|
Name |
Accession |
Description |
Interval |
E-value |
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
19-489 |
0e+00 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 1018.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 19 MLARYERECRSLTLREIHRFNNGLHSQNGYVTWNVDRLESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQRVGL 98
Cdd:PRK10640 1 MLARYERECRSLTLREIHRFNNGLHSQDGFDTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDYVLLDKQGQRVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 99 PVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYFSYRLTGKMNWEYTN 178
Cdd:PRK10640 81 PVSYRDSRTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 179 ATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNGSRAAYLSSG 258
Cdd:PRK10640 161 ATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNDSDAAYLSSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 259 TWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQINDLPALIAATQALPACRFIINPNDDR 338
Cdd:PRK10640 241 TWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQITDLPALIAATAALPACRFLINPNDDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 339 FINPDEMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACG 418
Cdd:PRK10640 321 FINPPSMCSEIQAACRETAQPVPESDAELARCIFDSLALLYADVLHELAQLRGEPFSQLHIVGGGCQNALLNQLCADACG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 535687901 419 IRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTTANLTTFTPNPDSEIAHYVAQIHSTRQTKELCA 489
Cdd:PRK10640 401 IRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTNFPLTTFTPNPDSEIARHVAQFQSLRQTKELCA 471
|
|
| rhamnulo_kin |
TIGR02627 |
rhamnulokinase; This model describes rhamnulokinase, an enzyme that catalyzes the second step ... |
7-460 |
0e+00 |
|
rhamnulokinase; This model describes rhamnulokinase, an enzyme that catalyzes the second step in rhamnose catabolism.
Pssm-ID: 274237 [Multi-domain] Cd Length: 454 Bit Score: 886.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVMLARYERECRSLTLREIHRFNNGLHSQNGYVTWNVDRLESAIRLGLNKVCEEGIRIDSIGIDTWGVDF 86
Cdd:TIGR02627 1 VAVDLGASSGRVMLASYENECQKLTLEEIHRFKNGLVSQNGHECWDIDALEQEIRLGLNKVDAEGIAPDSIGIDTWGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 87 VLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYFSY 166
Cdd:TIGR02627 81 VLLDQNGQRVGDPVSYRDSRTDGVMAQVQSELGKEAIYQRTGIQFLPFNTLYQLRALTEQQPDLLEKVAHFLLIPDYLNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 167 RLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASP 246
Cdd:TIGR02627 161 RLTGKKVWEYTNATTTQLVNINTDDWDEDLLAYLGVPAAWFGRPTHPGNVIGLWECPQGNQIPVVAVATHDTASAVVAAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 247 LNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQINDLPALIAATQALP 326
Cdd:TIGR02627 241 LQGENAAYLSSGTWSLMGFESQTPITNEQALAANITNEGGADGRYRVLKNIMGLWLLQRVCRERDINDLPALIEQAQALP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 327 ACRFIINPNDDRFINPDEMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQN 406
Cdd:TIGR02627 321 AFKSIINPNDDRFINPENMCEEIQAYCRETNQPIPESDAELARCIFDSLALLYRQVLLELAELRGKPISQLHIVGGGSQN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 535687901 407 ALLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTTANL 460
Cdd:TIGR02627 401 AFLNQLCADACGIRVIAGPVEASTLGNIGVQLMALDEINDMAAFRQIVSNNFPL 454
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
5-457 |
0e+00 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 658.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 5 NCVAVDLGASSGRVMLARYEREcrSLTLREIHRFNNGLHSQNGYVTWNVDRLESAIRLGLNKVCEEGIRIDSIGIDTWGV 84
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGG--KLELEEIHRFPNRPVEINGHLYWDIDRLFDEIKEGLKKAAEQGGDIDSIGIDTWGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 85 DFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYF 164
Cdd:cd07771 79 DFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 165 SYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHW---ICPQG--NEIPVVAVASHDTA 239
Cdd:cd07771 159 NYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLkpeVAEELglKGIPVIAVASHDTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 240 SAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQINDLP--- 316
Cdd:cd07771 239 SAVAAVPAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGFTNEGGADGTIRLLKNITGLWLLQECRREWEEEGKDysy 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 317 -ALIAATQALPACRFIINPNDDRFINPDEMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFS 395
Cdd:cd07771 319 dELVALAEEAPPFGAFIDPDDPRFLNPGDMPEAIRAYCRETGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRID 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535687901 396 QLHIVGGGCQNALLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTT 457
