|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-436 |
1.08e-157 |
|
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: 455.09 E-value: 1.08e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 4 IGYDIGSSSVKAALVSDADGSEVARVQYPKKEMPIDspqPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGISYQ 83
Cdd:cd07809 3 LGIDLGTQSIKAVLIDAETGRVVASGSAPHENILID---PGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 84 MHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNGPGNFTLSKLVWVRDNQPDVFSQIHKIMLPGDY 163
Cdd:cd07809 80 MHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 164 IALRFSGNATTtasGLSE--GIMWDFRDDQPAGWLLEKAG----ISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPIL 237
Cdd:cd07809 160 LNWKLTGEKVT---GLGDasGTFPIDPRTRDYDAELLAAIdpsrDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 238 YRAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVNhtrkaprIGKLLCINGTGIQYSWMQQQ 317
Cdd:cd07809 237 PGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDST-------GGMLPLINTTNCLTAWTELF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 318 VSP-NASYPEMNQLASEIPVGCQGLRIYPFGNGaERMLGNARVGARIQGLNFNTHTRSHLYRAALEGIAFSFVYGMEIMA 396
Cdd:cd07809 310 RELlGVSYEELDELAAQAPPGAGGLLLLPFLNG-ERTPNLPHGRASLVGLTLSNFTRANLARAALEGATFGLRYGLDILR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 502528804 397 ADGVGLGRIKA-GndNLFRARTFAETIATLTGATIQMVATT 436
Cdd:cd07809 389 ELGVEIDEIRLiG--GGSKSPVWRQILADVFGVPVVVPETG 427
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-486 |
1.67e-152 |
|
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: 443.89 E-value: 1.67e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:COG1070 2 YVLGIDIGTTSVKAVLF-DADGEVVASAS---AEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNGPG-NFTLSKLVWVRDNQPDVFSQIHKIMLP 160
Cdd:COG1070 78 GQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHpGFTAPKLLWLKENEPEIFARIAKVLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 161 GDYIALRFSGNATTTASGLSEGIMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPILYRA 240
Cdd:COG1070 158 KDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 241 GDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVnhtrkAP-RIGKLLCINGTGIQYSWMQQQVS 319
Cdd:COG1070 238 GDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHA-----VPgRWLPMGATNNGGSALRWFRDLFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 320 PNA--SYPEMNQLASEIPVGCQGLRIYPFGNGAERMLGNARVGARIQGLNFNtHTRSHLYRAALEGIAFSFVYGMEIMAA 397
Cdd:COG1070 313 DGEldDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLS-HTRAHLARAVLEGVAFALRDGLEALEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 398 DGVGLGRIKAGnDNLFRARTFAETIATLTGATIQ----------------MVATTgavgaaraaavaagAFGSMSEAT-A 460
Cdd:COG1070 392 AGVKIDRIRAT-GGGARSPLWRQILADVLGRPVEvpeaeeggalgaallaAVGLG--------------LYDDLEEAAaA 456
|
490 500
....*....|....*....|....*..
gi 502528804 461 TDKVQLEYAP-LAGTEPYREAYADWKN 486
Cdd:COG1070 457 MVRVGETIEPdPENVAAYDELYERYRE 483
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
2-408 |
1.99e-112 |
|
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: 341.06 E-value: 1.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07808 1 YLLGIDLGTSSVKAVLV-DEDGRVLASAS---AEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEAcRERLLNGPGN-FTLSKLVWVRDNQPDVFSQIHKIMLP 160
Cdd:cd07808 77 GQMHGLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEI-LIITGNPPLPgFTLPKLLWLKENEPEIFARIRKILLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 161 GDYIALRFSGNATT---TASGLSegiMWDFRDDQpagW---LLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGI 234
Cdd:cd07808 156 KDYLRYRLTGELATdpsDASGTL---LFDVEKRE---WseeLLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 235 PILYRAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVNHtrkapriGKLL---CINGTGIQY 311
Cdd:cd07808 230 PVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVP-------GKWYamgVTLSAGLSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 312 SWMQQQVSPNA-SYPEMNQLASEIPVGCQGLRIYPFGNGaER---MLGNARvGARIqGLNFNtHTRSHLYRAALEGIAFS 387
Cdd:cd07808 303 RWLRDLFGPDReSFDELDAEAAKVPPGSEGLLFLPYLSG-ERtpyWDPNAR-GSFF-GLSLS-HTRAHLARAVLEGVAFS 378
|
410 420
....*....|....*....|.
gi 502528804 388 FVYGMEIMAADGVGLGRIKAG 408
Cdd:cd07808 379 LRDSLEVLKELGIKVKEIRLI 399
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
2-436 |
1.07e-94 |
|
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: 294.43 E-value: 1.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07804 1 YLLGIDIGTTGTKGVLV-DEDGKVLASAS---IEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 yQMHG-LVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNGPGN-FTLSKLVWVRDNQPDVFSQIHKIML 159
Cdd:cd07804 77 -GLVPaLVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSqSVGPKLLWIKRNEPEVFKKTRKFLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 160 PGDYIALRFSGNATT-TASGLSEGIMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPILY 238
Cdd:cd07804 156 AYDYIVYKLTGEYVIdYSSAGNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 239 RAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDatrtrEMNRVNNFAHVNHtrkaPRIGKLL---CINGTGIQYSWMQ 315
Cdd:cd07804 236 GTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTD-----KLPTDPRLWLDYH----DIPGTYVlngGMATSGSLLRWFR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 316 QQVSPNA----------SYPEMNQLASEIPVGCQGLRIYPFGNGAERMLGNARvgAR--IQGLNFNtHTRSHLYRAALEG 383
Cdd:cd07804 307 DEFAGEEveaeksggdsAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPD--ARgvIFGLTLS-HTRAHLYRALLEG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 502528804 384 IAFSFVYGMEIMAADGVGLGRIKAgNDNLFRARTFAETIATLTGATIQMVATT 436
Cdd:cd07804 384 VAYGLRHHLEVIREAGLPIKRLVA-VGGGAKSPLWRQIVADVTGVPQEYVKDT 435
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
4-436 |
1.39e-94 |
|
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: 294.99 E-value: 1.39e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 4 IGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGISYQ 83
Cdd:TIGR01312 1 LGIDLGTSGVKALLV-DEQGEVIASGS---APHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 84 MHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLN--GPGnFTLSKLVWVRDNQPDVFSQIHKIMLPG 161
Cdd:TIGR01312 77 MHGLVLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNlaLPG-FTAPKLLWVRKHEPEVFARIAKVMLPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 162 DYIALRFSGNATTTASGLSEGIMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPILYRAG 241
Cdd:TIGR01312 156 DYLRYRLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 242 DQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVNHTRKAPrigkLLCINGTGIQYSWMQQQVSPN 321
Cdd:TIGR01312 236 DNAAGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGWLP----MGVTLSATSSLEWFRELFGKE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 322 AsYPEMNQLASEIPVGCQGLRIYPFGNGaERMLGN-ARVGARIQGLNFNtHTRSHLYRAALEGIAFSFVYGMEIMA-ADG 399
Cdd:TIGR01312 312 D-VEALNELAEQSPPGAEGVTFLPYLNG-ERTPHLdPQARGSFIGLTHN-TTRADLTRAVLEGVTFALRDSLDILReAGG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 502528804 400 VGLGRIKA---GNdnlfRARTFAETIATLTGATIQMVATT 436
Cdd:TIGR01312 389 IPIQSIRLiggGA----KSPAWRQMLADIFGTPVDVPEGE 424
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
2-407 |
3.55e-93 |
|
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: 291.35 E-value: 3.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQYPKkemPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07805 1 YILAIDLGTSGVKAALV-DLDGELVASAFAPY---PTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNGP--GNFTLSKLVWVRDNQPDVFSQIHKIML 159
Cdd:cd07805 77 GQMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPpsGKDPLAKILWLKENEPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 160 PGDYIALRFSGNATTTASGLSEGIMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPILYR 239
Cdd:cd07805 157 AKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 240 AGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVNHTRKAPrIGKLLciNGtGIQYSWMQQQV- 318
