|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-553 |
0e+00 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 938.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 1 MAIAIGLDFGSDSVRALAVDCASGEEIATSVEWYPRWQKGQFCDAPNNQFRHHPRDYIESMEAALKTVLAELSVeQRAAV 80
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDCATGEELATAVVEYPHWVKGRYLDLPPNQALQHPLDYIESLEAAIPAVLKEAGV-DPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 81 VGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEAEEITRLCHAPGNVDYSRYIGGIYSSEWFWAKI 160
Cdd:PRK04123 81 VGIGVDFTGSTPAPVDADGTPLALLPEFAENPHAMVKLWKDHTAQEEAEEINRLAHERGEADLSRYIGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 161 LHVTRQDSAVAQSAASWIELCDWVPALLSGTTRPQDIRRGRCSAGHKSLWHESWGGLPPASFFDELDPILNRHLPSPLFT 240
Cdd:PRK04123 161 LHVLREDPAVYEAAASWVEACDWVVALLTGTTDPQDIVRSRCAAGHKALWHESWGGLPSADFFDALDPLLARGLRDKLFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 241 DTWTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGAQPNALVKVIGTSTCDILIADKQsvgeRAVKGICGQV 320
Cdd:PRK04123 241 ETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGAEPGTLVKVMGTSTCDILLADKQ----RAVPGICGQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 321 DGSVVPGFIGLEAGQSAFGDIYAWFGRVLGwpleqlaaqHPELKAQINASQKQLLPALTEAWAKNPSLDHLPVVLDWFNG 400
Cdd:PRK04123 317 DGSIVPGLIGYEAGQSAVGDIFAWFARLLV---------PPEYKDEAEARGKQLLELLTEAAAKQPPGEHGLVALDWFNG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 401 RRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARKNQVIMQACCDVLNRPL 480
Cdd:PRK04123 388 RRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIARKNPVLMQIYADVLNRPI 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1412217475 481 QIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASAVEKTLQPRSEQAQRFEQLYRRYQQWamsAEQHYLPT 553
Cdd:PRK04123 468 QVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASPVEKTYQPDPENVARYEQLYQEYKQL---HDYFGRGG 537
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
2-553 |
0e+00 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 872.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 2 AIAIGLDFGSDSVRALAVDCASGEEIATSVEWYPRWQKGQFCDA-----PNNQFRHHPRDYIESMEAALKTVLAELSVEQ 76
Cdd:TIGR01234 1 AYAIGVDFGTLSGRALAVDVATGEEIATAVEWYRHWVKGQFLPKtgaklPNDQALQHPADYIEVLEAAIPTVLAELGVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 77 rAAVVGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEAEEITRLCHAPGNVDYSRYiGGIYSSEWF 156
Cdd:TIGR01234 81 -ADVVGIGVDFTACTPAPIDSDGNPLCLLPEFAENPHAYFKLWKHHAAQEEADRINRLAHAPGEVDLSRY-GGIISSEWF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 157 WAKILHVTRQDSAVAQSAASWIELCDWVPALLSGttrpqDIRRGRCSAGHKSLWHESWGgLPPASFFDELDPILNRHLPS 236
Cdd:TIGR01234 159 WAKILQITEEDPAIYQAADRWIELADWIVAQLSG-----DIRRGRCTAGYKALWHESWG-YPSASFFDELNPILNRHLPD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 237 PLFTDTWTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAG-AQPNALVKVIGTSTCDILIADKQsvgeRAVKG 315
Cdd:TIGR01234 233 KLFTDIWTAGEPAGTLTPEWAQRTGLPEGVVVAVGNFDAHVGAVAAGiAQPGALVKIMGTSTCHVLIGDKQ----RAVPG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 316 ICGQVDGSVVPGFIGLEAGQSAFGDIYAWFGRVLgwpleqlaaQHPELKAQINASQKQLLPALTEAWAKNPSLDHLPVVL 395
Cdd:TIGR01234 309 MCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGKVC---------VPPELKTEANASQKQLHEALSEAAAKQPSGEHGLVAL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 396 DWFNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARKNQVIMQACCDV 475
Cdd:TIGR01234 380 DWFNGNRSPLVDQRLKGVITGLTLATDAPLLYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIARKNPVIMQIYADV 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1412217475 476 LNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASAVEKTLQPRSEQAQRFEQLYRRYQQWAMSAEQhYLPT 553
Cdd:TIGR01234 460 TNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLTPCSENAQRYEQLYARYQELAMSFGQ-YNPT 536
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-550 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 817.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 1 MAIAIGLDFGSDSVRALAVDCASGEEIATSVEWYPRWQKGQFCDAPNNQFRHHPRDYIESMEAALKTVLAELSVeQRAAV 80
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAADGEELASAVHPYPRWVIGLYLPPPPDQARQHPLDYLEALEAAVREALAQAGV-DPADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 81 VGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEAEEITRLCHApGNVDYSRYIGGIYSSEWFWAKI 160
Cdd:COG1069 80 VGIGVDATGCTPVPVDADGTPLALLPEFAENPHAMVILWKDHTAQEEAERINELAKA-RGEDYLRYVGGIISSEWFWPKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 161 LHVTRQDSAVAQSAASWIELCDWVPALLSGttrpqDIRRGRCSAGHKSLWHESWGGLPPASFFDELDPILNrHLPSPLFT 240
Cdd:COG1069 159 LHLLREDPEVYEAADSFVELCDWITWQLTG-----SLKRSRCTAGHKALWHAHEGGYPSEEFFAALDPLLD-GLADRLGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 241 DTWTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDILIADKqsvgERAVKGICGQ 319
Cdd:COG1069 233 EIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGvEPGTLVKVMGTSTCHMLVSPE----ERFVPGICGQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 320 VDGSVVPGFIGLEAGQSAFGDIYAWFGRVLGWPLEqlaaqhpeLKAQINASQKQLLPALTEAWAKNPSLDHLPVVLDWFN 399
Cdd:COG1069 309 VDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLE--------YEKEAEERGISLHPLLTEEAAKLPPGESGLHALDWFN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 400 GRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARKNQVIMQACCDVLNRP 479
Cdd:COG1069 381 GNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIATKNPLVMQIYADVTGRP 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1412217475 480 LQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASAVEKTLQPRSEQAQRFEQLYRRYQQWAMSAEQHY 550
Cdd:COG1069 461 IKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGFDKVYTPDPENVAVYDALYAEYLQLHDYFGRGR 531
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-548 |
0e+00 |
|
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: 642.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 3 IAIGLDFGSDSVRALAVDCASGEEIATSVEWYPRWqkgqFCDAPNNQFRHHPRDYIESMEAALKTVLAELSVeQRAAVVG 82
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLADGEELASAVVPYPTG----YIPPRPGWAEQNPADYWEALEEAVRGALAEAGV-DPEDVVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 83 IGVDSTGSTPAPIDADGNvlalrpefaenPNAMFVLWKDHTAVEEAEEITRLCHAPGNVDYSRYiGGIYSSEWFWAKILH 162
Cdd:cd07781 76 IGVDTTSSTVVPVDEDGN-----------PLAPAILWMDHRAQEEAAEINETAHPALEYYLAYY-GGVYSSEWMWPKALW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 163 VTRQDSAVAQSAASWIELCDWVPALLSGTtrpqdIRRGRCSAGHKSLWHEsWGGLPPASFFDELDPILNRhLPSPLFTDT 242
Cdd:cd07781 144 LKRNAPEVYDAAYTIVEACDWINARLTGR-----WVRSRCAAGHKWMYNE-WGGGPPREFLAALDPGLLK-LREKLPGEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 243 WTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDILIADKqsvgERAVKGICGQVD 321
Cdd:cd07781 217 VPVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVvEPGTLALIMGTSTCHLMVSPK----PVDIPGICGPVP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 322 GSVVPGFIGLEAGQSAFGDIYAWFGRVLGWPLEQLAaqhpelkaqinasqKQLLPALTEAWAKNPSLDHLPVVLDWFNGR 401
Cdd:cd07781 293 DAVVPGLYGLEAGQSAVGDIFAWFVRLFVPPAEERG--------------DSIYALLSEEAAKLPPGESGLVALDWFNGN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 402 RTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARKNQVIMQACCDVLNRPLQ 481
Cdd:cd07781 359 RTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAEKNPLWMQIYADVLGRPIK 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1412217475 482 IVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASaVEKTLQPRSEQAQRFEQLYRRYQQWAMSAEQ 548
Cdd:cd07781 439 VPKSDQAPALGAAILAAVAAGVYADIEEAADAMVR-VDRVYEPDPENHAVYEELYALYKELYDALGP 504
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
5-541 |
7.04e-68 |
|
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: 228.66 E-value: 7.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDCASGEEIAT-SVEWYprwqkgQFCDAPNNQFRHHPRDYIESMEAALKTVLAELSVEQrAAVVGI 83
Cdd:cd07768 3 IGVDVGTSSARAGVYDLYAGLEMAQePVPYY------QDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDA-YEVKGC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVDSTGSTpAPIDADGNVLALRPEFaeNPNAMFVLWKDHTAVEEAEEITRLCHAPGnvdySRYIGGIYSSEWFWAKILHV 163
Cdd:cd07768 76 GVDATCSL-AIFDREGTPLMALIPY--PNEDNVIFWMDHSAVNEAQWINMQCPQQL----LDYLGGKISPEMGVPKLKYF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 164 TRQDSAVAQSAASWIELCDWVPALLSGttrpqDIRRGRCSAGHKSLWHESWGGlPPASFFDELDPILNRHLPSPLFTDTW 243
Cdd:cd07768 149 LDEYSHLRDKHFHIFDLHDYIAYELTR-----LYEWNICGLLGKENLDGEESG-WSSSFFKNIDPRLEHLTTTKNLPSNV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 244 TADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMG--AVGAGAQPNALVKVIGTSTCDILIADKqsvgERAVKGICGQVD 321
Cdd:cd07768 223 PIGTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASwfAVASPHLETSLFMIAGTSSCHMYGTTI----SDRIPGVWGPFD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 322 GSVVPGFIGLEAGQSAFGDIYAWFgrvlgwpleqlAAQHPELKAQINASQK-----QLLPALTEAWAKNPSLDHLPVVLD 396
Cdd:cd07768 299 TIIDPDYSVYEAGQSATGKLIEHL-----------FESHPCARKFDEALKKgadiyQVLEQTIRQIEKNNGLSIHILTLD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 397 WFNGRRTPNANQRLKGVITDLNLAT---DTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIArKNQVIMQACC 473
Cdd:cd07768 368 MFFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQA-KNERLLQLIA 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1412217475 474 DVLNRPLQIVASDQCCALGAA--IFAAVAAKVHAD-IPSAQQKMaSAVEKTLQPRS-EQAQRFEQLYRRYQQ 541
Cdd:cd07768 447 LVTNVAIIKPKENMMGILGAAvlAKVAAGKKQLADsITEADISN-DRKSETFEPLAyRLGADYILLYKLLCV 517
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-541 |
2.60e-51 |
|
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: 183.50 E-value: 2.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPrwqkgqfCDAPNNQFR-HHPRDYIESMEAALKTVLAELSVEqRAAVVGI 83
Cdd:COG1070 4 LGIDIGTTSVKAVLFD-ADGEVVASASAEYP-------LSSPHPGWAeQDPEDWWEAVVEAIRELLAKAGVD-PEEIAAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVDSTGSTPAPIDADGNVLalRPefaenpnamFVLWKDHTAVEEAEEITRlchAPGNVDYSRYIGGIYSSEWFWAKILHV 163
