|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-537 |
0e+00 |
|
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: 766.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDATCS 83
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 84 LVAVAADGSPVAVGSSGDPKRNIIVWMDHRAAGEAEEINAGGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKHFF 163
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPETWAKAGHFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 164 DLADYLTWRATGSLTRSTCTVTCKWTYLAH---ESRWDTDYFNKIGLEELVAERFARIGTEIAWPGTPIASGLTETAAPE 240
Cdd:cd07782 161 DLPDFLTWKATGSLTRSLCSLVCKWTYLAHegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 241 LGLHPGTAVAASLIDAHA---GGLGTLGAAGEGVTSDIGRRLAYIFGTSACSMASSQEPVFVDGVWGPYFSAMIPDLWLN 317
Cdd:cd07782 241 LGLPEGTPVGVSLIDAHAgglGTLGADVGGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 318 EGGQSAAGAAIDHLVAMHPASASATELAEAAGIPLVGWLDAEASKMCSS-PEDVMALAHRIHVVPEFLGNRSPNADPDAR 396
Cdd:cd07782 321 EGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEkGLPLAYLTRDLHVLPDFHGNRSPLADPTLR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 397 AVIAGLSLDAGIPDLVALYIAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPV 476
Cdd:cd07782 401 GMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277285833 477 LLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEPaQGAPKKAHETRYRIFESLQLVDREIR 537
Cdd:cd07782 481 LLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEP-NEELKKYHDRKYEVFLKMYEDQREYR 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
2-537 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 618.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 2 AAHFIGVDVGTGSARAGVFN-ENGTLLAVAKRPINIWQE------AGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIR 74
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWVIglylppPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 75 GLGFDAT-CSLVAVAADGSPVAV--GSSGDPKRNIIVWMDHRAAGEAEEIN----AGGHEVLRYVGGRISPEMETPKLLW 147
Cdd:COG1069 81 GIGVDATgCTPVPVDADGTPLALlpEFAENPHAMVILWKDHTAQEEAERINelakARGEDYLRYVGGIISSEWFWPKILH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 148 LKRNLPDSFAAAKHFFDLADYLTWRATGSLTRSTCTVTCKWTYLAHESRW-DTDYFNKIGLE-ELVAErfaRIGTEIAWP 225
Cdd:COG1069 161 LLREDPEVYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAHEGGYpSEEFFAALDPLlDGLAD---RLGTEIYPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 226 GTPiASGLTETAAPELGLHPGTAVAASLIDAHAGGLgtlgaageGVTSDIGRRLAYIFGTSACSMASSQEPVFVDGVWGP 305
Cdd:COG1069 238 GEP-AGTLTAEWAARLGLPPGTAVAVGAIDAHAGAV--------GAGGVEPGTLVKVMGTSTCHMLVSPEERFVPGICGQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 306 YFSAMIPDLWLNEGGQSAAGAAIDHLVAMHPASASATELAEAAGIPLVGWLDAEASKMcsspedvMALAHRIHVVPEFLG 385
Cdd:COG1069 309 VDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLTEEAAKL-------PPGESGLHALDWFNG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 386 NRSPNADPDARAVIAGLSLDAGIPDlvaLYIAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQ-SDLVRQLLADATG 464
Cdd:COG1069 382 NRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIATkNPLVMQIYADVTG 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277285833 465 VRVAVIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSS-ISRVFEPaQGAPKKAHETRYRIFESLQLVDREIR 537
Cdd:COG1069 459 RPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSgFDKVYTP-DPENVAVYDALYAEYLQLHDYFGRGR 531
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
4-537 |
0e+00 |
|
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.
Pssm-ID: 273552 [Multi-domain] Cd Length: 541 Bit Score: 618.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDATCS 83
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLAESKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 84 LVAVAADGSPVAVGSSGDPKRNIIVWMDHRAAGEAEEINAGGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKHFF 163
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPELFARCKFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 164 DLADYLTWRATGSLTRSTCTVTCKWTYLAHES---RWDTDYFNKIGLEELVAERFARIGTEIAWPGTPIASGLTETAAPE 240
Cdd:TIGR01315 161 DLTDFLTWRATGKEIRSFCSVVCKWGFVPVDGsnkGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 241 LGLHPGTAVAASLIDAHAGG--LGTLGAAGEGVTSDIGRRLAYIFGTSACSMASSQEPVFVDGVWGPYFSAMIPDLWLNE 318
Cdd:TIGR01315 241 LGLPAGTAVGSGLIDAHAGWigTVGAKVAENGDVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 319 GGQSAAGAAIDHLVAMHPASASATELAEAAGIPLVGWLDAEASKMCSSPED--VMALAHRIHVVPEFLGNRSPNADPDAR 396
Cdd:TIGR01315 321 GGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHLKEMAAKTNApsISYLVRHFHVYPDLWGNRSPIADPNMR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 397 AVIAGLSLDAGIPDLVALYIAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPV 476
Cdd:TIGR01315 401 GVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277285833 477 LLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEPAQGAPKKAHETRYRIFESLQLVDREIR 537
Cdd:TIGR01315 481 LHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDPAKKLHDRKYEIFLQLARTQQEYR 541
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-529 |
6.47e-132 |
|
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: 393.44 E-value: 6.47e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFN-ENGTLLAVAKRPINIWQEAGDV--VEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDA 80
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYIPPRPgwAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 81 TCSlvavaadgSPVAVGSSGDPKRNIIVWMDHRAAGEAEEINAGGHEVLRY----VGGRISPEMETPKLLWLKRNLPDSF 156
Cdd:cd07781 81 TSS--------TVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHPALEYylayYGGVYSSEWMWPKALWLKRNAPEVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 157 AAAKHFFDLADYLTWRATGSLTRSTCTVTCKWTYLAHESRWDTDYFNKIGLEELVAERfaRIGTEIAWPGTPIAsGLTET 236
Cdd:cd07781 153 DAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGLLKLRE--KLPGEVVPVGEPAG-TLTAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 237 AAPELGLHPGTAVAASLIDAHAGGlgtlgaagegVTSDIGR--RLAYIFGTSACSMASSQEPVFVDGVWGPYFSAMIPDL 314
Cdd:cd07781 230 AAERLGLPAGIPVAQGGIDAHMGA----------IGAGVVEpgTLALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 315 WLNEGGQSAAGAAIDHLV--AMHPasasatelAEAAGIPLVGWLDAEASKMCSSPEDVMALAHrihvvpeFLGNRSPNAD 392
Cdd:cd07781 300 YGLEAGQSAVGDIFAWFVrlFVPP--------AEERGDSIYALLSEEAAKLPPGESGLVALDW-------FNGNRTPLVD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 393 PDARAVIAGLSLDAGIPDlvaLYIAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQ-SDLVRQLLADATGVRVAVID 471
Cdd:cd07781 365 PRLRGAIVGLTLGTTPAH---IYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAEkNPLWMQIYADVLGRPIKVPK 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1277285833 472 NPEPVLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEPAQGApKKAHETRYRIFESL 529
Cdd:cd07781 442 SDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPEN-HAVYEELYALYKEL 498
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-526 |
1.02e-129 |
|
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: 388.52 E-value: 1.02e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFN-ENGTLLAVAKRPINIWQEAG-DVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDAT 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSSKKsWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 82 CSLVAVAADGSPVAVGSSGDPKRNIIVWMDHRAAGEAEEINAGGHEVLR-YVGGRISPEMETPKLLWLKRNLPDSFAAAK 160
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHLRDKHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 161 HFFDLADYLTWRATGSLTRSTCTVTCKWTYLAHESRWDTDYFNKIGLEELvAERFARIGTEIAWPGTPIASGLTETAApE 240
