|
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: 1021.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 19 MLARYERECRSLTLREIHRFNNGLHSQNGYVTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQRVGL 98
Cdd:PRK10640 1 MLARYERECRSLTLREIHRFNNGLHSQDGFDTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDYVLLDKQGQRVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 99 PVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYFSYRLTGKMNWEYTN 178
Cdd:PRK10640 81 PVSYRDSRTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 179 ATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNGSRAAYLSSG 258
Cdd:PRK10640 161 ATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNDSDAAYLSSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 259 TWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQEQQINDLPALISATQALPACRFIINPNDDR 338
Cdd:PRK10640 241 TWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQITDLPALIAATAALPACRFLINPNDDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 339 FINPETMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACG 418
Cdd:PRK10640 321 FINPPSMCSEIQAACRETAQPVPESDAELARCIFDSLALLYADVLHELAQLRGEPFSQLHIVGGGCQNALLNQLCADACG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131744 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: 884.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVMLARYERECRSLTLREIHRFNNGLHSQNGYVTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDF 86
Cdd:TIGR02627 1 VAVDLGASSGRVMLASYENECQKLTLEEIHRFKNGLVSQNGHECWDIDALEQEIRLGLNKVDAEGIAPDSIGIDTWGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 87 VLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYFSY 166
Cdd:TIGR02627 81 VLLDQNGQRVGDPVSYRDSRTDGVMAQVQSELGKEAIYQRTGIQFLPFNTLYQLRALTEQQPDLLEKVAHFLLIPDYLNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 167 RLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASP 246
Cdd:TIGR02627 161 RLTGKKVWEYTNATTTQLVNINTDDWDEDLLAYLGVPAAWFGRPTHPGNVIGLWECPQGNQIPVVAVATHDTASAVVAAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 247 LNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQEQQINDLPALISATQALP 326
Cdd:TIGR02627 241 LQGENAAYLSSGTWSLMGFESQTPITNEQALAANITNEGGADGRYRVLKNIMGLWLLQRVCRERDINDLPALIEQAQALP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 327 ACRFIINPNDDRFINPETMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQN 406
Cdd:TIGR02627 321 AFKSIINPNDDRFINPENMCEEIQAYCRETNQPIPESDAELARCIFDSLALLYRQVLLELAELRGKPISQLHIVGGGSQN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16131744 407 TLLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTTANL 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 16131744 5 NCVAVDLGASSGRVMLARYEREcrSLTLREIHRFNNGLHSQNGYVTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGV 84
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGG--KLELEEIHRFPNRPVEINGHLYWDIDRLFDEIKEGLKKAAEQGGDIDSIGIDTWGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 85 DFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYF 164
Cdd:cd07771 79 DFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 165 SYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHW---ICPQG--NEIPVVAVASHDTA 239
Cdd:cd07771 159 NYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLkpeVAEELglKGIPVIAVASHDTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 240 SAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQEQQINDLP--- 316
Cdd:cd07771 239 SAVAAVPAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGFTNEGGADGTIRLLKNITGLWLLQECRREWEEEGKDysy 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 317 -ALISATQALPACRFIINPNDDRFINPETMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFS 395
Cdd:cd07771 319 dELVALAEEAPPFGAFIDPDDPRFLNPGDMPEAIRAYCRETGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRID 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131744 396 QLHIVGGGCQNTLLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTT 457
Cdd:cd07771 399 RIHIVGGGSRNALLCQLTADATGLPVIAGPVEATAIGNLLVQLIALGEIKSLEEGRELVRNS 460
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
7-432 |
1.22e-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: 186.64 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVMLarYERECRslTLREIHRFNNGLHSQNGYVTWDVDSLESAIRLGLNKVCEE--GIRIDSIGIDTWGV 84
Cdd:cd07773 3 LGIDIGTTNVKAVL--FDEDGR--ILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQagPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 85 DFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYF 164
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 165 SYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQG-------NEIPVVaVASHD 237
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGT-VTPEAaeelglpAGTPVV-VGGHD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 238 TASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVL-------------KNIMGLWLLQ 304