Cdd:cd07771 399 RIHIVGGGSRNALLCQLTADATGLPVIAGPVEATAIGNLLVQLIALGEIKSLEEGRELVRNS 460
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-433 |
5.99e-55 |
|
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: 188.54 E-value: 5.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 6 CVAVDLGASSGRVMLARyerecRSLTLREIHRFNNGLHS-QNGYVTWNVDRLESAIRLGLNKVCEEG----IRIDSIGID 80
Cdd:cd00366 2 LLGIDIGTTSVKAALFD-----EDGNLVASASREYPLIYpQPGWAEQDPEDWWQAVVEAIREVLAKAgidpSDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 81 TWGVDFVLLDQQGQRVGLPVAYRDSRtnglmaqaqqqlgkrdiyqrsgiqflpfntiyqlralteqqpeliphiAHALLI 160
Cdd:cd00366 77 GQMPGVVLVDADGNPLRPAIIWLDRR------------------------------------------------AKFLQP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 161 PDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHW------ICPQGNEIPVVAVA 234
Cdd:cd00366 109 NDYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVtpeaaeETGLPAGTPVVAGG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 235 sHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTalaaNITNEGGA-EGRYRVLKNI--MGL---WLLQRVLQ 308
Cdd:cd00366 189 -GDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDP----RLLNRCHVvPGLWLLEGAIntGGAslrWFRDEFGE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 309 ERQ----INDLPALiAATQALPACRFIINPNDDRFINPDEMCSeiqAACRETAQPIPESDAELARCIFDSLALLYADVLh 384
Cdd:cd00366 264 EEDsdaeYEGLDEL-AAEVPPGSDGLIFLPYLSGERSPIWDPA---ARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNL- 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 535687901 385 ELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGPV-EASTLGN 433
Cdd:cd00366 339 EILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVaEGAALGA 388
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
7-432 |
1.53e-53 |
|
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: 186.25 E-value: 1.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVMLarYERECRslTLREIHRFNNGLHSQNGYVTWNVDRLESAIRLGLNKVCEE--GIRIDSIGIDTWGV 84
Cdd:cd07773 3 LGIDIGTTNVKAVL--FDEDGR--ILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQagPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 85 DFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYF 164
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 165 SYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQG-------NEIPVVaVASHD 237
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGT-VTPEAaeelglpAGTPVV-VGGHD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 238 TASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRY----------RVLKnimglWLLQRVL 307
Cdd:cd07773 237 HLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSYGHHVPGGYyylagslpggALLE-----WFRDLFG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 308 QERQinDLPALIAATQALPAcrfiiNPNDDRFInPDEMCSEIQAACRETAQPI----PESD-AELARCIFDSLALLYADV 382
Cdd:cd07773 312 GDES--DLAAADELAEAAPP-----GPTGLLFL-PHLSGSGTPDFDPDARGAFlgltLGTTrADLLRAILEGLAFELRLN 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 535687901 383 LHELAQLrGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGPV-EASTLG 432
Cdd:cd07773 384 LEALEKA-GIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVpEATALG 433
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
7-468 |
7.99e-39 |
|
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: 147.29 E-value: 7.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVMLARYERECRSLTLRE--IHRFNNGLHSQNGYVTWNVdrLESAIRLGLNKVCEEGIRIDSIGIDTWGV 84
Cdd:COG1070 4 LGIDIGTTSVKAVLFDADGEVVASASAEypLSSPHPGWAEQDPEDWWEA--VVEAIRELLAKAGVDPEEIAAIGVSGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 85 DFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYF 164
Cdd:COG1070 82 GLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 165 SYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGH--------WICPQGneIPVVAvASH 236
Cdd:COG1070 162 RYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTltaeaaaeTGLPAG--TPVVA-GAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 237 DTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITneGGAEGRYrvlkNIMGL---------WlLQRVL 307
Cdd:COG1070 239 DNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFC--HAVPGRW----LPMGAtnnggsalrW-FRDLF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 308 QERQINDLPALIA-ATQALPAC------------RFIINPNDDR--FINPDemcseiqaacRETaqpipeSDAELARCIF 372
Cdd:COG1070 312 ADGELDDYEELNAlAAEVPPGAdgllflpylsgeRTPHWDPNARgaFFGLT----------LSH------TRAHLARAVL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 373 DSLALLYADVLHELAQLrGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAgpVEASTLGNIGIQLMTLDELNNVDDFRQ 452
Cdd:COG1070 376 EGVAFALRDGLEALEEA-GVKIDRIRATGGGARSPLWRQILADVLGRPVEV--PEAEEGGALGAALLAAVGLGLYDDLEE 452
|
490
....*....|....*..
