|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
12-465 |
5.41e-155 |
|
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: 449.69 E-value: 5.41e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAH-LQVLAKGEARYDFVPNLPeGCYEQRVEDWDHALSIAMQQALNELqkkigDKMLWKPLAIG 90
Cdd:cd07809 2 VLGIDLGTQSIKAVLIDAEtGRVVASGSAPHENILIDP-GWAEQDPEDWWDALQAAFAQLLKDA-----GAELRDVAAIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 91 ISGQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQFKVK--------VPKRVTCARFLWTCRERPELAAQVAHITT 162
Cdd:cd07809 76 ISGQMHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKkcllvglnIPARFTASKLLWLKENEPEHYARIAKILL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 163 PAGWCAFRLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYDAalrepgvSRRMVDLLPTPVRAGEDGGYLTAAGAALLN 242
Cdd:cd07809 156 PHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDP-------SRDLRDLLPEVLPAGEVAGRLTPEGAEELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 243 LPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYCaadGAPVNMVWLRNGTTFL 322
Cdd:cd07809 229 LP---AGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFC---DSTGGMLPLINTTNCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 323 NTIVESYNAGKNEDafATIMPQLI-DAPADCGGLLALPFMHDEPGLHVEQGGsALIVGWNTENAKVGNVAKAALLSTMFN 401
Cdd:cd07809 303 TAWTELFRELLGVS--YEELDELAaQAPPGAGGLLLLPFLNGERTPNLPHGR-ASLVGLTLSNFTRANLARAALEGATFG 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1210525310 402 LKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASaDEGCSWGAAVLAKYRH 465
Cdd:cd07809 380 LRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPET-GEGGALGAALQAAWGA 442
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
12-516 |
3.89e-94 |
|
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: 295.20 E-value: 3.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDfVPNLPEGCYEQRVEDWDHALsiamQQALNELQKKIGDKmLWKPLAIGI 91
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYP-LSSPHPGWAEQDPEDWWEAV----VEAIRELLAKAGVD-PEEIAAIGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 92 SGQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQFKVKVPKRVTC---------ARFLWTCRERPELAAQVAHITT 162
Cdd:COG1070 77 SGQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGnplhpgftaPKLLWLKENEPEIFARIAKVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 163 PAGWCAFRLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYdaalrepGVSRrmvDLLPTPVRAGEDGGYLTAAGAALLN 242
Cdd:COG1070 157 PKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEAL-------GIDR---ELLPELVPPGEVAGTLTAEAAAETG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 243 LPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYC-AADGAPVNMVWLRNGTTF 321
Cdd:COG1070 227 LP---AGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFChAVPGRWLPMGATNNGGSA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 322 LNTIVESYNAGKNEDaFATIMPQLIDAPADCGGLLALPFMHDEPGLHVEQGGSALIVGWNTENAKvGNVAKAALLSTMFN 401
Cdd:COG1070 304 LRWFRDLFADGELDD-YEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTR-AHLARAVLEGVAFA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 402 LKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLAsADEGCSWGAAVLAKYrhlcqsSATFSLNWAGFL 481
Cdd:COG1070 382 LRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPE-AEEGGALGAALLAAV------GLGLYDDLEEAA 454
|
490 500 510
....*....|....*....|....*....|....*
gi 1210525310 482 QSLIPPEEetlRFQPIADHVREYEAMFTRYQKLIQ 516
Cdd:COG1070 455 AAMVRVGE---TIEPDPENVAAYDELYERYRELYP 486
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
13-516 |
9.82e-60 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 204.86 E-value: 9.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 13 IGVDNGTQGLSVVLTDAHLQVLAKGEARYDFVPNLPeGCYEQRVEDWDHALSIAMQQALNELQKKIGDKmlwkpLAIGIS 92
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHP-GWSEQDPEDWWDATEEAIKELLEQASEMGQDI-----KGIGIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 93 GQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQ----QFKVKVPKRV-----TCARFLWTCRERPELAAQVAHITTP 163
Cdd:TIGR01312 75 GQMHGLVLLDANGEVLRPAILWNDTRTAQECEELEAelgdERVLEITGNLalpgfTAPKLLWVRKHEPEVFARIAKVMLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 164 AGWCAFRLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYDAALrepgvsrrmvDLLPTPVRAGEDGGYLTAAGAALLNL 243
Cdd:TIGR01312 155 KDYLRYRLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPE----------SQLPELIESSEKAGTVRPEVAARLGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 244 PkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYCAA-DGAPVNMVWLRNGTTFL 322
Cdd:TIGR01312 225 S---AGVPVAAGGGDNAAGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHAlPGGWLPMGVTLSATSSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 323 NTIVESYNAGknedAFATIMPQLIDAPADCGGLLALPFMHDEPGLHVEQGGSALIVGWNTENAKvGNVAKAALLSTMFNL 402
Cdd:TIGR01312 302 EWFRELFGKE----DVEALNELAEQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTR-ADLTRAVLEGVTFAL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 403 KMGCQIL-DAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLAsADEGCSWGAAVLAKYrhLCQSSATFSLnwagfL 481
Cdd:TIGR01312 377 RDSLDILrEAGGIPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPE-GEEGPALGAAILAAW--ALGEKDLAAL-----C 448
|
490 500 510
....*....|....*....|....*....|....*
gi 1210525310 482 QSLIPPEEETlrFQPIADHVREYEAMFTRYQKLIQ 516
Cdd:TIGR01312 449 SEAVVKQTES--VLPIAENVEAYEELYERYKKLYQ 481
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
12-514 |
5.07e-59 |
|
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: 202.77 E-value: 5.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDFvpNLP-EGCYEQRVEDWDHAlsiaMQQALNELQKKIGDKmLWKPLAIG 90
Cdd:cd07808 2 LLGIDLGTSSVKAVLVDEDGRVLASASAEYPT--SSPkPGWAEQDPEDWWQA----TKEALRELLAKAGIS-PSDIAAIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 91 ISGQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQFKVKVPKRV--------TCARFLWTCRERPELAAQVAHITT 162