Cdd:cd07773 237 HLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSYGHHVPGGYYYLagslpggallewfRDLFGGDESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 305 RVLQEQQINDLPALISATQALPacrfiinpnddRFINPETMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLH 384
Cdd:cd07773 317 LAAADELAEAAPPGPTGLLFLP-----------HLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16131744 385 ELAQLrGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPV-EASTLG 432
Cdd:cd07773 386 ALEKA-GIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVpEATALG 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-433 |
2.21e-53 |
|
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: 184.31 E-value: 2.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 6 CVAVDLGASSGRVMLARyerecRSLTLREIHRFNNGLHS-QNGYVTWDVDSLESAIRLGLNKVCEEG----IRIDSIGID 80
Cdd:cd00366 2 LLGIDIGTTSVKAALFD-----EDGNLVASASREYPLIYpQPGWAEQDPEDWWQAVVEAIREVLAKAgidpSDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 81 TWGVDFVLLDQQGQRVGLPVAYRDSRtnglmaqaqqqlgkrdiyqrsgiqflpfntlyqlralteqqpeliphiaHALLM 160
Cdd:cd00366 77 GQMPGVVLVDADGNPLRPAIIWLDRR-------------------------------------------------AKFLQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 161 P-DYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHW------ICPQGNEIPVVAV 233
Cdd:cd00366 108 PnDYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVtpeaaeETGLPAGTPVVAG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 234 AsHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTalaaNITNEGGA-EGRYRVLKNI--MGL---WLLQRVL 307
Cdd:cd00366 188 G-GDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDP----RLLNRCHVvPGLWLLEGAIntGGAslrWFRDEFG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 308 QE----QQINDLPALISATQAlPACRFIINPNDDRFINPETMCSeiqAACRETAQPIPESDAELARCIFDSLALLYADVL 383
Cdd:cd00366 263 EEedsdAEYEGLDELAAEVPP-GSDGLIFLPYLSGERSPIWDPA---ARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNL 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16131744 384 hELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPV-EASTLGN 433
Cdd:cd00366 339 -EILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVaEGAALGA 388
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
7-468 |
1.35e-38 |
|
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: 146.90 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVMLARYERECRSLTLRE--IHRFNNGLHSQNGYVTWDvdSLESAIRLGLNKVCEEGIRIDSIGIDTWGV 84
Cdd:COG1070 4 LGIDIGTTSVKAVLFDADGEVVASASAEypLSSPHPGWAEQDPEDWWE--AVVEAIRELLAKAGVDPEEIAAIGVSGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 85 DFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYF 164
Cdd:COG1070 82 GLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 165 SYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGH--------WICPQGneIPVVAvASH 236
Cdd:COG1070 162 RYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTltaeaaaeTGLPAG--TPVVA-GAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 237 DTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITneGGAEGRYrvlkNIMGL---------WlLQRVL 307
Cdd:COG1070 239 DNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFC--HAVPGRW----LPMGAtnnggsalrW-FRDLF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 308 QEQQINDLPALIS-ATQALPAC------------RFIINPNDDR--FI--NPETmcseiqaacretaqpipeSDAELARC 370
Cdd:COG1070 312 ADGELDDYEELNAlAAEVPPGAdgllflpylsgeRTPHWDPNARgaFFglTLSH------------------TRAHLARA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 371 IFDSLALLYADVLHELAQLrGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAgpVEASTLGNIGIQLMTLDELNNVDDF 450
Cdd:COG1070 374 VLEGVAFALRDGLEALEEA-GVKIDRIRATGGGARSPLWRQILADVLGRPVEV--PEAEEGGALGAALLAAVGLGLYDDL 450
|
490
....*....|....*....
gi 16131744 451 RQVVSTTANLT-TFTPNPD 468
Cdd:COG1070 451 EEAAAAMVRVGeTIEPDPE 469
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
253-441 |
7.55e-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: 128.98 E-value: 7.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 253 AYLSSGTWSLMGFESQTPFTNDTALAANITNE-----GGAEGRYRVLKNIMGlWLLQRVLQEQQIND------LPALISA 321
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEmlpgyWGLEGGQSAAGSLLA-WLLQFHGLREELRDagnvesLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 322 TQALPACRFIINPNDDRFINPetmCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVG 401
Cdd:pfam02782 80 AAVAPAGGLLFYPDFSGNRAP---GADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131744 402 GGCQNTLLNQLCADACGIRV-IAGPVEASTLGNIGIQLMTL 441
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVvVPGPDEATALGAALLAAVAA 197
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
51-471 |
5.84e-33 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 130.53 E-value: 5.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 51 WDVDS----LESAIRLGLNKVCEEGIRidSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQR 126
Cdd:PRK10331 47 WSLDAilqrFADCCRQINSELTECHIR--GITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 127 SGIQFLPFNTLYQLRALTEQQPELIPHiAHA-LLMPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKA 205
