|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
7-495 |
0e+00 |
|
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: 567.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWA 86
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRGAPFSRKAFGGRLQgyrprallSWLRRNGGIPSPSGDDPVGHMLHLQHNDPAVSGAAR 166
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGG--------IEGYRLGGGNPPSGKDPLAKILWLKENEPEIYAKTH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 167 WYLEPVDYLSMCFTGRAAASRASMMGAWLTDNRNLalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGISP 246
Cdd:cd07805 153 KFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKR---RWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 247 AAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSWISCPVAVKKTDAFHQLATVPGLDPSSYLLVNNQDTAGRALQWLRD 326
Cdd:cd07805 230 GTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASADPGRYLLAAEQETAGGALEWARD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 327 NVFGELD-----YDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWLL 401
Cdd:cd07805 310 NLGGDEDlgaddYELLDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 402 ECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCERVADPLNAQLRGAALFAGIGMGDV-DRDELRDLIPLDGVFEP 480
Cdd:cd07805 390 EALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQEAGALGAALLAAVGLGLLkSFDEAKALVKVEKVFEP 469
|
490
....*....|....*
gi 2179559870 481 IAANRAVYDRLFAEF 495
Cdd:cd07805 470 DPENRARYDRLYEVF 484
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-508 |
1.50e-138 |
|
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: 408.84 E-value: 1.50e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 6 RVVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQW 85
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 86 ASTVPVDADGRPVGPCVMWMDTRGAPFS---RKAFGGRlqgyrprallSWLRRNGGIPSPSgdDPVGHMLHLQHNDPAVS 162
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAaelREELGEE----------ALYEITGNPLHPG--FTAPKLLWLKENEPEIF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 163 GAARWYLEPVDYLSMCFTGRAAASRASMMGAWLTDNRNLalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAEL 242
Cdd:COG1070 149 ARIAKVLLPKDYLRYRLTGEFVTDYSDASGTGLLDVRTR---DWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAET 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 243 GISPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSWISCPVAVKKTDAFHQLATVPGLDPSSYLLVNNQDTAGRALQ 322
Cdd:COG1070 226 GLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 323 WLRDNVFGEL--DYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWL 400
Cdd:COG1070 306 WFRDLFADGEldDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 401 LECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCERVADPlNAQLRGAALFAGIGMGDVD--RDELRDLIPLDGVF 478
Cdd:COG1070 386 LEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAE-EGGALGAALLAAVGLGLYDdlEEAAAAMVRVGETI 464
|
490 500 510
....*....|....*....|....*....|
gi 2179559870 479 EPIAANRAVYDRLFAEFPGLYTAQKAMFAR 508
Cdd:COG1070 465 EPDPENVAAYDELYERYRELYPALKPLFER 494
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
7-499 |
2.50e-120 |
|
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: 361.86 E-value: 2.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWA 86
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRGAPFSR---KAFGGRlqgyrprallsWLRRNGGIPSPSGddPVGHMLHLQHNDPAVSG 163
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEeleARLGDE-----------ILIITGNPPLPGF--TLPKLLWLKENEPEIFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 164 AARWYLEPVDYLSMCFTGRAA--ASRASmmGAWLTDNRNLalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAE 241
Cdd:cd07808 148 RIRKILLPKDYLRYRLTGELAtdPSDAS--GTLLFDVEKR---EWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 242 LGISPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSWISCPVAVKKTDAFHQLATVPGLDPSSYLLVNNQDTAGRAL 321
Cdd:cd07808 223 LGLPEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 322 QWLRDNVFGE-LDYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWL 400
Cdd:cd07808 303 RWLRDLFGPDrESFDELDAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 401 LECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCERVADPlNAQLRGAALFAGIGMGDVD--RDELRDLIPLDGVF 478
Cdd:cd07808 383 LEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEE-EGSAYGAALLAAVGAGVFDdlEEAAAACIKIEKTI 461
|
490 500
....*....|....*....|.
gi 2179559870 479 EPIAANRAVYDRLFAEFPGLY 499
Cdd:cd07808 462 EPDPERHEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
7-456 |
1.68e-104 |
|
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: 317.97 E-value: 1.68e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWA 86
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRgapfsrkafggrlqgyrprallswlrrnggipspsgddpvghmlhlqhndpavsgaaR 166
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRR---------------------------------------------------------A 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 167 WYLEPVDYLSMCFTGRAA--ASRASMMGAWLTDNRnlalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGI 244
Cdd:cd00366 104 KFLQPNDYIVFRLTGEFAidYSNASGTGLYDIKTG-----DWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 245 SPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSWISCPVAVKKTDAfHQLATVPGLDPSSYLLVNNQDTAGRALQWL 324
Cdd:cd00366 179 PAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPD-PRLLNRCHVVPGLWLLEGAINTGGASLRWF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 325 RDNVFGELDYDA----LTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWL 400
Cdd:cd00366 258 RDEFGEEEDSDAeyegLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDN 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2179559870 401 LECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCERVADPLNAqLRGAALFA 456
Cdd:cd00366 338 LEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA-ALGAAILA 392
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
7-488 |
2.99e-102 |
|
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: 313.69 E-value: 2.99e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWA 86
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRgapfsrkafggrlqgyrprallswlrrnggipspsgddpvghmlhlqhndpavsgaAR 166
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKR--------------------------------------------------------TA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 167 WYLEPVDYLSMCFTGRAAASRASMMGAWLTDNRNLalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGISP 246
Cdd:cd07779 105 KFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTR---DWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 247 AAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSWISCPVAVKKTDAFHQLATVPGLDPSSYLLVNNQDTAGRALQWLRD 326
Cdd:cd07779 182 GTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 327 NVFGEL---------DYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNS 397
Cdd:cd07779 262 EFGQDEvaekelgvsPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFEL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 398 RWLLEcvnRFTGNDGPI---RIVGGGARSDLWCQIIADVCGRTCERVADPlNAQLRGAALFAGIGMG---DVDrDELRDL 471
Cdd:cd07779 342 RDNLE---AMEKAGVPIeeiRVSGGGSKSDLWNQIIADVFGRPVERPETS-EATALGAAILAAVGAGiypDFE-EAVKAM 416
|
490
....*....|....*..
gi 2179559870 472 IPLDGVFEPIAANRAVY 488
Cdd:cd07779 417 VRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
7-499 |
4.29e-102 |
|
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: 314.88 E-value: 4.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAesRVRGDQVAGVSITGQWA 86
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLA--KLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRGAPFSRKafggRLQGYRPRALLswlRRNGGIPSPSGddPVGHMLHLQHNDPAVSGAAR 166
Cdd:cd07770 79 SLLGVDEDGEPLTPVITWADTRAAEEAER----LRKEGDGSELY---RRTGCPIHPMY--PLAKLLWLKEERPELFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 167 WYLEPVDYLSMCFTGRAAASR--ASMMGawLTDNRNLalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGI 244
Cdd:cd07770 150 KFVSIKEYLLYRLTGELVTDYstASGTG--LLNIHTL---DWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 245 SPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSwiscpvAVKKTDAFHQLATVPGL-----DPSSYLL---VNNqdt 316
Cdd:cd07770 225 LAGTPVVLGASDGALANLGSGALDPGRAALTVGTSG------AIRVVSDRPVLDPPGRLwcyrlDENRWLVggaINN--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 317 AGRALQWLRDNVFG-ELDYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAF 395
Cdd:cd07770 296 GGNVLDWLRDTLLLsGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 396 NSRWLLECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCErVADPLNAQLRGAALFAGIGMGDVDRDELRDLIPLD 475
Cdd:cd07770 376 NLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVL-VPEEEEASALGAALLALEALGLISSLEADELVKIG 454
|
490 500
....*....|....*....|....
