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Conserved domains on  [gi|1622953868|ref|XP_028706936|]
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ADP-dependent glucokinase isoform X3 [Macaca mulatta]

Protein Classification

ADP-dependent glucokinase/phosphofructokinase( domain architecture ID 10112591)

ADP-dependent glucokinase/phosphofructokinase relies on ADP rather than ATP to donate a phosphoryl group to its substrate

CATH:  3.40.1190.20
EC:  2.7.1.-
Gene Ontology:  GO:0043843|GO:0005975|GO:0046872
PubMed:  8382990
SCOP:  4000759

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ADPGK_ADPPFK cd01938
ADP-dependent glucokinase (ADPGK) and phosphofructokinase (ADPPFK). ADPGK and ADPPFK are ...
1-370 0e+00

ADP-dependent glucokinase (ADPGK) and phosphofructokinase (ADPPFK). ADPGK and ADPPFK are proteins that rely on ADP rather than ATP to donate a phosphoryl group. They are found in certain hyperthermophilic archaea and in higher eukaryotes. A functional ADPGK has been characterized in mouse and is assumed to be desirable during ischemia/hypoxia. ADPGK and ADPPFK contain a large and a small domain with the binding site located in a groove between the domains. Partial domain closing is seen when ADP is bound, and further domain closing is observed when glucose is also bound. The oligomerization state apparently varies depending on the species, with some existing as monomers, some as dimers, and some as tetramers.


:

Pssm-ID: 238913  Cd Length: 445  Bit Score: 509.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868   1 MGKGAAAERFFGDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGP-VGPKLHELLDDNVFVPP--ES 77
Cdd:cd01938    72 FQRGAAAERFVSSEEVFEYLVEWAKEIPWDELRMGGNAGLMANRLAGEGDLKVLLGVPqSSKLQAELFLDGPIVVPtfEN 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  78 LQEVDEFHLILEYQAGEEWGQLKAPHANRFIFsHDLSNGAMNMLEVFVSSLEEFQPDLVVLSGLHMMEGQSK-ELQRKRL 156
Cdd:cd01938   152 LIEEDEIHLILEYPRGESWGDFVAPRANRFIF-HDDDNNPMLMREEFFSSILEFQPDLAVLSGLQMMEGQSFdEGTRKEL 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 157 LEVVTSISDIPT-GIPVHLELASMTNRELMSSIVHQqVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWN-GVPDVGMVS 234
Cdd:cd01938   231 LERVKSILEILPpLIPIHLELASTVDEELREEILHE-VVPYVDSLGLNEQELANLLQVLGGPHLSLASWNgGPPDVGAVL 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 235 DILFWILKEHGRSKSRASDLTRIHFHTLVYhILATVD----GHWANQLAAVAAGARVAGTQAcatETIDTSRVSLRAPQE 310
Cdd:cd01938   310 DILLWLLKEHGRDAATRTDLTRIHFHTLAY-ILATVSrkeeTRWANLFAALAAAARAAKGNI---ETIDTSRAGLRVPVS 385
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 311 FMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLGDAISAEGLFYSE 370
Cdd:cd01938   386 FAASASEGRLRIELNPEEPVVCWEREDVEFCFTPVLVCKEPKSTVGIGDTISASGLVYSF 445
 
Name Accession Description Interval E-value
ADPGK_ADPPFK cd01938
ADP-dependent glucokinase (ADPGK) and phosphofructokinase (ADPPFK). ADPGK and ADPPFK are ...
1-370 0e+00

ADP-dependent glucokinase (ADPGK) and phosphofructokinase (ADPPFK). ADPGK and ADPPFK are proteins that rely on ADP rather than ATP to donate a phosphoryl group. They are found in certain hyperthermophilic archaea and in higher eukaryotes. A functional ADPGK has been characterized in mouse and is assumed to be desirable during ischemia/hypoxia. ADPGK and ADPPFK contain a large and a small domain with the binding site located in a groove between the domains. Partial domain closing is seen when ADP is bound, and further domain closing is observed when glucose is also bound. The oligomerization state apparently varies depending on the species, with some existing as monomers, some as dimers, and some as tetramers.