gi 535687901 453 VVSTTANLT-TFTPNPD 468
Cdd:COG1070 453 AAAAMVRVGeTIEPDPE 469
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
253-441 |
1.89e-35 |
|
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: 130.52 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 253 AYLSSGTWSLMGFESQTPFTNDTALAANITNE-----GGAEGRYRVLKNIMGlWLLQRVLQERQIND------LPALIAA 321
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEmlpgyWGLEGGQSAAGSLLA-WLLQFHGLREELRDagnvesLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 322 TQALPACRFIINPNDDRFINPdemCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVG 401
Cdd:pfam02782 80 AAVAPAGGLLFYPDFSGNRAP---GADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 535687901 402 GGCQNALLNQLCADACGIRV-IAGPVEASTLGNIGIQLMTL 441
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVvVPGPDEATALGAALLAAVAA 197
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
51-471 |
4.11e-34 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 133.62 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 51 WNVD----RLESAIRLGLNKVCEEGIRidSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQR 126
Cdd:PRK10331 47 WSLDailqRFADCCRQINSELTECHIR--GITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 127 SGIQFLPFNTIYQLRALTEQQPELIPHiAHA-LLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKA 205
Cdd:PRK10331 125 SGVGAFSFNTLYKLVWLKENHPQLLEQ-AHAwLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 206 WFGRPTHPGNVIGH--------WICPQGneIPVVAvASHDTASAVIasplnGSRAAY----LSSGTWSLMGFESQTPFTN 273
Cdd:PRK10331 204 LFPRLVEAGEQIGTlqpsaaalLGLPVG--IPVIS-AGHDTQFALF-----GSGAGQnqpvLSSGTWEILMVRSAQVDTS 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 274 DTALAANITNEGGAE-GRYrvlkNIMGLWLLQRVLQ-ERQI-----NDLPALIAATQALPA--------CRFIINPNddr 338
Cdd:PRK10331 276 LLSQYAGSTCELDSQsGLY----NPGMQWLASGVLEwVRKLfwtaeTPYQTMIEEARAIPPgadgvkmqCDLLACQN--- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 339 finpdemcSEIQAACRETAQpipesdAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACG 418
Cdd:PRK10331 349 --------AGWQGVTLNTTR------GHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 535687901 419 --IRVIAGPvEASTLGNIGIQLMTLDELNNVDDFRQVVSTTanLTTFTPNPDSEI 471
Cdd:PRK10331 415 ipIKVLDDA-ETTVAGAAMFGWYGVGEFSSPEQARAQMKYQ--YRYFYPQTEPEF 466
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
7-432 |
2.97e-27 |
|
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: 113.47 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVMLARYERECrsltLREIHRFNNGLHSQNGYVTWNVDRLESAIRLGLNKVCEEGI--RIDSIGID-TWG 83
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTV----LASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRprRVVAIAVDgTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 84 VdFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGkrDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDY 163
Cdd:cd07783 79 T-LVLVDREGEPLRPAIMYNDARAVAEAEELAEAAG--AVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 164 FSYRLTGKMNW-EYTNATTTqLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQ-------GNEIPVVAVAS 235
Cdd:cd07783 156 LAGRLTGDRGVtDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGT-LTAEaaeelglPAGTPVVAGTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 236 hDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPftndtalaanitnEGGAEGRYRVLKNIMGLWL-----------LQ 304
Cdd:cd07783 234 -DSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKR-------------VPDPGGGVYSHRHGDGYWLvggasntggavLR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 305 RVLQERQINDLPALIAATQA-------LPAC--RFiinPnddrFINPDemcseIQAACRetaqPIPESDAELARCIFDSL 375
Cdd:cd07783 300 WFFSDDELAELSAQADPPGPsgliyypLPLRgeRF---P----FWDPD-----ARGFLL----PRPHDRAEFLRALLEGI 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 535687901 376 ALLYADVLHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGPVEASTLG 432
Cdd:cd07783 364 AFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAALG 420
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
7-243 |
1.75e-26 |
|
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: 107.42 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVMLarYERECRSLTlreIHRFNNGLHSQ-NGYVTWNVD----RLESAIRLGLNKVCEEGIRIDSIGIDT 81
Cdd:pfam00370 3 LGIDCGTTSTKAIL--FNEQGKIIA---VAQLENPQITPhPGWAEQDPDeiwqAVAQCIAKTLSQLGISLKQIKGIGISN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 82 WGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIP 161
Cdd:pfam00370 78 QGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 162 DYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGrPTHPGNVIGHWICPQG-------NEIPVVAVA 234
Cdd:pfam00370 158 DYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLP-PLVESSEIYGELNPELaamwgldEGVPVVGGG 236
|
....*....