Cdd:cd07768 161 HIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVALPEMAE-K 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 241 LGLHPGTAVAASLIDAHAGGLGTLGAAGEgvtsdigRRLAYIFGTSACSMASSQEPVFVDGVWGPYFSAMIPDLWLNEGG 320
Cdd:cd07768 239 MGLHPGTAVVVSCIDAHASWFAVASPHLE-------TSLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 321 QSAAGAAIDHLVAMHPaSASATELAEAAGIPLVGWLDAEASKMCSSPedvmALAHRIHVVPEFLGNRSPNADPDARAVIA 400
Cdd:cd07768 312 QSATGKLIEHLFESHP-CARKFDEALKKGADIYQVLEQTIRQIEKNN----GLSIHILTLDMFFGNRSEFADPRLKGSFI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 401 GLSLDAGIPDLVALYIAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGS 480
Cdd:cd07768 387 GESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGA 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1277285833 481 AMLAAVASGHRR---NLVDAMVTMSSISRVFEPAQGAPKKAHETRYRIF 526
Cdd:cd07768 467 AVLAKVAAGKKQladSITEADISNDRKSETFEPLAYRLGADYILLYKLL 515
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-529 |
3.87e-94 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 295.97 E-value: 3.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDAT-CS 83
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQmHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 84 LVAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEINA--GGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKH 161
Cdd:COG1070 83 LVLLDADGEPL---------RPAILWNDTRAAAEAAELREelGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 162 FFDLADYLTWRATGSLTRSTCTVTCKWTYLAHESRWDTDYFNKIGLEElvaERFArigtEIAWPGTpIASGLTETAAPEL 241
Cdd:COG1070 154 VLLPKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDR---ELLP----ELVPPGE-VAGTLTAEAAAET 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 242 GLHPGTAVAASLIDahagglgtlgaageGVTSDIG------RRLAYIFGTSACSMASSQEPVFVDGVWGPYFSAMIPDLW 315
Cdd:COG1070 226 GLPAGTPVVAGAGD--------------NAAAALGagavepGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 316 LNEGGQSAAGAAIDHLvamhpasasATELAEAAGIPlVGWLDAEASKMCSSPEDVMALahrihvvPEFLGNRSPNADPDA 395
Cdd:COG1070 292 LPMGATNNGGSALRWF---------RDLFADGELDD-YEELNALAAEVPPGADGLLFL-------PYLSGERTPHWDPNA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 396 RAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEP 475
Cdd:COG1070 355 RGAFFGLTLSHTRAHLAR---AVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEG 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1277285833 476 VLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEPAQGApKKAHETRYRIFESL 529
Cdd:COG1070 432 GALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPEN-VAAYDELYERYREL 484
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-527 |
8.10e-86 |
|
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: 274.01 E-value: 8.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 6 IGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDAT-CSL 84
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQmQGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 85 VAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEINAGGHEVLRY---VGGRISPEMETPKLLWLKRNLPDSFAAAKH 161
Cdd:cd07805 83 VPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEIYAKTHK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 162 FFDLADYLTWRATGSLTRSTCTVTCKWTYLAHESRWDTDYFNKIGLEelvAERFARIGteiawPGTPIASGLTETAAPEL 241
Cdd:cd07805 154 FLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGID---PDKLPELV-----PSTEVVGELTPEAAAEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 242 GLHPGTAVAASLIDAHAGGLGTlgaageGVTSDiGRrlAYI-FGTSACSMASSQEPVfVDGVWGPY-FSAMIPDLWLNEG 319
Cdd:cd07805 226 GLPAGTPVVGGGGDAAAAALGA------GAVEE-GD--AHIyLGTSGWVAAHVPKPK-TDPDHGIFtLASADPGRYLLAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 320 GQSAAGAAIDHLVAMH-PASASATELAEAagiplvgwLDAEASKMCSSPEDVMALahrihvvPEFLGNRSPNADPDARAV 398
Cdd:cd07805 296 EQETAGGALEWARDNLgGDEDLGADDYEL--------LDELAAEAPPGSNGLLFL-------PWLNGERSPVEDPNARGA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 399 IAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPV-L 477
Cdd:cd07805 361 FIGLSLEHTRADLAR---AVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQEAgA 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1277285833 478 LGSAMLAAVASGHRRNLVDAMvTMSSISRVFEPaQGAPKKAHETRYRIFE 527
Cdd:cd07805 438 LGAALLAAVGLGLLKSFDEAK-ALVKVEKVFEP-DPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-490 |
9.14e-75 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 246.93 E-value: 9.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGD--VVEQSSEDIWSAVSTSVREAVAASGVDTadIRGLGFDATC 82
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISYKQDPKDlwFVTQSSTEIWKAIKTALKELIEELSDYI--VSGIGVSATC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 SLVAVAADGS-----PVAVGS-SGDPKRNIIVWMDHRAAGEAEEIN-AGGHEVLRYVGGRISPEMETPKLLWLKRNLPDS 155
Cdd:cd07778 80 SMVVMQRDSDtsylvPYNVIHeKSNPDQDIIFWMDHRASEETQWLNnILPDDILDYLGGGFIPEMAIPKLKYLIDLIKED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 156 FAAAKHFFDLADYLTWRAtgsltrstCTVTCKW--TYLAHESR-----------WDTDYFNKIGLEELVA--ERFARIGT 220
Cdd:cd07778 160 TFKKLEVFDLHDWISYML--------ATNLGHSniVPVNAPPSigigidgslkgWSKDFYSKLKISTKVCnvGNTFKEAP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 221 EIAWPGTPIASgLTETAAPELGLHPGTAVAASLIDAHAGGLGTLGAAGEGVTSdigrrLAYIFGTSACSM-ASSQEPV-F 298
Cdd:cd07778 232 PLPYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFSTFAAAKTLDTT-----LFMVAGTSTCFLyATSSSQVgP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 299 VDGVWGPyFSAMIPDLWLNEGGQSAAGAAIDHLVAMHPAsasatelaeaagipLVGWLDAEASKMCSSpEDVMALAHRIH 378
Cdd:cd07778 306 IPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPA--------------IIELLKSDANFFETV-EEKIDKYERLL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 379 VVPEF------------LGNRSPNADPDARAVIAGLSLDAGIPDLVALYIAGLCGIGYGLKQLLVKLREDGIPIDLIIAS 446
Cdd:cd07778 370 GQSIHyltrhmffygdyLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVIS 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1277285833 447 GGAAQSDLVRQLLA---DATGVRVAVIDNPEPVLLGSAMLAAVASGH 490
Cdd:cd07778 450 GSQAKNARLLQLLStvlSKIHIIVPLSDSKYAVVKGAALLGKAAFLH 496
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-489 |
4.17e-74 |
|
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: 242.43 E-value: 4.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGfdatCS 83
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIG----VS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 84 lvavAADGSPVAVGSSGDPKRNIIVWMDHRAAGEAEEINA--GGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKH 161
Cdd:cd07804 77 ----GLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNEniGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 162 FFDLADYLTWRATGSLT--RST--CTVTCkwtYLAHESRWDTDYFNKIGLEELvaerfarIGTEIAWPgTPIASGLTETA 237
Cdd:cd07804 153 FLGAYDYIVYKLTGEYVidYSSagNEGGL---FDIRKRTWDEELLEALGIDPD-------LLPELVPS-TEIVGEVTKEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 238 APELGLHPGTAVAASLIDAhagglgTLGAAGEGVTSDiGRRLAYiFGTSACSMASSQEPVFVDGVWGPYFSamIPDLWLN 317
Cdd:cd07804 222 AEETGLAEGTPVVAGTVDA------AASALSAGVVEP-GDLLLM-LGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 318 EGGQSAAGAAIDHLVAMhpASASATELAEAAGIPLVGWLDAEASKMCSSPEDVMALahrihvvPEFLGNRSPNADPDARA 397
Cdd:cd07804 292 NGGMATSGSLLRWFRDE--FAGEEVEAEKSGGDSAYDLLDEEAEKIPPGSDGLIVL-------PYFMGERTPIWDPDARG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 398 VIAGLSLDAGIPDLvalYIAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVL 477
Cdd:cd07804 363 VIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGAS 439
|
490
....*....|..