Pssm-ID: 238913  Cd Length: 445  Bit Score: 509.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868   1 MGKGAAAERFFGDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGP-VGPKLHELLDDNVFVPP--ES 77
Cdd:cd01938    72 FQRGAAAERFVSSEEVFEYLVEWAKEIPWDELRMGGNAGLMANRLAGEGDLKVLLGVPqSSKLQAELFLDGPIVVPtfEN 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  78 LQEVDEFHLILEYQAGEEWGQLKAPHANRFIFsHDLSNGAMNMLEVFVSSLEEFQPDLVVLSGLHMMEGQSK-ELQRKRL 156
Cdd:cd01938   152 LIEEDEIHLILEYPRGESWGDFVAPRANRFIF-HDDDNNPMLMREEFFSSILEFQPDLAVLSGLQMMEGQSFdEGTRKEL 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 157 LEVVTSISDIPT-GIPVHLELASMTNRELMSSIVHQqVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWN-GVPDVGMVS 234
Cdd:cd01938   231 LERVKSILEILPpLIPIHLELASTVDEELREEILHE-VVPYVDSLGLNEQELANLLQVLGGPHLSLASWNgGPPDVGAVL 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 235 DILFWILKEHGRSKSRASDLTRIHFHTLVYhILATVD----GHWANQLAAVAAGARVAGTQAcatETIDTSRVSLRAPQE 310
Cdd:cd01938   310 DILLWLLKEHGRDAATRTDLTRIHFHTLAY-ILATVSrkeeTRWANLFAALAAAARAAKGNI---ETIDTSRAGLRVPVS 385
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 311 FMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLGDAISAEGLFYSE 370
Cdd:cd01938   386 FAASASEGRLRIELNPEEPVVCWEREDVEFCFTPVLVCKEPKSTVGIGDTISASGLVYSF 445
ADP_PFK_GK pfam04587
ADP-specific Phosphofructokinase/Glucokinase conserved region; In archaea a novel type of ...
1-368 3.30e-151

ADP-specific Phosphofructokinase/Glucokinase conserved region; In archaea a novel type of glycolytic pathway exists that is deviant from the classical Embden-Meyerhof pathway. This pathway utilizes two novel proteins: an ADP-dependent Glucokinase and an ADP-dependent Phosphofructokinase. This conserved region is present at the C-terminal of both these proteins. Interestingly this family contains sequences from higher eukaryotes..


Pssm-ID: 461360  Cd Length: 427  Bit Score: 433.20  E-value: 3.30e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868   1 MGKGAAAERFFGDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAaNSDLKVLLCGPVGPKLHELLDDNVFV---PPES 77
Cdd:pfam04587  54 MKHGAAAERFVSNKELFEWLVDAAKELPGDRWRMGGNAGIMANRLA-AEGAKVLLGGPLSKKLAELLDDKIVVlgpPIEA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  78 LQE-VDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEFQPDLVVLSGLHMMEGQSKE--LQRK 154
Cdd:pfam04587 133 YNEdTDEIHLILEYKKGEEWGGITAPRANRFIISSDPSNPRLSSLEEFKEYLPEFGPDLAVLSGLQMLDEQYFDggTREE 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 155 RLLEVVTSISDIP-TGIPVHLELASMTNRELMSSIVHqQVFPAVTSLGLNEQELLFLTQSASGPHSSLSS-WNGVPDVGM 232
Cdd:pfam04587 213 RLRKVKEQIKSLKnPDIPIHFELASFQDEELRKEILE-YILPYVDSLGLNEQELANLLSVLGGPHGNITEvSDGEPRIAT 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 233 VSDILFWILKEHgrsKSRASDLTRIHFHTLVYHILAT-VDGHWANQLAAVAAG--ARVAGTQACATetiDTSRVSLRAPQ 309
Cdd:pfam04587 292 VLDQMRWLLKLL---HSKLRKLTRIHVHTLAYHIIVTkKDSPWSNTASRKALAfaSLTAARQACGS---SPEDVELGLDD 365
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622953868 310 EFMTShSEAGSRIVLNPNKPVVEWHREG----ISFHFTPVLVCKDPIRTVGLGDAISAEGLFY 368
Cdd:pfam04587 366 SFSTS-KEGSKRVPFSEKEPVSCWAEELgrneYEVCVAPVLVCKKPVSTVGLGDTISAAGLVY 427
Pfk2 COG4809
Archaeal ADP-dependent glucokinase/phosphofructokinase [Carbohydrate transport and metabolism]; ...
1-371 9.55e-25