Cdd:cd07805 237 GGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASADPGRYLL-AAEQE--TA-GGALEWARDNLg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 319 ----SPNASYPEMNQLASEIPVGCQGLRIYP--FGNGAERMLGNARvGARIqGLNfNTHTRSHLYRAALEGIAFSFVYGM 392
Cdd:cd07805 313 gdedLGADDYELLDELAAEAPPGSNGLLFLPwlNGERSPVEDPNAR-GAFI-GLS-LEHTRADLARAVLEGVAFNLRWLL 389
|
410
....*....|....*
gi 502528804 393 EIMAADGVGLGRIKA 407
Cdd:cd07805 390 EALEKLTRKIDELRL 404
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
2-407 |
1.21e-86 |
|
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: 271.75 E-value: 1.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd00366 1 YLLGIDIGTTSVKAALF-DEDGNLVASAS---REYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRavgageklldlageeacrerllngpgnftlsklvwvrdnqpdvfsqiHKIMLPG 161
Cdd:cd00366 77 GQMPGVVLVDADGNPLRPAIIWLDRR-----------------------------------------------AKFLQPN 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 162 DYIALRFSGNATTTASGLSEGIMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPILYRAG 241
Cdd:cd00366 110 DYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 242 DQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMnRVNNFAHVnhtrkapRIGKLL---CINGTGIQYSWMQQQV 318
Cdd:cd00366 190 DTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDP-RLLNRCHV-------VPGLWLlegAINTGGASLRWFRDEF 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 319 SPN----ASYPEMNQLASEIPVGCQGLRIYPFGNGAERMLGNARVGARIQGLNFNtHTRSHLYRAALEGIAFSFVYGMEI 394
Cdd:cd00366 262 GEEedsdAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLS-HTRAHLIRAVLEGVAYALRDNLEI 340
|
410
....*....|...
gi 502528804 395 MAADGVGLGRIKA 407
Cdd:cd00366 341 LEELGVKIKEIRV 353
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
2-407 |
3.35e-76 |
|
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: 245.96 E-value: 3.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVqypKKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPkaIRGIGIS 81
Cdd:cd07773 1 YLLGIDIGTTNVKAVLF-DEDGRILASA---SRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDP--IAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRER--LLNGPgNFTLSKLVWVRDNQPDVFSQIHKIML 159
Cdd:cd07773 75 SQGESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRItgLPPSP-MYSLAKLLWLREHEPEIFAKAAKWLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 160 PGDYIALRFSGNATTTASGLSEGIMWDFRDDQpagW---LLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPI 236
Cdd:cd07773 154 VADYIAYRLTGEPVTDYSLASRTMLFDIRKRT---WseeLLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 237 LyrAG--DQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVNHTRkapriGKLLCING---TGIQY 311
Cdd:cd07773 231 V--VGghDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSYGHHVP-----GGYYYLAGslpGGALL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 312 SWMQQQVSPNASYPEM-NQLASEIPVGCQGLRIYPFGNGAERMLGNARVGARIQGLNfNTHTRSHLYRAALEGIAFSFVY 390
Cdd:cd07773 304 EWFRDLFGGDESDLAAaDELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLT-LGTTRADLLRAILEGLAFELRL 382
|
410
....*....|....*..
gi 502528804 391 GMEIMAADGVGLGRIKA 407
Cdd:cd07773 383 NLEALEKAGIPIDEIRA 399
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
2-407 |
2.58e-75 |
|
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: 243.58 E-value: 2.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07779 1 YILGIDVGTTSTRAIIF-DLDGNIVASGY---REYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAvgageklldlageeacrerllngpgnftlsklvwvrdnqpdvfsqiHKIMLPG 161
Cdd:cd07779 77 SQRSTFVPVDEDGRPLRPAISWQDKRT----------------------------------------------AKFLTVQ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 162 DYIALRFSGNATTTASGLSEGIMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPILYRAG 241
Cdd:cd07779 111 DYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 242 DQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVNHtrkapriGKLLC---INGTGIQYSWMQQQV 318
Cdd:cd07779 191 DQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVP-------GKWVLegsINTGGSAVRWFRDEF 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 319 SPN---------ASYPEMNQLASEIPVGCQGLRIYPFGNGAERMLGNARVGARIQGLNFnTHTRSHLYRAALEGIAFSFV 389
Cdd:cd07779 264 GQDevaekelgvSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTL-SHTRAHLARAILEGIAFELR 342
|
410
....*....|....*...
gi 502528804 390 YGMEIMAADGVGLGRIKA 407
Cdd:cd07779 343 DNLEAMEKAGVPIEEIRV 360
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
2-393 |
1.37e-71 |
|
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: 233.98 E-value: 1.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVqypKKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07802 1 YLLGIDNGTTNVKAVLF-DLDGREIAVA---SRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNG--PGNfTLSKLVWVRDNQPDVFSQIHKIML 159
Cdd:cd07802 77 GHGNGLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPlwPGQ-PVALLRWLKENEPERYDRIRTVLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 160 PGDYIALRFSGNATTTASGLSEGiMWDFRDDQPAGWLLEKAGISP--DLLPEIVPTFGVQATLSEAGARETGLPEGIPIL 237
Cdd:cd07802 156 CKDWIRYRLTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGIEElkDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 238 YRAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNnfahvnhtRKAPRIGKLLCINGT---GIQYSWM 314
Cdd:cd07802 235 AGAFDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSN--------SLHADPGLYLIVEASptsASNLDWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 315 QQQVSPNAS------YPEMNQLASEIPVGCQGLRIYPFGNGAeRMLGNARvgARIQGLNfNTHTRSHLYRAALEGIAFSF 388
Cdd:cd07802 307 LDTLLGEEKeaggsdYDELDELIAAVPPGSSGVIFLPYLYGS-GANPNAR--GGFFGLT-AWHTRAHLLRAVYEGIAFSH 382
|
....*
gi 502528804 389 VYGME 393
Cdd:cd07802 383 RDHLE 387
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
2-435 |
2.65e-71 |
|
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: 234.37 E-value: 2.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKmpGIDPKAIRGIGIS 81
Cdd:cd07770 1 LILGIDIGTTSTKAVLF-DEDGRVVASSS---AEYPLIRPEPGWAEQDPEEILEAVLEALKEVLA--KLGGGEVDAIGFS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERllngpgnfT---------LSKLVWVRDNQPDVFS 152
Cdd:cd07770 75 SAMHSLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRR--------TgcpihpmypLAKLLWLKEERPELFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 153 QIHKIMLPGDYIALRFSGNATT---TASGLSegiMWDFRD---DQPAgwlLEKAGISPDLLPEIVPTFGVQATLSEAGAR 226
Cdd:cd07770 147 KAAKFVSIKEYLLYRLTGELVTdysTASGTG---LLNIHTldwDEEA---LELLGIDEEQLPELVDPTEVLPGLKPEFAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 227 ETGLPEGIPILYRAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDatrtremnrvnnfahvnhtrkAPRI---GKLLC 303
Cdd:cd07770 221 RLGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSD---------------------RPVLdppGRLWC 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 304 -------------INGTGIQYSWMQQQVSPN-ASYPEMNQLASEIPVGCQGLRIYPFGNGaERMLG-NARVGARIQGLNF 368
Cdd:cd07770 280 yrldenrwlvggaINNGGNVLDWLRDTLLLSgDDYEELDKLAEAVPPGSHGLIFLPYLAG-ERAPGwNPDARGAFFGLTL 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502528804 369 NtHTRSHLYRAALEGIAFSFVYGMEIMAADGVGLGRIKAGNdNLFRARTFAETIATLTGATIQMVAT 435
Cdd:cd07770 359 N-HTRADILRAVLEGVAFNLKSIYEALEELAGPVKEIRASG-GFLRSPLWLQILADVLGRPVLVPEE 423
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
2-243 |
9.96e-61 |
|
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: 199.49 E-value: 9.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:pfam00370 1 YYLGIDCGTTSTKAILF-NEQGKIIAVAQ---LENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNG--PGnFTLSKLVWVRDNQPDVFSQIHKIML 159
Cdd:pfam00370 77 NQGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPiwPG-FTLSKLRWIKENEPEVFEKIHKFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 160 PGDYIALRFSGNATTTASGLSEGIMWDFR----DDQpagwLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIP 235
Cdd:pfam00370 156 IHDYLRWRLTGVFVTDHTNASRSMMFNIHkldwDPE----LLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVP 231
|
....*...