gi 2179559870 476 GVFEPIAANRAVYDRLFAEFPGLY 499
Cdd:cd07770 455 KVVEPDPENHAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
7-461 |
1.38e-98 |
|
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: 304.51 E-value: 1.38e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRglAESRVRGDQVAGVSITGQWA 86
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIRE--AAAQAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRGAPFSrKAFGGRLQGYRprallsWLRRNGGIPSPSgdDPVGHMLHLQHNDPAVSGAAR 166
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEA-EELAERIGAEE------LYRITGLPPSPM--YSLAKLLWLREHEPEIFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 167 WYLEPVDYLSMCFTGRAAASR--ASMMGAWltDNRNLalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGI 244
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDYslASRTMLF--DIRKR---TWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 245 SPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSWISCPVAVKKTDA--FHQLATV-PGLDPSSYLLVNNQdTAGRAL 321
Cdd:cd07773 225 PAGTPVVVGGHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEmlAEGGLSYgHHVPGGYYYLAGSL-PGGALL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 322 QWLRDNVFGELDYDAL-TALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWL 400
Cdd:cd07773 304 EWFRDLFGGDESDLAAaDELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLN 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2179559870 401 LECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCERVADPlNAQLRGAALFAGIGMG 461
Cdd:cd07773 384 LEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVP-EATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
8-461 |
2.68e-90 |
|
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: 283.26 E-value: 2.68e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 8 VLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWAS 87
Cdd:cd07804 2 LLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 88 TVPVDADGRPVGPCVMWMDTRGApfsrkafggrlqgyrprALLSWLRRNGG---IPSPSG----DDPVG-HMLHLQHNDP 159
Cdd:cd07804 82 LVPVDENGKPLRPAILYGDRRAT-----------------EEIEWLNENIGedrIFEITGnpldSQSVGpKLLWIKRNEP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 160 AVSGAARWYLEPVDYLSMCFTGRAA---ASRASMMGAWLTDNRnlalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAP 236
Cdd:cd07804 145 EVFKKTRKFLGAYDYIVYKLTGEYVidySSAGNEGGLFDIRKR-----TWDEELLEALGIDPDLLPELVPSTEIVGEVTK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 237 AVAAELGISPAAQVVTGTPDLHSAAVGSGAVRQGELHLTI-STTSWISCpvaVKKTDAFHQLATVPGLDPSSYLLVNNQD 315
Cdd:cd07804 220 EAAEETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLgTAGDIGVV---TDKLPTDPRLWLDYHDIPGTYVLNGGMA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 316 TAGRALQWLRDNVFGEL----------DYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADL 385
Cdd:cd07804 297 TSGSLLRWFRDEFAGEEveaeksggdsAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2179559870 386 VRAVLEGVAFNSRWLLECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCERVADPLNAQLrGAALFAGIGMG 461
Cdd:cd07804 377 YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASL-GDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
7-461 |
3.00e-85 |
|
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: 270.19 E-value: 3.00e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWA 86
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRGApfsrkafgGRLQGYRPRALLSWLRRNGGIPSPSGdDPVGHMLHLQHNDPAVSGAAR 166
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAA--------DIVDRWEEDGTLEKVYPLTGQPLWPG-QPVALLRWLKENEPERYDRIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 167 WYLEPVDYLSMCFTGRAAASrASMMGAWLTDNRNLalpDYDDVLVRLAGVD--RTKLPPLVPTGSIISTVAPAVAAELGI 244
Cdd:cd07802 152 TVLFCKDWIRYRLTGEISTD-YTDAGSSLLDLDTG---EYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 245 SPAAQVVTGTPDLHSAAVGSGAVRQGELhLTISTTSWISCPVAVKKTDAFHQLATVPGLDPSSYLLVNNQDTAGRALQWL 324
Cdd:cd07802 228 PEGTPVAAGAFDVVASALGAGAVDEGQL-CVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSASNLDWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 325 RDNVFGEL------DYDALTALAAGAPAGSNGVIFTPWLKGEHspiDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSR 398
Cdd:cd07802 307 LDTLLGEEkeaggsDYDELDELIAAVPPGSSGVIFLPYLYGSG---ANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2179559870 399 WlleCVNRFT--GNDGPIRIVGGGARSDLWCQIIADVCGRTCERVAdplNAQL--RGAALFAGIGMG 461
Cdd:cd07802 384 D---HLERLLvaRKPETIRLTGGGARSPVWAQIFADVLGLPVEVPD---GEELgaLGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
7-459 |
5.69e-82 |
|
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: 261.00 E-value: 5.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRgdQVAGVSITGQWA 86
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRGAPFSRKafggrlqgyRPRALLSWLRRNGGIPSPSGddPVGHMLHLQHNDPAVSGAAR 166
Cdd:cd07783 79 TLVLVDREGEPLRPAIMYNDARAVAEAEE---------LAEAAGAVAPRTGLAVSPSS--SLAKLLWLKRHEPEVLAKTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 167 WYLEPVDYLSMCFTGRAAASRASMMGAWLTDNRNLALPDYddvLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGISP 246
Cdd:cd07783 148 KFLHQADWLAGRLTGDRGVTDYNNALKLGYDPETGRWPSW---LLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 247 AAQVVTGTPDLHSAAVGSGAVRQGELHLTISTtswiscpvavkkTDAFHQLATVPGLDPS----SYLLVNNQ-------D 315
Cdd:cd07783 225 GTPVVAGTTDSIAAFLASGAVRPGDAVTSLGT------------TLVLKLLSDKRVPDPGggvySHRHGDGYwlvggasN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 316 TAGRALQWLrdnvFGELDYDALTALAagAPAGSNGVIFTP-WLKGEHSPIDDRNARGGFhnLSLDTTRADLVRAVLEGVA 394
Cdd:cd07783 293 TGGAVLRWF----FSDDELAELSAQA--DPPGPSGLIYYPlPLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIA 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2179559870 395 FNSRWLLECVNRFTGND-GPIRIVGGGARSDLWCQIIADVCGRTCERVADPlnAQLRGAALFAGIG 459
Cdd:cd07783 365 FIERLGYERLEELGAPPvEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEE--EAALGAALLAAAG 428
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
7-501 |
9.96e-75 |
|
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: 244.37 E-value: 9.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFV-ALDGTVLWSDLVAVPTSYGP--GGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSI-- 81
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVdLADGEELASAVVPYPTGYIPprPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVdt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 82 TGqwaSTV-PVDADGRPVGPCVMWMDTRGAPFSRkafggRLQGYRPRALLSWLRRNGGIPSPsgDDPVGHMLHLQHNDPA 160
Cdd:cd07781 81 TS---STVvPVDEDGNPLAPAILWMDHRAQEEAA-----EINETAHPALEYYLAYYGGVYSS--EWMWPKALWLKRNAPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 161 VSGAARWYLEPVDYLSMCFTGRAAASRASMMGAWLTDNRNlALPD---YDDVLVRLAGVdRTKLP-PLVPTGSIISTVAP 236
Cdd:cd07781 151 VYDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWG-GGPPrefLAALDPGLLKL-REKLPgEVVPVGEPAGTLTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 237 AVAAELGISPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSwisCPVAVkkTDAFHQL---------ATVPGLdpss 307
Cdd:cd07781 229 EAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTST---CHLMV--SPKPVDIpgicgpvpdAVVPGL---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 308 YLLVNNQDTAGRALQWLRDNVFGEL------DYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTT 381
Cdd:cd07781 300 YGLEAGQSAVGDIFAWFVRLFVPPAeergdsIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 382 RADLVRAVLEGVAFNSRwllECVNRFTGNDGPIR--IVGGGA--RSDLWCQIIADVCGRTCERVADPlNAQLRGAALFAG 457
Cdd:cd07781 380 PAHIYRALLEATAFGTR---AIIERFEEAGVPVNrvVACGGIaeKNPLWMQIYADVLGRPIKVPKSD-QAPALGAAILAA 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2179559870 458 IGMG---DVDrDELRDLIPLDGVFEPIAANRAVYDRLFAEFPGLYTA 501
Cdd:cd07781 456 VAAGvyaDIE-EAADAMVRVDRVYEPDPENHAVYEELYALYKELYDA 501
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
7-461 |
3.47e-69 |
|
