSMEQALKGQDSPapSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGtk 112
Cdd:pfam00349   4 ELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSS--SLKMLPTYVTSLPTGTEKGTFLALDLGGT--NFRVCLVELGG-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   113 ECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQG---LKLGFNFSFPCHQTGLDRSTLISWTKGFRCS 189
Cdd:pfam00349  78 DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEekeLPLGFTFSFPVEQTSLDSGTLIRWTKGFDIP 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 74150193   190 GVEGQDVVQLLRDAIQRQGtYRIDVVAMVNDTVGTMMGC 228
Cdd:pfam00349 158 GVVGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAG 195
PLN02914 PLN02914
hexokinase
 70-469 1.77e-70

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 242.10  E-value: 1.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   70 VRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFL 149
Cdd:PLN02914  78 LKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  150 ----DAYPVEnQGLK--LGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRIDVVAMVNDTVG 223
Cdd:PLN02914 156 akegGKFHLP-EGRKreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  224 TMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSFYDedalGPVLTTFDSALDRESLTPG 300
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD----GLPLTEFDREMDAASINPG 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  301 AQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCIL-LDHVAEM-EDTATGTARVHTILQD-LGLSPRAS 377
Cdd:PLN02914 310 EQIFEKTISGMYLGEIVRRVLLKMAETSDLF-GHFVPEKLSTPFALrTPHLCAMqQDNSDDLQAVGSILYDvLGVEASLS 388

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  378 DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTL--QVAVATGGRVFERHPRFLRILKETVT-LLAP--NCDVS 452
Cdd:PLN02914 389 ARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTeLLGLelSKNIA 468

                        410
                 ....*....|....*..
gi 74150193  453 FIPSVDGGGRGVAMVTA 469
Cdd:PLN02914 469 IEHTKDGSGIGAALLAA 485
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 36-392 1.66e-62

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 218.29  E-value: 1.66e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  36 QQFKVTRTQLQQIQASLLCSMEQALKGQDSpapSVRMLPTYVrSTPHG-TEQGDFLVLELGATgaSLRVLWVTLTGTKEC 114
Cdd:COG5026  13 HGFDLSSIDLEEIAAKFQEEMEKGLEGKKS---SLKMLPSYL-GLPTGvKETGPVIALDAGGT--NFRVALVRFDGEGTF 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 115 RVEpRSREFVIP---QEVilgAGQQLFDFAARCLSEFLDaypvenQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGV 191
Cdd:COG5026  87 EIE-NFKSFPLPgtsSEI---TAEEFFDFIADYIEPLLD------ESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 192 EGQDVVQLLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPC----EVGLIVDTGTNACYMEEARHVAALDEDRGRTC 267
Cdd:COG5026 157 EGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMI 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 268 VSIEWGSFydedALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGvLFDGCASPALLSQGCIll 347
Cdd:COG5026 237 INMESGNF----NKLP-RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSL-- 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 74150193 348 dHVAEMEDTATGTARVHTILQDLGLSPRASDAELVQYVCVAVCTR 392
Cdd:COG5026 309 -TTVDMSRFLADPSDEKEILSQCLEAGSEEDREILREIADAIVER 352
 
Name Accession Description Interval E-value
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 489-915 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: 767.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIIN 562
Cdd:cd24091   1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24091  81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24091 161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24091 241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24091 321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                       410       420       430
                ....*....|....*....|....*....|...
gi 74150193 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTAVACR 915
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 ...
 489-915 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: 754.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY 565
Cdd:cd24129   1 QLSHDQLAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 566 SIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREA 645
Cdd:cd24129  81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 646 IRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSLGT 725
Cdd:cd24129 161 ATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCLAM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 726 LSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALRQV 805
Cdd:cd24129 241 ISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALRQV 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 806 RAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSATVR 885
Cdd:cd24129 321 RAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQATVR 400

                       410       420       430
                ....*....|....*....|....*....|
gi 74150193 886 KLAPQCTVTFLQSEDGSGKGAALVTAVACR 915
Cdd:cd24129 401 ELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 39-469 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: 710.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24090   1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24090  81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                       410       420       430
                ....*....|....*....|....*....|.
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 489-916 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: 661.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIIN 562
Cdd:cd24128   1 QLSHDQLLEVKRRMKVEMERGLSKEthaSAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGkwrGVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24128  81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24128 161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24128 241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24128 321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                       410       420       430
                ....*....|....*....|....*....|....
gi 74150193 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 916
Cdd:cd24128 401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 489-911 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: 652.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGS-VQIINQV 564
Cdd:cd24019   1 RLSDEQLEEIMDRLLKEMEKGLSKDthpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSqVKMESEI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 565 YSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLRE 644
Cdd:cd24019  81 YAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 645 AIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNV---ASVPGDSGLMCINMEWGAFGDDG 721
Cdd:cd24019 161 AIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVekwDGDEGDPGQVIINTEWGAFGDNG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 722 SLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSL- 800
Cdd:cd24019 241 VLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDNEg 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 801 ALRQVRAILEDLGLTLTSD-DALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRglqeltVSVGVDGTLYKLHPHFSKL 879
Cdd:cd24019 321 DFSNTREILKELGLEDASDeDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKE------VTVGVDGSLYKYHPKFHKR 394

                       410       420       430
                ....*....|....*....|....*....|...
gi 74150193 880 VSATVRKLAP-QCTVTFLQSEDGSGKGAALVTA 911
Cdd:cd24019 395 MHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 490-916 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: 638.11  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 490 LTLEQMTVVQAQMRVAMIRGLQG---EASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG---SVQIINQ 563
Cdd:cd24127   2 LTKDMLLEVKKRMRAEMELGLRKqthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGkkrTVEMHNK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 564 VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLR 643
Cdd:cd24127  82 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 644 EAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSL 723
Cdd:cd24127 162 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 724 GTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALR 803
Cdd:cd24127 242 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 804 QVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSAT 883
Cdd:cd24127 322 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQT 401

                       410       420       430
                ....*....|....*....|....*....|...
gi 74150193 884 VRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 916
Cdd:cd24127 402 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 489-916 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: 628.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG--SVQIINQ 563
Cdd:cd24130   1 QLTRDQLQEVKQKMRTELEYGLKKEThptASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGrrSVRMYNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 564 VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLR 643
Cdd:cd24130  81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 644 EAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSL 723
Cdd:cd24130 161 EAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGCI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 724 GTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALR 803
Cdd:cd24130 241 DDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 804 QVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSAT 883
Cdd:cd24130 321 QVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQET 400