Cdd:PRK10331 125 SGVGAFSFNTLYKLVWLKENHPQLLEQ-AHAwLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 206 WFGRPTHPGNVIGH--------WICPQGneIPVVAvASHDTASAVIasplnGSRAAY----LSSGTWSLMGFESQTPFTN 273
Cdd:PRK10331 204 LFPRLVEAGEQIGTlqpsaaalLGLPVG--IPVIS-AGHDTQFALF-----GSGAGQnqpvLSSGTWEILMVRSAQVDTS 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 274 DTALAANITNEGGAE-GRYR---------VLKnimglWLLQRVLQEQQIndLPALISATQALPA--------CRFIINPN 335
Cdd:PRK10331 276 LLSQYAGSTCELDSQsGLYNpgmqwlasgVLE-----WVRKLFWTAETP--YQTMIEEARAIPPgadgvkmqCDLLACQN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 336 ddrfinpetmcSEIQAACRETAQpipesdAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCAD 415
Cdd:PRK10331 349 -----------AGWQGVTLNTTR------GHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKAN 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131744 416 ACG--IRVIAGPvEASTLGNIGIQLMTLDELNNVDDFRQVVSTTanLTTFTPNPDSEI 471
Cdd:PRK10331 412 MLDipIKVLDDA-ETTVAGAAMFGWYGVGEFSSPEQARAQMKYQ--YRYFYPQTEPEF 466
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
7-432 |
5.70e-29 |
|
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: 118.48 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVMLARYERECrsltLREIHRFNNGLHSQNGYVTWDVDSLESAIRLGLNKVCEEGI--RIDSIGID-TWG 83
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTV----LASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRprRVVAIAVDgTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 84 VdFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGkrDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDY 163
Cdd:cd07783 79 T-LVLVDREGEPLRPAIMYNDARAVAEAEELAEAAG--AVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 164 FSYRLTGKMNW-EYTNATTTqLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQ-------GNEIPVVAVAS 235
Cdd:cd07783 156 LAGRLTGDRGVtDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGT-LTAEaaeelglPAGTPVVAGTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 236 hDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPftndtalaanitnEGGAEGRYRVLKNIMGLWL-----------LQ 304
Cdd:cd07783 234 -DSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKR-------------VPDPGGGVYSHRHGDGYWLvggasntggavLR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 305 RVLQEQQINDLPALISATQA-------LPAC--RFiinPnddrFINPetmcsEIQAACRetaqPIPESDAELARCIFDSL 375
Cdd:cd07783 300 WFFSDDELAELSAQADPPGPsgliyypLPLRgeRF---P----FWDP-----DARGFLL----PRPHDRAEFLRALLEGI 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131744 376 ALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPVEASTLG 432
Cdd:cd07783 364 AFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAALG 420
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
7-243 |
1.93e-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: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVMLarYERECRSLTlreIHRFNNGLHSQ-NGYVTWDVD----SLESAIRLGLNKVCEEGIRIDSIGIDT 81
Cdd:pfam00370 3 LGIDCGTTSTKAIL--FNEQGKIIA---VAQLENPQITPhPGWAEQDPDeiwqAVAQCIAKTLSQLGISLKQIKGIGISN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 82 WGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMP 161
Cdd:pfam00370 78 QGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 162 DYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGrPTHPGNVIGHWICPQG-------NEIPVVAVA 234
Cdd:pfam00370 158 DYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLP-PLVESSEIYGELNPELaamwgldEGVPVVGGG 236
|
....*....
gi 16131744 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 |
5.98e-26 |
|
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: 110.34 E-value: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVMLarYERECRSLtlrEIHRFNNGLHS-QNGYVTWDVDSLESAIRLGLNKVCE--EGIRIDSIGIDTWG 83
Cdd:cd07770 3 LGIDIGTTSTKAVL--FDEDGRVV---ASSSAEYPLIRpEPGWAEQDPEEILEAVLEALKEVLAklGGGEVDAIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 84 VDFVLLDQQGQRVGlPV-AYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPD 162
Cdd:cd07770 78 HSLLGVDEDGEPLT-PViTWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 163 YFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWIC------PQGNEIPVVAVASh 236
Cdd:cd07770 157 YLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPefaerlGLLAGTPVVLGAS- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 237 DTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDT------ALAAN------ITNEGGAegryrVLKnimglWLLQ 304
Cdd:cd07770 236 DGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPgrlwcyRLDENrwlvggAINNGGN-----VLD-----WLRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 305 RVLQEQQI-NDLPALISATQA-------LP---ACRFiinP--NDDR---F--INPETmcseiqaacretaqpipeSDAE 366
Cdd:cd07770 306 TLLLSGDDyEELDKLAEAVPPgshglifLPylaGERA---PgwNPDArgaFfgLTLNH------------------TRAD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 367 LARCIFDSLALLYADVLHELAQLRGEDfSQLHIVGGGCQNTLLNQLCADACGIRVIAGPV-EASTLGNIgiqLMTLDELN 445
Cdd:cd07770 365 ILRAVLEGVAFNLKSIYEALEELAGPV-KEIRASGGFLRSPLWLQILADVLGRPVLVPEEeEASALGAA---LLALEALG 440
|
490 500
....*....|....*....|....*....