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: 228.66 E-value: 3.47e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKvgFVA--LDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQ 84
Cdd:cd24121 1 ILIGIDAGTSVVK--AVAfdLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 85 WASTVPVDADGRPVGPCVMWMDTRGAPFSRkafggRLQ--GYRPRAllswLRRNGGIPSPSgdDPVGHMLHLQHNDPAVS 162
Cdd:cd24121 79 GDGTWLVDEDGRPVRDAILWLDGRAADIVE-----RWQadGIAEAV----FEITGTGLFPG--SQAAQLAWLKENEPERL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 163 GAARWYLEPVDYLSMCFTGRAAA--SRASMmgAWLtdnrNLALPDYDDVLVRLAGVD--RTKLPPLVPTGSIISTVAPAV 238
Cdd:cd24121 148 ERARTALHCKDWLFYKLTGEIATdpSDASL--TFL----DFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 239 AAELGISPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSW--ISCPVAVKKTDAFHqlATVPGLDPSSYLLVNNQDT 316
Cdd:cd24121 222 AAATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVheVVVDEPDLEPEGVG--YTICLGVPGRWLRAMANMA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 317 AGRALQWLRD----------NVFGELDYDALTALAAGAPAGSNGVIFTPWLK--GEHSPIDDRNARGGFHNLSLDTTRAD 384
Cdd:cd24121 300 GTPNLDWFLRelgevlkegaEPAGSDLFQDLEELAASSPPGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRAD 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2179559870 385 LVRAVLEGVAFNSRwllECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCERVADPlNAQLRGAALFAGIGMG 461
Cdd:cd24121 380 LLRAVYEGVALAMR---DCYEHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGE-EFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
7-459 |
1.30e-65 |
|
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: 218.96 E-value: 1.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFV-ALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQW 85
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIdAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 86 ASTVPVDADGRPVGPCVMWMDTRGAPFSRKAFggRLQGYRPRALLswlrrngGIPSPSGDDpVGHMLHLQHNDPAVSGAA 165
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELT--EALGGKKCLLV-------GLNIPARFT-ASKLLWLKENEPEHYARI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 166 RWYLEPVDYLSMCFTGRAAASR--ASMMGAWLTDNRnlalpDYDDVLVRLAGVDRT---KLPPLVPTGSIISTVAPAVAA 240
Cdd:cd07809 151 AKILLPHDYLNWKLTGEKVTGLgdASGTFPIDPRTR-----DYDAELLAAIDPSRDlrdLLPEVLPAGEVAGRLTPEGAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 241 ELGISPAAQVVTGTPDLHSAAVGSGAVRQGElhLTIST-TSWISCPVAVKKTDAFHQLATVPGLDPSSYLLVNNqdTAG- 318
Cdd:cd07809 226 ELGLPAGIPVAPGEGDNMTGALGTGVVNPGT--VAVSLgTSGTAYGVSDKPVSDPHGRVATFCDSTGGMLPLIN--TTNc 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 319 --RALQWLRDnvFGELDYDALTALAAGAPAGSNGVIFTPWLKGEHSPiDDRNARGGFHNLSL-DTTRADLVRAVLEGVAF 395
Cdd:cd07809 302 ltAWTELFRE--LLGVSYEELDELAAQAPPGAGGLLLLPFLNGERTP-NLPHGRASLVGLTLsNFTRANLARAALEGATF 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2179559870 396 NsrwLLECVNRFTGNDGP---IRIVGGGARSDLWCQIIADVCGRTcERVADPLNAQLRGAALFAGIG 459
Cdd:cd07809 379 G---LRYGLDILRELGVEideIRLIGGGSKSPVWRQILADVFGVP-VVVPETGEGGALGAALQAAWG 441
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
8-461 |
1.30e-59 |
|
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: 203.22 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 8 VLAVDLGTGGPKVGFVALDGTVLwsDLVAVPTSY----GPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITG 83
Cdd:cd07798 2 YLVIDIGTGGGRCALVDSEGKIV--AIAYREWEYytddDYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 84 QWASTVPVDADGRPV--GPCvmwMDTRGapfsrKAFGGRLQGYRPRALLSwlrrnGGIPSPSGDDPVGHMLHLQHNDPAV 161
Cdd:cd07798 80 QREGIVFLDKDGRELyaGPN---IDARG-----VEEAAEIDDEFGEEIYT-----TTGHWPTELFPAARLLWFKENRPEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 162 SGAARWYLEPVDYLSMCFTGRAAASRASMMGAWLTDNRNLalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAE 241
Cdd:cd07798 147 FERIATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKR---EWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 242 LGISPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSWISCPVAVKKTDAFHQLATVPGLDPSSYLLVNNQDTAGRAL 321
Cdd:cd07798 224 LGLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVLESNAGVTGLNY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 322 QWLRDNVFG--ELDYDALTALAAGAPAGSNGVI--FTPwlkgehSPIDDRNA---RGGFH----NLSLDTTRADLVRAVL 390
Cdd:cd07798 304 QWLKELLYGdpEDSYEVLEEEASEIPPGANGVLafLGP------QIFDARLSglkNGGFLfptpLSASELTRGDFARAIL 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2179559870 391 EGVAFNSRWLLECVNRFTGNDGP-IRIVGGGARSDLWCQIIADVCGRTCeRVADPLNAQLRGAALFAGIGMG 461
Cdd:cd07798 378 ENIAFAIRANLEQLEEVSGREIPyIILCGGGSRSALLCQILADVLGKPV-LVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
8-494 |
2.78e-37 |
|
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: 143.47 E-value: 2.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 8 VLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWAS 87
Cdd:cd07793 2 ILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 88 TVPVDAD-GRPVGPCVMWMDTRGAPFSRK--------------AFGGRLQGYRPRALLSWLRRNGGIPSPsgddpvgHML 152
Cdd:cd07793 82 FLTWDKKtGKPLHNFITWQDLRAAELCESwnrslllkalrggsKFLHFLTRNKRFLAASVLKFSTAHVSI-------RLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 153 HLQHNDPAVSGAAR-----------WylepvdyLSMCFTGRAA----ASRASMMGAWltdnrNLALPDYDDVLVRLAGVD 217
Cdd:cd07793 155 WILQNNPELKEAAEkgellfgtidtW-------LLWKLTGGKVhatdYSNASATGLF-----DPFTLEWSPILLSLFGIP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 218 RTKLPPLVPTGSIISTVAPAV-AAELgisPAAQVVTgtpDLHSAAVGSGAVRQGELHLTISTTSWISC-----PVAVKkt 291
Cdd:cd07793 223 SSILPEVKDTSGDFGSTDPSIfGAEI---PITAVVA---DQQAALFGECCFDKGDVKITMGTGTFIDIntgskPHASV-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 292 dafHQLATVPGL---DPSSYLLVNNQDTAGRALQWLRDnvFGELDYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRN 368
Cdd:cd07793 295 ---KGLYPLVGWkigGEITYLAEGNASDTGTVIDWAKS--IGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 369 ARGGFHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGND-GPIRIVGGGARSDLWCQIIADVCGRTCERVADpLNA 447
Cdd:cd07793 370 ACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKiSSIRVDGGVSNNDFILQLIADLLGKPVERPKN-TEM 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2179559870 448 QLRGAALFAGIGMGD-VDRDELRDLIPLDGVFEPiAANRAVYDRLFAE 494
Cdd:cd07793 449 SALGAAFLAGLASGIwKSKEELKKLRKIEKIFEP-KMDNEKREELYKN 495
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
8-480 |
9.76e-36 |
|
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: 139.14 E-value: 9.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 8 VLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWAS 87
Cdd:cd07769 2 ILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 88 TVPVDAD-GRPVGPCVMWMDTRGAPFSRKafggrlqgYRPRALLSWLRRNGGipspsgddpvghmLHLqhnDPAVSGA-A 165
Cdd:cd07769 82 TVVWDKKtGKPLYNAIVWQDRRTADICEE--------LKAKGLEERIREKTG-------------LPL---DPYFSATkI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 166 RWYLEPVDylsmcfTGRAAASRASM----MGAWL-----------TD--N--R----NLALPDYDDVLVRLAGVDRTKLP 222
Cdd:cd07769 138 KWILDNVP------GARERAERGELlfgtIDTWLiwkltggkvhvTDvtNasRtmlfNIHTLEWDDELLELFGIPRSMLP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 223 PLVPTGSIISTVAPA-------VAAELGispaaqvvtgtpDLHSAAVGSGAVRQGELHLTISTTSWISCPVAVKKTDAFH 295
Cdd:cd07769 212 EVRPSSEVFGYTDPEglgagipIAGILG------------DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 296 QLATVPGL---DPSSYLLVNNQDTAGRALQWLRDNVFGELDYDALTALAAGAPaGSNGVIFTPWLKGEHSPIDDRNARGG 372
Cdd:cd07769 280 GLLTTIAWqigGKVTYALEGSIFIAGAAIQWLRDNLGLIEDAAETEELARSVE-DNGGVYFVPAFSGLGAPYWDPDARGA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 373 FHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGNDGP-IRIVGGGARSDLWCQIIADVCGRTCERvadPLNAQL-- 449
Cdd:cd07769 359 IVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKeLRVDGGATANNFLMQFQADILGVPVVR---PKVAETta 435
|
490 500 510
....*....|....*....|....*....|...