gi 535687901 235 sHDTASAVI 243
Cdd:pfam00370 237 -GDQQAAAF 244
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
7-474 |
3.62e-25 |
|
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: 108.03 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVMLarYERECRslTLREIHRFNNGLHSQNGYVTWNVDRLESAIRLGLNKVCE--EGIRIDSIGIDTWGV 84
Cdd:cd07770 3 LGIDIGTTSTKAVL--FDEDGR--VVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAklGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 85 DFVLLDQQGQRVGlPV-AYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDY 163
Cdd:cd07770 79 SLLGVDEDGEPLT-PViTWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 164 FSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWIC------PQGNEIPVVAVAShD 237
Cdd:cd07770 158 LLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPefaerlGLLAGTPVVLGAS-D 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 238 TASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDT------ALAAN------ITNEGGAegryrVLKnimglWLLQR 305
Cdd:cd07770 237 GALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPgrlwcyRLDENrwlvggAINNGGN-----VLD-----WLRDT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 306 VLQERQI-NDLPALIAATQA-------LPacrfiinpnddrFIN----P---DEMCSEIQAACRETaqpipeSDAELARC 370
Cdd:cd07770 307 LLLSGDDyEELDKLAEAVPPgshglifLP------------YLAgeraPgwnPDARGAFFGLTLNH------TRADILRA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 371 IFDSLALLYADVLHELAQLRGEDfSQLHIVGGGCQNALLNQLCADACGIRVIAGPV-EASTLGNIgiqLMTLDELNNVDD 449
Cdd:cd07770 369 VLEGVAFNLKSIYEALEELAGPV-KEIRASGGFLRSPLWLQILADVLGRPVLVPEEeEASALGAA---LLALEALGLISS 444
|
490 500
....*....|....*....|....*
gi 535687901 450 FrQVVSTTANLTTFTPNPdSEIAHY 474
Cdd:cd07770 445 L-EADELVKIGKVVEPDP-ENHAIY 467
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
7-432 |
2.83e-22 |
|
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: 99.22 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVMLARYERECRSLTLREIHRFNNGLHSqNGYVtWNV----DRLESAIRLGLNKVCEEGIRIDSIGIDTW 82
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYP-DAKE-FDPeelwEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 83 GVDFVLLDQQGQRV-GLPvaYRDSRTNGLMAQAQQQLGKRdIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIP 161
Cdd:cd07798 81 REGIVFLDKDGRELyAGP--NIDARGVEEAAEIDDEFGEE-IYTTTGHWPTELFPAARLLWFKENRPEIFERIATVLSIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 162 DYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIG--------HWICPQGneIPVVaV 233
Cdd:cd07798 158 DWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGtvseeaarELGLPEG--TPVV-V 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 234 ASHDTASAVIASPLNGSRAAYLSSGTWS-LMGFESQtPFTNDTalaANI-TNEGGAEGRYRVLKN--IMGL---WLLQRV 306
Cdd:cd07798 235 GGADTQCALLGSGAIEPGDIGIVAGTTTpVQMVTDE-PIIDPE---RRLwTGCHLVPGKWVLESNagVTGLnyqWLKELL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 307 LQERQIN-DLPALIAATQALPACRFIInpnddrFINPDEMCSEIQAACR------ETAQPIPESDAELARCIFDSLAllY 379
Cdd:cd07798 311 YGDPEDSyEVLEEEASEIPPGANGVLA------FLGPQIFDARLSGLKNggflfpTPLSASELTRGDFARAILENIA--F 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 535687901 380 ADV--LHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVI-AGPVEASTLG 432
Cdd:cd07798 383 AIRanLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLvPEGREASALG 438
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
7-468 |
2.21e-21 |
|
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: 96.43 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVML----------ARYERECRSltlreihrFNNGLHSQNGYVTWnvDRLESAIRLGLNKVCEEGIRIDS 76
Cdd:cd07779 3 LGIDVGTTSTRAIIfdldgnivasGYREYPPYY--------PEPGWVEQDPDDWW--DALCEALKEAVAKAGVDPEDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 77 IGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTnglmaqaqqqlgkrdiyqrsgiqflpfntiyqlralteqqpeliphiAH 156
Cdd:cd07779 73 IGLTSQRSTFVPVDEDGRPLRPAISWQDKRT-----------------------------------------------AK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 157 ALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQ-------GNEIP 229
Cdd:cd07779 106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGT-LTKEaaeetglPEGTP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 230 VVAvASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNdtalaanitneggAEGRYRVLKNIM-GLWLLqrvlq 308
Cdd:cd07779 185 VVA-GGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVED-------------PERRIPCNPSAVpGKWVL----- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 309 ERQINDLPALI-----AATQALPACRFIINPNDDRFinpDEMCSEIQAACRE---------TAQPIPESDA--------- 365
Cdd:cd07779 246 EGSINTGGSAVrwfrdEFGQDEVAEKELGVSPYELL---NEEAAKSPPGSDGllflpylagAGTPYWNPEArgafigltl 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 366 -----ELARCIFDSLALLYADVLhELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGPV-EASTLGNIGIQLM 439
Cdd:cd07779 323 shtraHLARAILEGIAFELRDNL-EAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETsEATALGAAILAAV 401
|
490 500 510
....*....|....*....|....*....|
gi 535687901 440 TLDELNNVDD-FRQVVSTTAnltTFTPNPD 468
Cdd:cd07779 402 GAGIYPDFEEaVKAMVRVTD---TFEPDPE 428
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
7-468 |
1.34e-19 |
|
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: 91.43 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVMLARYERECRSLTLREIHRFnnglHSQNGYVT------WNVdrLESAIRLGLNKVCEEGIRIDSIGID 80
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTY----YPKPGWAEqdpedwWDA--VCRATRALLEKSGIDPSDIAAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 81 TWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFL-PFNTIYQLRALTEQQPELIPHIAHALL 159
Cdd:cd07805 77 GQMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPsGKDPLAKILWLKENEPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 160 IPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQGNE-------IPVVA 232
Cdd:cd07805 157 AKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGE-LTPEAAAelglpagTPVVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 233 vASHDTASAVIasplnGSRA-----AYLSSGTWSLMGFESQTPFTNDTALAANITneGGAEGRYrvlkNIMGL------- 300
Cdd:cd07805 236 -GGGDAAAAAL-----GAGAveegdAHIYLGTSGWVAAHVPKPKTDPDHGIFTLA--SADPGRY----LLAAEqetagga 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 301 --WLLQRVLQ-ERQINDLPALI--AATQALPAC------------RFIINPNDDR--FINpdemcseiqaacretaqpI- 360
Cdd:cd07805 304 leWARDNLGGdEDLGADDYELLdeLAAEAPPGSngllflpwlngeRSPVEDPNARgaFIG------------------Ls 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 361 PESD-AELARCIFDSLALLYADVLhELAQLRGEDFSQLHIVGGGCQNALLNQLCADACG--IRVIAGPVEASTLGNIGIQ 437
Cdd:cd07805 366 LEHTrADLARAVLEGVAFNLRWLL-EALEKLTRKIDELRLVGGGARSDLWCQILADVLGrpVEVPENPQEAGALGAALLA 444
|
490 500 510
....*....|....*....|....*....|.