gi 1277285833 478 LGSAMLAAVASG 489
Cdd:cd07804 440 LGDAFLAGVGVG 451
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-510 |
2.17e-71 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 237.82 E-value: 2.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 1 MAAHFIGVDVGTGSARAGVFN-ENGTLLAVAKRPINIWQE------AGDVVEQSSEDIWSAVSTSVREAVAASGVDTADI 73
Cdd:PRK04123 1 MMAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWVKgryldlPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 74 RGLGFDAT-CSLVAVAADGSPVAV--GSSGDPKRNIIVWMDHRAAGEAEEINAGGHE-----VLRYVGGRISPEMETPKL 145
Cdd:PRK04123 81 VGIGVDFTgSTPAPVDADGTPLALlpEFAENPHAMVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 146 LWLKRNLPDSFAAAKHFFDLADYLTWRATG-----SLTRSTCTVTCKWTYlaHESrWD----TDYFNKI--GLEELVAER 214
Cdd:PRK04123 161 LHVLREDPAVYEAAASWVEACDWVVALLTGttdpqDIVRSRCAAGHKALW--HES-WGglpsADFFDALdpLLARGLRDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 215 farIGTEIAWPGTPiASGLTETAAPELGLHPGTAVAASLIDAHAGGLgtlgaageGVTSDIGRRLAyIFGTSACSMASSQ 294
Cdd:PRK04123 238 ---LFTETWTAGEP-AGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAV--------GAGAEPGTLVK-VMGTSTCDILLAD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 295 EPVFVDGVWGPYFSAMIPDLWLNEGGQSAAGaaiDHL-----VAMHPASAsatELAEAAGIPLVGWLDAEASKMcssped 369
Cdd:PRK04123 305 KQRAVPGICGQVDGSIVPGLIGYEAGQSAVG---DIFawfarLLVPPEYK---DEAEARGKQLLELLTEAAAKQ------ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 370 vMALAHRIHVVPEFLGNRSPNADPDARAVIAGLSLDAGIPDLVALYIAGLCgigYGLKQLLVKLREDGIPIDLIIASGGA 449
Cdd:PRK04123 373 -PPGEHGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATA---FGTRAIMECFEDQGVPVEEVIAAGGI 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277285833 450 AQ-SDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSS-ISRVFEP 510
Cdd:PRK04123 449 ARkNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASpVEKTYQP 511
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-530 |
7.56e-70 |
|
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: 232.04 E-value: 7.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDA-TC 82
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 SLVAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEINAG-GHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKH 161
Cdd:cd07808 81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 162 FFdLA-DYLTWRATGSLtrstCT-VTCKWTYL---AHESRWDTDYFNKIGLEElvaERFARI--GTEIAwpGTpiasgLT 234
Cdd:cd07808 152 IL-LPkDYLRYRLTGEL----ATdPSDASGTLlfdVEKREWSEELLEALGLDP---SILPPIveSTEIV--GT-----LT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 235 ETAAPELGLHPGTAVAASLIDAhagglgtlgaagegVTSDIG------RRLAYIFGTSACSMASSQEPVFV--DGVWgpY 306
Cdd:cd07808 217 PEAAEELGLPEGTPVVAGAGDN--------------AAAALGagvvepGDALISLGTSGVVFAPTDKPVPDpkGRLH--T 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 307 FSAMIPDLWLNEGGQSAAGAAIDHLVAMHPASASATELaeaagiplvgwLDAEASKMCSSPEDVMALahrihvvPEFLGN 386
Cdd:cd07808 281 FPHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDRESFDE-----------LDAEAAKVPPGSEGLLFL-------PYLSGE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 387 RSPNADPDARAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVR 466
Cdd:cd07808 343 RTPYWDPNARGSFFGLSLSHTRAHLAR---AVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVP 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277285833 467 VAVIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEPAQGApKKAHETRYRIFESLQ 530
Cdd:cd07808 420 VVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPER-HEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-510 |
2.71e-66 |
|
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: 221.24 E-value: 2.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDAT-C 82
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 SLVAVAADGSPVavgssgdpkRNIIVWMDHRAAgeaeeinagghevlryvggrispemetpkllwlkrnlpdsfaaakHF 162
Cdd:cd07779 81 TFVPVDEDGRPL---------RPAISWQDKRTA---------------------------------------------KF 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 163 FDLADYLTWRATGSLTRSTCTVTCKWTYLAHESRWDTDYFNKIGLEElvaERFArigtEIAWPGTPIASgLTETAAPELG 242
Cdd:cd07779 107 LTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDR---DKLP----ELVPPGTVIGT-LTKEAAEETG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 243 LHPGTAVAASLID-------AhagglgtlgaageGVTSDigrRLAYI-FGTSACSMASSQEPVFVDGVWGPYFSAMIPDL 314
Cdd:cd07779 179 LPEGTPVVAGGGDqqcaalgA-------------GVLEP---GTASLsLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGK 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 315 WLNEGGQSAAGAAI----DHLVAMHPASASATELAEAAgiplvgwLDAEASKmcSSP--EDVMALAHrihvvpeFLGNRS 388
Cdd:cd07779 243 WVLEGSINTGGSAVrwfrDEFGQDEVAEKELGVSPYEL-------LNEEAAK--SPPgsDGLLFLPY-------LAGAGT 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 389 PNADPDARAVIAGLSLDAGIPDLvalYIAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVA 468
Cdd:cd07779 307 PYWNPEARGAFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVE 383
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1277285833 469 VIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEP 510
Cdd:cd07779 384 RPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEP 425
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
5-489 |
3.33e-66 |
|
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: 221.31 E-value: 3.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDtaDIRGLGFdAT--C 82
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPD--PIAAISV-SSqgE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 SLVAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEI--NAGGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAK 160
Cdd:cd07773 79 SGVPVDRDGEPL---------GPAIVWFDPRGKEEAEELaeRIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 161 HFFDLADYLTWRATGSLTrSTCTVTCKWTYL-AHESRWDTDYFNKIGLEElvaERFArigtEIAWPGTPIASgLTETAAP 239
Cdd:cd07773 150 KWLSVADYIAYRLTGEPV-TDYSLASRTMLFdIRKRTWSEELLEAAGIDA---SLLP----ELVPSGTVIGT-VTPEAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 240 ELGLHPGTAVAASLIDaHAGGLGTLGAAGEGVTSDIgrrlayiFGTSACSMASSQEPVFVDGVWGPYFS---AMIPDLWL 316
Cdd:cd07773 221 ELGLPAGTPVVVGGHD-HLCAALGAGVIEPGDVLDS-------TGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 317 NEGGQSAaGAAIDHLVAMHPASASATELAeaagiplvgwlDAEASKMCSSPEDVMALahrihvvPEFLGNRSPNADPDAR 396
Cdd:cd07773 293 LAGSLPG-GALLEWFRDLFGGDESDLAAA-----------DELAEAAPPGPTGLLFL-------PHLSGSGTPDFDPDAR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 397 AVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPV 476
Cdd:cd07773 354 GAFLGLTLGTTRADLLR---AILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
490
....*....|...
gi 1277285833 477 LLGSAMLAAVASG 489
Cdd:cd07773 431 ALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
5-529 |
2.87e-65 |
|
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: 219.73 E-value: 2.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDtaDIRGLGFDATC-S 83
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFSSAMhS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 84 LVAVAADGSPVAvgssgdpkrNIIVWMDHRAAGEAEEI--NAGGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKH 161
Cdd:cd07770 80 LLGVDEDGEPLT---------PVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 162 FFDLADYLTWRATGSLTRSTCTVTckWTYL--AHESRWDTDYFNKIGLEElvaERFARIGteiawPGTPIASGLTETAAP 239
Cdd:cd07770 151 FVSIKEYLLYRLTGELVTDYSTAS--GTGLlnIHTLDWDEEALELLGIDE---EQLPELV-----DPTEVLPGLKPEFAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 240 ELGLHPGTAVAASLIDahagglgtlgaageGVTSDIG------RRLAYIFGTSACSMASSQEPVFVD--GVWgPYFSAmi 311
Cdd:cd07770 221 RLGLLAGTPVVLGASD--------------GALANLGsgaldpGRAALTVGTSGAIRVVSDRPVLDPpgRLW-CYRLD-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 312 PDLWLNEGGQSAAGAAIDHLVAMHPASASATELaeaagiplvgwLDAEASKmcsspedVMALAHRIHVVPEFLGNRSPNA 391
Cdd:cd07770 284 ENRWLVGGAINNGGNVLDWLRDTLLLSGDDYEE-----------LDKLAEA-------VPPGSHGLIFLPYLAGERAPGW 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 392 DPDARAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVID 471
Cdd:cd07770 346 NPDARGAFFGLTLNHTRADILR---AVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPE 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1277285833 472 NPEPVLLGSAMLAAVASGHRRNLvdAMVTMSSISRVFEPAQGApKKAHETRYRIFESL 529
Cdd:cd07770 423 EEEASALGAALLALEALGLISSL--EADELVKIGKVVEPDPEN-HAIYAELYERFKKL 477
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
5-488 |
4.40e-65 |
|
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: 217.86 E-value: 4.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAAsgVDTADIRGLGFDATC-S 83
Cdd:cd07783 2 FLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAE--LRPRRVVAIAVDGTSgT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 84 LVAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEINAGGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKHFF 163
Cdd:cd07783 80 LVLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 164 DLADYLTWRATGSLTRSTCTVTCKWTYLAHESRWDTDYFNKIGLEElvaERFARIGTeiawPGTPIASgLTETAAPELGL 243
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGRWPSWLLALLGIPP---DLLPRVVA----PGTVIGT-LTAEAAEELGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 244 HPGTAVAASLIDahagglgtlgaageGVTSDIG------RRLAYIFGTSACSMASSQEPVFVDGVwGPYFSAMIPDLWLN 317
Cdd:cd07783 223 PAGTPVVAGTTD--------------SIAAFLAsgavrpGDAVTSLGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 318 EGGQSAAGAAIDHLVamhpasaSATELAEaagiplvgwLDAEASKMCSSPEDVMALAHRihvvpeflGNRSPNADPDARA 397
Cdd:cd07783 288 GGASNTGGAVLRWFF-------SDDELAE---------LSAQADPPGPSGLIYYPLPLR--------GERFPFWDPDARG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 398 VIAGLSLDAGipdlvALYIAGLCGIGYGLKQLLVKLREDG-IPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPv 476
Cdd:cd07783 344 FLLPRPHDRA-----EFLRALLEGIAFIERLGYERLEELGaPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA- 417
|
490
....*....|..