Cdd:COG1070 75 GVSGQMHGLVLLDADGEPL--RP---------AILWNDTRAAAEAAELRE---ELGEEALYEITGNPLHPGFTAPKLLWL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 164 TRQDSAVAQSAASWIELCDWV-----------PALLSGTTrPQDIRRGRcsaghkslWHE---SWGGLPPAsffdeldpi 229
Cdd:COG1070 141 KENEPEIFARIAKVLLPKDYLryrltgefvtdYSDASGTG-LLDVRTRD--------WSDellEALGIDRE--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 230 lnrHLPSPLftdtWTADIpVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDILIADKQSV 308
Cdd:COG1070 203 ---LLPELV----PPGEV-AGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGAvEPGDAAVSLGTSGVVFVVSDKPLP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 309 GER-AVKGICGQVDGSVVPGfigleAGQSAFGDIYAWFGRVLGwpleqlaaqhpelkaqinASQKQLLPALTEAWAKNPS 387
Cdd:COG1070 275 DPEgRVHTFCHAVPGRWLPM-----GATNNGGSALRWFRDLFA------------------DGELDDYEELNALAAEVPP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 388 LDHLPVVLDWFNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARkNQV 467
Cdd:COG1070 332 GADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGAR-SPL 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1412217475 468 IMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMAsAVEKTLQPRSEQAQRFEQLYRRYQQ 541
Cdd:COG1070 411 WRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMV-RVGETIEPDPENVAAYDELYERYRE 483
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
5-540 |
3.68e-44 |
|
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: 164.63 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDCaSGEEIATSVEwyprwqkgqfcdapNNQFRHHPRDYIE--SME------AALKTVLAELSVEq 76
Cdd:cd07782 3 IGVDVGTGSARAGLFDL-DGRLLATASQ--------------PITTWNPKPDFYEqsSEDiwqavcEAVKEVLEGAGVD- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 77 RAAVVGIGVDSTGSTPApIDADGNVLALRPEfaENPNAMFVLWKDHTAVEEAEEITRLCHAPgnvdySRYIGGIYSSEWF 156
Cdd:cd07782 67 PEQVKGIGFDATCSLVV-LDAEGKPVSVSPS--GDDERNVILWMDHRAVEEAERINATGHEV-----LKYVGGKISPEME 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 157 WAKILHVTRQDSAVAQSAASWIELCDWvpalLS-----GTTRPQdirrgrCSAGHKSLW------HESWgglpPASFFDE 225
Cdd:cd07782 139 PPKLLWLKENLPETWAKAGHFFDLPDF----LTwkatgSLTRSL------CSLVCKWTYlahegsEGGW----DDDFFKE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 226 LDP---------ILNRHLPSPlftdtwtADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVG-AGAQ---------- 285
Cdd:cd07782 205 IGLedlvednfaKIGSVVLPP-------GEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGtLGADvgglpceadp 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 286 -PNALVKVIGTSTCDILIADKQsvgeRAVKGICGQVDGSVVPGFIGLEAGQSAFGdiyAWFGRVLGWpleqlAAQHPELK 364
Cdd:cd07782 278 lTRRLALICGTSSCHMAVSPEP----VFVPGVWGPYYSAMLPGLWLNEGGQSATG---ALLDHIIET-----HPAYPELK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 365 AQINASQKQLLPALTE-----AWAKNPSLDHLPV---VLDWFNGRRTPNANQRLKGVITDLNLATDTP---LLFGGLIAA 433
Cdd:cd07782 346 EEAKAAGKSIYEYLNErleqlAEEKGLPLAYLTRdlhVLPDFHGNRSPLADPTLRGMISGLTLDTSLDdlaLLYLATLQA 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 434 TAFGARAIMECFTDQGIAVNNVMALGGIArKNQVIMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQQK 513
Cdd:cd07782 426 LAYGTRHIIEAMNAAGHKIDTIFMCGGLS-KNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAA 504
|
570 580
....*....|....*....|....*..
gi 1412217475 514 MaSAVEKTLQPrSEQAQRFEQlyRRYQ 540
Cdd:cd07782 505 M-SGPGKVVEP-NEELKKYHD--RKYE 527
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
5-492 |
9.29e-41 |
|
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: 153.13 E-value: 9.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPRwqkgqfCDAPNNQFRHHPRDYIESMEAALKTVLAELSVEQraaVVGIG 84
Cdd:cd07773 3 LGIDIGTTNVKAVLFD-EDGRILASASRETPL------IHPGPGWAELDPEELWEAVKEAIREAAAQAGPDP---IAAIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 85 VDSTGSTPAPIDADGNVLAlrpefaenpNAMfvLWKDHTAVEEAEEITRLChapGNVDYSRYIGGIYSSEWFWAKILHVT 164
Cdd:cd07773 73 VSSQGESGVPVDRDGEPLG---------PAI--VWFDPRGKEEAEELAERI---GAEELYRITGLPPSPMYSLAKLLWLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 165 RQDSAVAQSAASWIELCDWVPALLSG---TTRPQ-------DIRRGRcsaghkslWHE---SWGGLPPasffdeldpiln 231
Cdd:cd07773 139 EHEPEIFAKAAKWLSVADYIAYRLTGepvTDYSLasrtmlfDIRKRT--------WSEellEAAGIDA------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 232 RHLPSPLFTDTwtadiPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDILIADKQSVGE 310
Cdd:cd07773 199 SLLPELVPSGT-----VIGTVTPEAAEELGLPAGTPVVVGGHDHLCAALGAGViEPGDVLDSTGTAEALLAVVDEPPLDE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 311 RAVKGICgQVDGSVVPGFIGLEAGQSAfGDIYAWFGRVLGWPLEQLAAQHPELKAQINASQKqllpalteawaknpsldh 390
Cdd:cd07773 274 MLAEGGL-SYGHHVPGGYYYLAGSLPG-GALLEWFRDLFGGDESDLAAADELAEAAPPGPTG------------------ 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 391 lPVVLDWFNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARkNQVIMQ 470
Cdd:cd07773 334 -LLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGAR-SPLWLQ 411
|
490 500
....*....|....*....|..