                       410       420       430
                ....*....|....*....|....*....|...
gi 74150193 884 VRKLAPQCTVTFLQSEDGSGKGAALVTAVACRL 916
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 ...
 489-911 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: 607.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGS---VQIIN 562
Cdd:cd24089   1 RLSDETLLDISRRFRKEMEKGLGKDThptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKnqkVEMES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24089  81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24089 161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24089 241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24089 321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 74150193 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 911
Cdd:cd24089 401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 489-911 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: 553.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGEASS---LRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAE---GSVQIIN 562
Cdd:cd24126   1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPtaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEdgkQKVQMES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24126  81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24126 161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24126 241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24126 321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 74150193 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 911
Cdd:cd24126 401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 39-469 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: 550.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGtkECRVEP 118
Cdd:cd24019   1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLG--GTNFRVLLVTLNG--GSQVKM 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24019  77 ESEIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVR 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSF 275
Cdd:cd24019 157 LLQEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEgdpGQVIINTEWGAF 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 276 YDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEME- 354
Cdd:cd24019 237 GDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIEs 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 355 DTATGTARVHTILQDLGLSPR-ASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLqhsreqQTLQVAVATGGRVFERHPR 433
Cdd:cd24019 317 DNEGDFSNTREILKELGLEDAsDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRM------NRKEVTVGVDGSLYKYHPK 390

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 74150193 434 FLRILKETVTLLAP-NCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24019 391 FHKRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 489-911 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: 537.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGEA---SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQII---N 562
Cdd:cd24125   1 RLSDETLLEISKRFRKEMEKGLGATThptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVemeN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 563 QVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLL 642
Cdd:cd24125  81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 643 REAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGS 722
Cdd:cd24125 161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 723 LGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLAL 802
Cdd:cd24125 241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 803 RQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSA 882
Cdd:cd24125 321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                       410       420
                ....*....|....*....|....*....
gi 74150193 883 TVRKLAPQCTVTFLQSEDGSGKGAALVTA 911
Cdd:cd24125 401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 481-915 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: 529.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 481 LEETLAPFQLTLEQMTVVQAQMRVAMIRGLQ---GEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEG- 556
Cdd:cd24092   2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRletHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGe 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 557 ----SVQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASG 632
Cdd:cd24092  82 egqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 633 CEGQDVVYLLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINM 712
Cdd:cd24092 162 AEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 713 EWGAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFL 792
Cdd:cd24092 242 EWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFV 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 793 SEIESDSLALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKL 872
Cdd:cd24092 322 SQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 401

                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 74150193 873 HPHFSKLVSATVRKLAPQCTVTFLQSEDGSGKGAALVTAVACR 915
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 ...
 481-918 4.12e-174

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: 513.40  E-value: 4.12e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 481 LEETLAPFQLTLEQMTVVQAQMRVAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVA--- 554
Cdd:cd24124  21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNhek 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 555 EGSVQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCE 634
Cdd:cd24124 101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 635 GQDVVYLLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEW 714
Cdd:cd24124 181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 715 GAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSE 794
Cdd:cd24124 261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 795 IESDSLALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHP 874
Cdd:cd24124 341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 74150193 875 HFSKLVSATVRKLAPQCTVTFLQSEDGSGKGAALVTAVACRLTQ 918
Cdd:cd24124 421 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAE 464
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 44-469 1.04e-170

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: 503.15  E-value: 1.04e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  44 QLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREF 123
Cdd:cd24089   6 TLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLG--GSNFRVLWVQVNDEKNQKVEMESQVY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 124 VIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDA 203
Cdd:cd24089  84 AIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLRKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 204 IQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGP 283
Cdd:cd24089 164 IRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGSLED 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 284 VLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARV 363
Cdd:cd24089 244 IRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGLANA 323

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 364 HTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVT 443
Cdd:cd24089 324 KEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHKAVR 403

                       410       420
                ....*....|....*....|....*.
gi 74150193 444 LLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24089 404 RLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 492-909 9.20e-165

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: 487.91  E-value: 9.20e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 492 LEQMTVVQAQMRVAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV--AEGSVQIINQVYSIPE 569
Cdd:cd24018   1 VSKLEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLdgNGGIFIIVQRKYKIPD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 570 CRAQGSGQKLFDHIVDCIVDFQKRQGLSGQS---LPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAI 646
Cdd:cd24018  81 EAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 647 RRRQaVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNV------ASVPGDSGLMCINMEWGAFGDD 720
Cdd:cd24018 161 DRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWGAFDNE 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 721 GS-LGTlsTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDS 799
Cdd:cd24018 240 REvLPL--TKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADT 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 800 LA-LRQVRAILEDLGLT--LTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIREnrgLQELTVSVGVDGTLYKLHPHF 876
Cdd:cd24018 318 SPdLDAVRDILKELLAIdnTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGS---LLPEPVTVGIDGSVYEKYPGF 394

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 74150193 877 SKLVSATVRKLAPQCT---VTFLQSEDGSGKGAALV 909
Cdd:cd24018 395 KDRLSEALRELFGPEVkanISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 489-911 1.69e-151

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: 453.61  E-value: 1.69e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 489 QLTLEQMTVVQAQMRVAMIRGLQGE---ASSLRMLPTYVRATPDGSERGDFLALDLG--GTNFRVLLVRVA--EG-SVQI 560
Cdd:cd24090   1 KVTRAQLQQIQASLLGSMEQALRGQaspAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTgiEGhRVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 561 INQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVY 640
Cdd:cd24090  81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 641 LLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDD 720
Cdd:cd24090 161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 721 GSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSL 800
Cdd:cd24090 241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 801 ALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLV 880
Cdd:cd24090 321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                       410       420       430
                ....*....|....*....|....*....|.
gi 74150193 881 SATVRKLAPQCTVTFLQSEDGSGKGAALVTA 911
Cdd:cd24090 401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 39-469 4.40e-146

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: 439.71  E-value: 4.40e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24125   1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLG--GTNFRVLWVKVSDNGLQKVEM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24125  79 ENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24125 159 LLRKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDD 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24125 239 GSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKD 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24125 319 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRL 398

                       410       420       430
                ....*....|....*....|....*....|.
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTA 469
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 ...
 39-473 3.25e-145