Archaeal ADP-dependent glucokinase/phosphofructokinase [Carbohydrate transport and metabolism]; Archaeal ADP-dependent glucokinase/phosphofructokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 443837  Cd Length: 456  Bit Score: 104.62  E-value: 9.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868   1 MGKGAAAERFFGDKETFhdiAQVASEFPGAQHYVGGNAALIgqkfaAN--SDL---KVLlcgPVGPKLHELL------DD 69
Cdd:COG4809    59 MKRGKAAEVPVYTDDLH---EWLKARLGYDELRMGGQAGIM-----ANllASLgakPVI---AYVPLLSKRQaslfvdKD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  70 NVFVPPESLQEVDEFHL--------------ILEYQAGEE----WGQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEF 131
Cdd:COG4809   128 NLLYPVVEDGKLVLKPPaeaydpdeetkinwIFEFSKGDEfflgGEEIRVPRENRFIAASRPENLRLEIKPELEEHLPEI 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 132 QP--DLVVLSGLHMM-----EGQSKELQRKRLLEVVTSISDIPTGIPVHLELASMTNRELMSSIVhQQVFPAVTSLGLNE 204
Cdd:COG4809   208 GEevDGAILSGYQMLkeeypDGSTYEEYLEKAVEVIRRLKRANPDLKVHVEFASIQDEEIRKKIL-ERILPEVDSVGLDE 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 205 QELLFLTQSASGPH--SSLSSWNGVPDVGMVSDILfwiLKEHGrsksrasdLTRIHFHTLVYHILATvdgHWANQLAAVA 282
Cdd:COG4809   287 VELANLLNVLGYDElaARILEKMEIEALYEGAVIL---LEELG--------LERIQVHTLGYYLAVT---RSDNPLSEEE 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 283 AGARVAGTQACAT--------ETIDTSRVSLRAPqefmtsHSEAGSRIV--LNPNKPVVEWHREGI------SFHFTPVL 346
Cdd:COG4809   353 VRDALLFAALAAAakaalgniTSPDDLEAGLKVP------VSEKGREALerLEEALGARGAGRKGIgrltgyTVVAIPTR 426
                         410       420
                  ....*....|....*....|....*
gi 1622953868 347 VCKDPIRTVGLGDAISAeGLFYSEV 371
Cdd:COG4809   427 VVEKPVSTVGLGDTISA-SAFVAEL 450
PRK14038 PRK14038
ADP-specific glucokinase;
80-370 1.11e-13

ADP-specific glucokinase;


Pssm-ID: 172532 [Multi-domain]  Cd Length: 453  Bit Score: 72.12  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  80 EVDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEF--QPDLVVLSGLHMMegqsKELQRKRLL 157
Cdd:PRK14038  170 EENCIHYIYEFPRGFRVFDFEAPRENRFIGAADDYNPNLYIRPEFRERFEEIakKAELAIISGLQAL----TEENYREPF 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 158 EVVTSISDI--PTGIPVHLELASMTNRELMSSIVhqQVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWNGVP-DVGMVS 234
Cdd:PRK14038  246 ETVREHLKVlnERGIPAHLEFAFTPDETVREEIL--GLLGKFYSVGLNEVELASIMEVMGEKTLAEKLLAKDPvDPIAVT 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 235 DILFWILKEHGrsksrasdLTRIHFHTLVYHI-LATVDGHWANQLAAVAAGARVAGTQACATETIDTSRVSLRAPQEFMT 313
Cdd:PRK14038  324 EAMLKLAEKTG--------VKRIHFHTYGYYLaLTKYRGEHVRDALLFAALAAAAKAMLGNIEKIDDVRKALDVPVNEKA 395
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953868 314 SHSEAGSRIVLNPNKPVVEwhREGISFHFTPVLVCKDPIRTVGLGDAISAEGlFYSE 370
Cdd:PRK14038  396 LEVEEALEKEYGMENGIGE--VEDYQLAFIPTKIVAKPKSTVGIGDTISSSA-FVGE 449
 
Name Accession Description Interval E-value
ADPGK_ADPPFK cd01938
ADP-dependent glucokinase (ADPGK) and phosphofructokinase (ADPPFK). ADPGK and ADPPFK are ...
1-370 0e+00

ADP-dependent glucokinase (ADPGK) and phosphofructokinase (ADPPFK). ADPGK and ADPPFK are proteins that rely on ADP rather than ATP to donate a phosphoryl group. They are found in certain hyperthermophilic archaea and in higher eukaryotes. A functional ADPGK has been characterized in mouse and is assumed to be desirable during ischemia/hypoxia. ADPGK and ADPPFK contain a large and a small domain with the binding site located in a groove between the domains. Partial domain closing is seen when ADP is bound, and further domain closing is observed when glucose is also bound. The oligomerization state apparently varies depending on the species, with some existing as monomers, some as dimers, and some as tetramers.