gi 502528804 236 ILYRAGDQ 243
Cdd:pfam00370 232 VVGGGGDQ 239
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
2-395 |
8.40e-60 |
|
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: 202.84 E-value: 8.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQYPKKEMpidSPQPGWGEQDPDLWWEQVRLATAELLKmpGIDPKAIRGIGIS 81
Cdd:cd07783 1 LFLGIDLGTSGVRAVVV-DEDGTVLASASEPYPTS---RPGPGWVEQDPEDWWEALRSLLRELPA--ELRPRRVVAIAVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNGPgNFTLSKLVWVRDNQPDVFSQIHKIMLPG 161
Cdd:cd07783 75 GTSGTLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSP-SSSLAKLLWLKRHEPEVLAKTAKFLHQA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 162 DYIALRFSG--------NATTTasglsegiMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEG 233
Cdd:cd07783 154 DWLAGRLTGdrgvtdynNALKL--------GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 234 IPILyrAG--DQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVnhtrkaprIGKLL---CINGTG 308
Cdd:cd07783 226 TPVV--AGttDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHG--------DGYWLvggASNTGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 309 IQYSWmqqqVSPNASYPEMNQLASeiPVGCQGLRIYPFGNGAERM-LGNARVGARIQGlnfNTHTRSHLYRAALEGIAFS 387
Cdd:cd07783 296 AVLRW----FFSDDELAELSAQAD--PPGPSGLIYYPLPLRGERFpFWDPDARGFLLP---RPHDRAEFLRALLEGIAFI 366
|
....*...
gi 502528804 388 FVYGMEIM 395
Cdd:cd07783 367 ERLGYERL 374
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
2-430 |
2.00e-56 |
|
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: 194.36 E-value: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVArVQYPKKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALV-DSEGKIVA-IAYREWEYYTDDDYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLR--PSIiwcDSRAVGAGEKLLDLAGEEACRERLLNGPGNFTLSKLVWVRDNQPDVFSQIHKIML 159
Cdd:cd07798 79 SQREGIVFLDKDGRELYagPNI---DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIATVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 160 PGDYIALRFSGNATTTASGLSEGIMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPILYR 239
Cdd:cd07798 156 ISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 240 AGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVnhtrkaprIGKLLCI--NG--TGIQYSWMQ 315
Cdd:cd07798 236 GADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHL--------VPGKWVLesNAgvTGLNYQWLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 316 Q--QVSPNASYPEMNQLASEIPVGCQGlrIYPFgngaermLGNARVGARIQGL-----------NFNTHTRSHLYRAALE 382
Cdd:cd07798 308 EllYGDPEDSYEVLEEEASEIPPGANG--VLAF-------LGPQIFDARLSGLknggflfptplSASELTRGDFARAILE 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 502528804 383 GIAFSFVYGMEIMAAD-GVGLGRIKAGNdNLFRARTFAETIATLTGATI 430
Cdd:cd07798 379 NIAFAIRANLEQLEEVsGREIPYIILCG-GGSRSALLCQILADVLGKPV 426
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
2-386 |
1.80e-52 |
|
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: 185.05 E-value: 1.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVSDADGSEVAR--VQYPKKEMPidsPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIG 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLADGEELASavVPYPTGYIP---PRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 80 ISYQMHGLVVVDASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEAcRERLLNGPGNFT----LSKLVWVRDNQPDVFSQIH 155
Cdd:cd07781 78 VDTTSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHPAL-EYYLAYYGGVYSsewmWPKALWLKRNAPEVYDAAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 156 KIMLPGDYIALRFSGNATTTASGLSEGIMWDFRDDQPAGWLLEKAGisPDLLP-------EIVPTFGVQATLSEAGARET 228
Cdd:cd07781 157 TIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALD--PGLLKlreklpgEVVPVGEPAGTLTAEAAERL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 229 GLPEGIPILYRAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDatrtremnrvnnfahvnhtrkAPRIGKLLC----- 303
Cdd:cd07781 235 GLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSP---------------------KPVDIPGICgpvpd 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 304 --ING----------TGIQYSWMQQQVSPNA------SYPEMNQLASEIPVGCQGLRIYPFGNGAERMLGNARVGARIQG 365
Cdd:cd07781 294 avVPGlygleagqsaVGDIFAWFVRLFVPPAeergdsIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVG 373
|
410 420
....*....|....*....|.
gi 502528804 366 LNFNtHTRSHLYRAALEGIAF 386
Cdd:cd07781 374 LTLG-TTPAHIYRALLEATAF 393
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
1-400 |
2.40e-45 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 165.53 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 1 MYwIGYDIGSSSVKAALVSDAdgSEVARVQYPKkeMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIdpKAIRGIGI 80
Cdd:PRK15027 1 MY-IGIDLGTSGVKVILLNEQ--GEVVASQTEK--LTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 81 SYQMHGLVVVDASLRPLRPSIIWCDSRAvgaGEKLlDLAGEEACRERLLNG----PGnFTLSKLVWVRDNQPDVFSQIHK 156
Cdd:PRK15027 74 AGQMHGATLLDAQQRVLRPAILWNDGRC---AQEC-ALLEARVPQSRVITGnlmmPG-FTAPKLLWVQRHEPEIFRQIDK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 157 IMLPGDYIALRFSGNattTASGLSE--GIMW-DFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEg 233
Cdd:PRK15027 149 VLLPKDYLRLRMTGE---FASDMSDaaGTMWlDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMAT- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 234 IPILYRAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVnhtrkAPRIGKLLCINGTGIQYSW 313
Cdd:PRK15027 225 VPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHA-----LPQRWHLMSVMLSAASCLD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 314 MQQQVSPNASYPEMNQLASEIPVGCQGLRIYPFGNGAERMLGNARVGARIQGLNfNTHTRSHLYRAALEGIAFSFVYGME 393
Cdd:PRK15027 300 WAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLT-HQHGPNELARAVLEGVGYALADGMD 378
|
....*..