Cdd:cd07808 75 LTGQMHGLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEILIITgnpplpgfTLPKLLWLKENEPEIFARIRKILL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 163 PAGWCAFRLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYdaalrepGVSRrmvDLLPTPVRAGEDGGYLTAAGAALLN 242
Cdd:cd07808 155 PKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEAL-------GLDP---SILPPIVESTEIVGTLTPEAAEELG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 243 LPKewaGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYCAADGApvnmVWLRNGTTF- 321
Cdd:cd07808 225 LPE---GTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPG----KWYAMGVTLs 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 322 ----LNTIVEsyNAGKNEDAFATIMPQLIDAPADCGGLLALPFMHDEPGLHveqggsalivgWN----------TENAKV 387
Cdd:cd07808 298 aglsLRWLRD--LFGPDRESFDELDAEAAKVPPGSEGLLFLPYLSGERTPY-----------WDpnargsffglSLSHTR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 388 GNVAKAALLSTMFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASADEGcSWGAAVLAkyrhlc 467
Cdd:cd07808 365 AHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGS-AYGAALLA------ 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1210525310 468 QSSATFSLNWAGFLQSLIPPEEetlRFQPIADHVREYEAMFTRYQKL 514
Cdd:cd07808 438 AVGAGVFDDLEEAAAACIKIEK---TIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
12-514 |
2.32e-55 |
|
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: 193.16 E-value: 2.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDFVPNLPeGCYEQRVED-WDhalsiAMQQALNELQKKIGDKmlwKPLAIG 90
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEP-GWAEQDPEEiLE-----AVLEALKEVLAKLGGG---EVDAIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 91 ISGQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQFKVK-VPKRVTC--------ARFLWTCRERPELAAQVAHIT 161
Cdd:cd07770 73 FSSAMHSLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSeLYRRTGCpihpmyplAKLLWLKEERPELFAKAAKFV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 162 TPAGWCAFRLTNEFKLGIGEAS--GMFpmdtthnhyrtDLLE-QYDA-ALREPGVSRRMvdlLPTPVRAGEDGGYLTAAG 237
Cdd:cd07770 153 SIKEYLLYRLTGELVTDYSTASgtGLL-----------NIHTlDWDEeALELLGIDEEQ---LPELVDPTEVLPGLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 238 AALLNLPkewAGIPVAPAEGDqiAALA--GSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYCAAD-----GAPV 310
Cdd:cd07770 219 AERLGLL---AGTPVVLGASD--GALAnlGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDEnrwlvGGAI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 311 N---MV--WLRNgtTFLNtivesynagkNEDAFATIMPQLIDAPADCGGLLALPFMHDE--PGLHVEQGGSalIVG--WN 381
Cdd:cd07770 294 NnggNVldWLRD--TLLL----------SGDDYEELDKLAEAVPPGSHGLIFLPYLAGEraPGWNPDARGA--FFGltLN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 382 TENAkvgNVAKAALLSTMFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVkLLASADEGCSWGAAVLA 461
Cdd:cd07770 360 HTRA---DILRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPV-LVPEEEEASALGAALLA 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1210525310 462 KYrhlcqssatfSLNWAGFLQSLIPPEEETlRFQPIADHVREYEAMFTRYQKL 514
Cdd:cd07770 436 LE----------ALGLISSLEADELVKIGK-VVEPDPENHAIYAELYERFKKL 477
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
12-461 |
1.88e-54 |
|
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: 188.16 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDF-VPNlpEGCYEQRVEDWDHALsiamQQALNELQKKIGDKMlWKPLAIG 90
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLiYPQ--PGWAEQDPEDWWQAV----VEAIREVLAKAGIDP-SDIAAIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 91 ISGQMHGECLIKNDGSILGPVRLWCDARnadtaeeltqqfkvkvpkrvtcarflwtcrerpelaaqvAHITTPAGWCAFR 170
Cdd:cd00366 75 ISGQMPGVVLVDADGNPLRPAIIWLDRR---------------------------------------AKFLQPNDYIVFR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 171 LTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYdaalrepGVSRrmvDLLPTPVRAGEDGGYLTAAGAALLNLPkewAGI 250
Cdd:cd00366 116 LTGEFAIDYSNASGTGLYDIKTGDWSEELLDAL-------GIPR---EKLPPIVESGEVVGRVTPEAAEETGLP---AGT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 251 PVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYCAADGapvnmVWLRNGTT---------F 321
Cdd:cd00366 183 PVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHVVPG-----LWLLEGAIntggaslrwF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 322 LNTIVESYNagknEDAFATIMPQLID-APADCGGLLALPFMHDE--PGLHVEQGGSALIVGWNTenaKVGNVAKAALLST 398
Cdd:cd00366 258 RDEFGEEED----SDAEYEGLDELAAeVPPGSDGLIFLPYLSGErsPIWDPAARGVFFGLTLSH---TRAHLIRAVLEGV 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1210525310 399 MFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASADEGCsWGAAVLA 461
Cdd:cd00366 331 AYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAA-LGAAILA 392
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
13-511 |
2.95e-49 |
|
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: 176.56 E-value: 2.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 13 IGVDNGTQGLSVVLTDAHLQVLAKGEARYDfVPNLPEGCYEQRVEDWDHAlsiaMQQALNELQKKIGDKmLWKPLAIGIS 92
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYP-TYYPKPGWAEQDPEDWWDA----VCRATRALLEKSGID-PSDIAAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 93 GQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQFKVKVPKRVTC----------ARFLWTCRERPELAAQVAHITT 162
Cdd:cd07805 77 GQMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGgnppsgkdplAKILWLKENEPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 163 PAGWCAFRLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYdaalrepGVSRrmvDLLPTPVRAGEDGGYLTAAGAALLN 242
Cdd:cd07805 157 AKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAA-------GIDP---DKLPELVPSTEVVGELTPEAAAELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 243 LPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTS--VCANVvgDRPFQGVSAAVDQYCAADGAPVNMV------- 313
Cdd:cd07805 227 LP---AGTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSgwVAAHV--PKPKTDPDHGIFTLASADPGRYLLAaeqetag 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 314 ----WLRNgtTFLntivesYNAGKNEDAFAtIMPQLI-DAPADCGGLLALPFMHDEPGLHVEQGGSALIVGWNTENAKvG 388