gi 1412217475 471 ACCDVLNRPLQIVASDQCCALG 492
Cdd:cd07773 412 LKADILGRPIEVPEVPEATALG 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
5-492 |
2.21e-34 |
|
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: 134.23 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPRwqkgqfcDAPNNQFR-HHPRDYIESMEAALKTVLAELSVEqRAAVVGI 83
Cdd:cd00366 3 LGIDIGTTSVKAALFD-EDGNLVASASREYPL-------IYPQPGWAeQDPEDWWQAVVEAIREVLAKAGID-PSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVDSTGSTPAPIDADGNVLalRPefaenpnamFVLWKDHTAveeaeeitRLCHAPGnvdysrYIG----GIYSSEWfwak 159
Cdd:cd00366 74 GISGQMPGVVLVDADGNPL--RP---------AIIWLDRRA--------KFLQPND------YIVfrltGEFAIDY---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 160 ilhvtrqdsavaqSAASWIELCDwvpallsgttrpqdIRRGRcsaghkslWHESwgglppasFFDELDpILNRHLPSPLf 239
Cdd:cd00366 125 -------------SNASGTGLYD--------------IKTGD--------WSEE--------LLDALG-IPREKLPPIV- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 240 tdtWTADIpVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDILIADKQSVGERAVKGICg 318
Cdd:cd00366 160 ---ESGEV-VGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVvEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRC- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 319 qvdgSVVPGFIGLEAGQSAFGDIYAWFGRVLGwPLEQLAAQHPELKAQInasqkqllpalteawAKNPSLDHLPVVLDWF 398
Cdd:cd00366 235 ----HVVPGLWLLEGAINTGGASLRWFRDEFG-EEEDSDAEYEGLDELA---------------AEVPPGSDGLIFLPYL 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 399 NGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIArKNQVIMQACCDVLNR 478
Cdd:cd00366 295 SGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGA-KSRLWNQIKADVLGV 373
|
490
....*....|....
gi 1412217475 479 PLQIVASDQCCALG 492
Cdd:cd00366 374 PVVVPEVAEGAALG 387
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-486 |
4.68e-34 |
|
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: 133.89 E-value: 4.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 3 IAIGLDFGSDSVRALAVDcASGEEIATSVEWYPRWQKGQFCDapnnqfRHHPRDYIESMEAALKTVLAELSVEQraaVVG 82
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVD-EDGTVLASASEPYPTSRPGPGWV------EQDPEDWWEALRSLLRELPAELRPRR---VVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 83 IGVDSTGSTPAPIDADGNVLAlrpefaenpNAMfvLWKDHTAVEEAEEITRL--CHAPGNvdysryiGGIYSSEWFWAKI 160
Cdd:cd07783 71 IAVDGTSGTLVLVDREGEPLR---------PAI--MYNDARAVAEAEELAEAagAVAPRT-------GLAVSPSSSLAKL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 161 LHVTRQDSAVAQSAASWIELCDWVPALLSGTTRPQDirrgrCSAGHKSLW---HESWgglppASFFDELDPILNRHLPSP 237
Cdd:cd07783 133 LWLKRHEPEVLAKTAKFLHQADWLAGRLTGDRGVTD-----YNNALKLGYdpeTGRW-----PSWLLALLGIPPDLLPRV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 238 LftDTWTadiPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTC-----DILIADKQSvger 311
Cdd:cd07783 203 V--APGT---VIGTLTAEAAEELGLPAGTPVVAGTTDSIAAFLASGAvRPGDAVTSLGTTLVlkllsDKRVPDPGG---- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 312 avkGIcgqvdgSVVPGFIGL---EAGQSAFGDIYAWFGRvlgwpLEQLAaqhpELKAQINAsqkqllpalteawAKNPSL 388
Cdd:cd07783 274 ---GV------YSHRHGDGYwlvGGASNTGGAVLRWFFS-----DDELA----ELSAQADP-------------PGPSGL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 389 DHLPVVLdwfNGRRTPNANQRLKGVItdLNLATDTPLLFGGLIAATAFGARAIMECFTDQG-IAVNNVMALGGIARkNQV 467
Cdd:cd07783 323 IYYPLPL---RGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLEELGaPPVEEVRTAGGGAR-NDL 396
|
490
....*....|....*....