gi 1277285833 477 LLGSAMLAAVAS 488
Cdd:cd07783 418 ALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-484 |
6.00e-63 |
|
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: 211.27 E-value: 6.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDAT-C 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 SLVAVAADGSPVavgssgdpkRNIIVWMDHRAageaeeinagghevlryvggrispemetpkllwlkrnlpdsfaaakHF 162
Cdd:cd00366 81 GVVLVDADGNPL---------RPAIIWLDRRA----------------------------------------------KF 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 163 FDLADYLTWRATGSLTRSTCTVTckWTYL--AHESRWDTDYFNKIGLEElvaERFARIgteiAWPGTpIASGLTETAAPE 240
Cdd:cd00366 106 LQPNDYIVFRLTGEFAIDYSNAS--GTGLydIKTGDWSEELLDALGIPR---EKLPPI----VESGE-VVGRVTPEAAEE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 241 LGLHPGTAVAASLIDAHAGGLGTlgaageGVTSDigRRLAYIFGTSACSMASSQEPVFVDGVWGPYFSAmIPDLWLNEGG 320
Cdd:cd00366 176 TGLPAGTPVVAGGGDTAAAALGA------GVVEP--GDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLWLLEGA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 321 QSAAGAAI----DHLVAMHPASASATELAEAAgiplvgwldaeaskmcsspEDVMALAHRIHVVPEFLGNRSPNADPDAR 396
Cdd:cd00366 247 INTGGASLrwfrDEFGEEEDSDAEYEGLDELA-------------------AEVPPGSDGLIFLPYLSGERSPIWDPAAR 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 397 AVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPV 476
Cdd:cd00366 308 GVFFGLTLSHTRAHLIR---AVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
....*...
gi 1277285833 477 LLGSAMLA 484
Cdd:cd00366 385 ALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
5-489 |
7.08e-61 |
|
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: 207.40 E-value: 7.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDAT-CS 83
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHgNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 84 LVAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEINAGG--HEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKH 161
Cdd:cd07802 82 LYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEDGtlEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 162 FFDLADYLTWRATGsltrstcTVTCKWT------YLAHESRWDTDYFNKIGLEELvAERFARIGteiawPGTPIASGLTE 235
Cdd:cd07802 153 VLFCKDWIRYRLTG-------EISTDYTdagsslLDLDTGEYDDELLDLLGIEEL-KDKLPPLV-----PSTEIAGRVTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 236 TAAPELGLHPGTAVAASLIDAHAGGLGTlgaageGVTSDigRRLAYIFGTSACSMASSQEPVFVDGVWGpYFSAMIPDLW 315
Cdd:cd07802 220 EAAALTGLPEGTPVAAGAFDVVASALGA------GAVDE--GQLCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 316 LNEGGQSAAGAAIDHLVAMHpasasaTELAEAAGIPLVGWLDAEASKMCSSPEDVMALahrihvvPeFLgnRSPNADPDA 395
Cdd:cd07802 291 LIVEASPTSASNLDWFLDTL------LGEEKEAGGSDYDELDELIAAVPPGSSGVIFL-------P-YL--YGSGANPNA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 396 RAVIAGLSLDAGIPDLV-ALYIaglcGIGYGLKQLLVKLREDGiPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPE 474
Cdd:cd07802 355 RGGFFGLTAWHTRAHLLrAVYE----GIAFSHRDHLERLLVAR-KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEE 429
|
490
....*....|....*
gi 1277285833 475 PVLLGSAMLAAVASG 489
Cdd:cd07802 430 LGALGAAICAAVAAG 444
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
279-487 |
4.47e-54 |
|
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: 181.37 E-value: 4.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 279 LAYIFGTSACSMASSQEPV-FVDGVWGPYFSAMIPDLWLNEGGQSAAGAAIDHLVAMHPAsasATELAEAAGIPLVGWLD 357
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGL---REELRDAGNVESLAELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 358 AEASKmcsspedvmALAHRIHVVPEFLGNRSPNADPDARAVIAGLSLDagiPDLVALYIAGLCGIGYGLKQLLVKL-RED 436
Cdd:pfam02782 78 ALAAV---------APAGGLLFYPDFSGNRAPGADPGARGSITGLSSP---TTLAHLYRAILESLALQLRQILEALtKQE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1277285833 437 GIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVA 487
Cdd:pfam02782 146 GHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
5-489 |
1.74e-44 |
|
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: 163.18 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDATcsl 84
Cdd:cd24121 2 LIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQ--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 85 vavaADGSPVaVGSSGDPKRNIIVWMDHRAAGEAEEINAGG--HEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKHF 162
Cdd:cd24121 79 ----GDGTWL-VDEDGRPVRDAILWLDGRAADIVERWQADGiaEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 163 FDLADYLTWRATGSltRSTCTVTCKWTYLAHESR-WDTDYFNKIGLEELvAERFARIGteiawPGTPIASGLTETAAPEL 241
Cdd:cd24121 154 LHCKDWLFYKLTGE--IATDPSDASLTFLDFRTRqYDDEVLDLLGLEEL-RHLLPPIR-----PGTEVIGPLTPEAAAAT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 242 GLHPGTAVAASLID-AHAGGLGTLGAAGEGVTsdigrrlayIFGTSACSMASSQEPVFVDGVWGPYFSAMIPDLWLNEGG 320
Cdd:cd24121 226 GLPAGTPVVLGPFDvVATALGSGAIEPGDACS---------ILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWLRAMA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 321 QSAAGAAIDHLvaMHPASASATELAEAAGIPLVGWLDAEASKMCSSPEDVMALahrihvvPeFL---GNRSPNADPDARA 397
Cdd:cd24121 297 NMAGTPNLDWF--LRELGEVLKEGAEPAGSDLFQDLEELAASSPPGAEGVLYH-------P-YLspaGERAPFVNPNARA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 398 VIAGLSLDAGIPDLV-ALYIaglcGIGYGLKQLLVKLredGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPV 476
Cdd:cd24121 367 QFTGLSLEHTRADLLrAVYE----GVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFG 439
|
490
....*....|...
gi 1277285833 477 LLGSAMLAAVASG 489
Cdd:cd24121 440 ARGAAMNAAVALG 452
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
6-489 |
3.43e-44 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 163.25 E-value: 3.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 6 IGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDATC-SL 84
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMhGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 85 VAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEINA--GGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKHF 162
Cdd:TIGR01312 81 VLLDANGEVL---------RPAILWNDTRTAQECEELEAelGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 163 FDLADYLTWRATGSLT--RSTCTVTckwTYLAHESR-WDTDYFNKIGLEELVAERFarigteiaWPGTPIASGLTETAAP 239
Cdd:TIGR01312 152 MLPKDYLRYRLTGEYVteYSDASGT---GWFDVAKRaWSKELLDALDLPESQLPEL--------IESSEKAGTVRPEVAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 240 ELGLHPGTAVAASLIDAHAGGLGTLGAAGEGVTSDIgrrlayifGTSACSMASSQEPV--FVDGVwgPYFSAMIPDLWLn 317
Cdd:TIGR01312 221 RLGLSAGVPVAAGGGDNAAGAIGTGTVDPGDAMMSL--------GTSGVVYAVTDKPLpdPAGAV--HGFCHALPGGWL- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 318 eggqsaagaaidHLVAMHPASASATELAEAAGIPLVGWLDAEASKmcsSPEDvmalAHRIHVVPEFLGNRSPNADPDARA 397
Cdd:TIGR01312 290 ------------PMGVTLSATSSLEWFRELFGKEDVEALNELAEQ---SPPG----AEGVTFLPYLNGERTPHLDPQARG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 398 VIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLRE-DGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPV 476
Cdd:TIGR01312 351 SFIGLTHNTTRADLTR---AVLEGVTFALRDSLDILREaGGIPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGP 427
|
490
....*....|...
gi 1277285833 477 LLGSAMLAAVASG 489
Cdd:TIGR01312 428 ALGAAILAAWALG 440
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-489 |
6.93e-44 |
|
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: 161.56 E-value: 6.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFN-ENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDATC 82
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 -SLVAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEI-NAGGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAK 160
Cdd:cd07809 81 hGLVALDADGKVL---------RPAKLWCDTRTAPEAEELtEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 161 HFFDLADYLTWRATG--SLTRSTCTVTCkWTYLAHEsRWDTDYFNKIGLEELVAERFARIGTeiawPGTPiASGLTETAA 238
Cdd:cd07809 152 KILLPHDYLNWKLTGekVTGLGDASGTF-PIDPRTR-DYDAELLAAIDPSRDLRDLLPEVLP----AGEV-AGRLTPEGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 239 PELGLHPGTAVAASLIDAHagglgtlgaagegvTSDIG------RRLAYIFGTSACSMASSQEPVF-VDGVWGPYFSAmi 311
Cdd:cd07809 225 EELGLPAGIPVAPGEGDNM--------------TGALGtgvvnpGTVAVSLGTSGTAYGVSDKPVSdPHGRVATFCDS-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 312 PDLWLneggqsaagaaidHLVAMHPASASATELAEAAGIPLVGWLDAEASKmcsSPEDvmalAHRIHVVPEFLGNRSPNa 391
Cdd:cd07809 289 TGGML-------------PLINTTNCLTAWTELFRELLGVSYEELDELAAQ---APPG----AGGLLLLPFLNGERTPN- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 392 DPDARAVIAGLSL-DAGIPDLV--ALYiAGLCGIGYGLKqllvKLREDGIPIDLIIASGGAAQSDLVRQLLADATGVRVA 468
Cdd:cd07809 348 LPHGRASLVGLTLsNFTRANLAraALE-GATFGLRYGLD----ILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVV 422
|
490 500
....*....|....*....|.