gi 2179559870 450 RGAALFAGIGMG--DvDRDELRDLIPLDGVFEP 480
Cdd:cd07769 436 LGAAYLAGLAVGfwK-DLDELASLWQVDKRFEP 467
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
9-499 |
3.20e-35 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 137.41 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 9 LAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGdqVAGVSITGQWAST 88
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQD--VKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 89 VPVDADGRPVGPCVMWMDTRGA----------PFSRKAFGGRLQGyrprallswlrrngGIPSPSgddpvghMLHLQHND 158
Cdd:PRK15027 81 TLLDAQQRVLRPAILWNDGRCAqecallearvPQSRVITGNLMMP--------------GFTAPK-------LLWVQRHE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 159 PAVSGAARWYLEPVDYLSMCFTGRAAASRASMMGA-WLtdnrNLALPDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPA 237
Cdd:PRK15027 140 PEIFRQIDKVLLPKDYLRLRMTGEFASDMSDAAGTmWL----DVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 238 VAAELGIsPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTS---WISCPVAVKKTDAFHQLATVPgldPSSYLLVNNQ 314
Cdd:PRK15027 216 VAKAWGM-ATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGvyfAVSEGFLSKPESAVHSFCHAL---PQRWHLMSVM 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 315 DTAGRALQWLRdNVFGELDYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVA 394
Cdd:PRK15027 292 LSAASCLDWAA-KLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 395 FNSRWLLECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCG-----RTCERVADPLnaqlrGAALFAGIGMG-DVDRDEL 468
Cdd:PRK15027 371 YALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGqqldyRTGGDVGPAL-----GAARLAQIAANpEKSLIEL 445
|
490 500 510
....*....|....*....|....*....|.
gi 2179559870 469 RDLIPLDGVFEPIAANRAVYDRLFAEFPGLY 499
Cdd:PRK15027 446 LPQLPLEQSHLPDAQRYAAYQPRRETFRRLY 476
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
55-495 |
6.60e-33 |
|
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: 130.92 E-value: 6.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 55 WAIIRDATRRGLAESRVRGDQVAGVSITGQWASTVPVDADGRPVGPCVMwMDTRGAPfsrkafggrlQGYRPRALLSWL- 133
Cdd:cd07775 51 WKLICECIREALKKAGIAPKSIAAISTTSMREGIVLYDNEGEEIWACAN-VDARAAE----------EVSELKELYNTLe 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 134 ----RRNGGIPSpSGDDPvgHMLHLQHNDPAVSGAArWYLEPV-DYLSMCFTGRAAA--SRASMMGAWLTDNRNlalpdY 206
Cdd:cd07775 120 eevyRISGQTFA-LGAIP--RLLWLKNNRPEIYRKA-AKITMLsDWIAYKLSGELAVepSNGSTTGLFDLKTRD-----W 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 207 DDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGISPAAQVVTGTPDLHSAAVGSGAVRQGELHLTISTTSWISCPV 286
Cdd:cd07775 191 DPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 287 AVKKTDAFHQLATVPGLDPSsylLVNNQDTA---GRALQWLRDNVFGEL----------DYDALTALAAGAPAGSNGVI- 352
Cdd:cd07775 271 AAPVTDPAMNIRVNCHVIPD---MWQAEGISffpGLVMRWFRDAFCAEEkeiaerlgidAYDLLEEMAKDVPPGSYGIMp 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 353 -------FTPWlkgehspiddRNARGGFHNLSLD---TTRADLVRAVLEGVAFNSRWLLECVNRFTGNDgPIRIV--GGG 420
Cdd:cd07775 348 ifsdvmnYKNW----------RHAAPSFLNLDIDpekCNKATFFRAIMENAAIVSAGNLERIAEFSGIF-PDSLVfaGGA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2179559870 421 ARSDLWCQIIADVCGRTCeRVADPLNAQLRGAALFAGIGMGDVD--RDELRDLIPLDGVFEPIAANRAVYDRLFAEF 495
Cdd:cd07775 417 SKGKLWCQILADVLGLPV-KVPVVKEATALGAAIAAGVGAGIYSslEEAVESLVKWEREYLPNPENHEVYQDLYEKW 492
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
6-493 |
1.26e-32 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 130.18 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 6 RVVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSY-GPGgaAV-QDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITG 83
Cdd:COG0554 3 KYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYpQPG--WVeHDPEEIWESVLAVIREALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 84 QWASTVPVD-ADGRPVGPCVMWMDTRGAPFSRKafggrlqgYRPRALLSWLRRNGGIPspsgddpvghmlhlqhNDPAVS 162
Cdd:COG0554 81 QRETTVVWDrKTGKPLYNAIVWQDRRTADICEE--------LKADGLEDLIREKTGLV----------------LDPYFS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 163 GA-ARWYLEPVD------------------YLSMCFTGRAA-------ASRASMMgawltDNRNLalpDYDDVLVRLAGV 216
Cdd:COG0554 137 ATkIKWILDNVPgareraeagellfgtidsWLIWKLTGGKVhvtdvtnASRTMLF-----NIHTL---DWDDELLELFGI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 217 DRTKLPPLVPTGSIISTVAPAV-AAELGISPAAqvvtGtpDLHSAAVGSGAVRQGELHLTISTTSWI-----SCPVAVKk 290
Cdd:COG0554 209 PRSMLPEVRPSSEVFGETDPDLfGAEIPIAGIA----G--DQQAALFGQACFEPGMAKNTYGTGCFLlmntgDEPVRSK- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 291 tdafHQLATVPGL---DPSSYLLVNNQDTAGRALQWLRDNVfgEL--DYDALTALAAGAPaGSNGVIFTPWLKGEHSPID 365
Cdd:COG0554 282 ----NGLLTTIAWglgGKVTYALEGSIFVAGAAVQWLRDGL--GLidSAAESEALARSVE-DNGGVYFVPAFTGLGAPYW 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 366 DRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGND-GPIRIVGGGARSDLWCQIIADVCGRTCERvadP 444
Cdd:COG0554 355 DPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPlKELRVDGGASANDLLMQFQADILGVPVER---P 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2179559870 445 LNAQL--RGAALFAGIGMGD-VDRDELRDLIPLDGVFEPiAANRAVYDRLFA 493
Cdd:COG0554 432 KVTETtaLGAAYLAGLAVGFwKSLEELAALWKVDRRFEP-QMDEEERERLYA 482
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
8-493 |
2.48e-32 |
|
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: 129.15 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 8 VLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWAS 87