gi 502528804 394 IMAADGV 400
Cdd:PRK15027 379 VVHACGI 385
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
2-434 |
1.60e-43 |
|
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: 159.71 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVSDaDGSEVARVQYPkkeMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDL-DGRELAVAARR---NAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRavgAGEKLLDLAGEEACRERL-LNGPGNFT---LSKLVWVRDNQPDVFSQIHKI 157
Cdd:cd24121 77 GQGDGTWLVDEDGRPVRDAILWLDGR---AADIVERWQADGIAEAVFeITGTGLFPgsqAAQLAWLKENEPERLERARTA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 158 MLPGDYIALRFSGNATTTASGLSEgIMWDFRDDQPAGWLLEKAGISP--DLLPEIVPTFGVQATLSEAGARETGLPEGIP 235
Cdd:cd24121 154 LHCKDWLFYKLTGEIATDPSDASL-TFLDFRTRQYDDEVLDLLGLEElrHLLPPIRPGTEVIGPLTPEAAAATGLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 236 ILYRAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVNNFAHVNHTRKAPRIGKLLC------INGTGI 309
Cdd:cd24121 233 VVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWLRAMANMAGtpnldwFLRELG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 310 QYSWMQQQVSPNASYPEMNQLASEIPVGCQGLRIYPFGN-GAER---MLGNARvgARIQGLNFNtHTRSHLYRAALEGIA 385
Cdd:cd24121 313 EVLKEGAEPAGSDLFQDLEELAASSPPGAEGVLYHPYLSpAGERapfVNPNAR--AQFTGLSLE-HTRADLLRAVYEGVA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 502528804 386 FSFVYGMEIMAADgVGLGRIKAGndnLFRARTFAETIATLTGATIQMVA 434
Cdd:cd24121 390 LAMRDCYEHMGED-PGELRLSGG---GARSDTWCQILADALGVPVRVPA 434
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
2-405 |
3.18e-35 |
|
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: 136.58 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVSDADGSEVARVQYPKKEmPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDpkaIRGIGIS 81
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVSRPTPA-PISSDDPGRSEQDPEKILEAVRNLIDELPREYLSD---VTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPLRPSIIWCDSRavgAGEKLLDLAGEEACRERLLNG----PGnFTLSKLVWVRDNQPDvFSQIHKI 157
Cdd:cd07777 77 GQMHGIVLWDEDGNPVSPLITWQDQR---CSEEFLGGLSTYGEELLPKSGmrlkPG-YGLATLFWLLRNGPL-PSKADRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 158 MLPGDYIALRFSGNA-----TTTASGlsegimWDFRDDQPAGW---LLEKAGISPDLLPEIVPTFgvqatlSEAGARETG 229
Cdd:cd07777 152 GTIGDYIVARLTGLPkpvmhPTNAAS------WGLFDLETGTWnkdLLEALGLPVILLPEIVPSG------EIVGTLSSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 230 LPEGIPILYRAGDQPNNALSLDVMQPGDVAATGGTSG-VVYAVTDATRTREMNRV----NNFAHVnhtrkAPRI--GKLL 302
Cdd:cd07777 220 LPKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAqLSFLTPKFELSGSVEIRpffdGRYLLV-----AASLpgGRAL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 303 -CINGTgIQySWMQQ---QVSPNASYPEMNQLASEIPVgcQGLRIYPFGNGaERMLGNARvgARIQGLNFNTHTRSHLYR 378
Cdd:cd07777 295 aVLVDF-LR-EWLRElggSLSDDEIWEKLDELAESEES--SDLSVDPTFFG-ERHDPEGR--GSITNIGESNFTLGNLFR 367
|
410 420
....*....|....*....|....*..
gi 502528804 379 AALEGIAFSFVYGMEIMAADGVGLGRI 405
Cdd:cd07777 368 ALCRGIAENLHEMLPRLDLDLSGIERI 394
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
7-407 |
2.30e-26 |
|
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: 111.81 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 7 DIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGISYQMHG 86
Cdd:cd07786 6 DQGTTSSRAILF-DHDGNIVAVAQ---REFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 87 LVVVD-ASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRER--LLNGPgNFTLSKLVWVRDNQPDVFSQIHKimlpGD- 162
Cdd:cd07786 82 TVVWDrETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKtgLVLDP-YFSATKIRWILDNVPGARERAER----GEl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 163 -------YIALRFSGNAT--TTASGLSEGIMWDFRDDQpagW---LLEKAGISPDLLPEIVPTFGVQATlseagARETGL 230
Cdd:cd07786 157 afgtidsWLIWKLTGGKVhaTDVTNASRTMLFNIHTLE---WddeLLELFGIPASMLPEVKPSSEVFGY-----TDPDLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 231 PEGIPILYRAGDQpNNALsldVMQ----PGDVAATGGTSGVVYavtdatrtreMNRVNNFAHVNH---TRKAPRIGKLLC 303
Cdd:cd07786 229 GAEIPIAGIAGDQ-QAAL---FGQacfePGMAKNTYGTGCFML----------MNTGEKPVRSKNgllTTIAWQLGGKVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 304 --------INGTGIQysWMQQQVSPNASYPEMNQLASEIPvGCQGLRIYP-F-GNGAERMLGNARvGArIQGLNFNThTR 373
Cdd:cd07786 295 yalegsifIAGAAVQ--WLRDGLGLIESAAETEALARSVP-DNGGVYFVPaFtGLGAPYWDPDAR-GA-IFGLTRGT-TR 368
|
410 420 430
....*....|....*....|....*....|....*
gi 502528804 374 SHLYRAALEGIAFSFVYGMEIMAAD-GVGLGRIKA 407
Cdd:cd07786 369 AHIARAALESIAYQTRDLLEAMEADsGIPLKELRV 403
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
2-289 |
7.33e-26 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 110.48 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQYPKKEMPiDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:PRK10939 4 YLMALDAGTGSIRAVIF-DLNGNQIAVGQAEWRHLA-VPDVPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDASLRPlrpsiIW-C---DSRAVgagEKLLDLAGEEACRERLLNGPGNFTLS-----KLVWVRDNQPDVFS 152
Cdd:PRK10939 82 SMREGIVLYDRNGTE-----IWaCanvDARAS---REVSELKELHNNFEEEVYRCSGQTLAlgalpRLLWLAHHRPDIYR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 153 QIHKIMLPGDYIALRFSG-------NATTTAsglsegiMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGA 225
Cdd:PRK10939 154 QAHTITMISDWIAYMLSGelavdpsNAGTTG-------LLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 226 RETGLPEGIPILYRAGDQPNNALSLDVMQPGDVAATGGT--SGVV---YAVTDAtrtrEMN-RVNnfAHV 289
Cdd:PRK10939 227 AETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTfwQQVVnlpAPVTDP----NMNiRIN--PHV 290
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
2-407 |
3.56e-25 |
|