gi 1277285833 469 VIDNPEPVLLGSAMLAAVASG 489
Cdd:cd07809 423 VPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-489 |
3.64e-37 |
|
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: 142.75 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQE--AGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLgfdAT 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 82 CS----LVAVAADGSPVAVGSsgdpkrNIivwmDHRAAGEAEEINAGGHEVLRYVGGRISPEMETP-KLLWLKRNLPDSF 156
Cdd:cd07798 78 TSqregIVFLDKDGRELYAGP------NI----DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEIF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 157 AAAKHFFDLADYLTWRATGSLT--RSTCTVTCkwTYLAHESRWDTDYFNKIGLEElvaERFArigtEIAWPGTpIASGLT 234
Cdd:cd07798 148 ERIATVLSISDWIGYRLTGELVsePSQASETQ--LFDIKKREWSQELLEALGLPP---EILP----EIVPSGT-VLGTVS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 235 ETAAPELGLHPGTAVAASLIDAHAGGLGTLGAagegVTSDIGrrlaYIFGTSACSMASSQEPVFVD--GVW-GPYfsaMI 311
Cdd:cd07798 218 EEAARELGLPEGTPVVVGGADTQCALLGSGAI----EPGDIG----IVAGTTTPVQMVTDEPIIDPerRLWtGCH---LV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 312 PDLWLNEGGQSAAGAAIDHLVAMHPASASATelaeaagiplVGWLDAEASKMCSSPEDVMAlahrihvvpeFLGNRSPNA 391
Cdd:cd07798 287 PGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANGVLA----------FLGPQIFDA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 392 DpdARAVI-AGLS----LDAGIPDLVALYIAGLCGIGYGLKQLLVKLRED-GIPIDLIIASGGAAQSDLVRQLLADATGV 465
Cdd:cd07798 347 R--LSGLKnGGFLfptpLSASELTRGDFARAILENIAFAIRANLEQLEEVsGREIPYIILCGGGSRSALLCQILADVLGK 424
|
490 500
....*....|....*....|....
gi 1277285833 466 RVAVIDNPEPVLLGSAMLAAVASG 489
Cdd:cd07798 425 PVLVPEGREASALGAAICAAVGAG 448
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
6-242 |
1.99e-29 |
|
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: 116.28 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 6 IGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFDATC-SL 84
Cdd:pfam00370 3 LGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGhGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 85 VAVAADGSPVavgssgdpkRNIIVWMDHRAAGEAEEINA--GGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAAAKHF 162
Cdd:pfam00370 83 VLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 163 FDLADYLTWRATGSL-TRSTCTVTCKWTYLaHESRWDTDYFNKIGLEELV-------AERFARIGTEIA-----WPGTPI 229
Cdd:pfam00370 154 LTIHDYLRWRLTGVFvTDHTNASRSMMFNI-HKLDWDPELLAALGIPRDHlpplvesSEIYGELNPELAamwglDEGVPV 232
|
250
....*....|...
gi 1277285833 230 ASGLTETAAPELG 242
Cdd:pfam00370 233 VGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-524 |
4.41e-29 |
|
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: 120.36 E-value: 4.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFdAT-- 81
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 82 CSLVAVAADgspvavgsSGDPKRNIIVWMDHRAAGEAEEINA--------GGHEVL-------RYVGG---RISPEMETP 143
Cdd:cd07793 80 NTFLTWDKK--------TGKPLHNFITWQDLRAAELCESWNRslllkalrGGSKFLhfltrnkRFLAAsvlKFSTAHVSI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 144 KLLWLKRNLPDSFAAAKH---FFDLAD-YLTWRATGS---LTRSTCtVTCKWTYLAHESRWDTDYFNKIGleelvaerfa 216
Cdd:cd07793 152 RLLWILQNNPELKEAAEKgelLFGTIDtWLLWKLTGGkvhATDYSN-ASATGLFDPFTLEWSPILLSLFG---------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 217 rIGTEIAWPGTPIASGLTETAaPELGLH--PGTAVA----ASLIdahagglgtlgaaGEGVTSDigrrlayifGTSACSM 290
Cdd:cd07793 221 -IPSSILPEVKDTSGDFGSTD-PSIFGAeiPITAVVadqqAALF-------------GECCFDK---------GDVKITM 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 291 ASSqepVFVDGVWG--PYFSA--MIPdL--W--------LNEGGQSAAGAAIDHLVAMhpasasatelaeaAGIPLVgwl 356
Cdd:cd07793 277 GTG---TFIDINTGskPHASVkgLYP-LvgWkiggeityLAEGNASDTGTVIDWAKSI-------------GLFDDP--- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 357 dAEASKMCSSPEDvmalAHRIHVVPEFLGNRSPNADPDARAVIAGLSLDAGIPDLValyIAGLCGIGYGLKQLL-VKLRE 435
Cdd:cd07793 337 -SETEDIAESVED----TNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLV---RAILESIAFRVKQLLeTMEKE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 436 DGIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLvDAMVTMSSISRVFEPAQGap 515
Cdd:cd07793 409 TSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPKMD-- 485
|
....*....
gi 1277285833 516 KKAHETRYR 524
Cdd:cd07793 486 NEKREELYK 494
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-510 |
2.86e-27 |
|
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: 115.12 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPiniWQEAGDVVEQSSEDI-----WSAVSTSVREAVAASGVDTADIRGLgf 78
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQRE---WRHKEVPDVPGSMDFdteknWKLICECIREALKKAGIAPKSIAAI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 79 dATCS----LVAVAADGSPVAVGSSGDPkrniivwmdhRAAGEAEEINAGGHEVLRYVGgRISPEMET----PKLLWLKR 150
Cdd:cd07775 76 -STTSmregIVLYDNEGEEIWACANVDA----------RAAEEVSELKELYNTLEEEVY-RISGQTFAlgaiPRLLWLKN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 151 NLPDSFAAAKHFFDLADYLTWRATGSLTR--STCTVTCkwTYLAHESRWDTDYFNKIGLEelvaerfARIGTEIAWPGTP 228
Cdd:cd07775 144 NRPEIYRKAAKITMLSDWIAYKLSGELAVepSNGSTTG--LFDLKTRDWDPEILEMAGLK-------ADILPPVVESGTV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 229 IASgLTETAAPELGLHPGTAVAASLIDAHAGGLGTlgaageGVTSDIGRrlAYIFGTSACSMASSQEPVfVDGVWGPYFS 308
Cdd:cd07775 215 IGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL------GVVRPGQT--AVLGGSFWQQEVNTAAPV-TDPAMNIRVN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 309 -AMIPDLWLNEGGQSAAGAAI----DHLvamhpaSASATELAEAAGIPLVGWLDAEASK--------MCSSpEDVMALAH 375
Cdd:cd07775 285 cHVIPDMWQAEGISFFPGLVMrwfrDAF------CAEEKEIAERLGIDAYDLLEEMAKDvppgsygiMPIF-SDVMNYKN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 376 RIHVVPEFLgNRSPNADPDARAVIAGLSLDAGIpdLVAlyiaglcgigYGLKQLLVKLreDGIPIDLIIASGGAAQSDLV 455
Cdd:cd07775 358 WRHAAPSFL-NLDIDPEKCNKATFFRAIMENAA--IVS----------AGNLERIAEF--SGIFPDSLVFAGGASKGKLW 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1277285833 456 RQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEP 510
Cdd:cd07775 423 CQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLP 477
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
4-510 |
3.29e-27 |
|
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: 114.87 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFNENGTLLAVAKRPIN-IWQEAGdVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFdaTC 82
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEqIYPQPG-WVEHDPEEIWENTLEVIREALAKAGISASDIAAIGI--TN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 ----SLVAVAADGSPVAvgssgdpkrNIIVWMDHRAAGEAEEINAGGHE--VLRYVGGRISPEMETPKLLWLKRNLPDSF 156
Cdd:cd07769 78 qretTVVWDKKTGKPLY---------NAIVWQDRRTADICEELKAKGLEerIREKTGLPLDPYFSATKIKWILDNVPGAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 157 AAAKH----FFDLADYLTWRATGS---LT------RstctvtckwTYL--AHESRWD---TDYFN--KIGLEELV--AER 214