Cdd:cd07786 2 ILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 88 TVPVDAD-GRPVGPCVMWMDTRGAPFSRKAfggRLQGYrpralLSWLRRNGGipspsgddpvghmLHLqhnDPAVSGA-A 165
Cdd:cd07786 82 TVVWDREtGKPVYNAIVWQDRRTADICEEL---KAEGH-----EEMIREKTG-------------LVL---DPYFSATkI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 166 RWYLEPVD------------------YLSMCFTGRAA-------ASRASMMgawltdnrNLALPDYDDVLVRLAGVDRTK 220
Cdd:cd07786 138 RWILDNVPgareraergelafgtidsWLIWKLTGGKVhatdvtnASRTMLF--------NIHTLEWDDELLELFGIPASM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 221 LPPLVPTGSIISTVAPAVA-AELGISPAAqvvtGtpDLHSAAVGSGAVRQGELHLTISTTSWI-----SCPVAVKktdaf 294
Cdd:cd07786 210 LPEVKPSSEVFGYTDPDLLgAEIPIAGIA----G--DQQAALFGQACFEPGMAKNTYGTGCFMlmntgEKPVRSK----- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 295 HQLATVPGL---DPSSYLLVNNQDTAGRALQWLRDNVfgELDYDAL--TALAAGAPaGSNGVIFTPWLKGEHSPIDDRNA 369
Cdd:cd07786 279 NGLLTTIAWqlgGKVTYALEGSIFIAGAAVQWLRDGL--GLIESAAetEALARSVP-DNGGVYFVPAFTGLGAPYWDPDA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 370 RGGFHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGND-GPIRIVGGGARSDLWCQIIADVCGRTCERvadPLNAQ 448
Cdd:cd07786 356 RGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPlKELRVDGGASANDFLMQFQADILGVPVER---PKVTE 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2179559870 449 L--RGAALFAGIGMGdV--DRDELRDLIPLDGVFEPiAANRAVYDRLFA 493
Cdd:cd07786 433 TtaLGAAYLAGLAVG-LwkSLDELAKLWQVDRRFEP-SMSEEEREALYA 479
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
8-472 |
1.48e-31 |
|
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: 126.49 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 8 VLAVDLGTGGPKVGFVALDGTVLwsDLVAV---PTsygpgGAAVQDAGLWWAI--IRDATRRGLAESRVRGDQVAGVSIT 82
Cdd:cd07771 2 YLAVDLGASSGRVILGSLDGGKL--ELEEIhrfPN-----RPVEINGHLYWDIdrLFDEIKEGLKKAAEQGGDIDSIGID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 83 GqWAST-VPVDADGRPVGPCVMWMDTRGAPFSRKAFggrlQGYRPRALLswlRRNGGIPSPSgdDPVGHMLHLQHNDPAV 161
Cdd:cd07771 75 T-WGVDfGLLDKNGELLGNPVHYRDPRTEGMMEELF----EKISKEELY---ERTGIQFQPI--NTLYQLYALKKEGPEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 162 SGAARWYLEPVDYLSMCFTGRAAASR--ASMMGawLTDNRNLalpDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVA 239
Cdd:cd07771 145 LERADKLLMLPDLLNYLLTGEKVAEYtiASTTQ--LLDPRTK---DWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 240 AELGISPAAQVVTGTPDLHSAAVGSGAVRQGELHltISTTSW----ISCPVAVKKTDAFHQLATVPGLDPSSYLLVNNQd 315
Cdd:cd07771 220 EELGLKGIPVIAVASHDTASAVAAVPAEDEDAAF--ISSGTWsligVELDEPVITEEAFEAGFTNEGGADGTIRLLKNI- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 316 tAGRAL------QWLRDNVfgELDYDALTALAAGAPagSNGVIFtpwlkgehSPIDDRNARGG-----------FHNLSL 378
Cdd:cd07771 297 -TGLWLlqecrrEWEEEGK--DYSYDELVALAEEAP--PFGAFI--------DPDDPRFLNPGdmpeairaycrETGQPV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 379 DTTRADLVRAVLEGVAFNSRWLLECVNRFTGND-GPIRIVGGGARSDLWCQIIADVCGRTCerVADPLNAQLRGAALFAG 457
Cdd:cd07771 364 PESPGEIARCIYESLALKYAKTIEELEELTGKRiDRIHIVGGGSRNALLCQLTADATGLPV--IAGPVEATAIGNLLVQL 441
|
490
....*....|....*.
gi 2179559870 458 IGMGDV-DRDELRDLI 472
Cdd:cd07771 442 IALGEIkSLEEGRELV 457
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
7-263 |
2.22e-31 |
|
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: 121.29 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQWA 86
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 87 STVPVDADGRPVGPCVMWMDTRGAPFSRKAfggRLQGYRPRallswLRRNGGIPSPSGdDPVGHMLHLQHNDPAVSGAAR 166
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENL---KEEGNNQK-----LYEITGLPIWPG-FTLSKLRWIKENEPEVFEKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 167 WYLEPVDYLSMCFTGRAA-----ASRASMMgawltdnrNLALPDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAE 241
Cdd:pfam00370 152 KFLTIHDYLRWRLTGVFVtdhtnASRSMMF--------NIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAM 223
|
250 260
....*....|....*....|..
gi 2179559870 242 LGISPAAQVVTGTPDLHSAAVG 263
Cdd:pfam00370 224 WGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
7-456 |
7.53e-31 |
|
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: 124.26 E-value: 7.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTggPKVGFVALD---GTVLwsDLVAVPTSYG----PGGAAVQDAGLWWAIIRDATRRGLAESRVRgdqVAGV 79
Cdd:cd07777 1 NVLGIDIGT--TSIKAALLDlesGRIL--ESVSRPTPAPissdDPGRSEQDPEKILEAVRNLIDELPREYLSD---VTGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 80 SITGQWASTVPVDADGRPVGPCVMWMDTRGApfsrKAFGGRLQGYRPrallsWLRRNGGIPSPSGdDPVGHMLHLQHNDP 159
Cdd:cd07777 74 GITGQMHGIVLWDEDGNPVSPLITWQDQRCS----EEFLGGLSTYGE-----ELLPKSGMRLKPG-YGLATLFWLLRNGP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 160 AVSGAARWYLEPvDYLSMCFTGRA--------AASrasmMGAWltdnrNLALPDYDDVLVRLAGVDRTKLPPLVPTGSII 231
Cdd:cd07777 144 LPSKADRAGTIG-DYIVARLTGLPkpvmhptnAAS----WGLF-----DLETGTWNKDLLEALGLPVILLPEIVPSGEIV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 232 STVAPAVAAelGISpaaqVVTGTPDlHSAAV-GSGAVRQGELHLTISTTSWIScpVAVKKTDAFHQLATVPGLDpSSYLL 310
Cdd:cd07777 214 GTLSSALPK--GIP----VYVALGD-NQASVlGSGLNEENDAVLNIGTGAQLS--FLTPKFELSGSVEIRPFFD-GRYLL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 311 VNNQDTAGRALQWLRD-------NVFGELDYDALTA--LAAGAPAGSNGVIFTPWLKGE-HSPiddrNARGGFHNLSLD- 379
Cdd:cd07777 284 VAASLPGGRALAVLVDflrewlrELGGSLSDDEIWEklDELAESEESSDLSVDPTFFGErHDP----EGRGSITNIGESn 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 380 TTRADLVRAVLEGVAFNsrwLLECVNRFTGNDGPI-RIVG-GGA--RSDLWCQIIADVCGRTCERVADPLNAqLRGAALF 455
Cdd:cd07777 360 FTLGNLFRALCRGIAEN---LHEMLPRLDLDLSGIeRIVGsGGAlrKNPVLRRIIEKRFGLPVVLSEGSEEA-AVGAALL 435
|
.