Pssm-ID: 238913  Cd Length: 445  Bit Score: 509.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868   1 MGKGAAAERFFGDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGP-VGPKLHELLDDNVFVPP--ES 77
Cdd:cd01938    72 FQRGAAAERFVSSEEVFEYLVEWAKEIPWDELRMGGNAGLMANRLAGEGDLKVLLGVPqSSKLQAELFLDGPIVVPtfEN 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  78 LQEVDEFHLILEYQAGEEWGQLKAPHANRFIFsHDLSNGAMNMLEVFVSSLEEFQPDLVVLSGLHMMEGQSK-ELQRKRL 156
Cdd:cd01938   152 LIEEDEIHLILEYPRGESWGDFVAPRANRFIF-HDDDNNPMLMREEFFSSILEFQPDLAVLSGLQMMEGQSFdEGTRKEL 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 157 LEVVTSISDIPT-GIPVHLELASMTNRELMSSIVHQqVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWN-GVPDVGMVS 234
Cdd:cd01938   231 LERVKSILEILPpLIPIHLELASTVDEELREEILHE-VVPYVDSLGLNEQELANLLQVLGGPHLSLASWNgGPPDVGAVL 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 235 DILFWILKEHGRSKSRASDLTRIHFHTLVYhILATVD----GHWANQLAAVAAGARVAGTQAcatETIDTSRVSLRAPQE 310
Cdd:cd01938   310 DILLWLLKEHGRDAATRTDLTRIHFHTLAY-ILATVSrkeeTRWANLFAALAAAARAAKGNI---ETIDTSRAGLRVPVS 385
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 311 FMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLGDAISAEGLFYSE 370
Cdd:cd01938   386 FAASASEGRLRIELNPEEPVVCWEREDVEFCFTPVLVCKEPKSTVGIGDTISASGLVYSF 445
ADP_PFK_GK pfam04587
ADP-specific Phosphofructokinase/Glucokinase conserved region; In archaea a novel type of ...
1-368 3.30e-151

ADP-specific Phosphofructokinase/Glucokinase conserved region; In archaea a novel type of glycolytic pathway exists that is deviant from the classical Embden-Meyerhof pathway. This pathway utilizes two novel proteins: an ADP-dependent Glucokinase and an ADP-dependent Phosphofructokinase. This conserved region is present at the C-terminal of both these proteins. Interestingly this family contains sequences from higher eukaryotes..


Pssm-ID: 461360  Cd Length: 427  Bit Score: 433.20  E-value: 3.30e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868   1 MGKGAAAERFFGDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAaNSDLKVLLCGPVGPKLHELLDDNVFV---PPES 77
Cdd:pfam04587  54 MKHGAAAERFVSNKELFEWLVDAAKELPGDRWRMGGNAGIMANRLA-AEGAKVLLGGPLSKKLAELLDDKIVVlgpPIEA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  78 LQE-VDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEFQPDLVVLSGLHMMEGQSKE--LQRK 154
Cdd:pfam04587 133 YNEdTDEIHLILEYKKGEEWGGITAPRANRFIISSDPSNPRLSSLEEFKEYLPEFGPDLAVLSGLQMLDEQYFDggTREE 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 155 RLLEVVTSISDIP-TGIPVHLELASMTNRELMSSIVHqQVFPAVTSLGLNEQELLFLTQSASGPHSSLSS-WNGVPDVGM 232
Cdd:pfam04587 213 RLRKVKEQIKSLKnPDIPIHFELASFQDEELRKEILE-YILPYVDSLGLNEQELANLLSVLGGPHGNITEvSDGEPRIAT 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 233 VSDILFWILKEHgrsKSRASDLTRIHFHTLVYHILAT-VDGHWANQLAAVAAG--ARVAGTQACATetiDTSRVSLRAPQ 309
Cdd:pfam04587 292 VLDQMRWLLKLL---HSKLRKLTRIHVHTLAYHIIVTkKDSPWSNTASRKALAfaSLTAARQACGS---SPEDVELGLDD 365
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622953868 310 EFMTShSEAGSRIVLNPNKPVVEWHREG----ISFHFTPVLVCKDPIRTVGLGDAISAEGLFY 368
Cdd:pfam04587 366 SFSTS-KEGSKRVPFSEKEPVSCWAEELgrneYEVCVAPVLVCKKPVSTVGLGDTISAAGLVY 427
Pfk2 COG4809
Archaeal ADP-dependent glucokinase/phosphofructokinase [Carbohydrate transport and metabolism]; ...
1-371 9.55e-25