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: 108.32 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07769 1 YILAIDQGTTSTRAILF-DEDGNIVASAQ---KEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVD-ASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRER--LLNGPgNFTLSKLVWVRDNQPDVFSQIHKim 158
Cdd:cd07769 77 NQRETTVVWDkKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKtgLPLDP-YFSATKIKWILDNVPGARERAER-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 159 lpGD--------YIALRFSG---------NATTTasglseGIM------WDfrDDqpagwLLEKAGISPDLLPEIVPTFG 215
Cdd:cd07769 154 --GEllfgtidtWLIWKLTGgkvhvtdvtNASRT------MLFnihtleWD--DE-----LLELFGIPRSMLPEVRPSSE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 216 VQATlseagARETGLPEGIPILYRAGDQpNNALsldVMQ----PGDVAATGGTSGVVYAVTDATRTREMNRVNnfahvnh 291
Cdd:cd07769 219 VFGY-----TDPEGLGAGIPIAGILGDQ-QAAL---FGQgcfePGMAKNTYGTGCFLLMNTGEKPVPSKNGLL------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 292 TRKAPRIGKLLC--------INGTGIQysWMQQQVSPNASYPEMNQLASEIPvGCQGLRIYP-F-GNGAERMLGNARvGA 361
Cdd:cd07769 283 TTIAWQIGGKVTyalegsifIAGAAIQ--WLRDNLGLIEDAAETEELARSVE-DNGGVYFVPaFsGLGAPYWDPDAR-GA 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 502528804 362 rIQGLNFNThTRSHLYRAALEGIAFSFVYGMEIMAAD-GVGLGRIKA 407
Cdd:cd07769 359 -IVGLTRGT-TKAHIVRAALESIAYQTRDVLEAMEKDsGIKLKELRV 403
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
2-430 |
3.28e-24 |
|
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: 105.34 E-value: 3.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07793 1 YILAVDVGTTNIRCHIF-DKKGKIIGSSS---EKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVDA-SLRPLRPSIIWCDSRAvgageklldlagEEACRE-------RLLNGPGNF------------------ 135
Cdd:cd07793 77 TQRNTFLTWDKkTGKPLHNFITWQDLRA------------AELCESwnrslllKALRGGSKFlhfltrnkrflaasvlkf 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 136 ----TLSKLVWVRDNQPDVFSQIHKimlpGD--------YIALRFSG---------NATTTAsglsegiMWDFRDDQPAG 194
Cdd:cd07793 145 stahVSIRLLWILQNNPELKEAAEK----GEllfgtidtWLLWKLTGgkvhatdysNASATG-------LFDPFTLEWSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 195 WLLEKAGISPDLLPEIVPT---FGVqaTLSEAGAREtglpegIPILYRAGDQPNNALSLDVMQPGDVAATGGTSGVVyav 271
Cdd:cd07793 214 ILLSLFGIPSSILPEVKDTsgdFGS--TDPSIFGAE------IPITAVVADQQAALFGECCFDKGDVKITMGTGTFI--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 272 tdatrtrEMNrVNNFAHVNHTRKAPRIG-----KLLCI-------NGTGIQysWMQQQV-SPNASypEMNQLASEIPvGC 338
Cdd:cd07793 283 -------DIN-TGSKPHASVKGLYPLVGwkiggEITYLaegnasdTGTVID--WAKSIGlFDDPS--ETEDIAESVE-DT 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 339 QGLRIYPFGNGAERMLGNARVGARIQGLNFNThTRSHLYRAALEGIAFSFVYGMEIMAAD-GVGLGRIKA-G----NDNL 412
Cdd:cd07793 350 NGVYFVPAFSGLQAPYNDPTACAGFIGLTPST-TKAHLVRAILESIAFRVKQLLETMEKEtSIKISSIRVdGgvsnNDFI 428
|
490
....*....|....*...
gi 502528804 413 frartfAETIATLTGATI 430
Cdd:cd07793 429 ------LQLIADLLGKPV 440
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
7-406 |
3.84e-24 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 105.14 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 7 DIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGISYQMHG 86
Cdd:COG0554 9 DQGTTSTRAILF-DRDGNIVAVAQ---REFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQRET 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 87 LVVVD-ASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRER--LLNGPgNFTLSKLVWVRDNQPDVFSQIHKimlpGD- 162
Cdd:COG0554 85 TVVWDrKTGKPLYNAIVWQDRRTADICEELKADGLEDLIREKtgLVLDP-YFSATKIKWILDNVPGARERAEA----GEl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 163 -------YIALRFSGNAT--TTASGLSEGIMWDFRDDQpagW---LLEKAGISPDLLPEIVPTFGVQATlseagARETGL 230
Cdd:COG0554 160 lfgtidsWLIWKLTGGKVhvTDVTNASRTMLFNIHTLD---WddeLLELFGIPRSMLPEVRPSSEVFGE-----TDPDLF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 231 PEGIPILYRAGDQpnnalsldvmQ----------PGDVAATGGTSGVVYAVTDATRTREMNRVNnfahvnhTRKAPRIGK 300
Cdd:COG0554 232 GAEIPIAGIAGDQ----------QaalfgqacfePGMAKNTYGTGCFLLMNTGDEPVRSKNGLL-------TTIAWGLGG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 301 LLC--------INGTGIQysWMQQQVSPNASYPEMNQLASEIPvGCQGLRIYPFGNGaermLG------NARvGArIQGL 366
Cdd:COG0554 295 KVTyalegsifVAGAAVQ--WLRDGLGLIDSAAESEALARSVE-DNGGVYFVPAFTG----LGapywdpDAR-GA-IFGL 365
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 502528804 367 NFNThTRSHLYRAALEGIAFSFVYGMEIMAAD-GVGLGRIK 406
Cdd:COG0554 366 TRGT-TRAHIARAALESIAYQTRDVLDAMEADsGIPLKELR 405
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
7-385 |
7.14e-24 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 104.34 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 7 DIGSSSVKAALVsDADGSEVARVQYPKKEMPiDSPQPGWGEQDPDLWWEqvRLATAELLKMPGIDPKAIRGIGIS-YQMH 85
Cdd:PRK10331 8 DCGATNVRAIAV-DRQGKIVARASTPNASDI-AAENSDWHQWSLDAILQ--RFADCCRQINSELTECHIRGITVTtFGVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 86 GlVVVDASLRPLRPSIIWCDSRAVGAGEKLldlaGEEACRERL--LNGPGNF---TLSKLVWVRDNQPDVFSQIHKIMLP 160
Cdd:PRK10331 84 G-ALVDKQGNLLYPIISWKCPRTAAVMENI----ERYISAQQLqqISGVGAFsfnTLYKLVWLKENHPQLLEQAHAWLFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 161 GDYIALRFSGNATT--TASGLSEgiMWDFRDDQPAGWLLEKAGISPDLLPEIVPTFGVQATLSEAGARETGLPEGIPILy 238
Cdd:PRK10331 159 SSLINHRLTGEFTTdiTMAGTSQ--MLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVI- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 239 RAGDQPNNAL---SLDVMQPgdVAATGgtsgvvyavtdatrTRE--MNRVnnfAHVNHTRKAPRIGKLL-------CINg 306
Cdd:PRK10331 236 SAGHDTQFALfgsGAGQNQP--VLSSG--------------TWEilMVRS---AQVDTSLLSQYAGSTCeldsqsgLYN- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 307 TGIQY------SWMQQQV-SPNASYPEMNQLASEIPVGCQGLRIYPfgngaeRMLGNARVGarIQGLNFNThTRSHLYRA 379
Cdd:PRK10331 296 PGMQWlasgvlEWVRKLFwTAETPYQTMIEEARAIPPGADGVKMQC------DLLACQNAG--WQGVTLNT-TRGHFYRA 366
|
....*.