gi 16131744 446 NVDDFrQVVSTTANLTTFTPNPdSEIAHY 474
Cdd:cd07770 441 LISSL-EADELVKIGKVVEPDP-ENHAIY 467
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
7-432 |
3.95e-23 |
|
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: 101.53 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVMLARYERECRSLTLREIHRFNNGLHSqNGYVtWDV----DSLESAIRLGLNKVCEEGIRIDSIGIDTW 82
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYP-DAKE-FDPeelwEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 83 GVDFVLLDQQGQRV-GLPvaYRDSRTNGLMAQAQQQLGKRdIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMP 161
Cdd:cd07798 81 REGIVFLDKDGRELyAGP--NIDARGVEEAAEIDDEFGEE-IYTTTGHWPTELFPAARLLWFKENRPEIFERIATVLSIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 162 DYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIG--------HWICPQGneIPVVaV 233
Cdd:cd07798 158 DWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGtvseeaarELGLPEG--TPVV-V 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 234 ASHDTASAVIASPLNGSRAAYLSSGTWS-LMGFESQtPFTNDTalaANI-TNEGGAEGRYRVLKN--IMGL---WLLQRV 306
Cdd:cd07798 235 GGADTQCALLGSGAIEPGDIGIVAGTTTpVQMVTDE-PIIDPE---RRLwTGCHLVPGKWVLESNagVTGLnyqWLKELL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 307 LQEQQIN--DLPALISatQALPACRFIINpnddrFINPETMCSEIQAACR------ETAQPIPESDAELARCIFDSLAll 378
Cdd:cd07798 311 YGDPEDSyeVLEEEAS--EIPPGANGVLA-----FLGPQIFDARLSGLKNggflfpTPLSASELTRGDFARAILENIA-- 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131744 379 YADV--LHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVI-AGPVEASTLG 432
Cdd:cd07798 382 FAIRanLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLvPEGREASALG 438
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
7-468 |
1.21e-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: 94.12 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVML----------ARYERECRSltlreihrFNNGLHSQNGYVTWDvdSLESAIRLGLNKVCEEGIRIDS 76
Cdd:cd07779 3 LGIDVGTTSTRAIIfdldgnivasGYREYPPYY--------PEPGWVEQDPDDWWD--ALCEALKEAVAKAGVDPEDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 77 IGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTnglmaqaqqqlgkrdiyqrsgiqflpfntlyqlralteqqpeliphiAH 156
Cdd:cd07779 73 IGLTSQRSTFVPVDEDGRPLRPAISWQDKRT-----------------------------------------------AK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 157 ALLMPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQ-------GNEIP 229
Cdd:cd07779 106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGT-LTKEaaeetglPEGTP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 230 VVAvASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNdtalaanitneggAEGRYRVLKNIM-GLWLLQrvlq 308
Cdd:cd07779 185 VVA-GGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVED-------------PERRIPCNPSAVpGKWVLE---- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 309 eqqindlpALISAT------------QALPACRFIINPNDDRFinpETMCSEIQAACRE---------TAQPIPESDA-- 365
Cdd:cd07779 247 --------GSINTGgsavrwfrdefgQDEVAEKELGVSPYELL---NEEAAKSPPGSDGllflpylagAGTPYWNPEArg 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 366 ------------ELARCIFDSLALLYADVLhELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPV-EASTLG 432
Cdd:cd07779 316 afigltlshtraHLARAILEGIAFELRDNL-EAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETsEATALG 394
|
490 500 510
....*....|....*....|....*....|....*..