gi 535687901 438 LMTLDELNNVDDFRQVVSTTAnltTFTPNPD 468
Cdd:cd07805 445 AVGLGLLKSFDEAKALVKVEK---VFEPDPE 472
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
7-432 |
3.37e-19 |
|
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: 89.92 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLgasSGRvMLARYERECRSLTLReihrfnNGLHSQNGYVTWnvDRLESAIRlglnKVCEEGI----RIDSIGIDTW 82
Cdd:cd07802 15 VLFDL---DGR-EIAVASRPTPVISPR------PGWAERDMDELW--QATAEAIR----ELLEKSGvdpsDIAGVGVTGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 83 GVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPD 162
Cdd:cd07802 79 GNGLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 163 YFSYRLTGKMNWEYTNATTTqLVNINSDDWDESLLAWSG--ANKAWFGRPTHPGNVIGHwI---------CPQGneIPVV 231
Cdd:cd07802 159 WIRYRLTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGieELKDKLPPLVPSTEIAGR-VtaeaaaltgLPEG--TPVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 232 AVAsHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTaLAANITNegGAEGRYRVLKNIMG----L-WLLQRV 306
Cdd:cd07802 235 AGA-FDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDS-VGSNSLH--ADPGLYLIVEASPTsasnLdWFLDTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 307 L---QERQINDLPALIAATQALP----------------------ACRFIINPNDDRfinpdemcseiqaacretaqpip 361
Cdd:cd07802 311 LgeeKEAGGSDYDELDELIAAVPpgssgviflpylygsganpnarGGFFGLTAWHTR----------------------- 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535687901 362 esdAELARCIFDSLALLYADvlHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGPV-EASTLG 432
Cdd:cd07802 368 ---AHLLRAVYEGIAFSHRD--HLERLLVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGeELGALG 434
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-431 |
1.78e-18 |
|
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: 87.66 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 5 NCVAVDLGASSgrVMLARYEREcrSLTLREIHRFNNGL---HSQNGYVTWNVDRLESAIRLGLNKVCEE-GIRIDSIGID 80
Cdd:cd07777 1 NVLGIDIGTTS--IKAALLDLE--SGRILESVSRPTPApisSDDPGRSEQDPEKILEAVRNLIDELPREyLSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 81 TW--GvdFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIyQRSGIQF---LPFNTIYQLRalteQQPELIPHIA 155
Cdd:cd07777 77 GQmhG--IVLWDEDGNPVSPLITWQDQRCSEEFLGGLSTYGEELL-PKSGMRLkpgYGLATLFWLL----RNGPLPSKAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 156 HALLIPDYFSYRLTGK----MNWeyTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVV 231
Cdd:cd07777 150 RAGTIGDYIVARLTGLpkpvMHP--TNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKGIPVY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 232 aVASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQT----------PFTNDT--ALAANITneGGaegryRVLKNIMG 299
Cdd:cd07777 228 -VALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKfelsgsveirPFFDGRylLVAASLP--GG-----RALAVLVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 300 lwLLQRVLQER-------QINDLpaLIAATQALPACRFIINPnddRF----INPDEmcseiqaacRETAQPIPESD---A 365
Cdd:cd07777 300 --FLREWLRELggslsddEIWEK--LDELAESEESSDLSVDP---TFfgerHDPEG---------RGSITNIGESNftlG 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535687901 366 ELARCIFDSLALLYADVLHELaQLRGEDFSQLHIVGGGCQ-NALLNQLCADACGIRVIAGPVEASTL 431
Cdd:cd07777 364 NLFRALCRGIAENLHEMLPRL-DLDLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAA 429
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
7-432 |
1.25e-15 |
|
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: 79.12 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVML-ARYERECRSLTLR-EIHRFNNGLHSQNGYVTWNVdrLESAIRLGLNKVCEEGIRIDSIGID--TW 82