gi 502528804 380 ALEGIA 385
Cdd:PRK10331 367 ALEGLT 372
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
2-341 |
2.56e-22 |
|
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: 99.71 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQ--YPKKEMPIDspqPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIG 79
Cdd:cd07775 1 YLLALDAGTGSGRAVIF-DLEGNQIAVAQreWRHKEVPDV---PGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 80 ISYQMHGLVVVDASLRPlrpsiIW-C---DSRAVgAGEKLLDLAGEEACRERLLNGPGNFTLS---KLVWVRDNQPDVFS 152
Cdd:cd07775 77 TTSMREGIVLYDNEGEE-----IWaCanvDARAA-EEVSELKELYNTLEEEVYRISGQTFALGaipRLLWLKNNRPEIYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 153 QIHKIMLPGDYIALRFSGN-ATTTASGLSEGIMwdfrDDQPAGW---LLEKAGISPDLLPEIVPTFGVQATLSEAGARET 228
Cdd:cd07775 151 KAAKITMLSDWIAYKLSGElAVEPSNGSTTGLF----DLKTRDWdpeILEMAGLKADILPPVVESGTVIGKVTKEAAEET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 229 GLPEGIPILYRAGDQPNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREMNRVN-NFAHVNHTRKAPRIGKLlcingT 307
Cdd:cd07775 227 GLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRvNCHVIPDMWQAEGISFF-----P 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 502528804 308 GIQYSWMQQQVSPNAS----------YPEMNQLASEIPVGCQGL 341
Cdd:cd07775 302 GLVMRWFRDAFCAEEKeiaerlgidaYDLLEEMAKDVPPGSYGI 345
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
2-236 |
3.90e-20 |
|
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: 93.37 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQYPKKempIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGI- 80
Cdd:cd07782 1 YYIGVDVGTGSARAGLF-DLDGRLLATASQPIT---TWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 81 ---SyqmhgLVVVDASLRPLRPS---------IIWCDSRAV-------GAGEKLLDLAGEeacrerllngpgnfTLS--- 138
Cdd:cd07782 77 atcS-----LVVLDAEGKPVSVSpsgddernvILWMDHRAVeeaerinATGHEVLKYVGG--------------KISpem 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 139 ---KLVWVRDNQPDVFSQIHKIM-LPgDYIALRFSGNatTTASGLSEGIMWDFRDDQPA--GW---LLEKAGISpDLLPE 209
Cdd:cd07782 138 eppKLLWLKENLPETWAKAGHFFdLP-DFLTWKATGS--LTRSLCSLVCKWTYLAHEGSegGWdddFFKEIGLE-DLVED 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 502528804 210 IVPTFGVQAT---------LSEAGARETGLPEGIPI 236
Cdd:cd07782 214 NFAKIGSVVLppgepvgggLTAEAAKELGLPEGTPV 249
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-434 |
9.11e-19 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 89.02 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 1 MYWIGYDIGSSSVKAALVSDADGSEVAR--VQYP--KKEMPIDsPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIR 76
Cdd:COG1069 2 KYVIGVDFGTDSVRAVVVDAADGEELASavHPYPrwVIGLYLP-PPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 77 GIGISYQMHGLVVVDASLRPL--------RPS---IIWCDSRAVGAGEKLLDLAgeEACRERLLNGPGN------FTlSK 139
Cdd:COG1069 81 GIGVDATGCTPVPVDADGTPLallpefaeNPHamvILWKDHTAQEEAERINELA--KARGEDYLRYVGGiissewFW-PK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 140 LVWVRDNQPDVFSQIHKIMLPGDYIALRFSGNATTTASGLSEGIMWDFRDDqpaGWLLEK--AGISPDL------LPEIV 211
Cdd:COG1069 158 ILHLLREDPEVYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAHEG---GYPSEEffAALDPLLdgladrLGTEI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 212 PTFGVQA-TLSEAGARETGLPEGIPILYRAGDQPNNALSLDVMQPGDVAATGGTS-----------------GVVY---- 269
Cdd:COG1069 235 YPLGEPAgTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGTStchmlvspeerfvpgicGQVDgsiv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 270 -----------AVTDAtrtremnrvnnFAHV--NHtrkAPRIGKLLCINGTGIQYswmqqqvspnasYPEMNQLASEIPV 336
Cdd:COG1069 315 pgmwgyeagqsAVGDI-----------FAWFvrLL---VPPLEYEKEAEERGISL------------HPLLTEEAAKLPP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 337 GCQGLRIYPFGNGAERMLGNARVGARIQGLNFNThTRSHLYRAALEGIAFsfvyG----MEIMAADGV------GLGRIk 406
Cdd:COG1069 369 GESGLHALDWFNGNRSPLADQRLKGVILGLTLGT-DAEDIYRALVEATAF----GtraiIERFEEEGVpideiiACGGI- 442
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502528804 407 AGNDNLFRartfaETIATLTGATIQ-------------MVA 434
Cdd:COG1069 443 ATKNPLVM-----QIYADVTGRPIKvaaseqacalgaaMFA 478
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
7-398 |
6.36e-18 |
|
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: 86.42 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 7 DIGSSSVKAaLVSDADGSEVARVQYPKKEMpidSPQPGWGEQDPDLWWEQVRLA---TAELLKMPGIDPKAIRGIGISYQ 83
Cdd:cd07792 7 DQGTTSTRF-IVFDSTGELVASHQVEHKQI---YPKPGWVEHDPMEILESVYECieeAVEKLKALGISPSDIKAIGITNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 84 MHGLVVVDASL-RPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNG-PGN--FTLSKLVWVRDNQPDVfsqiHKIML 159
Cdd:cd07792 83 RETTVVWDKSTgKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGlPIStyFSAVKLRWLLDNVPEV----KKAVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 160 PGDyiaLRF-----------SGNAT-----TTASGLSEGIMWDFRDDQPAGWLLEKAGISPDLLPEIVPTfgvqatlSEA 223
Cdd:cd07792 159 DGR---LLFgtvdswliwnlTGGKNggvhvTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSS-------SEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 224 -GARETGLPEGIPILYRAGDQpNNALsldV----MQPGDVAATGGTsGVvyavtdatrtremnrvnnFAHVNhTRKAPRI 298
Cdd:cd07792 229 yGKIASGPLAGVPISGCLGDQ-QAAL---VgqgcFKPGEAKNTYGT-GC------------------FLLYN-TGEEPVF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 299 GK--LL---------------------CINGTGIQysWMQQQVSPNASYPEMNQLASEIPvGCQGLRIYPFGNG--AERM 353
Cdd:cd07792 285 SKhgLLttvayklgpdappvyalegsiAIAGAAVQ--WLRDNLGIISSASEVETLAASVP-DTGGVYFVPAFSGlfAPYW 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 502528804 354 LGNARvgARIQGLNFNThTRSHLYRAALEGIAFSFVYGMEIMAAD 398
Cdd:cd07792 362 RPDAR--GTIVGLTQFT-TKAHIARAALEAVCFQTREILDAMNKD 403
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
7-398 |
6.92e-15 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 76.94 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 7 DIGSSSVKAALvSDADGSEVARVQYPKKEMpidSPQPGWGEQDPDLWWEQVRLATAELLK-MPGIDPKA-IRGIGISYQM 84
Cdd:PTZ00294 8 DQGTTSTRFII-FDEKGNVVSSHQIPHEQI---TPHPGWLEHDPEEILRNVYKCMNEAIKkLREKGPSFkIKAIGITNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 85 HGLVVVDASL-RPLRPSIIWCDSRAvgagEKLLDLAGEEACRERLL---NG-PGN--FTLSKLVWVRDNQPDVFSQIHKI 157
Cdd:PTZ00294 84 ETVVAWDKVTgKPLYNAIVWLDTRT----YDIVNELTKKYGGSNFFqkiTGlPIStyFSAFKIRWMLENVPAVKDAVKEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 158 MLPGDYI------ALRFSGNATTTASGLSEGIMWDFRDDQpagW---LLEKAGISPDLLPEIVPTFGVQATLSeagARET 228
Cdd:PTZ00294 160 TLLFGTIdtwliwNLTGGKSHVTDVTNASRTFLMNIKTLK---WdeeLLNKFGIPKETLPEIKSSSENFGTIS---GEAV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 229 GLPEGIPILYRAGDQPNNALSLDVMQPGDVAATGGTsGVVYAVTDATRTREMNrvnnfahvnhtrkapriGKLLC----- 303
Cdd:PTZ00294 234 PLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGT-GCFLLMNTGTEIVFSK-----------------HGLLTtvcyq 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 304 --------------INGTGIQYSWMQQQVSPNASYPEMNQLASEIPvGCQGLRIYP-F-GNGAERMLGNARvgARIQGLN 367
Cdd:PTZ00294 296 lgpngptvyalegsIAVAGAGVEWLRDNMGLISHPSEIEKLARSVK-DTGGVVFVPaFsGLFAPYWRPDAR--GTIVGMT 372
|
410 420 430
....*....|....*....|....*....|.