gi 1412217475 468 IMQACCDVLNRPLQIVASD 486
Cdd:cd07783 397 WNQIRADVLGVPVVIAEEE 415
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
289-495 |
6.86e-33 |
|
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: 124.74 E-value: 6.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 289 LVKVIGTSTCdILIADKQSVgeRAVKGICGQVDGSVVPGFIGLEAGQSAFGDIYAWFGRvlgwpleqlaaQHPELKAQIN 368
Cdd:pfam02782 1 LAISAGTSSF-VLVETPEPV--LSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQ-----------FHGLREELRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 369 ASQKQLLPALTEAWAKNPSLdhLPVVLDWFNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQ 448
Cdd:pfam02782 67 AGNVESLAELAALAAVAPAG--GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1412217475 449 -GIAVNNVMALGGIARkNQVIMQACCDVLNRPLQIVASDQCCALGAAI 495
Cdd:pfam02782 145 eGHPIDTIHVSGGGSR-NPLLLQLLADALGLPVVVPGPDEATALGAAL 191
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
5-492 |
1.79e-31 |
|
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: 126.87 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPrwqkgqfCDAPN-NQFRHHPRDYIESMEAALKTVLAELSVEQRAaVVGI 83
Cdd:cd07804 3 LGIDIGTTGTKGVLVD-EDGKVLASASIEHD-------LLTPKpGWAEHDPEVWWGAVCEIIRELLAKAGISPKE-IAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVdsTGSTPA--PIDADGNvlALRPefaenpnAMfvLWKDHTAVEEAEEITRLChapgNVDYSRYIGGIYSSEWFWA-KI 160
Cdd:cd07804 74 GV--SGLVPAlvPVDENGK--PLRP-------AI--LYGDRRATEEIEWLNENI----GEDRIFEITGNPLDSQSVGpKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 161 LHVTRQDSAVAQSAASWIELCDWVPALLSGTtRPQDIRRGRCSAGHKSLWHESWGglppASFFDELdpILNRHLPSPLFt 240
Cdd:cd07804 137 LWIKRNEPEVFKKTRKFLGAYDYIVYKLTGE-YVIDYSSAGNEGGLFDIRKRTWD----EELLEAL--GIDPDLLPELV- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 241 dtWTADIpVGTLCPEWAQRLGLPESV-VISGGAfDCHMGAVGAGA-QPNALVKVIGTSTCDILIADKQSVGERAVkgicg 318
Cdd:cd07804 209 --PSTEI-VGEVTKEAAEETGLAEGTpVVAGTV-DAAASALSAGVvEPGDLLLMLGTAGDIGVVTDKLPTDPRLW----- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 319 qVDGSVVPGFIGLEAGQSAFGDIYAWFgrvlgwpLEQLAaqhPELKAQINASQKQLLPALTEAWAK-NPSLDHLpVVLDW 397
Cdd:cd07804 280 -LDYHDIPGTYVLNGGMATSGSLLRWF-------RDEFA---GEEVEAEKSGGDSAYDLLDEEAEKiPPGSDGL-IVLPY 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 398 FNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIArKNQVIMQACCDVLN 477
Cdd:cd07804 348 FMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGA-KSPLWRQIVADVTG 426
|
490
....*....|....*
gi 1412217475 478 RPLQIVASDQCCALG 492
Cdd:cd07804 427 VPQEYVKDTVGASLG 441
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
5-539 |
4.08e-31 |
|
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: 126.48 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPRWQkgqfcdAPNNQFRHHPRDYIESMEAALKTVLAElSVEQRAAVVGIG 84
Cdd:cd07805 3 LAIDLGTSGVKAALVD-LDGELVASAFAPYPTYY------PKPGWAEQDPEDWWDAVCRATRALLEK-SGIDPSDIAAIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 85 VDSTGSTPAPIDADGNVLAlrpefaenpNAMfvLWKDHTAVEEAEEItrLCHAPGNVDYSRYIGGIYSSEWFWAKILHVT 164
Cdd:cd07805 75 FSGQMQGVVPVDKDGNPLR---------NAI--IWSDTRAAEEAEEI--AGGLGGIEGYRLGGGNPPSGKDPLAKILWLK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 165 RQDSAVAQSAASWIELCDWVPALLSG----------TTRPQDIRRGRcsaghkslWHESW---GGLPPAsffdeldpiln 231
Cdd:cd07805 142 ENEPEIYAKTHKFLDAKDYLNFRLTGraatdpstasTTGLMDLRKRR--------WSEELlraAGIDPD----------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 232 rHLPSPLftdtwTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDILIADKQSVGE 310
Cdd:cd07805 203 -KLPELV-----PSTEVVGELTPEAAAELGLPAGTPVVGGGGDAAAAALGAGAvEEGDAHIYLGTSGWVAAHVPKPKTDP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 311 RA-VKGICgqvdgSVVPGFIGLEAGQSAFGDIYAWFGRVLGwpleQLAAQHPELKAQINAsqkqllpaltEAWAKNPSLD 389
Cdd:cd07805 277 DHgIFTLA-----SADPGRYLLAAEQETAGGALEWARDNLG----GDEDLGADDYELLDE----------LAAEAPPGSN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 390 HLpVVLDWFNGRRTPNANQRLKGVITDLNLATDTpllfGGLIAAT----AFGARAIMECFTDQGIAVNNVMALGGIARkN 465
Cdd:cd07805 338 GL-LFLPWLNGERSPVEDPNARGAFIGLSLEHTR----ADLARAVlegvAFNLRWLLEALEKLTRKIDELRLVGGGAR-S 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 466 QVIMQACCDVLNRPLQIVASDQ--------CCA---LGAAIFAAVAAKVHadipsaqqkmasAVEKTLQPRSEQAQRFEQ 534
Cdd:cd07805 412 DLWCQILADVLGRPVEVPENPQeagalgaaLLAavgLGLLKSFDEAKALV------------KVEKVFEPDPENRARYDR 479
|
....*
gi 1412217475 535 LYRRY 539
Cdd:cd07805 480 LYEVF 484
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
5-542 |
2.27e-29 |
|
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: 121.49 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPrwqkgqfCDAP-NNQFRHHPRDYIESMEAALKTVLAELSVEqRAAVVGI 83
Cdd:cd07808 3 LGIDLGTSSVKAVLVD-EDGRVLASASAEYP-------TSSPkPGWAEQDPEDWWQATKEALRELLAKAGIS-PSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVDSTGSTPAPIDADGNVLalRPefaenpnAMfvLWKDHTAVEEAEEITRLCHApgnvDYSRYIGGIYSSEWFWAKILHV 163