Cdd:cd07808 3 LGIDLGTSSVKAVLvDEDGRVLASASAEyPTSSPKPGWAEQDPEDWWQA--TKEALRELLAKAGISPSDIAAIGLTgqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 83 GVdfVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRdIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPD 162
Cdd:cd07808 81 GL--VLLDKNGRPLRPAILWNDQRSAAECEELEARLGDE-ILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 163 YFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQGNE-------IPVVAVAS 235
Cdd:cd07808 158 YLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGT-LTPEAAEelglpegTPVVAGAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 236 hDTASAVIASPLNGSRAAYLSSGTwslmgfesqtpftndtalAANITnegGAEGRYRVLKN---------IMGLWLLQRV 306
Cdd:cd07808 237 -DNAAAALGAGVVEPGDALISLGT------------------SGVVF---APTDKPVPDPKgrlhtfphaVPGKWYAMGV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 307 LQerqindlpaliAATQALPACRFIINPNDDRFINPDEMCSEIQAACR----------ETAqPIPESDA----------- 365
Cdd:cd07808 295 TL-----------SAGLSLRWLRDLFGPDRESFDELDAEAAKVPPGSEgllflpylsgERT-PYWDPNArgsffglslsh 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535687901 366 ---ELARCIFD----SLALLYaDVLHELaqlrGEDFSQLHIVGGGCQNALLNQLCADACGIRV-IAGPVEASTLG 432
Cdd:cd07808 363 traHLARAVLEgvafSLRDSL-EVLKEL----GIKVKEIRLIGGGAKSPLWRQILADVLGVPVvVPAEEEGSAYG 432
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
8-432 |
6.84e-13 |
|
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: 70.44 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 8 AVDLGASSGRVMLARYERECRSLTLRE-IHRFNNGLH-SQNGYVTWNVDRLESAIRLGLNKVCEEGIRIDSIGIDTWGVD 85
Cdd:cd07775 4 ALDAGTGSGRAVIFDLEGNQIAVAQREwRHKEVPDVPgSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSMREG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 86 FVLLDQQGQRVgLPVAYRDSRtnglmaqAQQQLGK---------RDIYQRSGiQFLPFNTIYQLRALTEQQPELIPHIAH 156
Cdd:cd07775 84 IVLYDNEGEEI-WACANVDAR-------AAEEVSElkelyntleEEVYRISG-QTFALGAIPRLLWLKNNRPEIYRKAAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 157 ALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQGNE-------IP 229
Cdd:cd07775 155 ITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGK-VTKEAAEetglkegTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 230 VVaVASHDTASAVIA-SPLNGSRAAYLSSGTWSLMgFESQTPFTNdtalaanitneggAEGRYRVLKNIM-GLWllqrvl 307
Cdd:cd07775 234 VV-VGGGDVQLGCLGlGVVRPGQTAVLGGSFWQQE-VNTAAPVTD-------------PAMNIRVNCHVIpDMW------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 308 QERQINDLPALIA--------ATQALPACRFIINPNDdrFINpdEMCSEIQAACREtAQPI------------------- 360
Cdd:cd07775 293 QAEGISFFPGLVMrwfrdafcAEEKEIAERLGIDAYD--LLE--EMAKDVPPGSYG-IMPIfsdvmnyknwrhaapsfln 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 361 ----PE--SDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAgPV--EASTLG 432
Cdd:cd07775 368 ldidPEkcNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKV-PVvkEATALG 446
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
6-432 |
2.11e-11 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. 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: 466792 [Multi-domain] Cd Length: 424 Bit Score: 65.74 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 6 CVAV-DLGASSGRVMLARYEREC---RSLTLREIHRfnnglhsqNGYVTWNVDRLESAIRLGLNKVCEEGiRIDSIGIDT 81
Cdd:cd07772 1 VIAVfDIGKTNKKLLLFDENGEVlaeRSTPNPEIEE--------DGYPCEDVEAIWEWLLDSLAELAKRH-RIDAINFTT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 82 WGVDFVLLDQQGQRVGLPVAYrdsrTNGLMAQAQQQL-GKRDIYQRSGIQFLP--FNTIYQLRALTEQQPELIPHIAHAL 158
Cdd:cd07772 72 HGATFALLDENGELALPVYDY----EKPIPDEINEAYyAERGPFEETGSPPLPggLNLGKQLYWLKREKPELFARAKTIL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 159 LIPDYFSYRLTGKMNWEYTNATT-TQLVNINSDD---------WDESLLAWSGANKAwFGrPTHPGNVIGHWIcpqGNEI 228