gi 502528804 368 FNThTRSHLYRAALEGIAFSFVYGMEIMAAD 398
Cdd:PTZ00294 373 LKT-TRAHIVRAALEAIALQTNDVIESMEKD 402
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
7-398 |
3.29e-14 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 74.74 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 7 DIGSSSVKAaLVSDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELL---KMPGID-PKAIRGIGISY 82
Cdd:PLN02295 6 DQGTTSTRF-IIYDRDARPVASHQ---VEFTQIYPQAGWVEHDPMEILESVLTCIAKALekaAAKGHNvDSGLKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 83 QMHGLVVVDASL-RPLRPSIIWCDSRAVGAGEKLLDLAGEEACRERLLNG-PGN--FTLSKLVWVRDNQPDVFSQIHKim 158
Cdd:PLN02295 82 QRETTVAWSKSTgRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGlPIStyFSATKLLWLLENVDAVKEAVKS-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 159 lpGD--------YIALRFSGNAT-----TTASGLSEGIMWDFRD---DQPagwLLEKAGISPDLLPEIVPTFGVQATLSE 222
Cdd:PLN02295 160 --GDalfgtidsWLIWNLTGGASggvhvTDVTNASRTMLMNLKTldwDKP---TLEALGIPAEILPKIVSNSEVIGTIAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 223 AGARetglpEGIPILYRAGDQpNNALSLDVMQPGDVAATGGTSGVVYAVTDATRTREmnrvnnfahvNH---TRKAPRIG 299
Cdd:PLN02295 235 GWPL-----AGVPIAGCLGDQ-HAAMLGQRCRPGEAKSTYGTGCFILLNTGEEVVPS----------KHgllTTVAYKLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 300 K----------LLCINGTGIQysWMQQQVSPNASYPEMNQLASEIPvGCQGLRIYPFGNG--AERMLGNARvgARIQGLN 367
Cdd:PLN02295 299 PdaptnyalegSVAIAGAAVQ--WLRDNLGIIKSASEIEALAATVD-DTGGVYFVPAFSGlfAPRWRDDAR--GVCVGIT 373
|
410 420 430
....*....|....*....|....*....|.
gi 502528804 368 fNTHTRSHLYRAALEGIAFSFVYGMEIMAAD 398
Cdd:PLN02295 374 -RFTNKAHIARAVLESMCFQVKDVLDAMRKD 403
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
2-265 |
1.68e-13 |
|
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: 72.66 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVSDADGSEVArvQYPKKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYAGLEMA--QEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMhGLVVVDASLRPLRPS---------IIWCDSRAVGAGEKLldlagEEACRERLLNGPG-----NFTLSKLVWVRDNQ 147
Cdd:cd07768 79 ATC-SLAIFDREGTPLMALipypnednvIFWMDHSAVNEAQWI-----NMQCPQQLLDYLGgkispEMGVPKLKYFLDEY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 148 PDVFSQIHKIMLPGDYIALRFSGNATTTASGLSEGIMWDFRDDQPAGWLLEKAGISPD------LLPEIVPTFGVQATLS 221
Cdd:cd07768 153 SHLRDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLEhltttkNLPSNVPIGTTSGVAL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 502528804 222 EAGARETGLPEGIPILYRAGDQPNNALSLDVMQ-PGDVAATGGTS 265
Cdd:cd07768 233 PEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHlETSLFMIAGTS 277
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
2-400 |
1.72e-13 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 72.57 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVSDADGSEVAR--VQYP--KKEMPIDSPqPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRG 77
Cdd:PRK04123 4 YVIGLDFGTDSVRALLVDCATGEELATavVEYPhwVKGRYLDLP-PNQALQHPLDYIESLEAAIPAVLKEAGVDPAAVVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 78 IGISYQMHGLVVVDASLRPL--RPS---------IIWCDSRAVGAGEKLLDLA--GEEACRERLLNGpgnfTLS------ 138
Cdd:PRK04123 83 IGVDFTGSTPAPVDADGTPLalLPEfaenphamvKLWKDHTAQEEAEEINRLAheRGEADLSRYIGG----IYSsewfwa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 139 KLVWVRDNQPDVFSQIHKIMLPGDYIALRFSGnaTTTASGLSEGI-------MWDFRDDQ--PAGWLlekAGISPDL--- 206
Cdd:PRK04123 159 KILHVLREDPAVYEAAASWVEACDWVVALLTG--TTDPQDIVRSRcaaghkaLWHESWGGlpSADFF---DALDPLLarg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 207 ----LPEIVPTFGVQA-TLSEAGARETGLPEGIPILYRAGDQPNNALSLDVmQPGDVAATGGTSGVVYAVTDATRtremn 281
Cdd:PRK04123 234 lrdkLFTETWTAGEPAgTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTSTCDILLADKQR----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 282 rvnnfahvnhtrkaprigkllCING----------------------TGIQYSWMQQQVSPNA-----------SYPEMN 328
Cdd:PRK04123 308 ---------------------AVPGicgqvdgsivpgligyeagqsaVGDIFAWFARLLVPPEykdeaeargkqLLELLT 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502528804 329 QLASEIPVGCQGLRIYPFGNGAERMLGNARVGARIQGLNFnTHTRSHLYRAALEGIAFsfvyG----MEIMAADGV 400
Cdd:PRK04123 367 EAAAKQPPGEHGLVALDWFNGRRTPLADQRLKGVITGLTL-GTDAPDIYRALIEATAF----GtraiMECFEDQGV 437
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
7-236 |
8.69e-12 |
|
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: 67.17 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 7 DIGSSSVKAALVSDADGS----EVARvqYPKKEMPIDspqpG---WgeqDPDLWWEQVRLATAELLKMpGIDPKAIrGI- 78
Cdd:cd07771 6 DLGASSGRVILGSLDGGKleleEIHR--FPNRPVEIN----GhlyW---DIDRLFDEIKEGLKKAAEQ-GGDIDSI-GId 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 79 --GISYqmhglVVVDASLRPLRPsiIWC--DSRAVGAGEKLLDLAGEEACRERllNG----PGNfTLSKLVWVRDNQPDV 150
Cdd:cd07771 75 twGVDF-----GLLDKNGELLGN--PVHyrDPRTEGMMEELFEKISKEELYER--TGiqfqPIN-TLYQLYALKKEGPEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 151 FSQIHKIMLPGDYIALRFSG-------NATTTAsglsegiMWDFRDDQpagW---LLEKAGISPDLLPEIVPTFGVQATL 220
Cdd:cd07771 145 LERADKLLMLPDLLNYLLTGekvaeytIASTTQ-------LLDPRTKD---WseeLLEKLGLPRDLFPPIVPPGTVLGTL 214
|
250
....*....|....*.