gi 16131744 433 NIGIQLMTLDELNNVDD-FRQVVSTTAnltTFTPNPD 468
Cdd:cd07779 395 AAILAAVGAGIYPDFEEaVKAMVRVTD---TFEPDPE 428
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
7-468 |
2.26e-20 |
|
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: 93.74 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVMLARYERECRSLTLREIHRFnnglHSQNGYVT------WDvdSLESAIRLGLNKVCEEGIRIDSIGID 80
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTY----YPKPGWAEqdpedwWD--AVCRATRALLEKSGIDPSDIAAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 81 TWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFL-PFNTLYQLRALTEQQPELIPHiAHALL 159
Cdd:cd07805 77 GQMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPsGKDPLAKILWLKENEPEIYAK-THKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 160 MP-DYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQGNE-------IPVV 231
Cdd:cd07805 156 DAkDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGE-LTPEAAAelglpagTPVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 232 AvASHDTASAVIasplnGSRA-----AYLSSGTWSLMGFESQTPFTNDTALAANITneGGAEGRYrvlkNIMGL------ 300
Cdd:cd07805 235 G-GGGDAAAAAL-----GAGAveegdAHIYLGTSGWVAAHVPKPKTDPDHGIFTLA--SADPGRY----LLAAEqetagg 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 301 ---WLLQRVLQEQQINDLP-----ALISATQA-------LP---ACRFIINPNDDR--FIN--PETmcseiqaacretaq 358
Cdd:cd07805 303 aleWARDNLGGDEDLGADDyelldELAAEAPPgsngllfLPwlnGERSPVEDPNARgaFIGlsLEH-------------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 359 pipeSDAELARCIFDSLALLYADVLhELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACG--IRVIAGPVEASTLGNIGI 436
Cdd:cd07805 369 ----TRADLARAVLEGVAFNLRWLL-EALEKLTRKIDELRLVGGGARSDLWCQILADVLGrpVEVPENPQEAGALGAALL 443
|
490 500 510
....*....|....*....|....*....|..
gi 16131744 437 QLMTLDELNNVDDFRQVVSTTAnltTFTPNPD 468
Cdd:cd07805 444 AAVGLGLLKSFDEAKALVKVEK---VFEPDPE 472
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
7-432 |
8.18e-20 |
|
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: 91.84 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLgasSGRvMLARYERECRSLTLReihrfnNGLHSQNGYVTWDVDSleSAIRlglnKVCEEGI----RIDSIGIDTW 82
Cdd:cd07802 15 VLFDL---DGR-EIAVASRPTPVISPR------PGWAERDMDELWQATA--EAIR----ELLEKSGvdpsDIAGVGVTGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 83 GVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPD 162
Cdd:cd07802 79 GNGLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 163 YFSYRLTGKMNWEYTNATTTqLVNINSDDWDESLLAWSG--ANKAWFGRPTHPGNVIGHwI---------CPQGneIPVV 231
Cdd:cd07802 159 WIRYRLTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGieELKDKLPPLVPSTEIAGR-VtaeaaaltgLPEG--TPVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 232 AVAsHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTaLAANITNegGAEGRYRVLKNIMG----L-WLLQRV 306
Cdd:cd07802 235 AGA-FDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDS-VGSNSLH--ADPGLYLIVEASPTsasnLdWFLDTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 307 LQEQQ-------------INDLPALISATQALP------------ACRFIINPNDDRfinpetmcseiqaacretaqpip 361
Cdd:cd07802 311 LGEEKeaggsdydeldelIAAVPPGSSGVIFLPylygsganpnarGGFFGLTAWHTR----------------------- 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131744 362 esdAELARCIFDSLALLYADvlHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPV-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 |
1.61e-19 |
|
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: 90.74 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 5 NCVAVDLGASSgrVMLARYEREcrSLTLREIHRFNNGL---HSQNGYVTWDVDSLESAIRLGLNKVCEE-GIRIDSIGID 80
Cdd:cd07777 1 NVLGIDIGTTS--IKAALLDLE--SGRILESVSRPTPApisSDDPGRSEQDPEKILEAVRNLIDELPREyLSDVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 81 TW--GvdFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIyQRSGIQF---LPFNTLYQLRalteQQPELIPHIA 155
Cdd:cd07777 77 GQmhG--IVLWDEDGNPVSPLITWQDQRCSEEFLGGLSTYGEELL-PKSGMRLkpgYGLATLFWLL----RNGPLPSKAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 156 HALLMPDYFSYRLTGK----MNWeyTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVV 231
Cdd:cd07777 150 RAGTIGDYIVARLTGLpkpvMHP--TNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKGIPVY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 232 aVASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQT----------PFTNDT--ALAANITneGGaegryRVLKNIMG 299
Cdd:cd07777 228 -VALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKfelsgsveirPFFDGRylLVAASLP--GG-----RALAVLVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 300 lwLLQRVLQE-------QQINDLpaLISATQALPACRFIINPnddrFINPETMCSEIQAACREtaqpIPESD---AELAR 369
Cdd:cd07777 300 --FLREWLRElggslsdDEIWEK--LDELAESEESSDLSVDP----TFFGERHDPEGRGSITN----IGESNftlGNLFR 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131744 370 CIFDSLALLYADVLHELaQLRGEDFSQLHIVGGGCQ-NTLLNQLCADACGIRVIAGPVEASTL 431
Cdd:cd07777 368 ALCRGIAENLHEMLPRL-DLDLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAA 429
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
7-259 |
2.57e-16 |
|
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: 81.05 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVML-ARYERECRSLTLR-EIHRFNNGLHSQNGYVTWDvdSLESAIRLGLNKVCEEGIRIDSIGID--TW 82
Cdd:cd07808 3 LGIDLGTSSVKAVLvDEDGRVLASASAEyPTSSPKPGWAEQDPEDWWQ--ATKEALRELLAKAGISPSDIAAIGLTgqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 83 GVdfVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRdIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPD 162
Cdd:cd07808 81 GL--VLLDKNGRPLRPAILWNDQRSAAECEELEARLGDE-ILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 163 YFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQGNE-------IPVVAVAS 235
Cdd:cd07808 158 YLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGT-LTPEAAEelglpegTPVVAGAG 236
|
250 260
....*....|....*....|....