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: 437.36  E-value: 3.25e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24091   1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLG--GTNFRVLLVKVRSGKWRGVEM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24091  79 HNKIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24091 159 LLREAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDN 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24091 239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24091 319 ALLQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVM 398

                       410       420       430
                ....*....|....*....|....*....|....*
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAAR 473
Cdd:cd24091 399 HETVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 44-469 1.80e-143

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: 432.74  E-value: 1.80e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  44 QLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREF 123
Cdd:cd24126   6 TLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLG--GSKFRVLRVKVSEDGKQKVQMESQFY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 124 VIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDA 203
Cdd:cd24126  84 PTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLRKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 204 IQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGP 283
Cdd:cd24126 164 IRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGSLED 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 284 VLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARV 363
Cdd:cd24126 244 IRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGLYNT 323

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 364 HTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVT 443
Cdd:cd24126 324 REILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHKVVR 403

                       410       420
                ....*....|....*....|....*.
gi 74150193 444 LLAPNCDVSFIPSVDGGGRGVAMVTA 469
Cdd:cd24126 404 RLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 35-485 8.12e-142

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: 430.19  E-value: 8.12e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  35 LQQFKVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEC 114
Cdd:cd24124  25 LYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILRVQVNHEKNQ 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 115 RVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQ 194
Cdd:cd24124 103 NVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGA 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 195 DVVQLLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGS 274
Cdd:cd24124 183 DVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGA 262

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 275 FYDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEME 354
Cdd:cd24124 263 FGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIE 342

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 355 DTATGTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRF 434
Cdd:cd24124 343 KNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQY 422

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 74150193 435 LRILKETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARLAAHRRILEETL 485
Cdd:cd24124 423 SRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 39-473 2.40e-135

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: 411.97  E-value: 2.40e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTgtkECRVEP 118
Cdd:cd24129   1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLG--GTNFRVLLVHVG---TAGVQI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24129  76 TSEIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVS 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24129 156 LLREAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDN 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24129 236 GCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24129 316 ALRQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLV 395

                       410       420       430
                ....*....|....*....|....*....|....*
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAAR 473
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 ...
 39-474 9.48e-135

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: 410.44  E-value: 9.48e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24128   1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLG--GTNFRVLLVRVRNGKWRGVEM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24128  79 HNKIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24128 159 LLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDN 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24128 239 GCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24128 319 ALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVM 398

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARL 474
Cdd:cd24128 399 HETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 39-474 3.94e-133

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: 406.22  E-value: 3.94e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEP 118
Cdd:cd24127   1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLG--GTNFRVLLVKIRSGKKRTVEM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24127  79 HNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24127 159 LLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDN 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24127 239 GCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24127 319 ALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIM 398

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARL 474
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 ...
 39-474 3.18e-130

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: 398.54  E-value: 3.18e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  39 KVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEcRVEP 118
Cdd:cd24130   1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLG--GTNFRVLLVKIRSGRR-SVRM 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 119 RSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24130  78 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDE 278
Cdd:cd24130 158 MLREAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDN 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 279 DALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTAT 358
Cdd:cd24130 238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 359 GTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRIL 438
Cdd:cd24130 318 ALLQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRIL 397

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 74150193 439 KETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARL 474
Cdd:cd24130 398 QETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 493-910 2.38e-128

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: 390.87  E-value: 2.38e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 493 EQMTVVQAQMRVAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECR 571
Cdd:cd24000   2 EDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLdGKGIEVTISKKYEIPDEI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 572 AQGSGQKLFDHIVDCIVDFQKRQGLSgQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRQa 651
Cdd:cd24000  82 KTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALKKRG- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 652 VELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNvasVPGDSGLMCINMEWGAFGDDGSLGtlsTRFD 731
Cdd:cd24000 160 LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKNSLPR---TEYD 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 732 TSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLtnlgvlfrgqktqclqARDIFKTkflseiesdslalrqvrailed 811
Cdd:cd24000 234 REVDKASENPGFQPLEKMVSGKYLGELVRLILKDL----------------ADEILRK---------------------- 275

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 812 lgltltsddalmvleVCQAVSRRAAQLCGAGVAAVVEKIRENrglQELTVSVGVDGTLYKLHPHFSKLVSATVRKL-APQ 890
Cdd:cd24000 276 ---------------ICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLKELlGRG 337

                       410       420
                ....*....|....*....|
gi 74150193 891 CTVTFLQSEDGSGKGAALVT 910
Cdd:cd24000 338 IRIELVLVEDGSLIGAALAA 357
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 35-473 5.10e-125

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: 385.39  E-value: 5.10e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  35 LQQFKVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKE- 113
Cdd:cd24092   6 LAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLG--GTNFRVMLVKVGEGEEg 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 114 -CRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVE 192
Cdd:cd24092  84 qWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAE 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 193 GQDVVQLLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEW 272
Cdd:cd24092 164 GNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEW 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 273 GSFYDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAE 352
Cdd:cd24092 244 GAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQ 323

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 353 MEDTATGTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHP 432
Cdd:cd24092 324 VESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHP 403

                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 74150193 433 RFLRILKETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAAR 473
Cdd:cd24092 404 SFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 490-913 1.34e-119

nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth.


Pssm-ID: 466870 [Multi-domain]  Cd Length: 439  Bit Score: 371.22  E-value: 1.34e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 490 LTLEQMTVVQAQMRVAMIRGLQGEA-SSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY--- 565
Cdd:cd24020   1 TPVSRLRQVADAMVVEMEAGLASEGgSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYeev 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 566 SIPECRAQGSGQKLFDHIVDCIVDFQKRQG----LSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYL 641
Cdd:cd24020  81 PIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 642 LREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFg 718
Cdd:cd24020 161 LEEALER-QGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF- 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 719 DDGSLGtlSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEI-ES 797
Cdd:cd24020 239 RSSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhED 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 798 DSLALRQVRAILED-LGLTLTS-DDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI-RENRGLQELTVS-VGVDGTLYKLH 873
Cdd:cd24020 317 DSPDLETVARILKDaLGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGSSPAQRTvVAVDGGLYEHY 396

                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 74150193 874 PHFSKLVSATVRKL---APQCTVTFLQSEDGSGKGAALVTAVA 913
Cdd:cd24020 397 PKFREYMQQALVELlgdEAADSVELELSNDGSGIGAALLAAAH 439
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 43-467 8.84e-116

