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Conserved domains on  [gi|767924838|ref|XP_011532630|]
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xylulose kinase isoform X6 [Homo sapiens]

Protein Classification

xylulokinase( domain architecture ID 10167343)

xylulokinase catalyzes the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P) and ADP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_FGGY_SpXK-like cd07776
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ...
9-512 0e+00

nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


:

Pssm-ID: 466795 [Multi-domain]  Cd Length: 514  Bit Score: 873.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838   9 CCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:cd07776    1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEYGTKGGVHRDGDGGEVTSPVLMWVEALDLLLEKLKAAGFDFSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  89 VLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY 168
Cdd:cd07776   81 VKAISGSGQQHGSVYWSKGAESALANLDPSKSLAEQLEGAFSVPDSPIWMDSSTTKQCRELEKAVGGPEALAKLTGSRAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 169 ERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACL-GACAPHLEEKLSP 247
Cdd:cd07776  161 ERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGRYAPIDESDGSGMNLMDIRSRKWSPELLdAATAPDLKEKLGE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 248 PVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDS 327
Cdd:cd07776  241 LVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGLEPGDVAVSLGTSDTVFLVLDEPKPGPEGHVFANPVDP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 328 QHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHRFNTENHK-VAAFPGDV 406
Cdd:cd07776  321 GSYMAMLCYKNGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNLGLYFDEPEITPPVPGGGRRFFGDDGvDAFFDPAV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 407 EVRALIEGQFMAKRIHAEGLGYRVmSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTD 486
Cdd:cd07776  401 EVRAVVESQFLSMRLHAERLGSDI-PPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGS 479
                        490       500
                 ....*....|....*....|....*...
gi 767924838 487 VPFS--EVVKLAPNPRLAATPSPGASQR 512
Cdd:cd07776  480 GDFSpeFVVFSAEEPKLVAEPDPEAAEV 507
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_SpXK-like cd07776
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ...
9-512 0e+00

nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466795 [Multi-domain]  Cd Length: 514  Bit Score: 873.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838   9 CCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:cd07776    1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEYGTKGGVHRDGDGGEVTSPVLMWVEALDLLLEKLKAAGFDFSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  89 VLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY 168
Cdd:cd07776   81 VKAISGSGQQHGSVYWSKGAESALANLDPSKSLAEQLEGAFSVPDSPIWMDSSTTKQCRELEKAVGGPEALAKLTGSRAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 169 ERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACL-GACAPHLEEKLSP 247
Cdd:cd07776  161 ERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGRYAPIDESDGSGMNLMDIRSRKWSPELLdAATAPDLKEKLGE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 248 PVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDS 327
Cdd:cd07776  241 LVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGLEPGDVAVSLGTSDTVFLVLDEPKPGPEGHVFANPVDP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 328 QHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHRFNTENHK-VAAFPGDV 406
Cdd:cd07776  321 GSYMAMLCYKNGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNLGLYFDEPEITPPVPGGGRRFFGDDGvDAFFDPAV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 407 EVRALIEGQFMAKRIHAEGLGYRVmSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTD 486
Cdd:cd07776  401 EVRAVVESQFLSMRLHAERLGSDI-PPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGS 479
                        490       500
                 ....*....|....*....|....*...
gi 767924838 487 VPFS--EVVKLAPNPRLAATPSPGASQR 512
Cdd:cd07776  480 GDFSpeFVVFSAEEPKLVAEPDPEAAEV 507
PLN02669 PLN02669
xylulokinase
11-494 0e+00

xylulokinase


Pssm-ID: 178274 [Multi-domain]  Cd Length: 556  Bit Score: 605.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVH--VHKDGlTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:PLN02669  11 LGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHYGTKDGVYrdPKVNG-RIVSPTLMWVEALDLLLQKLAKEKFPFHK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  89 VLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY 168
Cdd:PLN02669  90 VVAISGSGQQHGSVYWRKGASAVLKSLDPSKSLVAQLQDAFSTKDSPIWMDSSTTKQCREIEEAVGGAAELSKLTGSRAY 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 169 ERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACLGACAPHLEEKLSPP 248
Cdd:PLN02669 170 ERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYASIDETDGAGMNLMDIEKRCWSKAALEATAPGLEEKLGKL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 249 VPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEE-GDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDS 327
Cdd:PLN02669 250 APAHAVAGKIHPYFVQRFGFSSNCLVVQWSGDNPNSLAGLTLSTpGDLAISLGTSDTVFGITREPQPSLEGHVFPNPVDP 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 328 QHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEI-IGRHRFNTEN---------- 396
Cdd:PLN02669 330 ESYMVMLCYKNGSLTREDIRNRCADGSWDVFNKLLEQTPPLNGGKLGFYYKEHEILPPLpVGFHRYILENfsgealdglv 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 397 -HKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKtKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAY 475
Cdd:PLN02669 410 eEEVGEFDPPSEVRAIIEGQFLSMRAHAERFGMPVPPK-RIIATGGASANQSILKLIASIFGCDVYTVQRPDSASLGAAL 488
                        490       500
                 ....*....|....*....|..
gi 767924838 476 RAFHGLA---GGTDVPFSEVVK 494
Cdd:PLN02669 489 RAAHGWLcneQGSFVPISCLYE 510
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
11-503 1.46e-52