gi 2179559870 456 A 456
Cdd:cd07777 436 A 436
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
301-460 |
2.58e-28 |
|
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: 111.26 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 301 PGLDPSSYLLVNNQDTAGRALQWLRDNVF---------GELDYDALTALAAGAPAGsnGVIFTPWLKGEHSPIDDRNARG 371
Cdd:pfam02782 31 NEMLPGYWGLEGGQSAAGSLLAWLLQFHGlreelrdagNVESLAELAALAAVAPAG--GLLFYPDFSGNRAPGADPGARG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 372 GFHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGNDG-PIRIVGGGARSDLWCQIIADVCGRTCErVADPLNAQLR 450
Cdd:pfam02782 109 SITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIdTIHVSGGGSRNPLLLQLLADALGLPVV-VPGPDEATAL 187
|
170
....*....|
gi 2179559870 451 GAALFAGIGM 460
Cdd:pfam02782 188 GAALLAAVAA 197
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
55-505 |
2.77e-28 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 117.80 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 55 WAIIRDATRRGLAESRVRGDQVAGVSITGQWASTVPVDADGRPVGPC----------VMWMDTRGAPFSRKAFGGRLQGY 124
Cdd:PRK10939 54 WQLACQCIRQALQKAGIPASDIAAVSATSMREGIVLYDRNGTEIWACanvdarasreVSELKELHNNFEEEVYRCSGQTL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 125 rprALlswlrrnGGIPspsgddpvgHMLHLQHNDPAVSGAARWYLEPVDYLSMCFTGRAAA--SRASMMGAWltdnrNLA 202
Cdd:PRK10939 134 ---AL-------GALP---------RLLWLAHHRPDIYRQAHTITMISDWIAYMLSGELAVdpSNAGTTGLL-----DLV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 203 LPDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGISPAAQVVTGTPDLHSAAVGSGAVRQGELhLTISTTSWi 282
Cdd:PRK10939 190 TRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQT-AVLGGTFW- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 283 scpvavkktdafHQLATVPG--LDPSSYLLVN-------NQDTA-----GRALQWLRDNVFGELD----------YDALT 338
Cdd:PRK10939 268 ------------QQVVNLPApvTDPNMNIRINphvipgmVQAESisfftGLTMRWFRDAFCAEEKllaerlgidaYSLLE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 339 ALAAGAPAGSNGVI--------FTPWlkgehspiddRNARGGFHNLSLD---TTRADLVRAVLEGVAFNSRWLLECVNRF 407
Cdd:PRK10939 336 EMASRVPVGSHGIIpifsdvmrFKSW----------YHAAPSFINLSIDpekCNKATLFRALEENAAIVSACNLQQIAAF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 408 TGNDgPIRIV--GGGARSDLWCQIIADVCGRTCeRVADPLNAQLRGAALFAGIGMGDVDR--DELRDLIPLDGVFEPIAA 483
Cdd:PRK10939 406 SGVF-PSSLVfaGGGSKGKLWSQILADVTGLPV-KVPVVKEATALGCAIAAGVGAGIYSSlaETGERLVRWERTFEPNPE 483
|
490 500
....*....|....*....|..
gi 2179559870 484 NRAVYDRLFAEFPGLYTAQKAM 505
Cdd:PRK10939 484 NHELYQEAKEKWQAVYADQLGL 505
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
57-499 |
4.16e-25 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 108.78 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 57 IIRDATRRGLAESRVRGDQVAGVSI--TGqwaST-VPVDADGRPVgpC-------------VMWMD-------------- 106
Cdd:PRK04123 61 SLEAAIPAVLKEAGVDPAAVVGIGVdfTG---STpAPVDADGTPL--AllpefaenphamvKLWKDhtaqeeaeeinrla 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 107 -TRGAPFsrkafggrlqgyrprallsWLRRNGGIPS-----PSgddpvghMLHLQHNDPAVSGAARWYLEPVDYLSMCFT 180
Cdd:PRK04123 136 hERGEAD-------------------LSRYIGGIYSsewfwAK-------ILHVLREDPAVYEAAASWVEACDWVVALLT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 181 GRAAA-----SRASMMGAWLTDNRNLALPDYD---DVLVRLAGVDRTKLP-PLVPTGSIISTVAPAVAAELGISPAAQVV 251
Cdd:PRK04123 190 GTTDPqdivrSRCAAGHKALWHESWGGLPSADffdALDPLLARGLRDKLFtETWTAGEPAGTLTAEWAQRLGLPEGVAVS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 252 TGTPDLHSAAVGSGAvRQGELHLTISTTSwisCPVAVKKtdafhQLATVPGL----D----PSSYLLVNNQDTAGRALQW 323
Cdd:PRK04123 270 VGAFDAHMGAVGAGA-EPGTLVKVMGTST---CDILLAD-----KQRAVPGIcgqvDgsivPGLIGYEAGQSAVGDIFAW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 324 LRDNV-----------FGELDYDALTALAAGAPAGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEG 392
Cdd:PRK04123 341 FARLLvppeykdeaeaRGKQLLELLTEAAAKQPPGEHGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 393 VAFNSRWLLECvnrFTGNDGPIR--IVGGG--ARSDLWCQIIADVCGRTCERVADPLNAQLrGAALFAGIGMGDVDrdel 468
Cdd:PRK04123 421 TAFGTRAIMEC---FEDQGVPVEevIAAGGiaRKNPVLMQIYADVLNRPIQVVASDQCPAL-GAAIFAAVAAGAYP---- 492
|
490 500 510
....*....|....*....|....*....|....*....
gi 2179559870 469 rDLI--------PLDGVFEPIAANRAVYDRLFAEFPGLY 499
Cdd:PRK04123 493 -DIPeaqqamasPVEKTYQPDPENVARYEQLYQEYKQLH 530
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
69-461 |
8.26e-25 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 107.04 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 69 SRVRGDQVAGVSITGQWASTVPVDADGRPVGPCVMWMDTRGAPFSRKafggrLQGYRPRALLSwlRRNGgipspsgddpV 148
Cdd:PRK10331 65 SELTECHIRGITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMEN-----IERYISAQQLQ--QISG----------V 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 149 GH--------MLHLQHNDPAVSGAARWYLEPVDYLSMCFTGRAAASRA----SMMgawltdnRNLALPDYDDVLVRLAGV 216
Cdd:PRK10331 128 GAfsfntlykLVWLKENHPQLLEQAHAWLFISSLINHRLTGEFTTDITmagtSQM-------LDIQQRDFSPEILQATGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 217 DRTKLPPLVPTGSIISTVAPAVAAELGISPAAQVVTGTPDLHSAAVGSGAvrqGELHLTISTTSW----ISCPVAVKKTD 292
Cdd:PRK10331 201 SRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISAGHDTQFALFGSGA---GQNQPVLSSGTWeilmVRSAQVDTSLL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 293 AFHQLATVPgLDPSSYLLvnN---QDTAGRALQWLRDNVF-GELDYDALTALAAGAPAGSNGVIFTPWLkgehspidDRN 368
Cdd:PRK10331 278 SQYAGSTCE-LDSQSGLY--NpgmQWLASGVLEWVRKLFWtAETPYQTMIEEARAIPPGADGVKMQCDL--------LAC 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 369 ARGGFHNLSLDTTRADLVRAVLEGVAFNSRW---LLECVNRFtgNDGPIRIVGGGARSDLWCQIIADVCGRTCeRVADPL 445
Cdd:PRK10331 347 QNAGWQGVTLNTTRGHFYRAALEGLTAQLKRnlqVLEKIGHF--KASELLLVGGGSRNALWNQIKANMLDIPI-KVLDDA 423
|
410
....*....|....*.