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: 360.80  E-value: 8.84e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  43 TQLQQIQASLLCSMEQALKGQDSpapSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKEcRVEPRSRE 122
Cdd:cd24018   2 SKLEEIVKHFLSEMEKGLEGDGG---SLPMLPSFVTERPTGKETGTYLALDLGGT--NLRVCLVTLDGNGG-IFIIVQRK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 123 FVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQG---LKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQL 199
Cdd:cd24018  76 YKIPDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVEL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 200 LRDAIQRQGtYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALD------EDRGRTCVSIEWG 273
Cdd:cd24018 156 LQNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsgsvTKSDEMIINTEWG 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 274 SFYDEDALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEM 353
Cdd:cd24018 235 AFDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 354 E-DTATGTARVHTILQDLGLSPRAS--DAELVQYVCVAVCTRaaqLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFER 430
Cdd:cd24018 314 EaDTSPDLDAVRDILKELLAIDNTTleDRKLIKRICELVSTR---AARLSAAAIAAILLKRGSLLPEPVTVGIDGSVYEK 390

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 74150193 431 HPRFLRILKETVTLLAPNC---DVSFIPSVDGGGRGVAMV 467
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) ...
 508-913 1.09e-113

nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.


Pssm-ID: 466937 [Multi-domain]  Cd Length: 428  Bit Score: 355.14  E-value: 1.09e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 508 RGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECRAQGSGQKLFDHIVDC 586
Cdd:cd24087  17 KGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLgGNGKFDITQSKYRLPEELKTGTGEELWDFIADC 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 587 IVDF---QKRQGLSGQsLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRQaVELNVVAIVNDT 663
Cdd:cd24087  97 LKKFveeHFPGGKSEP-LPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKKRN-VPIELVALINDT 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 664 VGTMMSCGYDDPRCEMGLIVGTGTNACYMEelrNVASVP-------GDSGLMCINMEWGAFgDDGSLGTLSTRFDTSVDQ 736
Cdd:cd24087 175 TGTLIASNYTDPETKIGVIFGTGCNAAYME---VVSNIPklehddiPPDSPMAINCEYGAF-DNEHLVLPRTKYDVIIDE 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 737 ASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLA--LRQVRAILEDLGL 814
Cdd:cd24087 251 ESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEnlEDTDDLFQHFFGL 330

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 815 TLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKirenRGLQelTVSVGVDGTLYKLHPHFSKLVSATVRKL----APQ 890
Cdd:cd24087 331 ETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYK--TCHVAADGSVYNKYPGFKERAAQALKDIfgwdGED 404

                       410       420
                ....*....|....*....|...
gi 74150193 891 CTVTFLQSEDGSGKGAALVTAVA 913
Cdd:cd24087 405 DPIKTVPAEDGSGVGAAIIAALT 427
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 506-909 1.44e-106

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: 337.06  E-value: 1.44e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 506 MIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRV-AEGSVQIINQVYSIPECRAQGSGQK-LFDHI 583
Cdd:cd24088  15 MEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELhGDGTFSLRQEKSKIPDELKTGVTAKdLFDYL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 584 VDCIVDFQK-------RQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRrQAVELNV 656
Cdd:cd24088  95 AKSVEAFLTkhhgdsfAAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDR-QGIPVKV 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 657 VAIVNDTVGTMMSCGYDDPRCE---MGLIVGTGTNACYMEELRNV-----ASVPGDS-GLMCINMEWGAFgdDGSLGTL- 726
Cdd:cd24088 174 VALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddSSRVGKGkTHMVINTEWGSF--DNELKVLp 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 727 STRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTN---LGVLFRGQKTQCLQARDIFKTKFLSEIESDSLA-L 802
Cdd:cd24088 252 TTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKqglFLIQYNDKSPSALNTPYGLDTAVLSAIEIDSEAeL 331

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 803 RQVRAIL-EDLGL-TLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLV 880
Cdd:cd24088 332 RATRKVLlDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEINIGVDGSVIEFYPGFESML 411

                       410       420       430
                ....*....|....*....|....*....|...
gi 74150193 881 SATVRKLAPQCT----VTFLQSEDGSGKGAALV 909
Cdd:cd24088 412 REALRLLLIGAEgekrIKIGIAKDGSGVGAALC 444
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 678-912 1.72e-102

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: 318.67  E-value: 1.72e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   678 EMGLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMY 754
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   755 LGEIVRHILLHLTNLGVLFRGQkTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGL-TLTSDDALMVLEVCQAV 831
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEElLGIeTVTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   832 SRRAAQLCGAGVAAVVEKIRENRglqelTVSVGVDGTLYKLHPHFSKLVSATVRK-LAPQCTVTFLQSEDGSGKGAALVT 910
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 74150193   911 AV 912
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 488-913 5.20e-101

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 323.17  E-value: 5.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  488 FQLTLEQMTVVQAQMRVAMIRGLQG----------EASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGS 557
Cdd:PTZ00107  18 FTMSKEKLKELVDYFLYELVEGLEAhrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  558 VQIINQ-VYSIPECRAQG---------SGQKLFDHIVDCIVDFQKRQGL---SGQSLPLGFTFSFPCKQLGLDQGILLNW 624
Cdd:PTZ00107  98 KMERTQsKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPVGFTFSFPCTQLSVNNAILIDW 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  625 TKGF-----NASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPR----CEMGLIVGTGTNACYME-- 693
Cdd:PTZ00107 178 TKGFetgraTNDPVEGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVIIGTGSNACYFEpe 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  694 -ELRNVASVPgdsglmcINMEWGAFgdDGSLGTlsTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVL 772
Cdd:PTZ00107 257 vSAYGYAGTP-------INMECGNF--DSKLPI--TPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKAP 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  773 FRGQKtqclqaRDIFKTKFLSEIESD-SLALRQVRAILEDL-GLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI 850
Cdd:PTZ00107 326 PKMWQ------SGSFESEDASMILNDqSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKT 399

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74150193  851 RENRGLqeltVSVGVDGTLYKLHPHFSKLVSATVRK-LAPQ-CTVTFLQSEDGSGKGAALVTAVA 913
Cdd:PTZ00107 400 RTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 488-914 3.71e-97