Cdd:cd07805 302 galeWARD--NLG------GDEDLGADDYE-LLDELAaEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTR-A 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 389 NVAKAALLSTMFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASADEGCSWGAAVLAKYRhlcq 468
Cdd:cd07805 372 DLARAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQEAGALGAALLAAVG---- 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1210525310 469 ssatfsLNWAGFLQ---SLIPPEEetlRFQPIADHVREYEAMFTRY 511
Cdd:cd07805 448 ------LGLLKSFDeakALVKVEK---VFEPDPENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
13-461 |
1.38e-44 |
|
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: 162.69 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 13 IGVDNGTQGLSVVLTDAHLQVLAKGEARYDfvPNLPE-GCYEQRVEDWDHALSIAMQQALNELQKKIGDkmlwkPLAIGI 91
Cdd:cd07779 3 LGIDVGTTSTRAIIFDLDGNIVASGYREYP--PYYPEpGWVEQDPDDWWDALCEALKEAVAKAGVDPED-----IAAIGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 92 SGQmhGECLI--KNDGSILGPVRLWCDARnadtaeeltqqfkvkvpkrvtcarflwtcrerpelaaqVAHITTPAGWCAF 169
Cdd:cd07779 76 TSQ--RSTFVpvDEDGRPLRPAISWQDKR--------------------------------------TAKFLTVQDYLLY 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 170 RLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYdaalrepGVSRrmvDLLPTPVRAGEDGGYLTAAGAALLNLPkewAG 249
Cdd:cd07779 116 RLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAF-------GIDR---DKLPELVPPGTVIGTLTKEAAEETGLP---EG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 250 IPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYCAA-DGAPVNMV----------WLRNg 318
Cdd:cd07779 183 TPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAvPGKWVLEGsintggsavrWFRD- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 319 tTFLNTIVESynAGKNEDAFATIMPQLIDAPADCGGLLALPFMHDEPGLHVEQGGSALIVGWNTENAKvGNVAKAALLST 398
Cdd:cd07779 262 -EFGQDEVAE--KELGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTR-AHLARAILEGI 337
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1210525310 399 MFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASAdEGCSWGAAVLA 461
Cdd:cd07779 338 AFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETS-EATALGAAILA 399
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-461 |
1.33e-40 |
|
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: 151.97 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDFVPNLPEGCyEQRVED-WDhalsiAMQQALNELQKKIGDKmlwKPLAIG 90
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWA-ELDPEElWE-----AVKEAIREAAAQAGPD---PIAAIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 91 ISGQmhGE--CLIKNDGSILGPVRLWCDARNADTAEELTQQFKVKVPKRVT---------CARFLWTCRERPELAAQVAH 159
Cdd:cd07773 73 VSSQ--GEsgVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITglppspmysLAKLLWLREHEPEIFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 160 ITTPAGWCAFRLTNEFKLGIGEAS--GMFpmDTTHNHYRTDLLEqydaalrEPGVSRrmvDLLPTPVRAGEDGGYLTAAG 237
Cdd:cd07773 151 WLSVADYIAYRLTGEPVTDYSLASrtMLF--DIRKRTWSEELLE-------AAGIDA---SLLPELVPSGTVIGTVTPEA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 238 AALLNLPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRP-----------FQGVSAAVDQYCAAD 306
Cdd:cd07773 219 AEELGLP---AGTPVVVGGHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPpldemlaegglSYGHHVPGGYYYLAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 307 GAPVNMV--WLRNgtTFlntivesynaGKNEDAFATIMPQLIDAPADCGGLLALPFMHDEPGLHVEQGGSALIVGWnTEN 384
Cdd:cd07773 296 SLPGGALleWFRD--LF----------GGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGL-TLG 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1210525310 385 AKVGNVAKAALLSTMFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASADEGCsWGAAVLA 461
Cdd:cd07773 363 TTRADLLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATA-LGAALLA 438
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-461 |
4.13e-36 |
|
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: 139.58 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDF-VPNLpeGCYEQRVEDWDHALSIAMQQALNELQ---KKIGdkmlwkpl 87
Cdd:cd07804 2 LLGIDIGTTGTKGVLVDEDGKVLASASIEHDLlTPKP--GWAEHDPEVWWGAVCEIIRELLAKAGispKEIA-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 88 AIGISGqMHGECL-IKNDGSILGPVRLWCDARNADTAEELTQQFKVKVPKRVTCARF---------LWTCRERPELAAQV 157
Cdd:cd07804 72 AIGVSG-LVPALVpVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLdsqsvgpklLWIKRNEPEVFKKT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 158 AHITTPAGWCAFRLTNEFKLGIGEASGMFPM-DTTHNHYRTDLLEqydaalrEPGVSRrmvDLLPTPVRAGEDGGYLTAA 236
Cdd:cd07804 151 RKFLGAYDYIVYKLTGEYVIDYSSAGNEGGLfDIRKRTWDEELLE-------ALGIDP---DLLPELVPSTEIVGEVTKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 237 GAALLNLPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYC-----------AA 305
Cdd:cd07804 221 AAEETGLA---EGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDYHDipgtyvlnggmAT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 306 DGAPVNmvWLRNgtTFLNTIVESYNAGKnEDAFATIMPQLIDAPADCGGLLALPFM-------HDepglhveQGGSALIV 378
Cdd:cd07804 298 SGSLLR--WFRD--EFAGEEVEAEKSGG-DSAYDLLDEEAEKIPPGSDGLIVLPYFmgertpiWD-------PDARGVIF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 379 GWNTENAKvGNVAKAALLSTMFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASaDEGCSWGAA 458
Cdd:cd07804 366 GLTLSHTR-AHLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKD-TVGASLGDA 443
|
...
gi 1210525310 459 VLA 461
Cdd:cd07804 444 FLA 446
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
12-514 |
5.85e-36 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 140.36 E-value: 5.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHL-QVLAKGEARY-DFVPNLPEGCYEQRVEDWDHALSIAMQQALNELqKKIGDKMLwkplAI 89
Cdd:cd07781 2 VIGIDFGTQSVRAGLVDLADgEELASAVVPYpTGYIPPRPGWAEQNPADYWEALEEAVRGALAEA-GVDPEDVV----GI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 90 GI---SGQMhgeCLIKNDGSILGPVRLWCDARNADTAEELTQ-------QFKVKVPKRVTC----ARFLWTCRERPELAA 155
Cdd:cd07781 77 GVdttSSTV---VPVDEDGNPLAPAILWMDHRAQEEAAEINEtahpaleYYLAYYGGVYSSewmwPKALWLKRNAPEVYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 156 QVAHITTPAGWCAFRLTNEFKLGIGEAsgmfpmdtTHN-HYRT-------DLLEQYDaaLREPGVSRRmvdlLPTPV-RA 226