Archaeal ADP-dependent glucokinase/phosphofructokinase [Carbohydrate transport and metabolism]; Archaeal ADP-dependent glucokinase/phosphofructokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 443837  Cd Length: 456  Bit Score: 104.62  E-value: 9.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868   1 MGKGAAAERFFGDKETFhdiAQVASEFPGAQHYVGGNAALIgqkfaAN--SDL---KVLlcgPVGPKLHELL------DD 69
Cdd:COG4809    59 MKRGKAAEVPVYTDDLH---EWLKARLGYDELRMGGQAGIM-----ANllASLgakPVI---AYVPLLSKRQaslfvdKD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  70 NVFVPPESLQEVDEFHL--------------ILEYQAGEE----WGQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEF 131
Cdd:COG4809   128 NLLYPVVEDGKLVLKPPaeaydpdeetkinwIFEFSKGDEfflgGEEIRVPRENRFIAASRPENLRLEIKPELEEHLPEI 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 132 QP--DLVVLSGLHMM-----EGQSKELQRKRLLEVVTSISDIPTGIPVHLELASMTNRELMSSIVhQQVFPAVTSLGLNE 204
Cdd:COG4809   208 GEevDGAILSGYQMLkeeypDGSTYEEYLEKAVEVIRRLKRANPDLKVHVEFASIQDEEIRKKIL-ERILPEVDSVGLDE 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 205 QELLFLTQSASGPH--SSLSSWNGVPDVGMVSDILfwiLKEHGrsksrasdLTRIHFHTLVYHILATvdgHWANQLAAVA 282
Cdd:COG4809   287 VELANLLNVLGYDElaARILEKMEIEALYEGAVIL---LEELG--------LERIQVHTLGYYLAVT---RSDNPLSEEE 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 283 AGARVAGTQACAT--------ETIDTSRVSLRAPqefmtsHSEAGSRIV--LNPNKPVVEWHREGI------SFHFTPVL 346
Cdd:COG4809   353 VRDALLFAALAAAakaalgniTSPDDLEAGLKVP------VSEKGREALerLEEALGARGAGRKGIgrltgyTVVAIPTR 426
                         410       420
                  ....*....|....*....|....*
gi 1622953868 347 VCKDPIRTVGLGDAISAeGLFYSEV 371
Cdd:COG4809   427 VVEKPVSTVGLGDTISA-SAFVAEL 450
PRK14038 PRK14038
ADP-specific glucokinase;
80-370 1.11e-13

ADP-specific glucokinase;


Pssm-ID: 172532 [Multi-domain]  Cd Length: 453  Bit Score: 72.12  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  80 EVDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEF--QPDLVVLSGLHMMegqsKELQRKRLL 157
Cdd:PRK14038  170 EENCIHYIYEFPRGFRVFDFEAPRENRFIGAADDYNPNLYIRPEFRERFEEIakKAELAIISGLQAL----TEENYREPF 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 158 EVVTSISDI--PTGIPVHLELASMTNRELMSSIVhqQVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWNGVP-DVGMVS 234
Cdd:PRK14038  246 ETVREHLKVlnERGIPAHLEFAFTPDETVREEIL--GLLGKFYSVGLNEVELASIMEVMGEKTLAEKLLAKDPvDPIAVT 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 235 DILFWILKEHGrsksrasdLTRIHFHTLVYHI-LATVDGHWANQLAAVAAGARVAGTQACATETIDTSRVSLRAPQEFMT 313
Cdd:PRK14038  324 EAMLKLAEKTG--------VKRIHFHTYGYYLaLTKYRGEHVRDALLFAALAAAAKAMLGNIEKIDDVRKALDVPVNEKA 395
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953868 314 SHSEAGSRIVLNPNKPVVEwhREGISFHFTPVLVCKDPIRTVGLGDAISAEGlFYSE 370
Cdd:PRK14038  396 LEVEEALEKEYGMENGIGE--VEDYQLAFIPTKIVAKPKSTVGIGDTISSSA-FVGE 449
PRK03979 PRK03979
ADP-specific phosphofructokinase; Provisional
33-363 3.49e-12