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 311.89  E-value: 3.71e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 488 FQLTLEQMTVVQAQMRVAMIRGLQGEASSLRMLPTYVrATPDGS-ERGDFLALDLGGTNFRVLLVRVA-EGSVQIIN-QV 564
Cdd:COG5026  15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFDgEGTFEIENfKS 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 565 YSIPECRAQGSGQKLFDHIVDCIVDfqkrqgLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLRE 644
Cdd:COG5026  94 FPLPGTSSEITAEEFFDFIADYIEP------LLDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEA 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 645 AIRRRQAVELNVVAIVNDTVGTMMSCGYDDP----RCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGdd 720
Cdd:COG5026 168 ALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIINMESGNFN-- 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 721 gslGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGvLFRGQKTQCLQARDIFKTKFLSE-IESDS 799
Cdd:COG5026 246 ---KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVDMSRfLADPS 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 800 LALRQVRAILEDlgltLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKI-RENRGLQELTVSvgVDGTLYKLHPHFSK 878
Cdd:COG5026 322 DEKEILSQCLEA----GSEEDREILREIADAIVERAARLVAATLAGILLHLgPGKTPLKPHCIA--IDGSTYEKMPGLAE 395

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 74150193 879 LVSATVRK-LAPQCT--VTFLQSEDGSGKGAALVTAVAC 914
Cdd:COG5026 396 KIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 44-468 1.69e-91

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: 294.18  E-value: 1.69e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  44 QLQQIQASLLCSMEQALKGQDSpapSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKEcrVEPRSREF 123
Cdd:cd24000   3 DLKEITDAFLEELEKGLAGEPS---SLKMLPSYVSPLPTGLESGEFLAIDLG--GTNLRVALVSLDGKGI--EVTISKKY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 124 VIPQEVILGAGQQLFDFAARCLSEFLDAYPVeNQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDA 203
Cdd:cd24000  76 EIPDEIKTASAEEFFDFIADCIAEFLKENGL-KKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 204 IQRQGtYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVaalDEDRGRTCVSIEWGSFYDEDAlgp 283
Cdd:cd24000 155 LKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI---LLGDGGMIINTEWGNFGKNSL--- 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 284 VLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHgvlfdgcaspallsqgciLLDHVAEMedtatgtarv 363
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------ILRKICEL---------- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 364 htilqdlgLSPRAsdAELVQYVCVAVctraaqlcaaalaavlsrLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVT 443
Cdd:cd24000 280 --------VAERS--ARLAAAAIAAL------------------LRKTGDSPEKKITIAVDGSLFEKYPGYRERLEEYLK 331

                       410       420
                ....*....|....*....|....*.
gi 74150193 444 -LLAPNCDVSFIPSVDGGGRGVAMVT 468
Cdd:cd24000 332 eLLGRGIRIELVLVEDGSLIGAALAA 357
PLN02914 PLN02914
hexokinase
 452-911 6.29e-91

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 297.18  E-value: 6.29e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  452 SFIPSVDGGGRGVAMvTAVAARLAAHRRILEETLAPFQLTLEQMTVVQAQMRVAMIRGLQGE-ASSLRMLPTYVRATPDG 530
Cdd:PLN02914  13 SFTFSSRPRRRPRSR-MAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDgGGDLKMILSYVDSLPSG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  531 SERGDFLALDLGGTNFRVLLVRVAEGSVQII----NQVySIPECRAQGSGQKLFDHIVDCIVDFQKRQG-----LSGQSL 601
Cdd:PLN02914  92 NEKGLFYALDLGGTNFRVLRVQLGGKDERVIatefEQV-SIPQELMFGTSEELFDFIASGLANFVAKEGgkfhlPEGRKR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  602 PLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGL 681
Cdd:PLN02914 171 EIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMER-QGLDMRVSALVNDTVGTLAGARYWDDDVMVAV 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  682 IVGTGTNACYMEELRNVASVPG---DSGLMCINMEWGAFGDdgslGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEI 758
Cdd:PLN02914 250 ILGTGTNACYVERTDAIPKLQGqksSSGRTIINTEWGAFSD----GLPLTEFDREMDAASINPGEQIFEKTISGMYLGEI 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  759 VRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGLTLTSDDALMVLEVCQAVSRRAA 836
Cdd:PLN02914 326 VRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDnSDDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGG 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  837 QLCGAGVAAVVEKIRENR---GLQELTVsVGVDGTLYKLHPHFSK-LVSATVRKLAPQCT--VTFLQSEDGSGKGAALVT 910
Cdd:PLN02914 406 RLAGAGIVGILEKMEEDSkgmIFGKRTV-VAMDGGLYEKYPQYRRyMQDAVTELLGLELSknIAIEHTKDGSGIGAALLA 484


                 .
gi 74150193  911 A 911
Cdd:PLN02914 485 A 485
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 44-476 9.56e-88

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: 286.86  E-value: 9.56e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  44 QLQQIQASLLCSMEQALKGQdsPAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGtKECRVEPR-SRE 122
Cdd:cd24020   5 RLRQVADAMVVEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLG--GTNFRVLRVQLGG-KEGRVDKQeYEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 123 FVIPQEVILGAGQQLFDFAARCLSEFLDAYP----VENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:cd24020  80 VPIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 199 LLRDAIQRQGtYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRT---CVSIEWGSF 275
Cdd:cd24020 160 LLEEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSgemVINTEWGNF 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 276 YdeDALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEM-E 354
Cdd:cd24020 239 R--SSHLP-RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhE 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 355 DTATGTARVHTILQDLGLSPRAS--DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQH--SREQQTLQVAVATGGRVFER 430
Cdd:cd24020 316 DDSPDLETVARILKDALGIDDTSleARKVVVEVCDLVAERGARLAAAGIVGILKKLGRdgGGSSPAQRTVVAVDGGLYEH 395

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 74150193 431 HPRFLRILKETVT-LLAPNC--DVSFIPSVDGGGRGvamvtavAARLAA 476
Cdd:cd24020 396 YPKFREYMQQALVeLLGDEAadSVELELSNDGSGIG-------AALLAA 437
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 480-672 1.07e-84

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: 269.76  E-value: 1.07e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   480 ILEETLAPFQLTLEQMTVVQAQMRVAMIRGLQGE-ASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVA-EGS 557
Cdd:pfam00349   1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEgSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGgDGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   558 VQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLS---GQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCE 634
Cdd:pfam00349  81 FEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGVV 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 74150193   635 GQDVVYLLREAIRRRQaVELNVVAIVNDTVGTMMSCGY 672
Cdd:pfam00349 161 GKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAGAY 197
PLN02405 PLN02405
hexokinase
 463-911 1.24e-78