Cdd:cd07781 154 AAYTIVEACDWINARLTGRWVRSRCAA--------GHKwMYNEwgggpprEFLAALD--PGLLKLREK----LPGEVvPV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 227 GEDGGYLTAAGAALLNLPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQ--GVSAAVDqyca 304
Cdd:cd07781 220 GEPAGTLTAEAAERLGLP---AGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDipGICGPVP---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 305 aDGAPVNMVWLRNGTT--------FLNTIVESYNAGKnedafATIMPQLIDA----PADCGGLLALPFMHDEPGLHVEQG 372
Cdd:cd07781 293 -DAVVPGLYGLEAGQSavgdifawFVRLFVPPAEERG-----DSIYALLSEEaaklPPGESGLVALDWFNGNRTPLVDPR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 373 GSALIVGWnTENAKVGNVAKAALLSTMFNLKMgcqILD---AQGYPRSELVLTGGLS-RTPECGQILADVFNTPVKLLAS 448
Cdd:cd07781 367 LRGAIVGL-TLGTTPAHIYRALLEATAFGTRA---IIErfeEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKS 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1210525310 449 aDEGCSWGAAVLA-----KYRHLcQSSAtfslnwagflQSLIPPEEEtlrFQPIADHVREYEAMFTRYQKL 514
Cdd:cd07781 443 -DQAPALGAAILAavaagVYADI-EEAA----------DAMVRVDRV---YEPDPENHAVYEELYALYKEL 498
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-461 |
1.01e-35 |
|
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: 138.45 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDfVPNLPEGCYEQRVED-WDHALsiamqQALNELQKKIGDKMlWKPLAIG 90
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTP-VISPRPGWAERDMDElWQATA-----EAIRELLEKSGVDP-SDIAGVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 91 ISGQMHGECLIKNDGsilGPVR---LWCDARNADTAEELTQQfkvKVPKRV--TCARFLWTC----------RERPELAA 155
Cdd:cd07802 75 VTGHGNGLYLVDKDG---KPVRnaiLSNDSRAADIVDRWEED---GTLEKVypLTGQPLWPGqpvallrwlkENEPERYD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 156 QVAHITTPAGWCAFRLTNEFKLGIGEASGMFpMDTTHNHYRTDLLEQYDaaLREpgvsrrMVDLLPTPVRAGEDGGYLTA 235
Cdd:cd07802 149 RIRTVLFCKDWIRYRLTGEISTDYTDAGSSL-LDLDTGEYDDELLDLLG--IEE------LKDKLPPLVPSTEIAGRVTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 236 AGAALLNLPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAV-------DQYCAADGA 308
Cdd:cd07802 220 EAAALTGLP---EGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSnslhadpGLYLIVEAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 309 P---VNMVWLRNgtTFLNTIVESynagkNEDAFATIMPQLIDAPADCGGLLALPFMHdEPGLHVEQGGSAL-IVGWNTEn 384
Cdd:cd07802 297 PtsaSNLDWFLD--TLLGEEKEA-----GGSDYDELDELIAAVPPGSSGVIFLPYLY-GSGANPNARGGFFgLTAWHTR- 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1210525310 385 akvGNVAKAALLSTMFNLKMGCQILDAQGYPRsELVLTGGLSRTPECGQILADVFNTPVKLLASADEGCsWGAAVLA 461
Cdd:cd07802 368 ---AHLLRAVYEGIAFSHRDHLERLLVARKPE-TIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGA-LGAAICA 439
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
12-461 |
2.30e-32 |
|
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: 128.88 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDfVPNLPEGCYEQRVEDWDHALSIAMQQALNEL-QKKIGdkmlwkplAIG 90
Cdd:cd07783 2 FLGIDLGTSGVRAVVVDEDGTVLASASEPYP-TSRPGPGWVEQDPEDWWEALRSLLRELPAELrPRRVV--------AIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 91 ISGQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQFKVKVPKRVTC-------ARFLWTCRERPELAAQVAHITTP 163
Cdd:cd07783 73 VDGTSGTLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAvspssslAKLLWLKRHEPEVLAKTAKFLHQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 164 AGWCAFRLT---------NEFKLGIgeasgmfpmDTTHNHYRTDLLEQydaalrePGVSrrmVDLLPTPVRAGEDGGYLT 234
Cdd:cd07783 153 ADWLAGRLTgdrgvtdynNALKLGY---------DPETGRWPSWLLAL-------LGIP---PDLLPRVVAPGTVIGTLT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 235 AAGAALLNLPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYCAADGApvnmvW 314
Cdd:cd07783 214 AEAAEELGLP---AGTPVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGDGY-----W 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 315 LRNGTTflNT---IVESYNAGKNEDAfatiMPQLIDaPADCGGLLALPfmhdepglHVEQG------GSALIVGWNTENA 385
Cdd:cd07783 286 LVGGAS--NTggaVLRWFFSDDELAE----LSAQAD-PPGPSGLIYYP--------LPLRGerfpfwDPDARGFLLPRPH 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1210525310 386 KVGNVAKAALLSTMFNLKMGCQILDAQGYPR-SELVLTGGLSRTPECGQILADVFNTPVKLLASaDEGCsWGAAVLA 461
Cdd:cd07783 351 DRAEFLRALLEGIAFIERLGYERLEELGAPPvEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAA-LGAALLA 425
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
12-461 |
6.70e-30 |
|
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: 121.95 E-value: 6.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAH-LQVLAKGEARY-DFVPNLPEGCYEQRVEDWDHALSIAMQQALNELQKKIGdkmlwkplAI 89
Cdd:cd07777 2 VLGIDIGTTSIKAALLDLEsGRILESVSRPTpAPISSDDPGRSEQDPEKILEAVRNLIDELPREYLSDVT--------GI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 90 GISGQMHGECLIKNDGSILGPVRLWCDARnADTAEELTQQFKVKVPKRVT---------CARFLWTCRERPELAaQVAHI 160
Cdd:cd07777 74 GITGQMHGIVLWDEDGNPVSPLITWQDQR-CSEEFLGGLSTYGEELLPKSgmrlkpgygLATLFWLLRNGPLPS-KADRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 161 TTPAGWCAFRLTNEFKLGI----GEASGMFpmDTTHNHYRTDLLEqydaALREPgvsrrmVDLLPTPVRAGEDGGYLTAA 236
Cdd:cd07777 152 GTIGDYIVARLTGLPKPVMhptnAASWGLF--DLETGTWNKDLLE----ALGLP------VILLPEIVPSGEIVGTLSSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 237 GAAllnlpkewaGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTS--VCANVVGD--------RPFQGvsaavDQYCAAd 306
Cdd:cd07777 220 LPK---------GIPVYVALGDNQASVLGSGLNEENDAVLNIGTGaqLSFLTPKFelsgsveiRPFFD-----GRYLLV- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 307 GAPVN----MVWLrngTTFLNTIVESYNAGKNEDafaTIMPQLIDAPADCG--GLLALPFMHDEPGlHVEQGGSalIVGW 380
Cdd:cd07777 285 AASLPggraLAVL---VDFLREWLRELGGSLSDD---EIWEKLDELAESEEssDLSVDPTFFGERH-DPEGRGS--ITNI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 381 NTENAKVGNVAKAALLSTMFNLKMGCQILDAQGYPRSELVLTGG-LSRTPECGQILADVFNTPVKLLASADEGcSWGAAV 459
Cdd:cd07777 356 GESNFTLGNLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEA-AVGAAL 434
|
..