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 186.96  E-value: 1.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNVFYEESVHFDrdlpefgtqggVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVL 90
Cdd:COG1070    4 LGIDIGTTSVKAVLFDADGEVVASASAEYP-----------LSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  91 ALSGAGQQHGsiYWKAGAQQALtslspdlrlhqqlqdcfsISDCPVWMDSSTTAQCRQLEAAVGGAQALScLTGSRAyer 170
Cdd:COG1070   73 AIGVSGQMHG--LVLLDADGEP------------------LRPAILWNDTRAAAEAAELREELGEEALYE-ITGNPL--- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 171 FTGNQIAKIY---QQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSP 247
Cdd:COG1070  129 HPGFTAPKLLwlkENEPEIFARIAKVLLPKDYLRYRLTGEFV-TDYSDASGTGLLDVRTRDWSDELLEALGID-RELLPE 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 248 PVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGTSDTLFLWLQEPM--PALEGHIFCNP 324
Cdd:COG1070  207 LVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGaVEPGDAAVSLGTSGVVFVVSDKPLpdPEGRVHTFCHA 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 325 VDsQHYMALLCFKNGSLMREKIRNE---SVSRSWSDFSKALQSTEMGNGGnLGFY---------FDVMEITPEIIGRhrf 392
Cdd:COG1070  287 VP-GRWLPMGATNNGGSALRWFRDLfadGELDDYEELNALAAEVPPGADG-LLFLpylsgertpHWDPNARGAFFGL--- 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 393 nTENHKVAAFpgdveVRALIEGQFMAKRIHAE---GLGYRVmskTKILATGGASHNREILQVLADVFDAPVYVIDTANSA 469
Cdd:COG1070  362 -TLSHTRAHL-----ARAVLEGVAFALRDGLEaleEAGVKI---DRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGG 432
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 767924838 470 CVGSAYRAFHGLAGGTDVP--FSEVVKLA----PNPRLAA 503
Cdd:COG1070  433 ALGAALLAAVGLGLYDDLEeaAAAMVRVGetiePDPENVA 472
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
296-481 3.19e-17

FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.


Pssm-ID: 426979 [Multi-domain]  Cd Length: 197  Bit Score: 80.06  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  296 AVSLGTSDTLFLWLQEPmpALEGHIFCNPVDSQH-----YMALLCFKNGSLM---------REKIRNESVSRSWSDFSKA 361
Cdd:pfam02782   2 AISAGTSSFVLVETPEP--VLSVHGVWGPYTNEMlpgywGLEGGQSAAGSLLawllqfhglREELRDAGNVESLAELAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  362 LQSTEMGnggnlGFYFDvmeitPEIIGRHRFNTENHKVAAFPG-------DVEVRALIEGQFMAKRIHAEGL----GYRV 430
Cdd:pfam02782  80 AAVAPAG-----GLLFY-----PDFSGNRAPGADPGARGSITGlsspttlAHLYRAILESLALQLRQILEALtkqeGHPI 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767924838  431 MSktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 481
Cdd:pfam02782 150 DT---IHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_SpXK-like cd07776
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ...
9-512 0e+00

nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466795 [Multi-domain]  Cd Length: 514  Bit Score: 873.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838   9 CCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:cd07776    1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEYGTKGGVHRDGDGGEVTSPVLMWVEALDLLLEKLKAAGFDFSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  89 VLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY 168
Cdd:cd07776   81 VKAISGSGQQHGSVYWSKGAESALANLDPSKSLAEQLEGAFSVPDSPIWMDSSTTKQCRELEKAVGGPEALAKLTGSRAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 169 ERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACL-GACAPHLEEKLSP 247
Cdd:cd07776  161 ERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGRYAPIDESDGSGMNLMDIRSRKWSPELLdAATAPDLKEKLGE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 248 PVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDS 327
Cdd:cd07776  241 LVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGLEPGDVAVSLGTSDTVFLVLDEPKPGPEGHVFANPVDP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 328 QHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHRFNTENHK-VAAFPGDV 406
Cdd:cd07776  321 GSYMAMLCYKNGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNLGLYFDEPEITPPVPGGGRRFFGDDGvDAFFDPAV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 407 EVRALIEGQFMAKRIHAEGLGYRVmSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTD 486
Cdd:cd07776  401 EVRAVVESQFLSMRLHAERLGSDI-PPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGS 479
                        490       500
                 ....*....|....*....|....*...
gi 767924838 487 VPFS--EVVKLAPNPRLAATPSPGASQR 512
Cdd:cd07776  480 GDFSpeFVVFSAEEPKLVAEPDPEAAEV 507
PLN02669 PLN02669
xylulokinase
11-494 0e+00

xylulokinase


Pssm-ID: 178274 [Multi-domain]  Cd Length: 556  Bit Score: 605.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVH--VHKDGlTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:PLN02669  11 LGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHYGTKDGVYrdPKVNG-RIVSPTLMWVEALDLLLQKLAKEKFPFHK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  89 VLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY 168
Cdd:PLN02669  90 VVAISGSGQQHGSVYWRKGASAVLKSLDPSKSLVAQLQDAFSTKDSPIWMDSSTTKQCREIEEAVGGAAELSKLTGSRAY 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 169 ERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACLGACAPHLEEKLSPP 248
Cdd:PLN02669 170 ERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYASIDETDGAGMNLMDIEKRCWSKAALEATAPGLEEKLGKL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 249 VPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEE-GDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDS 327
Cdd:PLN02669 250 APAHAVAGKIHPYFVQRFGFSSNCLVVQWSGDNPNSLAGLTLSTpGDLAISLGTSDTVFGITREPQPSLEGHVFPNPVDP 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 328 QHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEI-IGRHRFNTEN---------- 396
Cdd:PLN02669 330 ESYMVMLCYKNGSLTREDIRNRCADGSWDVFNKLLEQTPPLNGGKLGFYYKEHEILPPLpVGFHRYILENfsgealdglv 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 397 -HKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKtKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAY 475
Cdd:PLN02669 410 eEEVGEFDPPSEVRAIIEGQFLSMRAHAERFGMPVPPK-RIIATGGASANQSILKLIASIFGCDVYTVQRPDSASLGAAL 488
                        490       500
                 ....*....|....*....|..
gi 767924838 476 RAFHGLA---GGTDVPFSEVVK 494
Cdd:PLN02669 489 RAAHGWLcneQGSFVPISCLYE 510
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
9-477 3.95e-65

nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466787 [Multi-domain]  Cd Length: 392  Bit Score: 217.82  E-value: 3.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838   9 CCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPefgtqggvhvhKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQ 88
Cdd:cd00366    1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYP-----------QPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  89 VLALSGAGQQHGSIYWKAgAQQALTslspdlrlhqqlqdcfsisDCPVWMDSsttaqcrqleaavggaqalscltgsRAy 168
Cdd:cd00366   70 IAAIGISGQMPGVVLVDA-DGNPLR-------------------PAIIWLDR-------------------------RA- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 169 erftgnqiakiyqqnpeayshteRISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPhLEEKLSPP 248
Cdd:cd00366  104 -----------------------KFLQPNDYIVFRLTGEFA-IDYSNASGTGLYDIKTGDWSEELLDALGI-PREKLPPI 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 249 VPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDS 327
Cdd:cd00366  159 VESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVvEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHVVP 238
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 328 QHYMALLCFKNGSLMREKIRNESVSRSWSD-----FSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHR---FN-TENHK 398
Cdd:cd00366  239 GLWLLEGAINTGGASLRWFRDEFGEEEDSDaeyegLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARgvfFGlTLSHT 318
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924838 399 VAAFpgdveVRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRA 477
Cdd:cd00366  319 RAHL-----IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
11-503 1.46e-52

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 186.96  E-value: 1.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNVFYEESVHFDrdlpefgtqggVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVL 90
Cdd:COG1070    4 LGIDIGTTSVKAVLFDADGEVVASASAEYP-----------LSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  91 ALSGAGQQHGsiYWKAGAQQALtslspdlrlhqqlqdcfsISDCPVWMDSSTTAQCRQLEAAVGGAQALScLTGSRAyer 170
Cdd:COG1070   73 AIGVSGQMHG--LVLLDADGEP------------------LRPAILWNDTRAAAEAAELREELGEEALYE-ITGNPL--- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 171 FTGNQIAKIY---QQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSP 247
Cdd:COG1070  129 HPGFTAPKLLwlkENEPEIFARIAKVLLPKDYLRYRLTGEFV-TDYSDASGTGLLDVRTRDWSDELLEALGID-RELLPE 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 248 PVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGTSDTLFLWLQEPM--PALEGHIFCNP 324
Cdd:COG1070  207 LVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGaVEPGDAAVSLGTSGVVFVVSDKPLpdPEGRVHTFCHA 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 325 VDsQHYMALLCFKNGSLMREKIRNE---SVSRSWSDFSKALQSTEMGNGGnLGFY---------FDVMEITPEIIGRhrf 392
Cdd:COG1070  287 VP-GRWLPMGATNNGGSALRWFRDLfadGELDDYEELNALAAEVPPGADG-LLFLpylsgertpHWDPNARGAFFGL--- 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 393 nTENHKVAAFpgdveVRALIEGQFMAKRIHAE---GLGYRVmskTKILATGGASHNREILQVLADVFDAPVYVIDTANSA 469
Cdd:COG1070  362 -TLSHTRAHL-----ARAVLEGVAFALRDGLEaleEAGVKI---DRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGG 432
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 767924838 470 CVGSAYRAFHGLAGGTDVP--FSEVVKLA----PNPRLAA 503
Cdd:COG1070  433 ALGAALLAAVGLGLYDDLEeaAAAMVRVGetiePDPENVA 472
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
11-477 6.76e-44

nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466809 [Multi-domain]  Cd Length: 443  Bit Score: 161.95  E-value: 6.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNvfyeESVHFDR-DLPEFGTQGGVHvhkdgltvTSPVLMWVQALDIILEKM-KASGFDFSQ 88
Cdd:cd07809    3 LGIDLGTQSIKAVLIDAETG----RVVASGSaPHENILIDPGWA--------EQDPEDWWDALQAAFAQLlKDAGAELRD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  89 VLALSGAGQQHGsiYWKAGAQQALtslspdLRlhqqlqdcfsisdcPV--WMDSSTTAQCRQLEAAVGGAQALSCLTGSR 166
Cdd:cd07809   71 VAAIGISGQMHG--LVALDADGKV------LR--------------PAklWCDTRTAPEAEELTEALGGKKCLLVGLNIP 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 167 AyeRFTgnqIAKIYQ---QNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACL--GACAPHL 241
Cdd:cd07809  129 A--RFT---ASKLLWlkeNEPEHYARIAKILLPHDYLNWKLTGEKV-TGLGDASGTFPIDPRTRDYDAELLaaIDPSRDL 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 242 EEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGTSDTLFLWLQEPMPALEGHI 320
Cdd:cd07809  203 RDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGvVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRV 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 321 --FCNPVDsqHYMALLCFKNG--SLMrEKIRnESVSRSWSDFSKALQSTEMGNGGNLGF-YFDVMEIT--PEIIGR-HRF 392
Cdd:cd07809  283 atFCDSTG--GMLPLINTTNCltAWT-ELFR-ELLGVSYEELDELAAQAPPGAGGLLLLpFLNGERTPnlPHGRASlVGL 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 393 NTENHKVAAFpgdveVRALIEGQFMAKRIhaeglGYRVMSK-----TKILATGGASHNREILQVLADVFDAPVYVIDTAN 467
Cdd:cd07809  359 TLSNFTRANL-----ARAALEGATFGLRY-----GLDILRElgveiDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGE 428
                        490
                 ....*....|
gi 767924838 468 SACVGSAYRA 477
Cdd:cd07809  429 GGALGAALQA 438
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
11-483 1.62e-36

nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466793 [Multi-domain]  Cd Length: 443  Bit Score: 141.57  E-value: 1.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNVFYEESvhfdRDLPefgtqggVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDfsQVL 90
Cdd:cd07773    3 LGIDIGTTNVKAVLFDEDGRILASAS----RETP-------LIHPGPGWAELDPEELWEAVKEAIREAAAQAGPD--PIA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  91 ALSGAGQqhgsiywkaGaqQALTSLSPDLRlhqqlqdcfSISDCPVWMDSSTTAQCRQLEAAVGgAQALSCLTGSRAYER 170
Cdd:cd07773   70 AISVSSQ---------G--ESGVPVDRDGE---------PLGPAIVWFDPRGKEEAEELAERIG-AEELYRITGLPPSPM 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 171 FTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSPPVP 250
Cdd:cd07773  129 YSLAKLLWLREHEPEIFAKAAKWLSVADYIAYRLTGEPV-TDYSLASRTMLFDIRKRTWSEELLEAAGID-ASLLPELVP 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 251 SCSVVGAISSYYVQRYGFPPGCKVVafTG--DNPASLAGMRL-EEGDIAVSLGTSDTLFLWLQEPMP--ALEGHIFCNP- 324
Cdd:cd07773  207 SGTVIGTVTPEAAEELGLPAGTPVV--VGghDHLCAALGAGViEPGDVLDSTGTAEALLAVVDEPPLdeMLAEGGLSYGh 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 325 -VDSQHYMALLCFKNGSLMrEKIRNESVSRSWSDFSKALQSTEMGNGGN-LGF--YFDVMEiTPEIIGRHRFNTENHKVA 400
Cdd:cd07773  285 hVPGGYYYLAGSLPGGALL-EWFRDLFGGDESDLAAADELAEAAPPGPTgLLFlpHLSGSG-TPDFDPDARGAFLGLTLG 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 401 AFPGDVeVRALIEG-QFMAKRIHA--EGLGYRVmskTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYra 477
Cdd:cd07773  363 TTRADL-LRAILEGlAFELRLNLEalEKAGIPI---DEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAAL-- 436

                 ....*.
gi 767924838 478 fhgLAG 483
Cdd:cd07773  437 ---LAG 439
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
11-503 7.19e-35

nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466808 [Multi-domain]  Cd Length: 482  Bit Score: 137.67  E-value: 7.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPefgtqggvhvhKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVL 90
Cdd:cd07808    3 LGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSP-----------KPGWAEQDPEDWWQATKEALRELLAKAGISPSDIA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  91 ALSGAGQQHGSIYwkagaqqaltslspdlrLHQQLQdcfSISDCPVWMDSSTTAQCRQLEAAVGGAQALscLTGSRAYER 170
Cdd:cd07808   72 AIGLTGQMHGLVL-----------------LDKNGR---PLRPAILWNDQRSAAECEELEARLGDEILI--ITGNPPLPG 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 171 FTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACapHL-EEKLSPPV 249
Cdd:cd07808  130 FTLPKLLWLKENEPEIFARIRKILLPKDYLRYRLTGELA-TDPSDASGTLLFDVEKREWSEELLEAL--GLdPSILPPIV 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 250 PSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTSDTLFLWLQEPMPALEG--HIFCNPVD 326
Cdd:cd07808  207 ESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGAGVvEPGDALISLGTSGVVFAPTDKPVPDPKGrlHTFPHAVP 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 327 SQHY-MALLCFKNGSL--MREKIRNESVsrSWSDFSKALQSTEMGNGGnLGF----------YFDvmeitPEIigRHRFN 393
Cdd:cd07808  287 GKWYaMGVTLSAGLSLrwLRDLFGPDRE--SFDELDAEAAKVPPGSEG-LLFlpylsgertpYWD-----PNA--RGSFF 356
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 394 --TENHKVAAFpgdveVRALIEGQFMA-----KRIHAEGLGYRvmsktKILATGGASHNREILQVLADVFDAPVYVIDTA 466
Cdd:cd07808  357 glSLSHTRAHL-----ARAVLEGVAFSlrdslEVLKELGIKVK-----EIRLIGGGAKSPLWRQILADVLGVPVVVPAEE 426
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 767924838 467 NSACVGSAYRAFHGLAGGTDVPF--SEVVKLA----PNPRLAA 503
Cdd:cd07808  427 EGSAYGAALLAAVGAGVFDDLEEaaAACIKIEktiePDPERHE 469
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
11-503 7.82e-30

nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466790 [Multi-domain]  Cd Length: 478  Bit Score: 122.66  E-value: 7.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNVFYEESvhfdRDLPEFGTQGGVHVHkDGLTVTSPVlmwVQALDIILEKMKASgfdfsQVL 90
Cdd:cd07770    3 LGIDIGTTSTKAVLFDEDGRVVASSS----AEYPLIRPEPGWAEQ-DPEEILEAV---LEALKEVLAKLGGG-----EVD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  91 ALSGAGQQHGSIywkA--GAQQALTSLSPdlrlhqqlqdcfsisdcpvWMDSSTTAQCRQLEAAvggaqalscLTGSRAY 168
Cdd:cd07770   70 AIGFSSAMHSLL---GvdEDGEPLTPVIT-------------------WADTRAAEEAERLRKE---------GDGSELY 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 169 ERfTG---------NQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYsPIDYSDGSGMNLLQIQDKVWSQACLGACAP 239
Cdd:cd07770  119 RR-TGcpihpmyplAKLLWLKEERPELFAKAAKFVSIKEYLLYRLTGEL-VTDYSTASGTGLLNIHTLDWDEEALELLGI 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 240 HlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPAS-LAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEG 318
Cdd:cd07770  197 D-EEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALAnLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPG 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 319 HIFCNPVDSQHY---MALlcfKNGSL----MREKIRNESVsrSWSDFSKALQSTEMGNGGNLGFYFdvmeITPE------ 385
Cdd:cd07770  276 RLWCYRLDENRWlvgGAI---NNGGNvldwLRDTLLLSGD--DYEELDKLAEAVPPGSHGLIFLPY----LAGErapgwn 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 386 ------IIGRhrfnTENHKVAAFpgdveVRALIEGqfMAKRIH--AEGLGYRVMSKTKILATGGASHNREILQVLADVFD 457
Cdd:cd07770  347 pdargaFFGL----TLNHTRADI-----LRAVLEG--VAFNLKsiYEALEELAGPVKEIRASGGFLRSPLWLQILADVLG 415
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 767924838 458 APVYVIDTANSACVGSAYRAFHGLAGGTDVPFSEVVKLA----PNPRLAA 503
Cdd:cd07770  416 RPVLVPEEEEASALGAALLALEALGLISSLEADELVKIGkvvePDPENHA 465
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
133-503 6.05e-22

nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466807 [Multi-domain]  Cd Length: 485  Bit Score: 99.13  E-value: 6.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 133 DCPVWMDSSTTAQCRQLEAAVGGAqalscltgsRAYERFTGNQ------IAKI--YQQN-PEAYSHTERISLVSSFAASL 203
Cdd:cd07805   94 NAIIWSDTRAAEEAEEIAGGLGGI---------EGYRLGGGNPpsgkdpLAKIlwLKENePEIYAKTHKFLDAKDYLNFR 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 204 FLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPA 283
Cdd:cd07805  165 LTGRAA-TDPSTASTTGLMDLRKRRWSEELLRAAGID-PDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDAAA 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 284 SLAG-MRLEEGDIAVSLGTSDtlflWL----QEPMPALEGHIFCNP-VDSQHYMALLCFKNGSLMREKIRN------ESV 351
Cdd:cd07805  243 AALGaGAVEEGDAHIYLGTSG----WVaahvPKPKTDPDHGIFTLAsADPGRYLLAAEQETAGGALEWARDnlggdeDLG 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 352 SRSWSDFSKALQSTEMGNGGnLGFyfdvmeiTPEIIGRhRFNTENHKV-AAF--------PGDVeVRALIEGQFMAKRIH 422
Cdd:cd07805  319 ADDYELLDELAAEAPPGSNG-LLF-------LPWLNGE-RSPVEDPNArGAFiglslehtRADL-ARAVLEGVAFNLRWL 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 423 AEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTA-NSACVGSAYRAFHGLagGTDVPFSEVVKL------ 495
Cdd:cd07805  389 LEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGL--GLLKSFDEAKALvkvekv 466

                 ....*....
gi 767924838 496 -APNPRLAA 503
Cdd:cd07805  467 fEPDPENRA 475
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
190-481 1.08e-20

nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466798 [Multi-domain]  Cd Length: 433  Bit Score: 94.89  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 190 TERISLVSSFAASLFLGSYsPIDYSDGSGMNLLQIQDKVWSQACLGACA-PhlEEKLSPPVPSCSVVGAISSYYVQRYGF 268
Cdd:cd07779  103 TAKFLTVQDYLLYRLTGEF-VTDTTSASRTGLPDIRTRDWSDDLLDAFGiD--RDKLPELVPPGTVIGTLTKEAAEETGL 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 269 PPGCKVVAFTGDNP-ASL-AGMrLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNP--VDSQHYMALLCFKNGSLMR- 343
Cdd:cd07779  180 PEGTPVVAGGGDQQcAALgAGV-LEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPsaVPGKWVLEGSINTGGSAVRw 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 344 --------EKIRNESVSRSWSDFSKALQSTEMGNGGnlgfyfdVMEItPEIIGRHRFNTENHKVAAF--------PGDVe 407
Cdd:cd07779  259 frdefgqdEVAEKELGVSPYELLNEEAAKSPPGSDG-------LLFL-PYLAGAGTPYWNPEARGAFigltlshtRAHL- 329
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924838 408 VRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 481
Cdd:cd07779  330 ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGA 403
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
137-484 3.53e-20

nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466806 [Multi-domain]  Cd Length: 451  Bit Score: 93.36  E-value: 3.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 137 WMDSSTTAQCRQLEAAVGgAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDG 216
Cdd:cd07804   98 YGDRRATEEIEWLNENIG-EDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYIVYKLTGEYV-IDYSSA 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 217 SGMN-LLQIQDKVWSQACLGACAPHlEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASL--AGMrLEEG 293
Cdd:cd07804  176 GNEGgLFDIRKRTWDEELLEALGID-PDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDAAASAlsAGV-VEPG 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 294 DIAVSLGTSdTLFLWLQEPMPALEGHIFCNPVDSQHYMALLC-FKNGSL---MREKIRNESVSRSWSDFSKALQSTEM-- 367
Cdd:cd07804  254 DLLLMLGTA-GDIGVVTDKLPTDPRLWLDYHDIPGTYVLNGGmATSGSLlrwFRDEFAGEEVEAEKSGGDSAYDLLDEea 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 368 -----GNGGnLGF--YFdvM-EITPE--------IIGRHRFNTenhkvaafPGDVeVRALIEGQFMAKRIHAEGLGYRVM 431
Cdd:cd07804  333 ekippGSDG-LIVlpYF--MgERTPIwdpdargvIFGLTLSHT--------RAHL-YRALLEGVAYGLRHHLEVIREAGL 400
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767924838 432 SKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG 484
Cdd:cd07804  401 PIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLA--GVGVG 451
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
296-481 3.19e-17

FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.


Pssm-ID: 426979 [Multi-domain]  Cd Length: 197  Bit Score: 80.06  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  296 AVSLGTSDTLFLWLQEPmpALEGHIFCNPVDSQH-----YMALLCFKNGSLM---------REKIRNESVSRSWSDFSKA 361
Cdd:pfam02782   2 AISAGTSSFVLVETPEP--VLSVHGVWGPYTNEMlpgywGLEGGQSAAGSLLawllqfhglREELRDAGNVESLAELAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  362 LQSTEMGnggnlGFYFDvmeitPEIIGRHRFNTENHKVAAFPG-------DVEVRALIEGQFMAKRIHAEGL----GYRV 430
Cdd:pfam02782  80 AAVAPAG-----GLLFY-----PDFSGNRAPGADPGARGSITGlsspttlAHLYRAILESLALQLRQILEALtkqeGHPI 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767924838  431 MSktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 481
Cdd:pfam02782 150 DT---IHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
11-287 6.23e-15

FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.