gi 16131744 236 hDTASAVIASPLNGSRAAYLSSGT 259
Cdd:cd07808 237 -DNAAAALGAGVVEPGDALISLGT 259
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
8-432 |
8.86e-12 |
|
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: 66.97 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 8 AVDLGASSGRVMLARYERECRSLTLRE-IHRFNNGLHsqnGYVTWDVDS----LESAIRLGLNKVCEEGIRIDSIGIDTW 82
Cdd:cd07775 4 ALDAGTGSGRAVIFDLEGNQIAVAQREwRHKEVPDVP---GSMDFDTEKnwklICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 83 GVDFVLLDQQGQRVgLPVAYRDSRtnglmaqAQQQLGK---------RDIYQRSGiQFLPFNTLYQLRALTEQQPELIPH 153
Cdd:cd07775 81 REGIVLYDNEGEEI-WACANVDAR-------AAEEVSElkelyntleEEVYRISG-QTFALGAIPRLLWLKNNRPEIYRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 154 IAHALLMPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQGNE------ 227
Cdd:cd07775 152 AAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGK-VTKEAAEetglke 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 228 -IPVVaVASHDTASAVIA-SPLNGSRAAYLSSGTWSLMgFESQTPFTNdtalaanitneggAEGRYRVLKNIM-GLWllq 304
Cdd:cd07775 231 gTPVV-VGGGDVQLGCLGlGVVRPGQTAVLGGSFWQQE-VNTAAPVTD-------------PAMNIRVNCHVIpDMW--- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 305 rvlQEQQINDLPAL--------ISATQALPACRFIINPNDdrFInpETMCSEIQAACREtAQPI---------------- 360
Cdd:cd07775 293 ---QAEGISFFPGLvmrwfrdaFCAEEKEIAERLGIDAYD--LL--EEMAKDVPPGSYG-IMPIfsdvmnyknwrhaaps 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 361 -------PE--SDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAgPV--EAS 429
Cdd:cd07775 365 flnldidPEkcNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKV-PVvkEAT 443
|
...
gi 16131744 430 TLG 432
Cdd:cd07775 444 ALG 446
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
6-432 |
2.24e-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: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 6 CVAV-DLGASSGRVMLARYEREC---RSLTLREIHRfnnglhsqNGYVTWDVDSLESAIRLGLNKVCEEGiRIDSIGIDT 81
Cdd:cd07772 1 VIAVfDIGKTNKKLLLFDENGEVlaeRSTPNPEIEE--------DGYPCEDVEAIWEWLLDSLAELAKRH-RIDAINFTT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 82 WGVDFVLLDQQGQRVGLPVAYrdsrTNGLMAQAQQQL-GKRDIYQRSGIQFLP--FNTLYQLRALTEQQPELIPHIAHAL 158
Cdd:cd07772 72 HGATFALLDENGELALPVYDY----EKPIPDEINEAYyAERGPFEETGSPPLPggLNLGKQLYWLKREKPELFARAKTIL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 159 LMPDYFSYRLTGKMNWEYTNATT-TQLVNINSDD---------WDESLLAWSGANKAwFGrPTHPGNVIGHWIcpqGNEI 228
Cdd:cd07772 148 PLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEysslvkkegWDKLFPPLRKAWEV-LG-PLRPDLARRTGL---PKDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 229 PVVAVAsHDTASAVIASPLNG-SRAAYLSSGTW--SLMGFESQTPFTNDTA--LAANITNEGgaegryRVLKN--IMGlw 301
Cdd:cd07772 223 PVGCGI-HDSNAALLPYLAAGkEPFTLLSTGTWciAMNPGNDLPLTELDLArdCLYNLDVFG------RPVKTarFMG-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 302 llQRVLqEQQINDLPALISATQALPACRFIInpNDDRFINPETMCSE----IQAACRETAQPIPESDAELARCIfdSLAL 377
Cdd:cd07772 294 --GREY-ERLVERIAKSFPQLPSLADLAKLL--ARGTFALPSFAPGGgpfpGSGGRGVLSAFPSAEEAYALAIL--YLAL 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131744 378 LYADVLHELaqlrGEDFSQLHIVGGGCQNTLLNQLCADAC-GIRVIAGPV-EASTLG 432
Cdd:cd07772 367 MTDYALDLL----GSGVGRIIVEGGFAKNPVFLRLLAALRpDQPVYLSDDsEGTALG 419
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
50-432 |
2.72e-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: 59.10 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 50 TWdVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQrvglPVA----YRDSRTNGLMAQAQQQLGKRDIYQ 125
Cdd:cd07809 48 DW-WDALQAAFAQLLKDAGAELRDVAAIGISGQMHGLVALDADGK----VLRpaklWCDTRTAPEAEELTEALGGKKCLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 126 RSGIQFLPFnTLYQLRALTEQQPELIPHIAHALLMPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKA 205