Cdd:cd07808 74 GLTGQMHGLVLLDKNGRPL--RP-------AI--LWNDQRSAAECEELEARLGD----EILIITGNPPLPGFTLPKLLWL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 164 TRQDSAVAQSAASWIeLC-DWVPALLSGT--TRPQDirrgrcSAGhkSLW----HESW-------GGLPPasffDELDPI 229
Cdd:cd07808 139 KENEPEIFARIRKIL-LPkDYLRYRLTGElaTDPSD------ASG--TLLfdveKREWseelleaLGLDP----SILPPI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 230 LNrhlpsplftdtwTADIpVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDILIADK-QS 307
Cdd:cd07808 206 VE------------STEI-VGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGAGVvEPGDALISLGTSGVVFAPTDKpVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 308 VGERAVKGICgqvdgSVVPG-FIGLEAGQSAfGDIYAWFGRVLGwPLEQLAAQHPELKAQINASQKQL--LPALteawak 384
Cdd:cd07808 273 DPKGRLHTFP-----HAVPGkWYAMGVTLSA-GLSLRWLRDLFG-PDRESFDELDAEAAKVPPGSEGLlfLPYL------ 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 385 npsldhlpvvldwfNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIArK 464
Cdd:cd07808 340 --------------SGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGA-K 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1412217475 465 NQVIMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMaSAVEKTLQPRSEQAQRFEQLYRRYQQW 542
Cdd:cd07808 405 SPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAAC-IKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
5-531 |
1.26e-28 |
|
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: 118.39 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPrwqkgqfCDAPN-NQFRHHPRDYIESMEAALKTVLAELSVEqRAAVVGI 83
Cdd:cd07779 3 LGIDVGTTSTRAIIFD-LDGNIVASGYREYP-------PYYPEpGWVEQDPDDWWDALCEALKEAVAKAGVD-PEDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVDSTGSTPAPIDADGNvlALRPefaenpnamFVLWKDhtaveeaEEITRLCHAPGnvdysrYIGGIYSSEWFwakilhv 163
Cdd:cd07779 74 GLTSQRSTFVPVDEDGR--PLRP---------AISWQD-------KRTAKFLTVQD------YLLYRLTGEFV------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 164 trqdsavaqsaaswielCDWVPALLSGttrPQDIRRGRCSAghKSLWhesWGGLPPASFFDELDPIlnrhlpsplftdtw 243
Cdd:cd07779 123 -----------------TDTTSASRTG---LPDIRTRDWSD--DLLD---AFGIDRDKLPELVPPG-------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 244 tadIPVGTLCPEWAQRLGLPESV-VISGGAfD--ChmGAVGAGA-QPNALVKVIGTSTcdILIADKQSVGERAVKGIcgQ 319
Cdd:cd07779 164 ---TVIGTLTKEAAEETGLPEGTpVVAGGG-DqqC--AALGAGVlEPGTASLSLGTAA--VVIAVSDKPVEDPERRI--P 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 320 VDGSVVPGFIGLEAGQSAFGDIYAWFGRVLGWPLEQLAAQHPELKAQINAsqkqllpaltEAWAKNPSLDHLpVVLDWFN 399
Cdd:cd07779 234 CNPSAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVAEKELGVSPYELLNE----------EAAKSPPGSDGL-LFLPYLA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 400 GRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIArKNQVIMQACCDVLNRP 479
Cdd:cd07779 303 GAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGS-KSDLWNQIIADVFGRP 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1412217475 480 LQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMaSAVEKTLQPRSEQAQR 531
Cdd:cd07779 382 VERPETSEATALGAAILAAVGAGIYPDFEEAVKAM-VRVTDTFEPDPENVAI 432
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-470 |
2.46e-26 |
|
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: 112.88 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPRWQkgqfcDAPNNQF-RHHPRDYIESMEAALKTVLAELSVEQraaVVGI 83
Cdd:cd07778 3 IGIDVGSTSVRIGIFD-YHGTLLATSERPISYKQ-----DPKDLWFvTQSSTEIWKAIKTALKELIEELSDYI---VSGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVDSTGSTPA--PIDADGNVLALRPEFAE-NPNAMFVLWKDHTAVEEAEEITRLCHApgnvDYSRYIGGIYSSEWFWAKI 160
Cdd:cd07778 74 GVSATCSMVVmqRDSDTSYLVPYNVIHEKsNPDQDIIFWMDHRASEETQWLNNILPD----DILDYLGGGFIPEMAIPKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 161 LHVTRQDSAVAQSAASWIELCDWVPALLS-----GTTRPQDIRRGRCSAGHKSL--WHES---WGGLPPASFFDELDPil 230
Cdd:cd07778 150 KYLIDLIKEDTFKKLEVFDLHDWISYMLAtnlghSNIVPVNAPPSIGIGIDGSLkgWSKDfysKLKISTKVCNVGNTF-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 231 NRHLPSPLftdtwtADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVG----AGAQPNALVKVIGTSTCDILIADKQ 306
Cdd:cd07778 228 KEAPPLPY------AGIPIGKVNVILASYLGIDKSTVVGHGCIDCYAGWFStfaaAKTLDTTLFMVAGTSTCFLYATSSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 307 SVGEraVKGICGQVDgSVVPGFIGLEAGQSAFGdiyawfgrVLgwpLEQLAAQHPELKAQI--NASQKQLLPALTEAWAK 384
Cdd:cd07778 302 QVGP--IPGIWGPFD-QLLKNYSVYEGGQSATG--------KL---IEKLFNSHPAIIELLksDANFFETVEEKIDKYER 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 385 --NPSLDHLpvVLDWF-----NGRRTPNANQRLKG-VITDLNLATDTPLLFGGL--IAATAFGARAIMECFTDQGIAVNN 454
Cdd:cd07778 368 llGQSIHYL--TRHMFfygdyLGNRTPYNDPNMSGsFIGESTDSSLTDLVLKYIliLEFLAFQTKLIIDNFQKEKIIIQK 445
|
490
....*....|....*.