gi 2179559870 446 NAQLRGAALFAGIGMG 461
Cdd:PRK10331 424 ETTVAGAAMFGWYGVG 439
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
185-481 |
1.22e-23 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 103.90 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 185 ASRASMMgawltdnrNLALPDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAEL-GISPAAqvVTGtpDLHSAAVG 263
Cdd:PTZ00294 187 ASRTFLM--------NIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPLLeGVPITG--CIG--DQQAALIG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 264 SGAVRQGELHLTISTTSWISCPVAVKKTDAFHQLATVPGL-----DPSSYLLVNNQDTAGRALQWLRDNVFGELDYDALT 338
Cdd:PTZ00294 255 HGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYqlgpnGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 339 ALAAGAPaGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGNDGP-IRIV 417
Cdd:PTZ00294 335 KLARSVK-DTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNsLRVD 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2179559870 418 GGGARSDLWCQIIADVCGRTCERvadPLNAQLR--GAALFAGIGMGdV--DRDELRDLI-PLDGVFEPI 481
Cdd:PTZ00294 414 GGLTKNKLLMQFQADILGKDIVV---PEMAETTalGAALLAGLAVG-VwkSLEEVKKLIrRSNSTFSPQ 478
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
7-480 |
8.56e-23 |
|
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: 101.45 E-value: 8.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIR---DATRRGLAESRVRGDQVAGVSITG 83
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYeciEEAVEKLKALGISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 84 QWASTVPVDAD-GRPVGPCVMWMDTRGAP----FSRKAFGGRLQgYRPR----------AL-LSWLRRNggipspsgddp 147
Cdd:cd07792 82 QRETTVVWDKStGKPLYNAIVWLDTRTSDtveeLSAKTPGGKDH-FRKKtglpistyfsAVkLRWLLDN----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 148 vghmlhlqhnDPAVSGAAR-----------WYLepvdylsMCFTGRAA----------ASRASMMgawltDNRNLalpDY 206
Cdd:cd07792 150 ----------VPEVKKAVDdgrllfgtvdsWLI-------WNLTGGKNggvhvtdvtnASRTMLM-----NLRTL---QW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 207 DDVLVRLAGVDRTKLPPLVPTGSIISTVAPAVAAELGISPaaqvVTGtpDLHSAAVGSGAVRQGELHLTISTTSWISCPV 286
Cdd:cd07792 205 DPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAGVPISG----CLG--DQQAALVGQGCFKPGEAKNTYGTGCFLLYNT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 287 AVKKTDAFHQLATVPGldpssYLLVNNQDT----------AGRALQWLRDNVFGELDYDALTALAAGAPaGSNGVIFTPW 356
Cdd:cd07792 279 GEEPVFSKHGLLTTVA-----YKLGPDAPPvyalegsiaiAGAAVQWLRDNLGIISSASEVETLAASVP-DTGGVYFVPA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 357 LKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGndGPIRI--VGGGA-RSDLWCQIIADV 433
Cdd:cd07792 353 FSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSG--IPLTSlrVDGGMtKNNLLMQIQADI 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2179559870 434 CGRTCERVADPLNAQLrGAALFAGIGMGDVDRDELRDLIPLDG--VFEP 480
Cdd:cd07792 431 LGIPVERPSMVETTAL-GAAIAAGLAVGVWKSLDELKSLNEGGrtVFEP 478
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
55-480 |
2.99e-22 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 99.51 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 55 WAIIRDATRRGLAESRVRGDQVAGVSITGQWASTVPVDAD-GRPVGPCVMWMDTRGAPFSRKAfggRLQGYRPrallsWL 133
Cdd:PRK00047 54 WASQLSVIAEALAKAGISPDQIAAIGITNQRETTVVWDKEtGRPIYNAIVWQDRRTADICEEL---KRDGYED-----YI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 134 RRNGGIPSpsgddpvghmlhlqhnDPAVSGA-ARWYLEPVD------------------YLSMCFTGRAA-------ASR 187
Cdd:PRK00047 126 REKTGLVI----------------DPYFSGTkIKWILDNVEgareraekgellfgtidtWLVWKLTGGKVhvtdytnASR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 188 ASMMgawltdnrNLALPDYDDVLVRLAGVDRTKLPPLVPTGSIISTVAPA--VAAELGISPAAqvvtGtpDLHSAAVGSG 265
Cdd:PRK00047 190 TMLF--------NIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgfFGGEVPIAGIA----G--DQQAALFGQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 266 AVRQGELHLTISTTSWISCPVAVKKTDAFHQLATVP--GLD-PSSYLLVNNQDTAGRALQWLRDNVfgELDYDALT--AL 340
Cdd:PRK00047 256 CFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIawGIDgKVVYALEGSIFVAGSAIQWLRDGL--KIISDASDseAL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 341 AAGAPaGSNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGNDGP-IRIVGG 419
Cdd:PRK00047 334 ARKVE-DNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKeLRVDGG 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2179559870 420 GARSDLWCQIIADVCGRTCERvadPLNAQL--RGAALFAGIGMGD-VDRDELRDLIPLDGVFEP 480
Cdd:PRK00047 413 AVANNFLMQFQADILGVPVER---PVVAETtaLGAAYLAGLAVGFwKDLDELKEQWKIDRRFEP 473
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
7-499 |
3.78e-21 |
|
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: 96.54 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGA--AVQDAGLWWAIIRDATRRGLAESRVRGDQVAGVSITGQ 84
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYAGLEMAQEPVPYYQDSSKKSwkFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 85 wASTVPVDADGRPV-----GP----CVMWMDTRGAPFSRkafggRLQGYRPRALLSWLrrnGGIPSPSGDDPvgHMLHLQ 155
Cdd:cd07768 81 -CSLAIFDREGTPLmalipYPnednVIFWMDHSAVNEAQ-----WINMQCPQQLLDYL---GGKISPEMGVP--KLKYFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 156 HNDPAVSGAARWYLEPVDYLSMCFTGRAAASRASMMGAWLTDNRNlALPD---YDDVLVRLAGVDRTKL-PPLVPTGSII 231
Cdd:cd07768 150 DEYSHLRDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEE-SGWSssfFKNIDPRLEHLTTTKNlPSNVPIGTTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 232 STVAPAVAAELGISPAAQVVTGTPDLHSAAVG-SGAVRQGELHLTISTTSwisCPVAVKKTDAFhqlatVPG-------- 302
Cdd:cd07768 229 GVALPEMAEKMGLHPGTAVVVSCIDAHASWFAvASPHLETSLFMIAGTSS---CHMYGTTISDR-----IPGvwgpfdti 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 303 LDPSSYLLVNNQDTAGRALQWL---------RDNVF--GELDYDALTALA---AGAPAGSNGVIFTPWLKGEHSPIDDRN 368
Cdd:cd07768 301 IDPDYSVYEAGQSATGKLIEHLfeshpcarkFDEALkkGADIYQVLEQTIrqiEKNNGLSIHILTLDMFFGNRSEFADPR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 369 ARGGFHNLSLDTTRADLV---RAVLEGVAFNSRWLLECVNRFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCeRVADPL 445
Cdd:cd07768 381 LKGSFIGESLDTSMLNLTykyIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAI-IKPKEN 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2179559870 446 NAQLRGAALFAGIGMGdvdRDELRDLIP--------LDGVFEPIAAN-RAVYDRLFAEFPGLY 499
Cdd:cd07768 460 MMGILGAAVLAKVAAG---KKQLADSITeadisndrKSETFEPLAYRlGADYILLYKLLCVKY 519