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 264.39  E-value: 1.24e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  463 GVAMVTAVAARLAAHR--------------RILEETLAPFQLTLEQmtvVQAQMRVAMIRGLQGEA-SSLRMLPTYVRAT 527
Cdd:PLN02405  12 CAAAVCAAAALVVRRRmkssgkwarameilKEFEEDCATPIGKLRQ---VADAMTVEMHAGLASEGgSKLKMLISYVDNL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  528 PDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVY---SIPECRAQGSGQKLFDHIVDCIVDFQKRQG-----LSGQ 599
Cdd:PLN02405  89 PSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFeevSIPPHLMTGSSDALFDFIAAALAKFVATEGedfhlPPGR 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  600 SLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEM 679
Cdd:PLN02405 169 QRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMER-VGLDMRVSALVNDTIGTLAGGRYYNPDVVA 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  680 GLIVGTGTNACYMEELRNVASVPGD---SGLMCINMEWGAFGddgSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLG 756
Cdd:PLN02405 248 AVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR---SSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLG 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  757 EIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESD-SLALRQVRAILED-LGLTLTS-DDALMVLEVCQAVSR 833
Cdd:PLN02405 325 EILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDtSPDLKVVGSKLKDiLEIPNTSlKMRKVVVELCNIVAT 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  834 RAAQLCGAGVAAVVEKI-RENRGLQELTVSV-GVDGTLYKLHPHFSKLVSATVRKLAPQ---CTVTFLQSEDGSGKGAAL 908
Cdd:PLN02405 405 RGARLSAAGIYGILKKLgRDTVKDGEKQKSViAMDGGLFEHYTEFSKCMESTLKELLGEevsESIEVEHSNDGSGIGAAL 484


                 ...
gi 74150193  909 VTA 911
Cdd:PLN02405 485 LAA 487
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 44-445 9.02e-78

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: 260.41  E-value: 9.02e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  44 QLQQIQASLLCSMEQALKGQDSPAPsvrMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKECRVepRSREF 123
Cdd:cd24088   3 KLDKLTAEFQRQMEKGLAKHGKGMA---MIPTYVTGVPDGTETGTYLALDLGGT--NFRVCSVELHGDGTFSL--RQEKS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 124 VIPQEVILGA-GQQLFDFAARCLSEFL-----DAYPVENQG--LKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQD 195
Cdd:cd24088  76 KIPDELKTGVtAKDLFDYLAKSVEAFLtkhhgDSFAAGKDDdrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 196 VVQLLRDAIQRQGTyRIDVVAMVNDTVGTMMGCELGTRPCE---VGLIVDTGTNACYMEEARHVAALD------EDRGRT 266
Cdd:cd24088 156 VVKLLQDELDRQGI-PVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIKKLDdssrvgKGKTHM 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 267 CVSIEWGSFYDEDALGPVlTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGC--ASPALLSQGC 344
Cdd:cd24088 235 VINTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYndKSPSALNTPY 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 345 IL----LDHVAemEDTATGTARV-HTILQDLGL-SPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQ 418
Cdd:cd24088 314 GLdtavLSAIE--IDSEAELRATrKVLLDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGE 391

                       410       420
                ....*....|....*....|....*..
gi 74150193 419 VAVATGGRVFERHPRFLRILKETVTLL 445
Cdd:cd24088 392 INIGVDGSVIEFYPGFESMLREALRLL 418
PLN02362 PLN02362
hexokinase
 463-911 1.35e-75

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 256.73  E-value: 1.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  463 GVAMVTAVAA----------RLAAHRR------ILEETLAPFQLTLEQMTVVQAQMRVAMIRGLQGEA-SSLRMLPTYVR 525
Cdd:PLN02362   7 GLAAAAAVAAcavaavmvgrRVKSRRKwrrvvgVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGgSKLKMLLTFVD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  526 ATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQ---VYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLP 602
Cdd:PLN02362  87 DLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQdveRHPIPQHLMNSTSEVLFDFIASSLKQFVEKEENGSEFSQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  603 -----LGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRqAVELNVVAIVNDTVGTMMSCGYDDPRC 677
Cdd:PLN02362 167 vrrreLGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDT 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  678 EMGLIVGTGTNACYMEELRNVASVPG---DSGLMCINMEWGAFgddGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMY 754
Cdd:PLN02362 246 VAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---WSSHLPRTSYDIDLDAESPNPNDQGFEKMISGMY 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  755 LGEIVRHILLHLTNLGVLFrGQKTQCLQARDIFKTKFLSEI-ESDSLALRQVRAIL-EDLGLtltSDDAL----MVLEVC 828
Cdd:PLN02362 323 LGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARILkETLGI---SEVPLkvrkLVVKIC 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  829 QAVSRRAAQLCGAGVAAVVEKI-------------RENRGLQELTVsVGVDGTLYKLHPHFSKLVSATVRKLAPQCT--- 892
Cdd:PLN02362 399 DVVTRRAARLAAAGIVGILKKIgrdgsggitsgrsRSDIQIMRRTV-VAVEGGLYTNYTMFREYLHEALNEILGEDVaqh 477

                        490
                 ....*....|....*....
gi 74150193  893 VTFLQSEDGSGKGAALVTA 911
Cdd:PLN02362 478 VILKATEDGSGIGSALLAA 496
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 33-228 4.37e-74

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: 241.25  E-value: 4.37e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193    33 ECLQQFKVTRTQLQQIQASLLCSMEQALKGQDSPapSVRMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGtk 112
Cdd:pfam00349   4 ELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSS--SLKMLPTYVTSLPTGTEKGTFLALDLGGT--NFRVCLVELGG-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   113 ECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQG---LKLGFNFSFPCHQTGLDRSTLISWTKGFRCS 189
Cdd:pfam00349  78 DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEekeLPLGFTFSFPVEQTSLDSGTLIRWTKGFDIP 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 74150193   190 GVEGQDVVQLLRDAIQRQGtYRIDVVAMVNDTVGTMMGC 228
Cdd:pfam00349 158 GVVGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAG 195
PLN02914 PLN02914
hexokinase
 70-469 1.77e-70