gi 1412217475 455 VMALGGIArKNQVIMQ 470
Cdd:cd07778 446 VVISGSQA-KNARLLQ 460
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
5-492 |
1.01e-25 |
|
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: 109.95 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDCASGEEIATSveWYPrWQKGQfcdaPNNQFR-HHPRDYIESMEAALKTVLAELSVEqRAAVVGI 83
Cdd:cd07809 3 LGIDLGTQSIKAVLIDAETGRVVASG--SAP-HENIL----IDPGWAeQDPEDWWDALQAAFAQLLKDAGAE-LRDVAAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVDSTGSTPAPIDADGNVlaLRPefaenpnamFVLWKDHTAVEEAEEITRLCHAPGNVDYSRYIGGIYSSewfwAKILHV 163
Cdd:cd07809 75 GISGQMHGLVALDADGKV--LRP---------AKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARFTA----SKLLWL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 164 TRQDSAVAQSAASWIELCDWVPALLSGTTR----------PQDIRRGRcsaghkslWHESWgglppASFFDElDPILNRH 233
Cdd:cd07809 140 KENEPEHYARIAKILLPHDYLNWKLTGEKVtglgdasgtfPIDPRTRD--------YDAEL-----LAAIDP-SRDLRDL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 234 LPSPLFTDTwtadiPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGAQPNALVKV-IGTSTCDILIADKQSVGER- 311
Cdd:cd07809 206 LPEVLPAGE-----VAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVsLGTSGTAYGVSDKPVSDPHg 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 312 AVKGICGqVDGSVVPgfigLEAGQSAFGDIYAWFGRVLGWP---LEQLAAQHPelkaqinasqkqllpalteawAKNPSL 388
Cdd:cd07809 281 RVATFCD-STGGMLP----LINTTNCLTAWTELFRELLGVSyeeLDELAAQAP---------------------PGAGGL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 389 dhlpVVLDWFNGRRTPNaNQRLKGVITDLNLATDTPllfgGLIA-----ATAFGARAIMECFTDQGIAVNNVMALGGIAr 463
Cdd:cd07809 335 ----LLLPFLNGERTPN-LPHGRASLVGLTLSNFTR----ANLAraaleGATFGLRYGLDILRELGVEIDEIRLIGGGS- 404
|
490 500
....*....|....*....|....*....
gi 1412217475 464 KNQVIMQACCDVLNRPLQIVASDQCCALG 492
Cdd:cd07809 405 KSPVWRQILADVFGVPVVVPETGEGGALG 433
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
5-541 |
7.38e-23 |
|
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: 101.86 E-value: 7.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPrwqkgQFCDAPNnQFRHHPRDYIESMEAALKTVLAELSVEQraaVVGIG 84
Cdd:cd07770 3 LGIDIGTTSTKAVLFD-EDGRVVASSSAEYP-----LIRPEPG-WAEQDPEEILEAVLEALKEVLAKLGGGE---VDAIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 85 VDSTGSTPAPIDADGNVLAlrpefaenpNAMfvLWKDHTAVEEAEEItRLCHAPGNVdYSRyiGG--IYSSEWFwAKILH 162
Cdd:cd07770 73 FSSAMHSLLGVDEDGEPLT---------PVI--TWADTRAAEEAERL-RKEGDGSEL-YRR--TGcpIHPMYPL-AKLLW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 163 VTRQDSAVAQSAASWIELCDWVPALLSGTTrPQDIrrgrCSAghkslwheSWGGLppasfFD--ELD---PILN------ 231
Cdd:cd07770 137 LKEERPELFAKAAKFVSIKEYLLYRLTGEL-VTDY----STA--------SGTGL-----LNihTLDwdeEALEllgide 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 232 RHLPSPLFTDTwtadiPVGTLCPEWAQRLGLPESVVISGGAFDchmGA---VGAGA-QPNALVKVIGTS-----TCDILI 302
Cdd:cd07770 199 EQLPELVDPTE-----VLPGLKPEFAERLGLLAGTPVVLGASD---GAlanLGSGAlDPGRAALTVGTSgairvVSDRPV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 303 ADKQsvgeravKGI-CGQVD-GSVVPGfigleagqSAF---GDIYAWFGRVLGwpleqLAAQHPELkaqinasqkqllpa 377
Cdd:cd07770 271 LDPP-------GRLwCYRLDeNRWLVG--------GAInngGNVLDWLRDTLL-----LSGDDYEE-------------- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 378 LTEAWAKNPSLDHLPVVLDWFNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMA 457
Cdd:cd07770 317 LDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAGPVKEIRA 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 458 LGGIARkNQVIMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQqkmASAVEKTLQPRSEQAQRFEQLYR 537
Cdd:cd07770 397 SGGFLR-SPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEADE---LVKIGKVVEPDPENHAIYAELYE 472
|
....