Cdd:cd07809 123 VGLNIPARF-TASKLLWLKENEPEHYARIAKILLPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 206 W---FGRPTHPGNVIGH--------WICPQGneIPvVAVASHDTASAVIASPLNGSRAAYLSSGTwS--LMGFeSQTPFT 272
Cdd:cd07809 202 LrdlLPEVLPAGEVAGRltpegaeeLGLPAG--IP-VAPGEGDNMTGALGTGVVNPGTVAVSLGT-SgtAYGV-SDKPVS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 273 NDTALaanITNEGGAEGRYRVLKNIMGL---WL-LQRVLQEQQINDLPALisATQALPACRFIINPNddrFINPETMcse 348
Cdd:cd07809 277 DPHGR---VATFCDSTGGMLPLINTTNCltaWTeLFRELLGVSYEELDEL--AAQAPPGAGGLLLLP---FLNGERT--- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 349 iqaACRETAQP----IPESD---AELARCIFDS--LALLYA-DVLHELaqlrGEDFSQLHIVGGGCQNTLLNQLCADACG 418
Cdd:cd07809 346 ---PNLPHGRAslvgLTLSNftrANLARAALEGatFGLRYGlDILREL----GVEIDEIRLIGGGSKSPVWRQILADVFG 418
|
410
....*....|....*
gi 16131744 419 IRV-IAGPVEASTLG 432
Cdd:cd07809 419 VPVvVPETGEGGALG 433
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
73-245 |
1.16e-08 |
|
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: 57.15 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 73 RIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGiqflpfNTLYQ------LRALTEQ 146
Cdd:cd07804 69 EIAAIGVSGLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITG------NPLDSqsvgpkLLWIKRN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 147 QPELIPHIAHALLMPDYFSYRLTGKMNWEYTNA-TTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHwICPQG 225
Cdd:cd07804 143 EPEVFKKTRKFLGAYDYIVYKLTGEYVIDYSSAgNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGE-VTKEA 221
|
170 180
....*....|....*....|....*..
gi 16131744 226 NE-------IPVVAvASHDTASAVIAS 245
Cdd:cd07804 222 AEetglaegTPVVA-GTVDAAASALSA 247
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
86-219 |
2.35e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 56.17 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 86 FVLLDQQGQRVgLPVAYRDSRTNGLMAQAQQQLG--KRDIYQRSGiQFLPFNTLYQLRALTEQQPElIPHIAHALLM-PD 162
Cdd:PRK10939 87 IVLYDRNGTEI-WACANVDARASREVSELKELHNnfEEEVYRCSG-QTLALGALPRLLWLAHHRPD-IYRQAHTITMiSD 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131744 163 YFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGH 219
Cdd:PRK10939 164 WIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGH 220
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
29-425 |
2.79e-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: 49.55 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 29 SLTLREIH---RFNNGLHSQNGYVTWDVDSLESA----IRLGLNKVCEEGIRIDSIGI----D-TWgvdfvLLDQQGQRV 96
Cdd:cd24121 18 DLDGRELAvaaRRNAVLYPQPGWAEQDMNETWQAvvatIREVVAKLDVLPDRVAAIGVtgqgDgTW-----LVDEDGRPV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 97 GLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYFSYRLTGKMNWEY 176
Cdd:cd24121 93 RDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWLFYKLTGEIATDP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 177 TNATTTQLvNINSDDWDESLLAWSGAnKAWFGR--PTHPGNVIGHWICPQGNE-------IPVVAvASHDTASAVIASPL 247
Cdd:cd24121 173 SDASLTFL-DFRTRQYDDEVLDLLGL-EELRHLlpPIRPGTEVIGPLTPEAAAatglpagTPVVL-GPFDVVATALGSGA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 248 NGSRAAYLSSGTWSLMGFESQTPFTNdtALAANITNEGGAEGRY-RVLKNIMGL----WLLQRV-------LQEQQINDL 315
Cdd:cd24121 250 IEPGDACSILGTTGVHEVVVDEPDLE--PEGVGYTICLGVPGRWlRAMANMAGTpnldWFLRELgevlkegAEPAGSDLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 316 PALISATQALP--ACRFI----INPNDDR--FINPETMCSEIQAACRETaqpipesDAELARCIFDSLALLYADVLHELa 387
Cdd:cd24121 328 QDLEELAASSPpgAEGVLyhpyLSPAGERapFVNPNARAQFTGLSLEHT-------RADLLRAVYEGVALAMRDCYEHM- 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16131744 388 qlrGEDFSQLHIVGGGCQNTLLNQLCADACG--IRVIAGP 425
Cdd:cd24121 400 ---GEDPGELRLSGGGARSDTWCQILADALGvpVRVPAGE 436