Cdd:cd07772 148 PLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEysslvkkegWDKLFPPLRKAWEV-LG-PLRPDLARRTGL---PKDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 229 PVVAVAsHDTASAVIASPLNG-SRAAYLSSGTW--SLMGFESQTPFTNDTA--LAANITNEGgaegryRVLKN--IMGlw 301
Cdd:cd07772 223 PVGCGI-HDSNAALLPYLAAGkEPFTLLSTGTWciAMNPGNDLPLTELDLArdCLYNLDVFG------RPVKTarFMG-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 302 llQRVLqERQINDLPALIAATQALPACRFIInpNDDRFINPD----EMCSEIQAACRETAQPIPESDAELARCIfdSLAL 377
Cdd:cd07772 294 --GREY-ERLVERIAKSFPQLPSLADLAKLL--ARGTFALPSfapgGGPFPGSGGRGVLSAFPSAEEAYALAIL--YLAL 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 535687901 378 LYADVLHELaqlrGEDFSQLHIVGGGCQNALLNQLCADAC-GIRVIAGPV-EASTLG 432
Cdd:cd07772 367 MTDYALDLL----GSGVGRIIVEGGFAKNPVFLRLLAALRpDQPVYLSDDsEGTALG 419
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
73-433 |
9.44e-10 |
|
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: 60.62 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 73 RIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGiqflpfNTIYQ------LRALTEQ 146
Cdd:cd07804 69 EIAAIGVSGLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITG------NPLDSqsvgpkLLWIKRN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 147 QPELIPHIAHALLIPDYFSYRLTGKMNWEYTNA-TTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQG 225
Cdd:cd07804 143 EPEVFKKTRKFLGAYDYIVYKLTGEYVIDYSSAgNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGE-VTKEA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 226 NE-------IPVVAvASHDTASAVIASPL--NGSRAAYL-SSGTWSLMGFESQT---------PFTNDTALAANITNEGG 286
Cdd:cd07804 222 AEetglaegTPVVA-GTVDAAASALSAGVvePGDLLLMLgTAGDIGVVTDKLPTdprlwldyhDIPGTYVLNGGMATSGS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 287 aegryrVLKnimglWLLQRVLQERQINDLPALIAATQALpacrfiinpnddrfinpDEMCSEIQAAC-----------RE 355
Cdd:cd07804 301 ------LLR-----WFRDEFAGEEVEAEKSGGDSAYDLL-----------------DEEAEKIPPGSdglivlpyfmgER 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 356 TaqPIPESDA--------------ELARCIFDSLAllYAdVLHELAQLRGEDF--SQLHIVGGGCQNALLNQLCADACG- 418
Cdd:cd07804 353 T--PIWDPDArgvifgltlshtraHLYRALLEGVA--YG-LRHHLEVIREAGLpiKRLVAVGGGAKSPLWRQIVADVTGv 427
|
410
....*....|....*.
gi 535687901 419 -IRVIAGPVEAStLGN 433
Cdd:cd07804 428 pQEYVKDTVGAS-LGD 442
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
56-432 |
5.50e-09 |
|
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: 58.33 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 56 LESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQrvglPVA----YRDSRTNGLMAQAQQQLGKRDIYQRSGIQF 131
Cdd:cd07809 53 LQAAFAQLLKDAGAELRDVAAIGISGQMHGLVALDADGK----VLRpaklWCDTRTAPEAEELTEALGGKKCLLVGLNIP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 132 LPFnTIYQLRALTEQQPELIPHIAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAW---FG 208
Cdd:cd07809 129 ARF-TASKLLWLKENEPEHYARIAKILLPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDLrdlLP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 209 RPTHPGNVIGH--------WICPQGneIPvVAVASHDTASAVIASPLNGSRAAYLSSGTwS--LMGFeSQTPFTNDTA-- 276
Cdd:cd07809 208 EVLPAGEVAGRltpegaeeLGLPAG--IP-VAPGEGDNMTGALGTGVVNPGTVAVSLGT-SgtAYGV-SDKPVSDPHGrv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 277 -----------LAANITNEggaegRYRVLKNIMGLWLLqrvlqerQINDLPALiaATQALPACRFIINPNddrFINPDEM 345
Cdd:cd07809 283 atfcdstggmlPLINTTNC-----LTAWTELFRELLGV-------SYEELDEL--AAQAPPGAGGLLLLP---FLNGERT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 346 cseiqaACRETAQP----IPESD---AELARCIFDS--LALLYA-DVLHELaqlrGEDFSQLHIVGGGCQNALLNQLCAD 415
Cdd:cd07809 346 ------PNLPHGRAslvgLTLSNftrANLARAALEGatFGLRYGlDILREL----GVEIDEIRLIGGGSKSPVWRQILAD 415
|
410
....*....|....*...