ADP-specific phosphofructokinase; Provisional


Pssm-ID: 235184  Cd Length: 463  Bit Score: 67.32  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  33 YVGGNAALIGQkFAANSDL-KVLLCGP-VGPKLHELLDDN-------------VFVPP-ESLQEVDEFHL--ILEYQAGE 94
Cdd:PRK03979  100 RMGGQAGIISN-LLAILDLkKVIAYTPwLSKKQAEMFVDSdnllypvvengklVLKKPrEAYKPNDPLKInrIFEFKKGL 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  95 EWG----QLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEE--FQPDLVVLSGLHMM-----EGQSKELQRKRLLEVVTSI 163
Cdd:PRK03979  179 EFKlggeKIIVPRSNRFIVSSRPEWLRIEIKDELKEFLPEigKMVDGAILSGYQGIkeeysDGKTAEYYLKRAKEDIKLL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 164 SDIPTGIPVHLELASMTNRELMSSIVhQQVFPAVTSLGLNEQELLFLTqSASGpHSSLS----SWNGVPDVGMVSDILfw 239
Cdd:PRK03979  259 KKKNKDIKIHVEFASIQNREIRKKII-TYILPHVDSVGMDETEIANIL-NVLG-YEELSerilKESRIEDVIEGAKIL-- 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 240 iLKEHgrsksrasDLTRIHFHTLVYHILATvdgHWANQLAAVAAGARVA-GTQACAT-------ETIDTSRVSLRAPqef 311
Cdd:PRK03979  334 -LDEL--------NLERVQVHTLYYIMYIC---KKDNPLSEEELRKSLEfATILAATkaklgdiKSIEDLKVGLEVP--- 398
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622953868 312 mtsHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLGDAISA 363
Cdd:PRK03979  399 ---YNEYGELLKERFEEAKKECRLEEYKIVLIPSRLVENPKSTVGLGDTISA 447
PRK14039 PRK14039
ADP-dependent glucokinase; Provisional
1-370 1.43e-11

ADP-dependent glucokinase; Provisional


Pssm-ID: 184471  Cd Length: 453  Bit Score: 65.59  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868   1 MGKGAAAERFFGDKETFHDIAQVAseFPGAQHYVGGNAALIGQKFAANSDLKVLLCGPVGPKLHELLDDN--VFVPPESL 78
Cdd:PRK14039   59 MKNGCGAEWLVFEQSVFEFLKNRF--FDNSEIRMGGNAGIMANVLSELGASRVVPNVAVPSKTQLSLFSKkaVYFPGMPL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868  79 QEVDE--------------FHLILEYQAGEEW----GQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEFQPDL--VVL 138
Cdd:PRK14039  137 QASETdgekvgasssdqepIHFVFDFREGETFslygTRIRAPRENRFIATFDHLNFRLFINPAFEQYALEHAGEMdgALI 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 139 SGLHMM-----EGQSKELQRKRLLEVVTSISDIPTGIPVHLELASMTNRELMSSiVHQQVFPAVTSLGLNEQELLFLTQS 213
Cdd:PRK14039  217 SGFHLLletypDGSTYREKLEDSLAQLKWWKSKNEKLRIHAELGHFASKEIANS-VFLILAGIVDSIGMNEDELAMLANL 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 214 ASGPHSSLSSWNgvpdVGMVSDILFWILKEHGrsksrasdLTRIHFHTLVYHILATVDGHWAnqlaAVAAGARVAGTQAC 293
Cdd:PRK14039  296 HGIPAEGILEMN----AEAIGEAACQLASESG--------LQRLIIHTREFVLCVSKPDVKM----AKKKIEAMEFGLKC 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953868 294 ATETIDTSRVSLRAPQEFMTSH---SEAGSRIVLNPNKPV--------VEWHREGISFHFTPVLVCKDPIRTVGLGDAIS 362
Cdd:PRK14039  360 AGVYAASGSLDGREFVEKEASKlqeSDFGREQVELFLKAFggkalglgAYGLREGYSVCILPTLVSKSPVTTVGLGDTLT 439

                  ....*...
gi 1622953868 363 AeGLFYSE 370
Cdd:PRK14039  440 A-GTFLRL 446
 
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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