gi 502528804 221 SEAGARETGLPeGIPI 236
Cdd:cd07771 215 KPEVAEELGLK-GIPV 229
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-407 |
2.07e-10 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 62.92 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 2 YWIGYDIGSSSVKAALVsDADGSEVARVQypkKEMPIDSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGIS 81
Cdd:PRK00047 6 YILALDQGTTSSRAIIF-DHDGNIVSVAQ---KEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 82 YQMHGLVVVD-ASLRPLRPSIIWCDSRAVGAGEKLLDLAGEEACRER--LLNGPgNFTLSKLVWVRDNQPDVFSQIHKim 158
Cdd:PRK00047 82 NQRETTVVWDkETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKtgLVIDP-YFSGTKIKWILDNVEGARERAEK-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 159 lpGDYIA--------LRFSGNAT--TTASGLSEGIMWDFRDDQpagW---LLEKAGISPDLLPEIVPT---FGVQATLSE 222
Cdd:PRK00047 159 --GELLFgtidtwlvWKLTGGKVhvTDYTNASRTMLFNIHTLD---WddeLLELLDIPRSMLPEVRPSsevYGKTNPYGF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 223 AGARetglpegIPILYRAGDQpNNALsldVMQ----PGDVAATGGTSgvvyavtdatrtremnrvnNFAHVNhTRKAPRI 298
Cdd:PRK00047 234 FGGE-------VPIAGIAGDQ-QAAL---FGQlcfePGMAKNTYGTG-------------------CFMLMN-TGEKAVK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 299 GK--LLC-------------------INGTGIQysWMQQQVSPNASYPEMNQLASEIPvGCQGLRIYP-F-GNGAERMLG 355
Cdd:PRK00047 283 SEngLLTtiawgidgkvvyalegsifVAGSAIQ--WLRDGLKIISDASDSEALARKVE-DNDGVYVVPaFtGLGAPYWDS 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 502528804 356 NARvGArIQGLNFNThTRSHLYRAALEGIAFSFVYGMEIMAAD-GVGLGRIKA 407
Cdd:PRK00047 360 DAR-GA-IFGLTRGT-TKEHIIRATLESIAYQTRDVLDAMQADsGIRLKELRV 409
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-237 |
2.84e-10 |
|
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: 62.28 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 7 DIGSSSVKAALVsDADGSEVARVQYPKKEmpidSPQPGWGEQDPDLWWEQVRLATAELLKMPGIDpkairgiGISYQMHG 86
Cdd:cd07772 6 DIGKTNKKLLLF-DENGEVLAERSTPNPE----IEEDGYPCEDVEAIWEWLLDSLAELAKRHRID-------AINFTTHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 87 --LVVVDASLRPLRPsiiwcdsravgagekLLDL--AGEEACRERLLNGPGNF--TLS-----------KLVWVRDNQPD 149
Cdd:cd07772 74 atFALLDENGELALP---------------VYDYekPIPDEINEAYYAERGPFeeTGSpplpgglnlgkQLYWLKREKPE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 150 VFSQIHKIMLPGDYIALRFSGNATTTASGLseGI---MWDFRDDQPAGWlLEKAGISPdLLPEIVPTFGVQATLSEAGAR 226
Cdd:cd07772 139 LFARAKTILPLPQYWAWRLTGKAASEITSL--GChtdLWDFEKNEYSSL-VKKEGWDK-LFPPLRKAWEVLGPLRPDLAR 214
|
250
....*....|.
gi 502528804 227 ETGLPEGIPIL 237
Cdd:cd07772 215 RTGLPKDIPVG 225
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
65-273 |
3.48e-06 |
|
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: 49.48 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 65 LKMPGIDPKAIRGIGISYQMHGLVV----VDASLRPLRP----------------SIIWCDS----------RAVGAGEK 114
Cdd:cd07776 71 LKAAGFDFSRVKAISGSGQQHGSVYwskgAESALANLDPskslaeqlegafsvpdSPIWMDSsttkqcreleKAVGGPEA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 115 LLDLAGEEAcRERllngpgnFTLSKLVWVRDNQPDVFSQIHKIML---------PGDYIALRFSgnattTASGLSegiMW 185
Cdd:cd07776 151 LAKLTGSRA-YER-------FTGPQIAKIAQTDPEAYENTERISLvssflasllLGRYAPIDES-----DGSGMN---LM 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 186 DFRDDQpagW---LLEKAGiSPDL---LPEIVPTFGVQATLSEAGARETGLPEGIPILYRAGDQPNNALSLdVMQPGDVA 259
Cdd:cd07776 215 DIRSRK---WspeLLDAAT-APDLkekLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGL-GLEPGDVA 289
|
250
....*....|....
gi 502528804 260 ATGGTSGVVYAVTD 273
Cdd:cd07776 290 VSLGTSDTVFLVLD 303
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-88 |
7.67e-06 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 47.58 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 1 MYWIGYDIGSSSVKAALVsDADGSEVARVQYPkkempidSPQpgwgEQDPDLWWEQVRLATAELLKMPGIDPKAIRGIGI 80
Cdd:COG1940 5 GYVIGIDIGGTKIKAALV-DLDGEVLARERIP-------TPA----GAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
....*...
gi 502528804 81 SyqMHGLV 88
Cdd:COG1940 73 G--VPGPV 78
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
315-398 |
2.54e-05 |
|
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: 45.01 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 315 QQQVSPNASYPEMNQLASEIPVGCQGLRIYPF--GNGAERMLGNARvgARIQGLNFNtHTRSHLYRAALEGIAFSFVYGM 392
Cdd:pfam02782 62 EELRDAGNVESLAELAALAAVAPAGGLLFYPDfsGNRAPGADPGAR--GSITGLSSP-TTLAHLYRAILESLALQLRQIL 138
|
....*.
gi 502528804 393 EIMAAD 398
Cdd:pfam02782 139 EALTKQ 144
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
4-171 |
6.60e-05 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. 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: 466797 [Multi-domain] Cd Length: 544 Bit Score: 45.47 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 4 IGYDIGSSSVKAALVSDADG------SEVARVQYPKKempidspqPGWGEQDPDLWWEQVRLATAELLKMpgIDPKAIRG 77
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTllatseRPISYKQDPKD--------LWFVTQSSTEIWKAIKTALKELIEE--LSDYIVSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 78 IGISYQMhGLVVV-----DASLRPLRPS----------IIWCDSRAVGAGEKLldlagEEACRERLLNG-PGNFT----L 137
Cdd:cd07778 73 IGVSATC-SMVVMqrdsdTSYLVPYNVIheksnpdqdiIFWMDHRASEETQWL-----NNILPDDILDYlGGGFIpemaI 146
|
170 180 190
....*....|....*....|....*....|....
gi 502528804 138 SKLVWVRDNQPDVFSQIHKIMLPGDYIALRFSGN 171
Cdd:cd07778 147 PKLKYLIDLIKEDTFKKLEVFDLHDWISYMLATN 180
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
4-88 |
5.70e-03 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 38.60 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502528804 4 IGYDIGSSSVKAALVsDADGSEVARVqypkkEMPIDSpqpgwgEQDPDLWWEQVRLATAELLKMPGIDPKaIRGIGISyq 83
Cdd:cd23763 1 IGIDIGGTKIRAALV-DLDGEILARE-----RVPTPA------EEGPEAVLDRIAELIEELLAEAGVRER-ILGIGIG-- 65
|
....*
gi 502528804 84 MHGLV 88
Cdd:cd23763 66 VPGPV 70
|
|
| |