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
88-438 |
6.71e-06 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 48.42 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 88 LLDQQGQRVGLPVAYRDSRTNGLMAQAQQQL-GKRDIyqrSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYFSY 166
Cdd:PRK15027 82 LLDAQQRVLRPAILWNDGRCAQECALLEARVpQSRVI---TGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 167 RLTGKMNWEYTNATTTQLVNINSDDWDESLLA------------WSGANKAWFGRPthpgNVIGHWICPQgneIPVVAVA 234
Cdd:PRK15027 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQachlsrdqmpalYEGSEITGALLP----EVAKAWGMAT---VPVVAGG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 235 SHDTASAVIASPLNGSRAAyLSSGTwSLMGFESQTPFTNDTALAAnitneggaegrYRVLKNIMGLWLLQRVLQEQQ--- 311
Cdd:PRK15027 232 GDNAAGAVGVGMVDANQAM-LSLGT-SGVYFAVSEGFLSKPESAV-----------HSFCHALPQRWHLMSVMLSAAscl 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 312 --------INDLPALISATQA----------LPACRFIINPNDdrfiNPETMCSEIQAacreTAQPIPesdAELARCIFD 373
Cdd:PRK15027 299 dwaakltgLSNVPALIAAAQQadesaepvwfLPYLSGERTPHN----NPQAKGVFFGL----THQHGP---NELARAVLE 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131744 374 SLALLYA---DVLHELaqlrGEDFSQLHIVGGGCQNTLLNQLCADACGIRviagpVEASTLGNIGIQL 438
Cdd:PRK15027 368 GVGYALAdgmDVVHAC----GIKPQSVTLIGGGARSEYWRQMLADISGQQ-----LDYRTGGDVGPAL 426
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|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
7-198 |
4.57e-05 |
|
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: 45.92 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 7 VAVDLGASSGRVML--------ARYEREcrsltLREIHRfnnglhsQNGYVTWD----VDSLESAIRLGLNKVCEEGIRI 74
Cdd:cd07769 3 LAIDQGTTSTRAILfdedgnivASAQKE-----HEQIYP-------QPGWVEHDpeeiWENTLEVIREALAKAGISASDI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 75 DSIGIDTWGVDFVLLDQQGqrvGLPVA----YRDSRTNGLMAQAQQQLGKRDIYQRSGiqfLPFNTLY---QLRALTEQQ 147
Cdd:cd07769 71 AAIGITNQRETTVVWDKKT---GKPLYnaivWQDRRTADICEELKAKGLEERIREKTG---LPLDPYFsatKIKWILDNV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131744 148 PELIPHIA--HALL--MPDYFSYRLTGKMNW--EYTNATTTQLVNINSDDWDESLLA 198
Cdd:cd07769 145 PGARERAErgELLFgtIDTWLIWKLTGGKVHvtDVTNASRTMLFNIHTLEWDDELLE 201
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
372-431 |
3.15e-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: 3.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 372 FDSLALLYADVLHELA-QLR---------GEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPVEASTL 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), ... |
365-432 |
8.33e-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: 41.68 E-value: 8.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131744 365 AELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPV-EASTLG 432
Cdd:cd07769 369 AHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVaETTALG 437
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
365-470 |
2.71e-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: 40.24 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131744 365 AELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGP-VEASTLG-------NIGI 436
Cdd:cd07793 384 AHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKnTEMSALGaaflaglASGI 463
|
90 100 110
....*....|....*....|....*....|....
gi 16131744 437 qlmtldeLNNVDDFRQVVSTTanlTTFTPNPDSE 470
Cdd:cd07793 464 -------WKSKEELKKLRKIE---KIFEPKMDNE 487
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
365-422 |
2.86e-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: 2.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131744 365 AELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVI 422
Cdd:cd07786 369 AHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVE 426
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