gi 1210525310 460 LA 461
Cdd:cd07777 435 LA 436
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
12-519 |
2.03e-27 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 115.06 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDFVPNLPEGCyEQRVEDWDHALSIAMQqALNELQKKIGDKmlwkplAIGI 91
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWS-EQDPEQWWQATDRAMK-ALGDQHSLQDVK------ALGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 92 SGQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQfkvkVPKR-----------VTCARFLWTCRERPELAAQVAHI 160
Cdd:PRK15027 74 AGQMHGATLLDAQQRVLRPAILWNDGRCAQECALLEAR----VPQSrvitgnlmmpgFTAPKLLWVQRHEPEIFRQIDKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 161 TTPAGWCAFRLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYDaalrepgVSRrmvDLLPTPVRAGEDGGYLTAAGAAL 240
Cdd:PRK15027 150 LLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACH-------LSR---DQMPALYEGSEITGALLPEVAKA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 241 LNLPKewagIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSVCANVVGDRPFQGVSAAVDQYCAAdgAPvnmvwlrnGTT 320
Cdd:PRK15027 220 WGMAT----VPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHA--LP--------QRW 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 321 FLNTIVESYNAGKNEDAFATIM---PQLIDAP--AD--CGGLLALPFMHDEPGLHVEQGGSALIVGWnTENAKVGNVAKA 393
Cdd:PRK15027 286 HLMSVMLSAASCLDWAAKLTGLsnvPALIAAAqqADesAEPVWFLPYLSGERTPHNNPQAKGVFFGL-THQHGPNELARA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 394 ALLSTMFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASADEGCSWGAAVLAKYRHLCQSSATF 473
Cdd:PRK15027 365 VLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIE 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1210525310 474 SLNWAGFLQSLIPPEEETLRFQPIADHVREYeamftrYQKLIQLQS 519
Cdd:PRK15027 445 LLPQLPLEQSHLPDAQRYAAYQPRRETFRRL------YQQLLPLMA 484
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
13-461 |
5.40e-26 |
|
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: 110.41 E-value: 5.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 13 IGVDNGTQGLSVVLTDAHLQVLAKgEARYDFVPNLPEGCYEQRVEdwdhALSIAMQQALNELQKKIGDKMLwKPLAIGIS 92
Cdd:cd24121 3 IGIDAGTSVVKAVAFDLDGRELAV-AARRNAVLYPQPGWAEQDMN----ETWQAVVATIREVVAKLDVLPD-RVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 93 GQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQFKVKVPKRVT-CARF--------LWTCRERPELAAQVAHITTP 163
Cdd:cd24121 77 GQGDGTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITgTGLFpgsqaaqlAWLKENEPERLERARTALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 164 AGWCAFRLTNEFKLGIGEASgmFPM-DTTHNHYRTDLLEQYD-AALREpgvsrrmvdLLPtPVRAGED-GGYLTAAGAAL 240
Cdd:cd24121 157 KDWLFYKLTGEIATDPSDAS--LTFlDFRTRQYDDEVLDLLGlEELRH---------LLP-PIRPGTEvIGPLTPEAAAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 241 LNLPkewAGIPVAPAEGDQIAALAGSLIGSAGTiSCS-FGTSVCANVVGDRPFQgvsaavdqycaaDGAPVNMV------ 313
Cdd:cd24121 225 TGLP---AGTPVVLGPFDVVATALGSGAIEPGD-ACSiLGTTGVHEVVVDEPDL------------EPEGVGYTiclgvp 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 314 --WLR-----NGTT----FLNTIVESYNAGKN---EDAFATIMPQLIDAPADCGGLLALPFMHD--EPGLHVEQGGSALI 377
Cdd:cd24121 289 grWLRamanmAGTPnldwFLRELGEVLKEGAEpagSDLFQDLEELAASSPPGAEGVLYHPYLSPagERAPFVNPNARAQF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 378 VGWNTENAKvGNVAKAALLStmfnlkMGCQILD---AQGYPRSELVLTGGLSRTPECGQILADVFNTPVKlLASADEGCS 454
Cdd:cd24121 369 TGLSLEHTR-ADLLRAVYEG------VALAMRDcyeHMGEDPGELRLSGGGARSDTWCQILADALGVPVR-VPAGEEFGA 440
|
....*..
gi 1210525310 455 WGAAVLA 461
Cdd:cd24121 441 RGAAMNA 447
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-265 |
2.76e-25 |
|
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: 104.34 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKGEARYDFVPNLPeGCYEQRVEDWDHALSIAMQQALNELQKKIGDkmlwkPLAIGI 91
Cdd:pfam00370 2 YLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHP-GWAEQDPDEIWQAVAQCIAKTLSQLGISLKQ-----IKGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 92 SGQMHGECLIKNDGSILGPVRLWCDARNADTAEELTQQF---KVKVPKRVTCARF------LWTCRERPELAAQVAHITT 162
Cdd:pfam00370 76 SNQGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGnnqKLYEITGLPIWPGftlsklRWIKENEPEVFEKIHKFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 163 PAGWCAFRLTNEFKLGIGEASGMFPMDTThnhyrtdLLEQYDAALREPGVSRRMvdlLPTPVRAGEDGGYLTAAGAALLN 242
Cdd:pfam00370 156 IHDYLRWRLTGVFVTDHTNASRSMMFNIH-------KLDWDPELLAALGIPRDH---LPPLVESSEIYGELNPELAAMWG 225
|
250 260
....*....|....*....|...
gi 1210525310 243 LPkewAGIPVAPAEGDQIAALAG 265
Cdd:pfam00370 226 LD---EGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
12-461 |
1.40e-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: 103.46 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAKG--EARYdFVPNLPEGCYEQRVEDWDHALSIAMQQALNELqkKIGDKmlwKPLAI 89
Cdd:cd07798 2 YLVIDIGTGGGRCALVDSEGKIVAIAyrEWEY-YTDDDYPDAKEFDPEELWEKICEAIREALKKA--GISPE---DISAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 90 GISGQMHGECLIKNDGSIL--GPVRlwcDARNADTAEELTQQFKVKVPKRVTC--------ARFLWTCRERPELAAQVAH 159
Cdd:cd07798 76 SSTSQREGIVFLDKDGRELyaGPNI---DARGVEEAAEIDDEFGEEIYTTTGHwptelfpaARLLWFKENRPEIFERIAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 160 ITTPAGWCAFRLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYDAAlrepgvsrrmVDLLPTPVRAGEDGGYLTAAGAA 239