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 242.10  E-value: 1.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   70 VRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFL 149
Cdd:PLN02914  78 LKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  150 ----DAYPVEnQGLK--LGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGtYRIDVVAMVNDTVG 223
Cdd:PLN02914 156 akegGKFHLP-EGRKreIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  224 TMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSFYDedalGPVLTTFDSALDRESLTPG 300
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD----GLPLTEFDREMDAASINPG 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  301 AQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCIL-LDHVAEM-EDTATGTARVHTILQD-LGLSPRAS 377
Cdd:PLN02914 310 EQIFEKTISGMYLGEIVRRVLLKMAETSDLF-GHFVPEKLSTPFALrTPHLCAMqQDNSDDLQAVGSILYDvLGVEASLS 388

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  378 DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTL--QVAVATGGRVFERHPRFLRILKETVT-LLAP--NCDVS 452
Cdd:PLN02914 389 ARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTeLLGLelSKNIA 468

                        410
                 ....*....|....*..
gi 74150193  453 FIPSVDGGGRGVAMVTA 469
Cdd:PLN02914 469 IEHTKDGSGIGAALLAA 485
PTZ00107 PTZ00107
hexokinase; Provisional
 37-472 2.85e-69

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 237.65  E-value: 2.85e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   37 QFKVTRTQLQQIQASLLCSMEQALKGQDS------PAP-SVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLT 109
Cdd:PTZ00107  17 QFTMSKEKLKELVDYFLYELVEGLEAHRRhrnlwiPNEcSFKMLDSCVYNLPTGKEKGVYYAIDFG--GTNFRAVRVSLR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  110 GTKEcrVEPRSREFVIPQEVILGA---------GQQLFDFAARCLSEFLD--AYPVE-NQGLKLGFNFSFPCHQTGLDRS 177
Cdd:PTZ00107  95 GGGK--MERTQSKFSLPKSALLGEkglldkkatATDLFDHIAKSIKKMMEenGDPEDlNKPVPVGFTFSFPCTQLSVNNA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  178 TLISWTKGFRCS-----GVEGQDVVQLLRDAIQRQGTyRIDVVAMVNDTVGTMMGC----ELGTRPCEVGLIVDTGTNAC 248
Cdd:PTZ00107 173 ILIDWTKGFETGratndPVEGKDVGELLNDAFKRNNV-PANVVAVLNDTVGTLISCayqkPKNTPPCQVGVIIGTGSNAC 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  249 YMEEArhVAAldedRGR--TCVSIEWGSFydeDALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQ 326
Cdd:PTZ00107 252 YFEPE--VSA----YGYagTPINMECGNF---DSKLP-ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQ 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  327 HGvlfdgcASPALLSQGCILLDHVAEM-EDTATGTARVHTILQDL-GLSPRASDAELVQYVCVAVCTRAAQLCAAALAAV 404
Cdd:PTZ00107 322 LK------APPKMWQSGSFESEDASMIlNDQSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAP 395

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  405 LSRLQHSREQQTlqvaVATGGRVFERHPRFLRILKETVTL-LAPN-CDVSFIPSVDGGGRGVAMVTAVAA 472
Cdd:PTZ00107 396 AKKTRTVQGKAT----VAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMVA 461
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 44-472 2.71e-67

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: 231.11  E-value: 2.71e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  44 QLQQIQASLLCSMEQAL--KGQDSPapsvrMLPTYVRSTPHGTEQGDFLVLELGATgaSLRVLWVTLTGTKEcrVEPRSR 121
Cdd:cd24087   3 RLRKITDHFISELEKGLskKGGNIP-----MIPTWVMGFPTGKETGDYLALDLGGT--NLRVCLVKLGGNGK--FDITQS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 122 EFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVEN--QGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQL 199
Cdd:cd24087  74 KYRLPEELKTGTGEELWDFIADCLKKFVEEHFPGGksEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPM 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 200 LRDAIQRQGTyRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAAL-------DEDRGRTCvsiEW 272
Cdd:cd24087 154 LQKALKKRNV-PIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLehddippDSPMAINC---EY 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 273 GSFYDEDALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDG----------CASPALLSQ 342
Cdd:cd24087 230 GAFDNEHLVLP-RTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGqdtsklekpyVMDTSFLSR 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 343 gcILLDHVAEMEDTATgtarvhTILQDLGLSPRASDAELVQYVCVAVCTRaaqlcaaalaavLSRL---------QHSRE 413
Cdd:cd24087 309 --IEEDPFENLEDTDD------LFQHFFGLETTVPERKFIRRLAELIGTR------------AARLsacgiaaicKKRGY 368

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74150193 414 QQTLqvaVATGGRVFERHPRF-------LR-ILKETVTllapNCDVSFIPSVDGGGRGVAMVTAVAA 472
Cdd:cd24087 369 KTCH---VAADGSVYNKYPGFkeraaqaLKdIFGWDGE----DDPIKTVPAEDGSGVGAAIIAALTK 428
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 36-392 1.66e-62

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 218.29  E-value: 1.66e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  36 QQFKVTRTQLQQIQASLLCSMEQALKGQDSpapSVRMLPTYVrSTPHG-TEQGDFLVLELGATgaSLRVLWVTLTGTKEC 114
Cdd:COG5026  13 HGFDLSSIDLEEIAAKFQEEMEKGLEGKKS---SLKMLPSYL-GLPTGvKETGPVIALDAGGT--NFRVALVRFDGEGTF 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 115 RVEpRSREFVIP---QEVilgAGQQLFDFAARCLSEFLDaypvenQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGV 191
Cdd:COG5026  87 EIE-NFKSFPLPgtsSEI---TAEEFFDFIADYIEPLLD------ESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 192 EGQDVVQLLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPC----EVGLIVDTGTNACYMEEARHVAALDEDRGRTC 267
Cdd:COG5026 157 EGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMI 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193 268 VSIEWGSFydedALGPvLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGvLFDGCASPALLSQGCIll 347
Cdd:COG5026 237 INMESGNF----NKLP-RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSL-- 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 74150193 348 dHVAEMEDTATGTARVHTILQDLGLSPRASDAELVQYVCVAVCTR 392
Cdd:COG5026 309 -TTVDMSRFLADPSDEKEILSQCLEAGSEEDREILREIADAIVER 352
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 236-470 7.93e-60