Cdd:cd07769 149 ERAERgellFGTIDTWLIWKLTGGkvhVTdvtnasR---------TMLfnIHTLEWDdelLELFGipRSMLPEVRpsSEV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 215 FARIGTEIAWPGTPIASGLTETAAPELG---LHPGTAVA-----ASLIdahagglgtLGAAGEGVTSDIGrrlayIFGTS 286
Cdd:cd07769 220 FGYTDPEGLGAGIPIAGILGDQQAALFGqgcFEPGMAKNtygtgCFLL---------MNTGEKPVPSKNG-----LLTTI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 287 ACSMAssQEPVFVdgvwgpyfsamipdlwLnEGGQSAAGAAIDhlvamhpasasatelaeaagiplvgWLD--------- 357
Cdd:cd07769 286 AWQIG--GKVTYA----------------L-EGSIFIAGAAIQ-------------------------WLRdnlglieda 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 358 AEASKMCSSPEDvmalAHRIHVVPEFLGNRSPNADPDARAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLRED- 436
Cdd:cd07769 322 AETEELARSVED----NGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVR---AALESIAYQTRDVLEAMEKDs 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277285833 437 GIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLvDAMVTMSSISRVFEP 510
Cdd:cd07769 395 GIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDL-DELASLWQVDKRFEP 467
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
9-519 |
6.16e-27 |
|
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: 114.13 E-value: 6.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 9 DVGTGSARAGVFNENGTLLAVAKRPINI------WqeagdvVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGFD--- 79
Cdd:cd07786 6 DQGTTSSRAILFDHDGNIVAVAQREFTQiypkpgW------VEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITnqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 80 ATCsLVAVAADGSPVAvgssgdpkrNIIVWMDHRAAGEAEEINAGGHE--VLRYVGGRISPEMETPKLLWLKRNLPDSFA 157
Cdd:cd07786 80 ETT-VVWDRETGKPVY---------NAIVWQDRRTADICEELKAEGHEemIREKTGLVLDPYFSATKIRWILDNVPGARE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 158 AAKH---FFDLAD-YLTWRatgsLTRSTCTVT----CKWTYL--AHESRWDTDYFNKIG-----LEELV--AERFARIGT 220
Cdd:cd07786 150 RAERgelAFGTIDsWLIWK----LTGGKVHATdvtnASRTMLfnIHTLEWDDELLELFGipasmLPEVKpsSEVFGYTDP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 221 EIAWPGTPIASGLTETAAPELG---LHPGTAVAAslidahagglgtlgaagegvtsdigrrlayiFGTSA-CSMASSQEP 296
Cdd:cd07786 226 DLLGAEIPIAGIAGDQQAALFGqacFEPGMAKNT-------------------------------YGTGCfMLMNTGEKP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 297 VFVDgvwgpyfSAMIPDLWLNEGGQSA---------AGAAidhlvamhpasasatelaeaagiplVGWLdAEASKMCSSP 367
Cdd:cd07786 275 VRSK-------NGLLTTIAWQLGGKVTyalegsifiAGAA-------------------------VQWL-RDGLGLIESA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 368 EDVMALAHR------IHVVPEFLGNRSPNADPDARAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLRED-GIPI 440
Cdd:cd07786 322 AETEALARSvpdnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIAR---AALESIAYQTRDLLEAMEADsGIPL 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277285833 441 DLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLvDAMVTMSSISRVFEPAQGAPKKAH 519
Cdd:cd07786 399 KELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSL-DELAKLWQVDRRFEPSMSEEEREA 476
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-484 |
9.60e-23 |
|
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: 100.76 E-value: 9.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARAGVFN-ENGTLLAVAKRPINIW--QEAGDVVEQSSEDIWSAVSTSVREAVAASGvdtADIRGLGFda 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPisSDDPGRSEQDPEKILEAVRNLIDELPREYL---SDVTGIGI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 81 TC---SLVAVAADGSPVavgssgdpkRNIIVWMDHRAAGE-AEEINAGGHEVLRYVGGRISPEMETPKLLWLKRNLPDsF 156
Cdd:cd07777 76 TGqmhGIVLWDEDGNPV---------SPLITWQDQRCSEEfLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGPL-P 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 157 AAAKHFFDLADYLTWRATGsLTRSTCTVTCkwtylAH--------ESRWDTDYFNKIGLEEL----VAERFARIGT--EI 222
Cdd:cd07777 146 SKADRAGTIGDYIVARLTG-LPKPVMHPTN-----AAswglfdleTGTWNKDLLEALGLPVIllpeIVPSGEIVGTlsSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 223 AWPGTPIASGltetaapeLGLHPgTAVAASLIDAHagglgtlgaagegvtsdigRRLAYIFGTSA---CSMASSQEPVFV 299
Cdd:cd07777 220 LPKGIPVYVA--------LGDNQ-ASVLGSGLNEE-------------------NDAVLNIGTGAqlsFLTPKFELSGSV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 300 DGVwgPYFSamipDLWLNEGGQSAAGAAIDHLVAMHpasasaTELAEAAGIPLV-----GWLDAEASKMCSSPedvmala 374
Cdd:cd07777 272 EIR--PFFD----GRYLLVAASLPGGRALAVLVDFL------REWLRELGGSLSddeiwEKLDELAESEESSD------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 375 hrIHVVPEFLGNRSpnaDPDARAVIAGLSLDagipDL-VALYIAGLC-GIGYGLKQLLVKLREDGIPIDLIIASGGAAQ- 451
Cdd:cd07777 333 --LSVDPTFFGERH---DPEGRGSITNIGES----NFtLGNLFRALCrGIAENLHEMLPRLDLDLSGIERIVGSGGALRk 403
|
490 500 510
....*....|....*....|....*....|...
gi 1277285833 452 SDLVRQLLADATGVRVAVIDNPEPVLLGSAMLA 484
Cdd:cd07777 404 NPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
5-524 |
5.16e-20 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 93.11 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLAVAKRPI-NIWQEAGdVVEQSSEDIWSAVSTSVREAVAAsgvdtADIRGLGFDATCS 83
Cdd:PTZ00294 4 IGSIDQGTTSTRFIIFDEKGNVVSSHQIPHeQITPHPG-WLEHDPEEILRNVYKCMNEAIKK-----LREKGPSFKIKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 84 LVA------VAADGSpvavgsSGDPKRNIIVWMDHRAAGEAEEINA--GGHEVLRYVGG-RISPEMETPKLLWLKRNLPD 154
Cdd:PTZ00294 78 GITnqretvVAWDKV------TGKPLYNAIVWLDTRTYDIVNELTKkyGGSNFFQKITGlPISTYFSAFKIRWMLENVPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 155 SFAAAKH----FFDLADYLTWratgSLTRSTCTVT----CKWTYLA--HESRWDTDYFNKIGLEELV-------AERFAR 217
Cdd:PTZ00294 152 VKDAVKEgtllFGTIDTWLIW----NLTGGKSHVTdvtnASRTFLMniKTLKWDEELLNKFGIPKETlpeikssSENFGT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 218 IGTEIAWP--GTPIASGLTETAAPELG---LHPGTAVAAslidahagglgtlgaagegvtsdigrrlayiFGTSACSMAS 292
Cdd:PTZ00294 228 ISGEAVPLleGVPITGCIGDQQAALIGhgcFEKGDAKNT-------------------------------YGTGCFLLMN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 293 S-QEPVFV-DGVWGP--Y-FSAMIPDLWLNEGGQSAAGAAIDhlvamhpasasatelaeaagiplvgWLDAEAsKMCSSP 367
Cdd:PTZ00294 277 TgTEIVFSkHGLLTTvcYqLGPNGPTVYALEGSIAVAGAGVE-------------------------WLRDNM-GLISHP 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 368 EDVMALAHRIH------VVPEFLGNRSPNADPDARAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLRED-GIPI 440
Cdd:PTZ00294 331 SEIEKLARSVKdtggvvFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVR---AALEAIALQTNDVIESMEKDaGIEL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 441 DLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEPAQGAPKKahE 520
Cdd:PTZ00294 408 NSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSNSTFSPQMSAEER--K 485
|
....