Cdd:cd07798 153 VLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLP----------PEILPEIVPSGTVLGTVSEEAAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 240 LLNLPkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTS-----VCANVVGD---RPFQGVSAAVDQY-----CAAD 306
Cdd:cd07798 223 ELGLP---EGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTtpvqmVTDEPIIDperRLWTGCHLVPGKWvlesnAGVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 307 GApvNMVWLRNgtTFLNTIVESY---------NAGKNEDAFATIMPQLIDAPAdcGGLLALPFMHDEPglhveqggsali 377
Cdd:cd07798 300 GL--NYQWLKE--LLYGDPEDSYevleeeaseIPPGANGVLAFLGPQIFDARL--SGLKNGGFLFPTP------------ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 378 vgWNTENAKVGNVAKAALLSTMFNLKMGCQILDAQ-GYPRSELVLTGGLSRTPECGQILADVFNTPVkLLASADEGCSWG 456
Cdd:cd07798 362 --LSASELTRGDFARAILENIAFAIRANLEQLEEVsGREIPYIILCGGGSRSALLCQILADVLGKPV-LVPEGREASALG 438
|
....*
gi 1210525310 457 AAVLA 461
Cdd:cd07798 439 AAICA 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
275-461 |
2.35e-16 |
|
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: 77.36 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 275 SCSFGTSVCANVVGDRPF---QGVSAAVDQYCAADGAPV---------NMVWLRNgttFLNTIVESYNAGKNEDAFATIm 342
Cdd:pfam02782 2 AISAGTSSFVLVETPEPVlsvHGVWGPYTNEMLPGYWGLeggqsaagsLLAWLLQ---FHGLREELRDAGNVESLAELA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 343 pqLIDAPADCGGLLALPFMHDEPGLHVEQGGSALIVGwNTENAKVGNVAKAALLSTMFNLKMGCQILDAQ-GYPRSELVL 421
Cdd:pfam02782 78 --ALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITG-LSSPTTLAHLYRAILESLALQLRQILEALTKQeGHPIDTIHV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1210525310 422 TGGLSRTPECGQILADVFNTPVKlLASADEGCSWGAAVLA 461
Cdd:pfam02782 155 SGGGSRNPLLLQLLADALGLPVV-VPGPDEATALGAALLA 193
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
12-510 |
2.78e-16 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 81.45 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTDAHLQVLAkgEARYDFVPNLPE-----GCYEQRVEDWDHALSI----AMQQALNELQKKIGDkm 82
Cdd:cd07776 2 YLGLDLSTQSLKAVVIDSDLKVVA--EESVNFDSDLPEygtkgGVHRDGDGGEVTSPVLmwveALDLLLEKLKAAGFD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 83 LWKPLAIGISGQMHG------------ECLIKNDG--SIL--------GPVrlWCDARNADTAEELTQQFK--------- 131
Cdd:cd07776 78 FSRVKAISGSGQQHGsvywskgaesalANLDPSKSlaEQLegafsvpdSPI--WMDSSTTKQCRELEKAVGgpealaklt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 132 -VKVPKRVTCARFLWTCRERPELAAQVAHITtpagwcafrLTNEFK----LG------IGEASGMFPMDtthnhYRTdll 200
Cdd:cd07776 156 gSRAYERFTGPQIAKIAQTDPEAYENTERIS---------LVSSFLasllLGryapidESDGSGMNLMD-----IRS--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 201 EQYDAALREPGVSRRMVDLLPTPV----RAGEDGGYLTaagaallnlpKEWAGIP---VAPAEGDQIAALAGSLIGsAGT 273
Cdd:cd07776 219 RKWSPELLDAATAPDLKEKLGELVpsstVAGGISSYFV----------ERYGFSPdclVVAFTGDNPASLAGLGLE-PGD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 274 ISCSFGTSVCANVVGDRPFQGVSAAVDQYCAADGAPVNMVWLRNGTTFLNTIVESYNAGKnEDAFATIMPQlidAPADCG 353
Cdd:cd07776 288 VAVSLGTSDTVFLVLDEPKPGPEGHVFANPVDPGSYMAMLCYKNGSLARERVRDRYAGGS-WEKFNELLES---TPPGNN 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 354 GLLALPFMHDE-----PGLHVEQGGSALIVGWNTENAKVgnvaKAALLSTMFNLK-----MGCQIldaqgyPRSELVLTG 423
Cdd:cd07776 364 GNLGLYFDEPEitppvPGGGRRFFGDDGVDAFFDPAVEV----RAVVESQFLSMRlhaerLGSDI------PPTRILATG 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 424 GLSRTPECGQILADVFNTPVKLLASADeGCSWGAAVLAKYRHLCQSSATFSLNWAGFlqsliPPEEETLRFQPIADHVRE 503
Cdd:cd07776 434 GASANKAILQVLADVFGAPVYTLDVAN-SAALGAALRAAHGLLCAGSGDFSPEFVVF-----SAEEPKLVAEPDPEAAEV 507
|
....*..
gi 1210525310 504 YEAMFTR 510
Cdd:cd07776 508 YDKLLER 514
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
87-461 |
2.95e-14 |
|
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: 75.06 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 87 LAIGISGQMHGECLIKNDGSILgpvrlW-C---DARNADTAEELTQQ---FKVKVPKRV--TCA-----RFLWTCRERPE 152
Cdd:cd07775 73 AAISTTSMREGIVLYDNEGEEI-----WaCanvDARAAEEVSELKELyntLEEEVYRISgqTFAlgaipRLLWLKNNRPE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 153 LAAQVAHITTPAGWCAFRLTNEFKL--GIGEASGMFpmDTTHNHYRTDLLEQydAALREpgvsrrmvDLLPTPVRAGEDG 230
Cdd:cd07775 148 IYRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLF--DLKTRDWDPEILEM--AGLKA--------DILPPVVESGTVI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 231 GYLTAAGAALLNLPKewaGIPVAPAEGD-QIAALAGSLIGSAGTISC--SFGTSVcANVvgDRPFQGVSAAVDQYCAAdg 307
Cdd:cd07775 216 GKVTKEAAEETGLKE---GTPVVVGGGDvQLGCLGLGVVRPGQTAVLggSFWQQE-VNT--AAPVTDPAMNIRVNCHV-- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 308 apVNMVWLRNGTTFLNTIVESY------------NAGKNEDAFATIMPQLIDAPADCGGLL---------------ALPF 360
Cdd:cd07775 288 --IPDMWQAEGISFFPGLVMRWfrdafcaeekeiAERLGIDAYDLLEEMAKDVPPGSYGIMpifsdvmnyknwrhaAPSF 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 361 MH---DEPGLHVEQGGSALIvgwntENakvgnvakAALLsTMFNLKmgcQILDAQGYPRSELVLTGGLSRTPECGQILAD 437
Cdd:cd07775 366 LNldiDPEKCNKATFFRAIM-----EN--------AAIV-SAGNLE---RIAEFSGIFPDSLVFAGGASKGKLWCQILAD 428
|
410 420
....*....|....*....|....