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
8-480 |
2.31e-19 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 90.91 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 8 VLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLWWAIIRDATRRGLAESRVRGDQVAG----VSITG 83
Cdd:PLN02295 2 VGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDSglkaIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 84 QWASTVP-VDADGRPVGPCVMWMDTRGAPFSRK----AFGGRlqgyrprallSWLRRNGGIP-SP--SGddpvGHMLHLQ 155
Cdd:PLN02295 82 QRETTVAwSKSTGRPLYNAIVWMDSRTSSICRRlekeLSGGR----------KHFVETCGLPiSTyfSA----TKLLWLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 156 HNDPAVSGAAR-----------WylepvdyLSMCFTGRAA----------ASRASMMgawltdnrNLALPDYDDVLVRLA 214
Cdd:PLN02295 148 ENVDAVKEAVKsgdalfgtidsW-------LIWNLTGGASggvhvtdvtnASRTMLM--------NLKTLDWDKPTLEAL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 215 GVDRTKLPPLVPTGSIISTVAP-------AVAAELGispaaqvvtgtpDLHSAAVGSGAvRQGELHLTISTTSWISCPVA 287
Cdd:PLN02295 213 GIPAEILPKIVSNSEVIGTIAKgwplagvPIAGCLG------------DQHAAMLGQRC-RPGEAKSTYGTGCFILLNTG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 288 VKKTDAFHQLATVP----GLD-PSSYLLVNNQDTAGRALQWLRDNVFGELDYDALTALAAGAPAgSNGVIFTPWLKGEHS 362
Cdd:PLN02295 280 EEVVPSKHGLLTTVayklGPDaPTNYALEGSVAIAGAAVQWLRDNLGIIKSASEIEALAATVDD-TGGVYFVPAFSGLFA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 363 PIDDRNARGGFHNLSLDTTRADLVRAVLEGVAFNSRWLLECVNRFTGNDGP------IRIVGGGARSDLWCQIIADVCGR 436
Cdd:PLN02295 359 PRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKShkglflLRVDGGATANNLLMQIQADLLGS 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2179559870 437 TCERVADpLNAQLRGAALFAGIGMGD-VDRDEL-RDLIPLDGVFEP 480
Cdd:PLN02295 439 PVVRPAD-IETTALGAAYAAGLAVGLwTEEEIFaSEKWKNTTTFRP 483
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
8-437 |
3.58e-19 |
|
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: 90.29 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 8 VLAVDLGTGGPKVGFVALDGTVLwsdlvavptsygpgGAAVQDAGLW--------------WAIIRDATRRGLAESRVRG 73
Cdd:cd07782 2 YIGVDVGTGSARAGLFDLDGRLL--------------ATASQPITTWnpkpdfyeqssediWQAVCEAVKEVLEGAGVDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 74 DQVAGVSITGQwASTVPVDADGRPVGP---------CVMWMDTRGAPFSRK--AFGGRLqgyrprallswLRRNGGIPSP 142
Cdd:cd07782 68 EQVKGIGFDAT-CSLVVLDAEGKPVSVspsgddernVILWMDHRAVEEAERinATGHEV-----------LKYVGGKISP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 143 SGDDPvgHMLHLQHNDPAV-SGAARWYLEPvDYLSMCFTGRAAASRASMMGAWLTDNRNLALPDYDDVLVRLAGVD---- 217
Cdd:cd07782 136 EMEPP--KLLWLKENLPETwAKAGHFFDLP-DFLTWKATGSLTRSLCSLVCKWTYLAHEGSEGGWDDDFFKEIGLEdlve 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 218 -------RTKLPPLVPTGSIIStvaPAVAAELGISPAAQVVTGTPDLHSAAVGS-GAVRQGELHLT---------ISTTS 280
Cdd:cd07782 213 dnfakigSVVLPPGEPVGGGLT---AEAAKELGLPEGTPVGVSLIDAHAGGLGTlGADVGGLPCEAdpltrrlalICGTS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 281 wiSCPVAVKKTDAFhqlatVPG--------LDPSSYLLVNNQDTAGRALQWL------------RDNVFGELDYDALTAL 340
Cdd:cd07782 290 --SCHMAVSPEPVF-----VPGvwgpyysaMLPGLWLNEGGQSATGALLDHIiethpaypelkeEAKAAGKSIYEYLNER 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 341 ------AAGAPAG--SNGVIFTPWLKGEHSPIDDRNARGGFHNLSLDTTRADLVR---AVLEGVAFNSRWLLECVNRftg 409
Cdd:cd07782 363 leqlaeEKGLPLAylTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNA--- 439
|
490 500 510
....*....|....*....|....*....|.
gi 2179559870 410 NDGPIRIV---GGGARSDLWCQIIADVCGRT 437
Cdd:cd07782 440 AGHKIDTIfmcGGLSKNPLFVQLHADVTGCP 470
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
179-491 |
8.69e-14 |
|
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: 73.75 E-value: 8.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 179 FTGRAA---ASRASMMGAWltdnrNLALPDYDDVLVRLAGVD--RTKLPPLVPTGSIISTVAPAVAAELGISPAAQVVTG 253
Cdd:cd07776 196 LLGRYApidESDGSGMNLM-----DIRSRKWSPELLDAATAPdlKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAF 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 254 TPDlHSAAVGSGAVRQGELhlTIST-TS-----WISCPVAVKKTDAF-HqlatvPgLDPSSY--LLV--NnqdtAGRALQ 322
Cdd:cd07776 271 TGD-NPASLAGLGLEPGDV--AVSLgTSdtvflVLDEPKPGPEGHVFaN-----P-VDPGSYmaMLCykN----GSLARE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 323 WLRDNvFGELDYDALTALAAGAPAGSNGVIFTPWLKGE---HSPIDDRNARGGFHNLSLDTTRADlVRAVLEG----VAF 395
Cdd:cd07776 338 RVRDR-YAGGSWEKFNELLESTPPGNNGNLGLYFDEPEitpPVPGGGRRFFGDDGVDAFFDPAVE-VRAVVESqflsMRL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 396 NSRWLLecvnrFTGNDGPIRIVGGGARSDLWCQIIADVCGRTCeRVADPLNAQLRGAALFAGIGMG------DVDRDELR 469
Cdd:cd07776 416 HAERLG-----SDIPPTRILATGGASANKAILQVLADVFGAPV-YTLDVANSAALGAALRAAHGLLcagsgdFSPEFVVF 489
|
330 340
....*....|....*....|..
gi 2179559870 470 DLIPLDGVFEPIAANRAVYDRL 491
Cdd:cd07776 490 SAEEPKLVAEPDPEAAEVYDKL 511
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-431 |
5.50e-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: 61.51 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 7 VVLAVDLGTGGPKVGFVALDGTVLWSDLVAVPTSYGPGGAAVQDAGLW-WAI--IRDATRRGlaesrvrgdQVAGVSITG 83
Cdd:cd07772 1 VIAVFDIGKTNKKLLLFDENGEVLAERSTPNPEIEEDGYPCEDVEAIWeWLLdsLAELAKRH---------RIDAINFTT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 84 QWASTVPVDADGRPVGPCVMWMDTRGAPFSR---KAFGGRLQGYRPRALLSwlrRNGGIpspsgddpvgHMLHLQHNDPA 160
Cdd:cd07772 72 HGATFALLDENGELALPVYDYEKPIPDEINEayyAERGPFEETGSPPLPGG---LNLGK----------QLYWLKREKPE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 161 VSGAARWYLEPVDYLSMCFTGRaAASRASMMGA----WltdnrNLALPDYDDvLVRLAGVDRtKLPPLVPTGSIISTVAP 236
Cdd:cd07772 139 LFARAKTILPLPQYWAWRLTGK-AASEITSLGChtdlW-----DFEKNEYSS-LVKKEGWDK-LFPPLRKAWEVLGPLRP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 237 AVAAELGISPAAQVVTGtpdLH--SAAVGSGAVRQGELHLTISTTSWIScpvavkktdAFHQLATVP--GLDPSSYLLVN 312
Cdd:cd07772 211 DLARRTGLPKDIPVGCG---IHdsNAALLPYLAAGKEPFTLLSTGTWCI---------AMNPGNDLPltELDLARDCLYN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179559870 313 NQDT----------AGRALQWLRDNVFGELDYDALTA-----LAAGA---PAGSNGVIFTPWLKGEHSPIDDRNARGGFH 374
Cdd:cd07772 279 LDVFgrpvktarfmGGREYERLVERIAKSFPQLPSLAdlaklLARGTfalPSFAPGGGPFPGSGGRGVLSAFPSAEEAYA 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2179559870 375 NLSLDTtradlvrAVLEgvafnsrwlLECVNRFTGNDGPIRIVGGGARSDLWCQIIA 431
Cdd:cd07772 359 LAILYL-------ALMT---------DYALDLLGSGVGRIIVEGGFAKNPVFLRLLA 399
|
|
| |