gi 1277285833 521 TRYR 524
Cdd:PTZ00294 486 AIYK 489
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-496 |
3.02e-17 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 84.63 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIGVDVGTGSARAGVFNENGTLLA------VAKRPINIWQEagdvveQSSEDIWSAVSTSVREAVAASGVDtaDIRGLGf 78
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVAsqteklTVSRPHPLWSE------QDPEQWWQATDRAMKALGDQHSLQ--DVKALG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 79 datcslVAVAADGSPVaVGSSGDPKRNIIVWMDHRAAGEAEEINAGGHEVLRYVGGRISPEMETPKLLWLKRNLPDSFAA 158
Cdd:PRK15027 73 ------IAGQMHGATL-LDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 159 AKHFFDLADYLTWRATGSLTRSTCTVT-CKWTYLAHESrWDTDYFNKIGL-EELVAERFAriGTEI----------AW-- 224
Cdd:PRK15027 146 IDKVLLPKDYLRLRMTGEFASDMSDAAgTMWLDVAKRD-WSDVMLQACHLsRDQMPALYE--GSEItgallpevakAWgm 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 225 PGTPIASGLTETAApelglhpgTAVAASLIDAHAGGLGtlgaagegvtsdigrrlayiFGTSACSMASSqepvfvDGVWG 304
Cdd:PRK15027 223 ATVPVVAGGGDNAA--------GAVGVGMVDANQAMLS--------------------LGTSGVYFAVS------EGFLS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 305 PYFSAM------IPDLWlneggqsaagaaidHLVAMHPASASATE-LAEAAGIPLVGWLDAEASKMCSSPEDVMALahri 377
Cdd:PRK15027 269 KPESAVhsfchaLPQRW--------------HLMSVMLSAASCLDwAAKLTGLSNVPALIAAAQQADESAEPVWFL---- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 378 hvvPEFLGNRSPNADPDARAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLREDGIPIDLIIASGGAAQSDLVRQ 457
Cdd:PRK15027 331 ---PYLSGERTPHNNPQAKGVFFGLTHQHGPNELAR---AVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQ 404
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1277285833 458 LLADATGVRVAVIDNPE--PVlLGSAMLAAVASGHRRNLVD 496
Cdd:PRK15027 405 MLADISGQQLDYRTGGDvgPA-LGAARLAQIAANPEKSLIE 444
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-524 |
1.36e-16 |
|
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: 82.57 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIG-VDVGTGSARAGVFNENGTLLAVAKRPI-NIWQEAGdVVEQSSEDIWSAVSTSVREAVA---ASGVDTADIRGLG-- 77
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHkQIYPKPG-WVEHDPMEILESVYECIEEAVEklkALGISPSDIKAIGit 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 78 --------FDAtcslvavaadgspvavgSSGDPKRNIIVWMDHRAAGEAEEI---NAGGHEVLRYVGG-RISPEMETPKL 145
Cdd:cd07792 81 nqrettvvWDK-----------------STGKPLYNAIVWLDTRTSDTVEELsakTPGGKDHFRKKTGlPISTYFSAVKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 146 LWLKRNLPDSFAAAK----HFFDLADYLTWRATGSLTRST-CT-VTckwtylaHESR----------WDTDYFNKIGLEE 209
Cdd:cd07792 144 RWLLDNVPEVKKAVDdgrlLFGTVDSWLIWNLTGGKNGGVhVTdVT-------NASRtmlmnlrtlqWDPELCEFFGIPM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 210 LV-------AERFARIGTEiAWPGTPIASGLTETAAPELG---LHPGTAvaaslidahagglgtlgaagegvtsdigrRL 279
Cdd:cd07792 217 SIlpeirssSEVYGKIASG-PLAGVPISGCLGDQQAALVGqgcFKPGEA-----------------------------KN 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 280 AYifGTsACSMASS--QEPVFVD-----------GVWGPYFSAMipdlwlnEGGQSAAGAAI----DHLvamhpasasat 342
Cdd:cd07792 267 TY--GT-GCFLLYNtgEEPVFSKhgllttvayklGPDAPPVYAL-------EGSIAIAGAAVqwlrDNL----------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 343 ELAEAAgiplvgwldAEASKMCSSPEDvmalAHRIHVVPEFLGNRSPNADPDARAVIAGLSLdagipdlvalYI------ 416
Cdd:cd07792 326 GIISSA---------SEVETLAASVPD----TGGVYFVPAFSGLFAPYWRPDARGTIVGLTQ----------FTtkahia 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 417 -AGLCGIGYGLKQLLVKLRED-GIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNL 494
Cdd:cd07792 383 rAALEAVCFQTREILDAMNKDsGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSL 462
|
570 580 590
....*....|....*....|....*....|
gi 1277285833 495 VDAMVTMSSISRVFEPAQGAPKKahETRYR 524
Cdd:cd07792 463 DELKSLNEGGRTVFEPQISEEER--ERRYK 490
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-540 |
8.23e-16 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 80.05 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 1 MAAHFIGVDVGTGSARAGVFNENGTLLAVAKRPiniWQEAGDV-VEQSSE-DI---WSAVSTSVREAVAASGVDTADIRG 75
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAE---WRHLAVPdVPGSMEfDLeknWQLACQCIRQALQKAGIPASDIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 76 LgfdATCSL----VAVAADGSPV-AVGSsgdpkrniivwMDHRAAGEAEEINAGgHEVLRYVGGRISPEM----ETPKLL 146
Cdd:PRK10939 78 V---SATSMregiVLYDRNGTEIwACAN-----------VDARASREVSELKEL-HNNFEEEVYRCSGQTlalgALPRLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 147 WLKRNLPDSFAAAKHFFDLADYLTWRATGSLT---RSTCTVtckwTYLAHESR-WDTDYFNKIGLEelvaerfARIGTEI 222
Cdd:PRK10939 143 WLAHHRPDIYRQAHTITMISDWIAYMLSGELAvdpSNAGTT----GLLDLVTRdWDPALLEMAGLR-------ADILPPV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 223 AWPGTPIASgLTETAAPELGLHPGTAVAASLIDAHAGGLGTlgaageGVTsDIGRrlAYIFGTSACSMASSQEPVFVDgv 302
Cdd:PRK10939 212 KETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDVQLGCLGL------GVV-RPGQ--TAVLGGTFWQQVVNLPAPVTD-- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 303 wgPYFS-----AMIPDLWLNEGGQSAAGAAI----DHLVAMHPAsasateLAEAAGIPLVGWLDAEASKMcssP------ 367
Cdd:PRK10939 280 --PNMNirinpHVIPGMVQAESISFFTGLTMrwfrDAFCAEEKL------LAERLGIDAYSLLEEMASRV---Pvgshgi 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 368 ----EDVMALAHRIHVVPEFLgNRSPNADPDARAVI-AGLSLDAGIPDLVAL-YIAGLCGigyglkqllVKLREdgipid 441
Cdd:PRK10939 349 ipifSDVMRFKSWYHAAPSFI-NLSIDPEKCNKATLfRALEENAAIVSACNLqQIAAFSG---------VFPSS------ 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 442 lIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEPAQG--APKKAH 519
Cdd:PRK10939 413 -LVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPEnhELYQEA 491
|
570 580
....*....|....*....|...
gi 1277285833 520 ETRY-RIFES-LQLVDREIRTEL 540
Cdd:PRK10939 492 KEKWqAVYADqLGLVDHGLTTSM 514
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-524 |
1.82e-14 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 76.02 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 1 MAAHFIG-VDVGTGSARAGVFNENGTLLAVAKRPIN-IWQEAGdVVEQSSEDIWSAVSTSVREAVAASGVDTADIRGLGF 78
Cdd:PRK00047 2 MMKKYILaLDQGTTSSRAIIFDHDGNIVSVAQKEFTqIFPQPG-WVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 79 daT----CSLVAVAADGSPVAvgssgdpkrNIIVWMDHRAAGEAEEINAGGHE--VLRYVGGRISPEMETPKLLWLKRNL 152
Cdd:PRK00047 81 --TnqreTTVVWDKETGRPIY---------NAIVWQDRRTADICEELKRDGYEdyIREKTGLVIDPYFSGTKIKWILDNV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 153 PDSFAAAKH---FFDLAD-YLTWRATGSLTRSTCTVTCKWTYL--AHESRWDT---DYFN--KIGLEELVA--ERFARI- 218
Cdd:PRK00047 150 EGARERAEKgelLFGTIDtWLVWKLTGGKVHVTDYTNASRTMLfnIHTLDWDDellELLDipRSMLPEVRPssEVYGKTn 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 219 -----GTEIawpgtPIASGLTETAAP---ELGLHPGTAVAAslidahagglgtlgaagegvtsdigrrlayiFGTsAC-- 288
Cdd:PRK00047 230 pygffGGEV-----PIAGIAGDQQAAlfgQLCFEPGMAKNT-------------------------------YGT-GCfm 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 289 SMASSQEPVFVD---------GVWGPYFSAMipdlwlnEGGQSAAGAAI----DHLVAMHPASASatelaeaagiplvgw 355
Cdd:PRK00047 273 LMNTGEKAVKSEngllttiawGIDGKVVYAL-------EGSIFVAGSAIqwlrDGLKIISDASDS--------------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 356 lDAEASKMCSSPEdvmalahrIHVVPEFLGNRSPNADPDARAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLRE 435
Cdd:PRK00047 331 -EALARKVEDNDG--------VYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIR---ATLESIAYQTRDVLDAMQA 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 436 D-GIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLvDAMVTMSSISRVFEPAQGA 514