gi 1210525310 438 VFNTPVKLLASAdEGCSWGAAVLA 461
Cdd:cd07775 429 VLGLPVKVPVVK-EATALGAAIAA 451
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
13-514 |
1.72e-12 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 69.87 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 13 IGVDNGTQGLSVVLTDAHL-QVLAKGEARY-----DFVPNLPEGCYEQRVEDWDHALSIAMQQALNE--LQKK--IGdkm 82
Cdd:PRK04123 6 IGLDFGTDSVRALLVDCATgEELATAVVEYphwvkGRYLDLPPNQALQHPLDYIESLEAAIPAVLKEagVDPAavVG--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 83 lwkplaIGI---SGQM-----HGECLIKNDGSILGP---VRLWCDARNADTAEELTQQFKVKVPKRVTC----------- 140
Cdd:PRK04123 83 ------IGVdftGSTPapvdaDGTPLALLPEFAENPhamVKLWKDHTAQEEAEEINRLAHERGEADLSRyiggiyssewf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 141 -ARFLWTCRERPELAAQVAHITTPAGWCAFRLTN-----EFKLGIGEA--SGMFpmdtthnHYRTDLLEQYD--AALrEP 210
Cdd:PRK04123 157 wAKILHVLREDPAVYEAAASWVEACDWVVALLTGttdpqDIVRSRCAAghKALW-------HESWGGLPSADffDAL-DP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 211 GVSRRMVDLLPTPVR-AGEDGGYLTAAGAALLNLPkewAGIPVAPAEGDQIAALAGSLIGsAGTISCSFGTSVCANVVGD 289
Cdd:PRK04123 229 LLARGLRDKLFTETWtAGEPAGTLTAEWAQRLGLP---EGVAVSVGAFDAHMGAVGAGAE-PGTLVKVMGTSTCDILLAD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 290 --RPFQGVSAAVDqycaaDGAPVNMVWLRNGTT--------FLNTIVESYNAGKNEDAFATIMPQLIDA----PADCGGL 355
Cdd:PRK04123 305 kqRAVPGICGQVD-----GSIVPGLIGYEAGQSavgdifawFARLLVPPEYKDEAEARGKQLLELLTEAaakqPPGEHGL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 356 LAL--------PFmhdepglhVEQGGSALIVGWN--TenaKVGNVAKAALLSTMFNLKMGCQILDAQGYPRSELVLTGGL 425
Cdd:PRK04123 380 VALdwfngrrtPL--------ADQRLKGVITGLTlgT---DAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 426 SR-TPECGQILADVFNTPVKLLASaDEGCSWGAAVLA-----KYRHLCQSSatfslnwagflQSLIPPEEETlrFQPIAD 499
Cdd:PRK04123 449 ARkNPVLMQIYADVLNRPIQVVAS-DQCPALGAAIFAavaagAYPDIPEAQ-----------QAMASPVEKT--YQPDPE 514
|
570
....*....|....*
gi 1210525310 500 HVREYEAMFTRYQKL 514
Cdd:PRK04123 515 NVARYEQLYQEYKQL 529
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
100-463 |
3.50e-10 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 62.35 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 100 LIKNDGSILGPVRLWCDARNADTAEELTQQFKVKVPKRV---------TCARFLWTCRERPELAAQVAHITTPAGWCAFR 170
Cdd:PRK10331 86 LVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQIsgvgafsfnTLYKLVWLKENHPQLLEQAHAWLFISSLINHR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 171 LTNEFKLGIGEA--SGMfpmdtthnhyrTDL-LEQYDAA-LREPGVSRRmvdLLPTPVRAGEDGGYLTAAGAALLNLPke 246
Cdd:PRK10331 166 LTGEFTTDITMAgtSQM-----------LDIqQRDFSPEiLQATGLSRR---LFPRLVEAGEQIGTLQPSAAALLGLP-- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 247 wAGIPVAPAEGDQIAALAGSLIG------SAGTISCSFGTSVCANVVGDRPFQGVSAAVDQyCAADGAPvNMVWLRNGTt 320
Cdd:PRK10331 230 -VGIPVISAGHDTQFALFGSGAGqnqpvlSSGTWEILMVRSAQVDTSLLSQYAGSTCELDS-QSGLYNP-GMQWLASGV- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 321 fLNTIVESYNAGknEDAFATIMPQLIDAPADCGGLLALPfmhdepglHVEQGGSAlivGWN--TENAKVGNVAKAALLST 398
Cdd:PRK10331 306 -LEWVRKLFWTA--ETPYQTMIEEARAIPPGADGVKMQC--------DLLACQNA---GWQgvTLNTTRGHFYRAALEGL 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1210525310 399 MFNLKMGCQILDAQGYPRS-ELVLTGGLSRTPECGQILADVFNTPVKLLASAdEGCSWGAAVLAKY 463
Cdd:PRK10331 372 TAQLKRNLQVLEKIGHFKAsELLLVGGGSRNALWNQIKANMLDIPIKVLDDA-ETTVAGAAMFGWY 436
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
12-516 |
1.62e-09 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). 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. 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: 466802 [Multi-domain] Cd Length: 499 Bit Score: 60.23 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIG-VDNGTQGLSVVLTDAHLQVLAKgeARYDFVPNLP-EGCYEQRVEDWDHALSIAMQQALNELQKKIGDKMLWKplAI 89
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVAS--HQVEHKQIYPkPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIK--AI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 90 GISGQMhgECLI---KNDGSILGPVRLWCDARNADTAEELTQqfkvKVPKRVTCAR----------F-----LWTCRERP 151
Cdd:cd07792 78 GITNQR--ETTVvwdKSTGKPLYNAIVWLDTRTSDTVEELSA----KTPGGKDHFRkktglpistyFsavklRWLLDNVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 152 ELAAQV----AHITTPAGWCAFRLTNefklgiGEASGMFPMDTThNHYRTDLLE----QYDAAL-REPGVSRrmvDLLPT 222
Cdd:cd07792 152 EVKKAVddgrLLFGTVDSWLIWNLTG------GKNGGVHVTDVT-NASRTMLMNlrtlQWDPELcEFFGIPM---SILPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 223 PVRAGEDGGYLtaAGAALlnlpkewAGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTSvC---ANvVGDRPFQ------ 293
Cdd:cd07792 222 IRSSSEVYGKI--ASGPL-------AGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTG-CfllYN-TGEEPVFskhgll 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 294 -------GVSAAVdQYC-----AADGAPVNmvWLRNGTTFLNTI--VESYnAGKNED--------AFAtimpqlidapad 351
Cdd:cd07792 291 ttvayklGPDAPP-VYAlegsiAIAGAAVQ--WLRDNLGIISSAseVETL-AASVPDtggvyfvpAFS------------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 352 cgGLLAlPFMHDEpglhveqgGSALIVGWnTENAKVGNVAKAALLSTMFNLkmgCQILDA----QGYPRSELVLTGGLSR 427
Cdd:cd07792 355 --GLFA-PYWRPD--------ARGTIVGL-TQFTTKAHIARAALEAVCFQT---REILDAmnkdSGIPLTSLRVDGGMTK 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 428 TPECGQILADVFNTPVkLLASADEGCSWGAAVLakyrhlcqssATFSLN-WAGFLQSLIPPEEETLRFQP-IADHVReyE 505
Cdd:cd07792 420 NNLLMQIQADILGIPV-ERPSMVETTALGAAIA----------AGLAVGvWKSLDELKSLNEGGRTVFEPqISEEER--E 486
|
570
....*....|.