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: 203.88  E-value: 7.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   236 EVGLIVDTGTNACYMEEARHVAALDEDR---GRTCVSIEWGSFYDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLY 312
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKLpksGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   313 LGELVRLVLVHLTQHGVLFDGcASPALLSQGCILLDHVAEME-DTATGTARVHTILQD-LGLSPRAS-DAELVQYVCVAV 389
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIEsDPSEDLETTREILEElLGIETVTEeDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   390 CTRaaqlcaaalaavLSRL---------QHSREQQTLQVAVatGGRVFERHPRFLRILKETV-TLLAPNCDVSFIPSVDG 459
Cdd:pfam03727 160 STR------------AARLvaagiaailKKIGRDKKVTVGV--DGSVYEKYPGFRERLQEALrELLGPGDKVVLVLAEDG 225

                         250
                  ....*....|.
gi 74150193   460 GGRGVAMVTAV 470
Cdd:pfam03727 226 SGVGAALIAAV 236
PLN02405 PLN02405
hexokinase
 44-469 3.06e-53

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 193.89  E-value: 3.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   44 QLQQIQASLLCSMEQALKGQDspAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKECRVEPRSREF 123
Cdd:PLN02405  54 KLRQVADAMTVEMHAGLASEG--GSKLKMLISYVDNLPSGDEKGLFYALDLG--GTNFRVLRVLLGGKDGRVVKQEFEEV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  124 VIPQEVILGAGQQLFDFAARCLSEFL-----DAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 198
Cdd:PLN02405 130 SIPPHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVG 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  199 LLRDAIQRQGTyRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVA---ALDEDRGRTCVSIEWGSF 275
Cdd:PLN02405 210 ELTKAMERVGL-DMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPkwhGLLPKSGEMVINMEWGNF 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  276 YDEDAlgpVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEM-E 354
Cdd:PLN02405 289 RSSHL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMhH 365

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  355 DTATGTARVHTILQDLGLSPRAS--DAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHS--REQQTLQVAVATGGRVFER 430
Cdd:PLN02405 366 DTSPDLKVVGSKLKDILEIPNTSlkMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEH 445

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 74150193  431 HPRFLRILKETVT-LLAPNC--DVSFIPSVDGGGRGVAMVTA 469
Cdd:PLN02405 446 YTEFSKCMESTLKeLLGEEVseSIEVEHSNDGSGIGAALLAA 487
PLN02596 PLN02596
hexokinase-like
 478-911 6.09e-46

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 172.75  E-value: 6.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  478 RRILEETLAPFQLTLEQMTVVQAQMRVAMIrglQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAeGS 557
Cdd:PLN02596  43 RKFARECATPVSKLWEVADALVSDMTASLT---AEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLG-GK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  558 VQIINQVY----SIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLP-----LGFTFSFPCKQLGLDQGILLNWtKGF 628
Cdd:PLN02596 119 NEPISDLYreeiSIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSF 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  629 NASGCEGQDVVYLLREAIRRrQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPG---DS 705
Cdd:PLN02596 198 SADDTVGKALVNDINRALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspES 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  706 GLMCINMEWGAFGddgSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARD 785
Cdd:PLN02596 277 QEIVISTEWGNFN---SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPY 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  786 IFKTKFLSEIESDSLALRQV--RAILEDLGLTLTSDDAL-MVLEVCQAVSRRAAQLCGAGVAAVVEKIREnrgLQELTVS 862
Cdd:PLN02596 354 LLRSPDMAAMHQDTSEDHEVvnEKLKEIFGITDSTPMAReVVAEVCDIVAERGARLAGAGIVGIIKKLGR---IENKKSV 430

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 74150193  863 VGVDGTLYKLHPHFSKLVSATV-RKLAPQCT--VTFLQSEDGSGKGAALVTA 911
Cdd:PLN02596 431 VTVEGGLYEHYRVFRNYLHSSVwEMLGSELSdnVVIEHSHGGSGAGALFLAA 482
PLN02362 PLN02362
hexokinase
 44-392 2.85e-44

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 168.14  E-value: 2.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   44 QLQQIQASLLCSMEQALKGQDspAPSVRMLPTYVRSTPHGTEQGDFLVLELGatGASLRVLWVTLTGTKE----CRVEPR 119
Cdd:PLN02362  54 RLRQVVDAMAVEMHAGLASEG--GSKLKMLLTFVDDLPTGSEIGTYYALDLG--GTNFRVLRVQLGGQRSsilsQDVERH 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  120 SrefvIPQEVILGAGQQLFDFAARCLSEFL-----DAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQ 194
Cdd:PLN02362 130 P----IPQHLMNSTSEVLFDFIASSLKQFVekeenGSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGK 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  195 DVVQLLRDAIQRQGtYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHV---AALDEDRGRTCVSIE 271
Cdd:PLN02362 206 DVAECLQGALNRRG-LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIikcQGLLTTSGSMVVNME 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  272 WGSFYDEDAlgpVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCILLDHVA 351
Cdd:PLN02362 285 WGNFWSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVA 360

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 74150193  352 EM-EDTATGTARVHTILQD-LGLSPRASDA-ELVQYVCVAVCTR 392
Cdd:PLN02362 361 AMhEDDSPELQEVARILKEtLGISEVPLKVrKLVVKICDVVTRR 404
PLN02596 PLN02596
hexokinase-like
 43-392 4.94e-38

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 149.26  E-value: 4.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193   43 TQLQQIQASLLCSMEQALKGQDSPapSVRMLPTYVRSTPHGTEQGDFLVLELgaTGASLRVLWVTLTGTKECRVEPRSRE 122
Cdd:PLN02596  54 SKLWEVADALVSDMTASLTAEETT--TLNMLVSYVASLPSGDEKGLYYGLNL--RGSNFLLLRARLGGKNEPISDLYREE 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  123 FVIPQEVILGAGQQLFDFAARCLSEFLDAYPVEN-----QGLKLGFNFSFPCHQTGLDRSTLISWtKGFRCSGVEGQDVV 197
Cdd:PLN02596 130 ISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEadtpeRVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALV 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  198 QLLRDAIQRQGTyRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDE---DRGRTCVSIEWGS 274
Cdd:PLN02596 209 NDINRALEKHGL-KIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGN 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74150193  275 FydeDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFdGCASPALLSQGCILLDH-VAEM 353
Cdd:PLN02596 288 F---NSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALF-GDTLPPKLTTPYLLRSPdMAAM 363

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 74150193  354 -EDTATGTARVHTILQD-LGLSPRASDA-ELVQYVCVAVCTR 392
Cdd:PLN02596 364 hQDTSEDHEVVNEKLKEiFGITDSTPMArEVVAEVCDIVAER 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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