Cdd:PRK00047 399 DsGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDL-DELKEQWKIDRRFEPQMDE 477
|
570
....*....|
gi 1277285833 515 PKKahETRYR 524
Cdd:PRK00047 478 EER--EKLYA 485
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
9-510 |
4.55e-13 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 71.21 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 9 DVGTGSARAGVFNENGTLLAVAKRPIN--IWQEAGDVVEQSSEDIWSAVSTSVREAvaASGVDTADIRGLgfdatcSLVA 86
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPNAsdIAAENSDWHQWSLDAILQRFADCCRQI--NSELTECHIRGI------TVTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 87 VAADGSPVavGSSGDPKRNIIVWMDHRAAGEAEEINagghevlRYvggrISPE------------METP-KLLWLKRNLP 153
Cdd:PRK10331 80 FGVDGALV--DKQGNLLYPIISWKCPRTAAVMENIE-------RY----ISAQqlqqisgvgafsFNTLyKLVWLKENHP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 154 DSFAAAKHFFDLADYLTWRATGSL-TRSTCTVTCKWTYLAHESrWDTDYFNKIGLEElvaERFARIgteiAWPGTPIASg 232
Cdd:PRK10331 147 QLLEQAHAWLFISSLINHRLTGEFtTDITMAGTSQMLDIQQRD-FSPEILQATGLSR---RLFPRL----VEAGEQIGT- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 233 LTETAAPELGLHPGTAVAASLIDAHAGGLGTLGAAGEGVTSDigrrlayifGTSACSMASSQEpvfVDGVWGPYFSAMIP 312
Cdd:PRK10331 218 LQPSAAALLGLPVGIPVISAGHDTQFALFGSGAGQNQPVLSS---------GTWEILMVRSAQ---VDTSLLSQYAGSTC 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 313 DL-----WLNEGGQSAAGAAIDHLVAM--HPASASATELAEAAGIPLvgwlDAEASKMcsspedvmalahrihvVPEFLG 385
Cdd:PRK10331 286 ELdsqsgLYNPGMQWLASGVLEWVRKLfwTAETPYQTMIEEARAIPP----GADGVKM----------------QCDLLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 386 NRspnadpdaRAVIAGLSLDAGIPDLvalYIAGLCGIGYGLKQLLVKLREDG-IPIDLIIASGGAAQSDLVRQLLADATG 464
Cdd:PRK10331 346 CQ--------NAGWQGVTLNTTRGHF---YRAALEGLTAQLKRNLQVLEKIGhFKASELLLVGGGSRNALWNQIKANMLD 414
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1277285833 465 VRVAVIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEP 510
Cdd:PRK10331 415 IPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYP 460
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
5-518 |
5.07e-13 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 71.27 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 5 FIG-VDVGTGSARAGVFNENGTLLAVAKRPI-NIWQEAGdVVEQSSEDIWSAVSTSVREAVAAsgvdtADIRGLGFDATC 82
Cdd:PLN02295 1 FVGaIDQGTTSTRFIIYDRDARPVASHQVEFtQIYPQAG-WVEHDPMEILESVLTCIAKALEK-----AAAKGHNVDSGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 SLVAVAADGSPVAV--GSSGDPKRNIIVWMDHRAAGEAEEIN---AGGHEVLRYVGG-RISPEMETPKLLWLKRNLPDSF 156
Cdd:PLN02295 75 KAIGITNQRETTVAwsKSTGRPLYNAIVWMDSRTSSICRRLEkelSGGRKHFVETCGlPISTYFSATKLLWLLENVDAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 157 AAAKH----FFDLADYLTWRATGSLTRST----CTVTCKWTYLAHESR-WDTDYFNKIG-----LEELV--AERFARIGT 220
Cdd:PLN02295 155 EAVKSgdalFGTIDSWLIWNLTGGASGGVhvtdVTNASRTMLMNLKTLdWDKPTLEALGipaeiLPKIVsnSEVIGTIAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 221 EIAWPGTPIASGLTETAAPELG--LHPGTA-----VAASLIdahagglgtLGAAGEGVTSDIG--RRLAYIFGTSAcsma 291
Cdd:PLN02295 235 GWPLAGVPIAGCLGDQHAAMLGqrCRPGEAkstygTGCFIL---------LNTGEEVVPSKHGllTTVAYKLGPDA---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 292 ssqepvfvdgvwgpyfsamiPDLWLNEGGQSAAGAAI----DHLVAMHPASasatelaeaagiplvgwldaEASKMCSSP 367
Cdd:PLN02295 302 --------------------PTNYALEGSVAIAGAAVqwlrDNLGIIKSAS--------------------EIEALAATV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 368 EDvmalAHRIHVVPEFLGNRSPNADPDARAVIAGLSLDAGIPDLVAlyiAGLCGIGYGLKQLLVKLREDGIPID------ 441
Cdd:PLN02295 342 DD----TGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIAR---AVLESMCFQVKDVLDAMRKDAGEEKshkglf 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277285833 442 LIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAAVASGHRRNLVDAMVTMSSISRVFEPAQGAPKKA 518
Cdd:PLN02295 415 LLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPKLDEEERA 491
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
4-497 |
4.77e-09 |
|
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: 58.69 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 4 HFIGVDVGTGSARA--GVFNENGTLLAVAKR----PINI-----WqeagDVveqssEDIWSAVSTSVREAVAASGvdtaD 72
Cdd:cd07771 1 NYLAVDLGASSGRVilGSLDGGKLELEEIHRfpnrPVEInghlyW----DI-----DRLFDEIKEGLKKAAEQGG----D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 73 IRGLGFDATCslvavaADGspVAVGSSGDPKRNIIVWMDHRaageaeeinagGHEVLRYVGGRISPE---MET------- 142
Cdd:cd07771 68 IDSIGIDTWG------VDF--GLLDKNGELLGNPVHYRDPR-----------TEGMMEELFEKISKEelyERTgiqfqpi 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 143 ---PKLLWLKRNLPDSFAAAKHFFDLADYLTWRATGSltrstctVTCKWT-------YLAHESRWDTDYFNKIGLEelvA 212
Cdd:cd07771 129 ntlYQLYALKKEGPELLERADKLLMLPDLLNYLLTGE-------KVAEYTiasttqlLDPRTKDWSEELLEKLGLP---R 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 213 ERFARIGTeiawPGTPIASgLTETAAPELGLHP-----------GTAVAAslidahagglgtlgaagegvTSDIGRRLAY 281
Cdd:cd07771 199 DLFPPIVP----PGTVLGT-LKPEVAEELGLKGipviavashdtASAVAA--------------------VPAEDEDAAF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 282 IF-GTSACSMASSQEPVFVDGVWGPYFSAM------------IPDLWL-NE--GGQSAAGAAIDHlvamhpasASATELA 345
Cdd:cd07771 254 ISsGTWSLIGVELDEPVITEEAFEAGFTNEggadgtirllknITGLWLlQEcrREWEEEGKDYSY--------DELVALA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 346 EAAgIPLVGWLD------AEASKMcssPEDVMALAHRihvvpefLGNRSPNADPD-ARAVIAGLsldagipdlvALYIAg 418
Cdd:cd07771 326 EEA-PPFGAFIDpddprfLNPGDM---PEAIRAYCRE-------TGQPVPESPGEiARCIYESL----------ALKYA- 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277285833 419 lcgigYGLKQlLVKLRedGIPIDLIIASGGAAQSDLVRQLLADATGVRVaVIDNPEPVLLGSAMLAAVASGHRRNLVDA 497
Cdd:cd07771 384 -----KTIEE-LEELT--GKRIDRIHIVGGGSRNALLCQLTADATGLPV-IAGPVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-78 |
1.05e-06 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 50.67 E-value: 1.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277285833 1 MAAHFIGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQssediwsaVSTSVREAVAASGVDTADIRGLGF 78
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEA--------IAELIEELLAEAGISRGRILGIGI 72
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
437-485 |
8.02e-05 |
|
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: 45.24 E-value: 8.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1277285833 437 GIPIDLIIASGGAAQSDLVRQLLADATGVRVAVIDNPEPVLLGSAMLAA 485
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAA 471
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
8-175 |
3.36e-04 |
|
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: 43.02 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 8 VDVGTGSARAGVFNENGTLLAVAKRPINIWQEAG----DVveqssEDIWSAVSTSVREAVaasgvDTADIRGLGFdaTC- 82
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEIEEDGypceDV-----EAIWEWLLDSLAELA-----KRHRIDAINF--TTh 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277285833 83 --SLVAVAADGSPV-AVgssgdpkrniivwMDHRAAGeAEEINAGGHEVLRYVGGRISPEMetP-------KLLWLKRNL 152
Cdd:cd07772 73 gaTFALLDENGELAlPV-------------YDYEKPI-PDEINEAYYAERGPFEETGSPPL--PgglnlgkQLYWLKREK 136
|
170 180
....*....|....*....|...
gi 1277285833 153 PDSFAAAKHFFDLADYLTWRATG 175
Cdd:cd07772 137 PELFARAKTILPLPQYWAWRLTG 159
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
6-77 |
3.61e-03 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 39.37 E-value: 3.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277285833 6 IGVDVGTGSARAGVFNENGTLLAVAKRPINIWQEAGDVVEQssediwsaVSTSVREAVAASGVDtADIRGLG 77
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDR--------IAELIEELLAEAGVR-ERILGIG 63
|
|
| |