Pssm-ID: 395295 [Multi-domain]  Cd Length: 245  Bit Score: 74.68  E-value: 6.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838   11 LGWDFSTQQVKVVAVDAELNVfyeesvhfdrdlpefgtqggVHVHKDGLTVTSPVLMWV--------QALDIILEK-MKA 81
Cdd:pfam00370   3 LGIDCGTTSTKAILFNEQGKI--------------------IAVAQLENPQITPHPGWAeqdpdeiwQAVAQCIAKtLSQ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838   82 SGFDFSQVLALSGAGQQHGSIYWKAGAQQaltslspdlrlhqqlqdcfsISDCPVWMDSSTTAQCRQLEAAvGGAQALSC 161
Cdd:pfam00370  63 LGISLKQIKGIGISNQGHGTVLLDKNDKP--------------------LYNAILWKDRRTAEIVENLKEE-GNNQKLYE 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  162 LTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAPHl 241
Cdd:pfam00370 122 ITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYLRWRLTGVFV-TDHTNASRSMMFNIHKLDWDPELLAALGIP- 199
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767924838  242 EEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAG 287
Cdd:pfam00370 200 RDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
PRK15027 PRK15027
xylulokinase; Provisional
49-334 7.54e-15

xylulokinase; Provisional


Pssm-ID: 184987 [Multi-domain]  Cd Length: 484  Bit Score: 77.31  E-value: 7.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  49 QGGV-HVHKDGLTVTSPVLMWV--------QALDiilEKMKASGFDFS--QVLALSGAGQQHGSiywkagaqqalTSLSP 117
Cdd:PRK15027  20 QGEVvASQTEKLTVSRPHPLWSeqdpeqwwQATD---RAMKALGDQHSlqDVKALGIAGQMHGA-----------TLLDA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 118 DLRLhqqlqdcfsISDCPVWMDSSTTAQCRQLEAAVGGAQALsclTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVS 197
Cdd:PRK15027  86 QQRV---------LRPAILWNDGRCAQECALLEARVPQSRVI---TGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 198 SFAASLFLGSYSPiDYSDGSGMNLLQIQDKVWSQACLGACapHLEEKLSPPVPSCS-VVGAISSYYVQRYGFpPGCKVVA 276
Cdd:PRK15027 154 DYLRLRMTGEFAS-DMSDAAGTMWLDVAKRDWSDVMLQAC--HLSRDQMPALYEGSeITGALLPEVAKAWGM-ATVPVVA 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924838 277 FTGDNPASLAGMRL-EEGDIAVSLGTSDTLFL----WLQEPMPALegHIFCNPVDSQ-HYMALL 334
Cdd:PRK15027 230 GGGDNAAGAVGVGMvDANQAMLSLGTSGVYFAvsegFLSKPESAV--HSFCHALPQRwHLMSVM 291
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
136-474 4.84e-13

nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466805 [Multi-domain]  Cd Length: 444  Bit Score: 71.43  E-value: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 136 VWMDSSTTAQCRQLEAAvGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYshtERISLVssFAASLFL-----GSYSp 210
Cdd:cd07802   97 LSNDSRAADIVDRWEED-GTLEKVYPLTGQPLWPGQPVALLRWLKENEPERY---DRIRTV--LFCKDWIryrltGEIS- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 211 IDYSDGSGmNLLQIQDKVWSQACLGAC-APHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGM- 288
Cdd:cd07802  170 TDYTDAGS-SLLDLDTGEYDDELLDLLgIEELKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVVASALGAg 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 289 RLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGS----------LMREKIRNESVSRSWSDF 358
Cdd:cd07802  249 AVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSAsnldwfldtlLGEEKEAGGSDYDELDEL 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 359 SKALQSTEMG-------NGGNL------GFYfdvmEITPEiigrHRfntenhkvaafPGDVeVRALIEGQFMAKRIHAEG 425
Cdd:cd07802  329 IAAVPPGSSGviflpylYGSGAnpnargGFF----GLTAW----HT-----------RAHL-LRAVYEGIAFSHRDHLER 388
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 767924838 426 LGYRVMSKTkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 474
Cdd:cd07802  389 LLVARKPET-IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAA 436
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
11-474 7.48e-12

nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466801 [Multi-domain]  Cd Length: 429  Bit Score: 67.63  E-value: 7.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  11 LGWDFSTQQVKVVAVDAELNVFYEESvhfdRDLPEFGTQGGVHVHkdgltvtSPvLMWVQALDIILEKMKASGfDFSQVL 90
Cdd:cd07783    3 LGIDLGTSGVRAVVVDEDGTVLASAS----EPYPTSRPGPGWVEQ-------DP-EDWWEALRSLLRELPAEL-RPRRVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  91 ALSGAGQQhGSIywkAGAQQALTSLSPDLrlhqqlqdcfsisdcpVWMDSSTTAQCRQLEAAVGGAQalscltgSRAYER 170
Cdd:cd07783   70 AIAVDGTS-GTL---VLVDREGEPLRPAI----------------MYNDARAVAEAEELAEAAGAVA-------PRTGLA 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 171 FTGNQ-IAKI---YQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDG--SGMNLlqiQDKVWSQAcLGACAPHLEEK 244
Cdd:cd07783  123 VSPSSsLAKLlwlKRHEPEVLAKTAKFLHQADWLAGRLTGDRGVTDYNNAlkLGYDP---ETGRWPSW-LLALLGIPPDL 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 245 LSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGD-NPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCN 323
Cdd:cd07783  199 LPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDsIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSH 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 324 PVDSQHYM----------ALLCFKNGSLMREKIRnesvsrswsdfskalQSTEMGNGGnLGFY--------FDVmeITPE 385
Cdd:cd07783  279 RHGDGYWLvggasntggaVLRWFFSDDELAELSA---------------QADPPGPSG-LIYYplplrgerFPF--WDPD 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 386 IIGrhRFNTENHKVAAFpgdveVRALIEGqfMAkriHAEGLGYRVMSK------TKILATGGASHNREILQVLADVFDAP 459
Cdd:cd07783  341 ARG--FLLPRPHDRAEF-----LRALLEG--IA---FIERLGYERLEElgappvEEVRTAGGGARNDLWNQIRADVLGVP 408
                        490
                 ....*....|....*
gi 767924838 460 VYVIDTaNSACVGSA 474
Cdd:cd07783  409 VVIAEE-EEAALGAA 422
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
177-474 4.50e-10

nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466804 [Multi-domain]  Cd Length: 448  Bit Score: 61.86  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 177 AKIY---QQNPEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGAC-APHleEKLSPPVPSC 252
Cdd:cd07798  134 ARLLwfkENRPEIFERIATVLSISDWIGYRLTGELV-SEPSQASETQLFDIKKREWSQELLEALgLPP--EILPEIVPSG 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 253 SVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMR-LEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNP-VDSQHY 330
Cdd:cd07798  211 TVLGTVSEEAARELGLPEGTPVVVGGADTQCALLGSGaIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGChLVPGKW 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 331 M----ALLCFKNGSLMREKIRnESVSRSWSDFSKALQSTEMGNGGNLGFY----FDvMEITPEIIGRHRFNTENHKVAAF 402
Cdd:cd07798  291 VlesnAGVTGLNYQWLKELLY-GDPEDSYEVLEEEASEIPPGANGVLAFLgpqiFD-ARLSGLKNGGFLFPTPLSASELT 368
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924838 403 PGDVeVRALIEGQFMAKRIHAEGLgyRVMSKT---KILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 474
Cdd:cd07798  369 RGDF-ARAILENIAFAIRANLEQL--EEVSGReipYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAA 440
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
10-477 1.76e-09

nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466796 [Multi-domain]  Cd Length: 436  Bit Score: 59.93  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  10 CLGWDFSTQQVKVVAVDAE-LNVFYEESVHFDRDLPefGTQGGVHVhkdgltvTSPVLMWvQALDIILEKMKAsgFDFSQ 88
Cdd:cd07777    2 VLGIDIGTTSIKAALLDLEsGRILESVSRPTPAPIS--SDDPGRSE-------QDPEKIL-EAVRNLIDELPR--EYLSD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838  89 VLALSGAGQQHGSIYWKAGaQQALTSLspdlrlhqqlqdcfsISdcpvWMDSSTTAQCRQleaavggaqalSCLTGSRAY 168
Cdd:cd07777   70 VTGIGITGQMHGIVLWDED-GNPVSPL---------------IT----WQDQRCSEEFLG-----------GLSTYGEEL 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 169 ERFTGNQIAKIY--------QQNPEAYSHTERISLVSSFAASLFLGSYSP-IDYSDGSGMNLLQIQDKVWSQACLGAcAP 239
Cdd:cd07777  119 LPKSGMRLKPGYglatlfwlLRNGPLPSKADRAGTIGDYIVARLTGLPKPvMHPTNAASWGLFDLETGTWNKDLLEA-LG 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 240 HLEEKLSPPVPSCSVVGAISSyyvqryGFPPGCKVVAFTGDNPASLAG-MRLEEGDIAVSLGTSDTL-FLwlqEPMPALE 317
Cdd:cd07777  198 LPVILLPEIVPSGEIVGTLSS------ALPKGIPVYVALGDNQASVLGsGLNEENDAVLNIGTGAQLsFL---TPKFELS 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 318 GHIFCNPVDSQHYMALLCFKNG------------SLMREKIRNESVSRSWSDFSKALQSTEMGNggnlgfyfdvMEITPE 385
Cdd:cd07777  269 GSVEIRPFFDGRYLLVAASLPGgralavlvdflrEWLRELGGSLSDDEIWEKLDELAESEESSD----------LSVDPT 338
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 386 IIG-RHRFNT---------ENhkvaaF-PGDVeVRALIEGqfMAKRIH--AEGLGYRVMSKTKILATGGAS-HNREILQV 451
Cdd:cd07777  339 FFGeRHDPEGrgsitnigeSN-----FtLGNL-FRALCRG--IAENLHemLPRLDLDLSGIERIVGSGGALrKNPVLRRI 410
                        490       500
                 ....*....|....*....|....*.
gi 767924838 452 LADVFDAPVYVIDTANSACVGSAYRA 477
Cdd:cd07777  411 IEKRFGLPVVLSEGSEEAAVGAALLA 436
ASKHA_NBD_FGGY_AI-2K cd07775
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ...
184-494 1.71e-08

nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466794 [Multi-domain]  Cd Length: 492  Bit Score: 56.96  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 184 PEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAphLEEKLSPPV-PSCSVVGAISSYY 262
Cdd:cd07775  146 PEIYRKAAKITMLSDWIAYKLSGELA-VEPSNGSTTGLFDLKTRDWDPEILEMAG--LKADILPPVvESGTVIGKVTKEA 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 263 VQRYGFPPGCKVVAFTGDNPASLAGM-RLEEGDIAVSLGTsdtlfLWLQE-----PMPALEGHIFCNP-VDSQHYMALLC 335
Cdd:cd07775  223 AEETGLKEGTPVVVGGGDVQLGCLGLgVVRPGQTAVLGGS-----FWQQEvntaaPVTDPAMNIRVNChVIPDMWQAEGI 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 336 -FKNGSLMR---------EKIRNESVSRSWSDF-SKALQSTEMGNGGNLGFYFDVMEI------TPEIIGrHRFNTENHK 398
Cdd:cd07775  298 sFFPGLVMRwfrdafcaeEKEIAERLGIDAYDLlEEMAKDVPPGSYGIMPIFSDVMNYknwrhaAPSFLN-LDIDPEKCN 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 399 VAAFpgdveVRALIEGQFMAKRIH----AEGLGYRVMSktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 474
Cdd:cd07775  377 KATF-----FRAIMENAAIVSAGNleriAEFSGIFPDS---LVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAA 448
                        330       340
                 ....*....|....*....|
gi 767924838 475 YRAfhGLAGGTDVPFSEVVK 494
Cdd:cd07775  449 IAA--GVGAGIYSSLEEAVE 466
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
137-474 3.22e-07

nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466799 [Multi-domain]  Cd Length: 504  Bit Score: 52.92  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 137 WMDSSTTAQCRQLEAAVGGAQALSCLTGSRAY--ERFtgnqIAKI---YQQNPEAYSHTERI-------------SLVSS 198
Cdd:cd07781  101 WMDHRAQEEAAEINETAHPALEYYLAYYGGVYssEWM----WPKAlwlKRNAPEVYDAAYTIveacdwinarltgRWVRS 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 199 FAASLFLGSYSPidysDGSGmnllqiqdkvWSQACLGACAPHL---EEKLSPPV-PSCSVVGAISSYYVQRYGFPPGCKV 274
Cdd:cd07781  177 RCAAGHKWMYNE----WGGG----------PPREFLAALDPGLlklREKLPGEVvPVGEPAGTLTAEAAERLGLPAGIPV 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 275 VAFTGDNPASLAGMR-LEEGDIAVSLGTSdTLFLwLQEPMP-ALEGhiFCNPVDS----QHYMA----------LLCFKN 338
Cdd:cd07781  243 AQGGIDAHMGAIGAGvVEPGTLALIMGTS-TCHL-MVSPKPvDIPG--ICGPVPDavvpGLYGLeagqsavgdiFAWFVR 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 339 GSLMREKIRNESVSRSWSDFSKALQSTEMG------NGGNLGFYFDvMEITPEIIGRhrfnTENHKvaafPGDVeVRALI 412
Cdd:cd07781  319 LFVPPAEERGDSIYALLSEEAAKLPPGESGlvaldwFNGNRTPLVD-PRLRGAIVGL----TLGTT----PAHI-YRALL 388
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924838 413 EG-QFMAKRI--HAEGLGYRVmskTKILATGG-ASHNREILQVLADVFDAPVYVIDTANSACVGSA 474
Cdd:cd07781  389 EAtAFGTRAIieRFEEAGVPV---NRVVACGGiAEKNPLWMQIYADVLGRPIKVPKSDQAPALGAA 451
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
408-484 2.40e-03

nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466803 [Multi-domain]  Cd Length: 501  Bit Score: 40.62  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 408 VRALIEGqfMAKRIHA--EGLGYRVMSK-TKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG 484
Cdd:cd07793  387 VRAILES--IAFRVKQllETMEKETSIKiSSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLA--GLASG 462
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
249-513 2.81e-03

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 40.34  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 249 VPSCSVVGAISSYYVQRYgfpPGCKVVAFTGDNPASLAG-MRLEEGDIAVSLGTSdtLFLWL---QEPMP---------- 314
Cdd:PTZ00294 219 KSSSENFGTISGEAVPLL---EGVPITGCIGDQQAALIGhGCFEKGDAKNTYGTG--CFLLMntgTEIVFskhgllttvc 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 315 -----------ALEGHIFCNpvdsqhymallcfknGSLMREKIRNESVSRSWSDFSKALQSTEmgngGNLGFYFdvmeit 383
Cdd:PTZ00294 294 yqlgpngptvyALEGSIAVA---------------GAGVEWLRDNMGLISHPSEIEKLARSVK----DTGGVVF------ 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 384 peiigrhrfntenhkVAAFPG------DVEVRALIEG-QFMAKRIHA-----EGLGYRV------MSK------TKILAT 439
Cdd:PTZ00294 349 ---------------VPAFSGlfapywRPDARGTIVGmTLKTTRAHIvraalEAIALQTndviesMEKdagielNSLRVD 413
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924838 440 GGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG--TDVpfSEVVKLAPNPRLAATPSPGASQRR 513
Cdd:PTZ00294 414 GGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLA--GLAVGvwKSL--EEVKKLIRRSNSTFSPQMSAEERK 485
PRK04123 PRK04123
ribulokinase; Provisional
409-488 7.76e-03

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 39.06  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 409 RALIEGQ-FMAKRI----HAEGlgyrvMSKTKILATGG-ASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFhgLA 482
Cdd:PRK04123 415 RALIEATaFGTRAImecfEDQG-----VPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAA--VA 487

                 ....*...
gi 767924838 483 GGT--DVP 488
Cdd:PRK04123 488 AGAypDIP 495
PRK10939 PRK10939
autoinducer-2 (AI-2) kinase; Provisional
184-311 9.63e-03

autoinducer-2 (AI-2) kinase; Provisional


Pssm-ID: 182853 [Multi-domain]  Cd Length: 520  Bit Score: 38.83  E-value: 9.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924838 184 PEAYSHTERISLVSSFAASLFLGSYSpIDYSDGSGMNLLQIQDKVWSQACLGACAphLEEKLSPPV-PSCSVVGAISSYY 262
Cdd:PRK10939 149 PDIYRQAHTITMISDWIAYMLSGELA-VDPSNAGTTGLLDLVTRDWDPALLEMAG--LRADILPPVkETGTVLGHVTAKA 225
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767924838 263 VQRYGFPPGCKVVAFTGDNPASLAGMRL-EEGDIAVSLGTsdtlfLWLQE 311
Cdd:PRK10939 226 AAETGLRAGTPVVMGGGDVQLGCLGLGVvRPGQTAVLGGT-----FWQQV 270
 
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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