gi 1210525310 506 AMFTRYQKLIQ 516
Cdd:cd07792 487 RRYKRWKKAVE 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
12-461 |
2.36e-09 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 59.60 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIG-VDNGTQGLSVVLTDAHLQVLAK-GEARYDFVPNlpEGCYEQRVEDWDHALSIAMQQALnelqKKIGDKMLWKPL-A 88
Cdd:PTZ00294 3 YIGsIDQGTTSTRFIIFDEKGNVVSShQIPHEQITPH--PGWLEHDPEEILRNVYKCMNEAI----KKLREKGPSFKIkA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 89 IGISGQMhgECLI---KNDGSILGPVRLWCDARnadtAEELTQQFKVKVPKR--------------VTCARFLWTCRERP 151
Cdd:PTZ00294 77 IGITNQR--ETVVawdKVTGKPLYNAIVWLDTR----TYDIVNELTKKYGGSnffqkitglpistyFSAFKIRWMLENVP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 152 ELAAQV----AHITTPAGWCAFRLTNE--FKLGIGEASGMFPMDTTHNHYRTDLLEQYDAALrepgvsrrmvDLLPTPVR 225
Cdd:PTZ00294 151 AVKDAVkegtLLFGTIDTWLIWNLTGGksHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPK----------ETLPEIKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 226 AGEDGGYLTAAGAALLNlpkewaGIPVAPAEGDQIAALAGSLIGSAGTISCSFGTS--VCANvVGDRP------------ 291
Cdd:PTZ00294 221 SSENFGTISGEAVPLLE------GVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGcfLLMN-TGTEIvfskhgllttvc 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 292 FQGVSAAVDQYC-----AADGAPVNmvWLRNGTTFLNTIVESynagknedafATIMPQLID------APAdCGGLLAlPF 360
Cdd:PTZ00294 294 YQLGPNGPTVYAlegsiAVAGAGVE--WLRDNMGLISHPSEI----------EKLARSVKDtggvvfVPA-FSGLFA-PY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 361 MHDEpglhveqgGSALIVGWnTENAKVGNVAKAALLSTMFNLKmgcQILDA----QGYPRSELVLTGGLSRTPECGQILA 436
Cdd:PTZ00294 360 WRPD--------ARGTIVGM-TLKTTRAHIVRAALEAIALQTN---DVIESmekdAGIELNSLRVDGGLTKNKLLMQFQA 427
|
490 500
....*....|....*....|....*
gi 1210525310 437 DVFNTPVKLLASAdEGCSWGAAVLA 461
Cdd:PTZ00294 428 DILGKDIVVPEMA-ETTALGAALLA 451
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-461 |
2.61e-08 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 56.25 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIG-VDNGTQGLSVVLTDAHLQVLAKGEAryDFVPNLPEG--CYEQRVEDWDHALsIAMQQALNELQKKIGDKMLWKpLA 88
Cdd:PLN02295 1 FVGaIDQGTTSTRFIIYDRDARPVASHQV--EFTQIYPQAgwVEHDPMEILESVL-TCIAKALEKAAAKGHNVDSGL-KA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 89 IGISGQMHGECLI-KNDGSILGPVRLWCDARNADTAEELTQQFK-VKVPKRVTCA----------RFLWTCRERPELAAQ 156
Cdd:PLN02295 77 IGITNQRETTVAWsKSTGRPLYNAIVWMDSRTSSICRRLEKELSgGRKHFVETCGlpistyfsatKLLWLLENVDAVKEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 157 V----AHITTPAGWCAFRLTNefklgiGEASGMFPMDTThNHYRTDLLEQYDAALREP-----GVSRRMvdlLPTPVRAG 227
Cdd:PLN02295 157 VksgdALFGTIDSWLIWNLTG------GASGGVHVTDVT-NASRTMLMNLKTLDWDKPtlealGIPAEI---LPKIVSNS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 228 EDGGyLTAAGAALlnlpkewAGIPVAPAEGDQIAALAGSLIgSAGTISCSFGTS--VCANvVGDRP------------FQ 293
Cdd:PLN02295 227 EVIG-TIAKGWPL-------AGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGcfILLN-TGEEVvpskhgllttvaYK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 294 GVSAAVDQYC-----AADGAPVNmvWLRNGTTFLNTIVESynagkneDAFATIMPqlidapaDCGGLLALPFMHdepGL- 367
Cdd:PLN02295 297 LGPDAPTNYAlegsvAIAGAAVQ--WLRDNLGIIKSASEI-------EALAATVD-------DTGGVYFVPAFS---GLf 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 368 --HVEQGGSALIVGWNTENAKvGNVAKAALLSTMFNLKmgcQILDA----QGYPRSELVLT-----GGLSRTPECGQILA 436
Cdd:PLN02295 358 apRWRDDARGVCVGITRFTNK-AHIARAVLESMCFQVK---DVLDAmrkdAGEEKSHKGLFllrvdGGATANNLLMQIQA 433
|
490 500
....*....|....*....|....*.
gi 1210525310 437 DVFNTPVklLASAD-EGCSWGAAVLA 461
Cdd:PLN02295 434 DLLGSPV--VRPADiETTALGAAYAA 457
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
142-264 |
2.00e-06 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 50.39 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 142 RFLWTCRERPELAAQVAHITTPAGWCAFRLTNEFKLGIGEA--SGMFpmDTTHNHYRTDLLEqyDAALREpgvsrrmvDL 219
Cdd:PRK10939 140 RLLWLAHHRPDIYRQAHTITMISDWIAYMLSGELAVDPSNAgtTGLL--DLVTRDWDPALLE--MAGLRA--------DI 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1210525310 220 LPTPVRAGEDGGYLTAAGAALLNLPkewAGIPVAPAEGD-QIAALA 264
Cdd:PRK10939 208 LPPVKETGTVLGHVTAKAAAETGLR---AGTPVVMGGGDvQLGCLG 250
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
12-462 |
3.06e-05 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. 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. 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: 466788 [Multi-domain] Cd Length: 522 Bit Score: 46.46 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 12 YIGVDNGTQGLSVVLTD-AHLQVLAKGEARYDFVPNLPEGCYEQRVEDWDHALSIAMQQALNElqkkiGDKMLWKPLAIG 90
Cdd:cd07768 2 GIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIR-----EGVDAYEVKGCG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 91 ISGQmhgeC---LIKNDG-----SILGP----VRLWCDARNADTAEELTQQFKVKVPKRV--------TCARFLWTCRER 150
Cdd:cd07768 77 VDAT----CslaIFDREGtplmaLIPYPnednVIFWMDHSAVNEAQWINMQCPQQLLDYLggkispemGVPKLKYFLDEY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 151 PELAAQVAHITTPAGWCAFRLTNEFKLGIGEASGMFPMDTTHNHYRTDLLEQYDAALREPGVSRrmvdLLPTPVRAGEDG 230
Cdd:cd07768 153 SHLRDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLEHLTTTK----NLPSNVPIGTTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 231 GYLTAAGAALLNLPkewAGIPVAPAEGDQIAALAGslIGSA---GTISCSFGTSVCANVVGDRP--FQGVSAAVDQ---- 301
Cdd:cd07768 229 GVALPEMAEKMGLH---PGTAVVVSCIDAHASWFA--VASPhleTSLFMIAGTSSCHMYGTTISdrIPGVWGPFDTiidp 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 302 ----YCAADGAPVNMV-WLRNGTTFLNTIVESYNAGKN-EDAFATIMPQLIDAPADCGGLLALPFMH--DEPGLHVEQGG 373
Cdd:cd07768 304 dysvYEAGQSATGKLIeHLFESHPCARKFDEALKKGADiYQVLEQTIRQIEKNNGLSIHILTLDMFFgnRSEFADPRLKG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210525310 374 SALIVGWNTENAKVGNVAKAALLSTMFNLKMGCQILDAQGYPRSELVLTGGLSRTPECGQILADVFNTPVKLLASADEGC 453
Cdd:cd07768 384 SFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGI 463
|
....*....
gi 1210525310 454 SwGAAVLAK 462
Cdd:cd07768 464 L-GAAVLAK 471
|
|
| |