gi 535687901 416 ACGIRV-IAGPVEASTLG 432
Cdd:cd07809 416 VFGVPVvVPETGEGGALG 433
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
86-219 |
1.52e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 56.94 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 86 FVLLDQQGQRVgLPVAYRDSRTNGLMAQAQQQLG--KRDIYQRSGiQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDY 163
Cdd:PRK10939 87 IVLYDRNGTEI-WACANVDARASREVSELKELHNnfEEEVYRCSG-QTLALGALPRLLWLAHHRPDIYRQAHTITMISDW 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 535687901 164 FSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGH 219
Cdd:PRK10939 165 IAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGH 220
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
88-438 |
3.43e-06 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 49.58 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 88 LLDQQGQRVGLPVAYRDSRTNGLMAQAQQQL-GKRDIyqrSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYFSY 166
Cdd:PRK15027 82 LLDAQQRVLRPAILWNDGRCAQECALLEARVpQSRVI---TGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 167 RLTGKMNWEYTNATTTQLVNINSDDWDESLLA------------WSGANKAWFGRPthpgNVIGHWICPQgneIPVVAVA 234
Cdd:PRK15027 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQachlsrdqmpalYEGSEITGALLP----EVAKAWGMAT---VPVVAGG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 235 SHDTASAVIASPLNGSRAAyLSSGTWSLMGFESQTPFTNDTALAANITNegGAEGRYRVLKNIMGL-----WLLQRVLQE 309
Cdd:PRK15027 232 GDNAAGAVGVGMVDANQAM-LSLGTSGVYFAVSEGFLSKPESAVHSFCH--ALPQRWHLMSVMLSAascldWAAKLTGLS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 310 rqinDLPALIAATQA----------LPACRFIINPNDdrfiNPdemcseiQAA---CRETAQPIPesdAELARCIFDSLA 376
Cdd:PRK15027 309 ----NVPALIAAAQQadesaepvwfLPYLSGERTPHN----NP-------QAKgvfFGLTHQHGP---NELARAVLEGVG 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535687901 377 LLYA---DVLHELaqlrGEDFSQLHIVGGGCQNALLNQLCADACGIRviagpVEASTLGNIGIQL 438
Cdd:PRK15027 371 YALAdgmDVVHAC----GIKPQSVTLIGGGARSEYWRQMLADISGQQ-----LDYRTGGDVGPAL 426
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
59-425 |
5.14e-06 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It 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: 466971 [Multi-domain] Cd Length: 452 Bit Score: 48.77 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 59 AIRLGLNKVCEEGIRIDSIGI----D-TWgvdfvLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLP 133
Cdd:cd24121 55 TIREVVAKLDVLPDRVAAIGVtgqgDgTW-----LVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 134 FNTIYQLRALTEQQPELIPHIAHALLIPDYFSYRLTGKMNWEYTNATTTQLvNINSDDWDESLLAWSGAnKAWFGR--PT 211
Cdd:cd24121 130 GSQAAQLAWLKENEPERLERARTALHCKDWLFYKLTGEIATDPSDASLTFL-DFRTRQYDDEVLDLLGL-EELRHLlpPI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 212 HPGNVIGHWICPQGNE-------IPVVAvASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNdtALAANITNE 284
Cdd:cd24121 208 RPGTEVIGPLTPEAAAatglpagTPVVL-GPFDVVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLE--PEGVGYTIC 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 285 GGAEGRY-RVLKNIMGL----WLLQRV-------LQERQINDLPALIAATQALP--ACRFI----INPNDDR--FINPDe 344
Cdd:cd24121 285 LGVPGRWlRAMANMAGTpnldWFLRELgevlkegAEPAGSDLFQDLEELAASSPpgAEGVLyhpyLSPAGERapFVNPN- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 345 mcseiqAACRETAQPIPESDAELARCIFDSLALLYADVLHELaqlrGEDFSQLHIVGGGCQNALLNQLCADACG--IRVI 422
Cdd:cd24121 364 ------ARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGvpVRVP 433
|
...
gi 535687901 423 AGP 425
Cdd:cd24121 434 AGE 436
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
372-431 |
2.62e-04 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 43.29 E-value: 2.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 372 FDSLALLYADVLHELA-QLR---------GEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGPVEASTL 431
Cdd:cd07782 412 LDDLALLYLATLQALAyGTRhiieamnaaGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVL 481
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
7-198 |
2.96e-04 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. 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: 466789 [Multi-domain] Cd Length: 486 Bit Score: 43.22 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 7 VAVDLGASSGRVML--------ARYEREcrsltLREIHRfNNGLHSQNGYVTWnvDRLESAIRLGLNKVCEEGIRIDSIG 78
Cdd:cd07769 3 LAIDQGTTSTRAILfdedgnivASAQKE-----HEQIYP-QPGWVEHDPEEIW--ENTLEVIREALAKAGISASDIAAIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 79 IDTWGVDFVLLDQQGqrvGLPVA----YRDSRTNGLMAQAQQQLGKRDIYQRSGiqfLPFNTiYQ----LRALTEQQPEL 150
Cdd:cd07769 75 ITNQRETTVVWDKKT---GKPLYnaivWQDRRTADICEELKAKGLEERIREKTG---LPLDP-YFsatkIKWILDNVPGA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 535687901 151 IPHIA--HAL-------LIpdyfsYRLTGKMNW--EYTNATTTQLVNINSDDWDESLLA 198
Cdd:cd07769 148 RERAErgELLfgtidtwLI-----WKLTGGKVHvtDVTNASRTMLFNIHTLEWDDELLE 201
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
365-432 |
1.54e-03 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. 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: 466789 [Multi-domain] Cd Length: 486 Bit Score: 40.91 E-value: 1.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535687901 365 AELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGPV-EASTLG 432
Cdd:cd07769 369 AHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVaETTALG 437
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
365-422 |
2.53e-03 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains 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. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 40.17 E-value: 2.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 535687901 365 AELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVI 422
Cdd:cd07786 369 AHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVE 426
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
365-470 |
3.55e-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: 39.85 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535687901 365 AELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGP-VEASTLG-------NIGI 436
Cdd:cd07793 384 AHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKnTEMSALGaaflaglASGI 463
|
90 100 110
....*....|....*....|....*....|....
gi 535687901 437 qlmtldeLNNVDDFRQVVSTTanlTTFTPNPDSE 470
Cdd:cd07793 464 -------WKSKEELKKLRKIE---KIFEPKMDNE 487
|
|
| |