gi 1412217475 538 RYQQ 541
Cdd:cd07770 473 RFKK 476
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
5-495 |
3.11e-14 |
|
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: 74.90 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVewyprwqkgqfcdAPNNQFRHHPRDYIESMEA-------ALKTVLAELSVEQr 77
Cdd:cd07802 3 LGIDNGTTNVKAVLFD-LDGREIAVAS-------------RPTPVISPRPGWAERDMDElwqataeAIRELLEKSGVDP- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 78 AAVVGIGVDSTGSTPAPIDADGNvlALRpefaenpNAmfVLWKDHTAVEEAEEITRlchAPGNVDYSRYIG-----GIYS 152
Cdd:cd07802 68 SDIAGVGVTGHGNGLYLVDKDGK--PVR-------NA--ILSNDSRAADIVDRWEE---DGTLEKVYPLTGqplwpGQPV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 153 SEWFWAKilhvtRQDSAVAQsAASWIELC-DWVPALLSG---------TTRPQDIRRGRCSAghkslwheswgglppaSF 222
Cdd:cd07802 134 ALLRWLK-----ENEPERYD-RIRTVLFCkDWIRYRLTGeistdytdaGSSLLDLDTGEYDD----------------EL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 223 FDELD-PILNRHLPSPLftdtWTADIpVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDI 300
Cdd:cd07802 192 LDLLGiEELKDKLPPLV----PSTEI-AGRVTAEAAALTGLPEGTPVAAGAFDVVASALGAGAvDEGQLCVILGTWSINE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 301 LIADKQSVGERAVKGICgqvdgSVVPG-FIGLEAGQSAfgdiyawfGRVLGWPLEQLAAQhpelkaqINASQKQLLPALT 379
Cdd:cd07802 267 VVTDEPVVPDSVGSNSL-----HADPGlYLIVEASPTS--------ASNLDWFLDTLLGE-------EKEAGGSDYDELD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 380 EAWAKNPSLDHLPVVLDWFNGrrtPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMEcFTDQGIAVNNVMALG 459
Cdd:cd07802 327 ELIAAVPPGSSGVIFLPYLYG---SGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLE-RLLVARKPETIRLTG 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 1412217475 460 GIARkNQVIMQACCDVLNRPLQIVASDQCCALGAAI 495
Cdd:cd07802 403 GGAR-SPVWAQIFADVLGLPVEVPDGEELGALGAAI 437
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
5-492 |
1.70e-13 |
|
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: 72.64 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDCASGEEIATSVEW-YPRwqkgqfCDAPNNQFRHHPRDYIESMEAALKTVLAELSVEqRAAVVGI 83
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWeYYT------DDDYPDAKEFDPEELWEKICEAIREALKKAGIS-PEDISAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 84 GVDSTGSTPAPIDADGNVL-ALrpefaenPNamfvlwKDHTAVEEAEEItrlchAPGNVDYSRYIGGIYSSEWF-WAKIL 161
Cdd:cd07798 76 SSTSQREGIVFLDKDGRELyAG-------PN------IDARGVEEAAEI-----DDEFGEEIYTTTGHWPTELFpAARLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 162 HVTRQDSAVAQSAASWIELCDWVPALLSGT----------TRPQDIRRGRcsaghkslWHeswgglppasffDELDPILN 231
Cdd:cd07798 138 WFKENRPEIFERIATVLSISDWIGYRLTGElvsepsqaseTQLFDIKKRE--------WS------------QELLEALG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 232 rhLPSPLFTDTWTADIPVGTLCPEWAQRLGLPESV-VISGGAfDCHMGAVGAGAQ-PNALVKVIGTST-----CDILIAD 304
Cdd:cd07798 198 --LPPEILPEIVPSGTVLGTVSEEAARELGLPEGTpVVVGGA-DTQCALLGSGAIePGDIGIVAGTTTpvqmvTDEPIID 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 305 KQsvgERAVKGiCgqvdgSVVPGFIGLEAGQSAFGDIYAWFGRVL-GWP------LEQLAAQHPELKAQINASqkqLLPA 377
Cdd:cd07798 275 PE---RRLWTG-C-----HLVPGKWVLESNAGVTGLNYQWLKELLyGDPedsyevLEEEASEIPPGANGVLAF---LGPQ 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 378 LteawaknpsldhlpvvldwFNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFTDQ-GIAVNNVM 456
Cdd:cd07798 343 I-------------------FDARLSGLKNGGFLFPTPLSASELTRGDFARAILENIAFAIRANLEQLEEVsGREIPYII 403
|
490 500 510
....*....|....*....|....*....|....*.
gi 1412217475 457 ALGGIARkNQVIMQACCDVLNRPLQIVASDQCCALG 492
Cdd:cd07798 404 LCGGGSR-SALLCQILADVLGKPVLVPEGREASALG 438
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-281 |
1.20e-09 |
|
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: 58.89 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 3 IAIGLDFGSDSVRALAVDcASGEEIATSVEWYPRwqkgqfcDAPNNQFRHH-PRDYIESMEAALKTVLAELSV--EQraa 79
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQ-------ITPHPGWAEQdPDEIWQAVAQCIAKTLSQLGIslKQ--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 80 VVGIGVDSTGSTPAPIDADGNVLAlrpefaenpNAmfVLWKDHTAVEEAEEITRlchaPGNVDYSRYIGGIYSSEWFWAK 159
Cdd:pfam00370 70 IKGIGISNQGHGTVLLDKNDKPLY---------NA--ILWKDRRTAEIVENLKE----EGNNQKLYEITGLPIWPGFTLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 160 ILH-VTRQDSAVAQSAASWIELCDWVPALLSG--TTRPQDIRRGRCSAGHKSLWHES---WGGLPPasffdeldpilnRH 233
Cdd:pfam00370 135 KLRwIKENEPEVFEKIHKFLTIHDYLRWRLTGvfVTDHTNASRSMMFNIHKLDWDPEllaALGIPR------------DH 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1412217475 234 LPsPLFTdtwTADIpVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVG 281
Cdd:pfam00370 203 LP-PLVE---SSEI-YGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
5-492 |
9.01e-06 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 48.39 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEwyprwqkgqfcdaPNNQFRHHPRDYIESMEA-------ALKTVLAELSVEQR 77
Cdd:cd24121 3 IGIDAGTSVVKAVAFD-LDGRELAVAAR-------------RNAVLYPQPGWAEQDMNEtwqavvaTIREVVAKLDVLPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 78 AaVVGIGVDSTGSTPAPIDADGNvlALRPEfaenpnamfVLWKDHTAveeAEEITRLcHAPGNVD-YSRYIGGIYSSEWF 156
Cdd:cd24121 69 R-VAAIGVTGQGDGTWLVDEDGR--PVRDA---------ILWLDGRA---ADIVERW-QADGIAEaVFEITGTGLFPGSQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 157 WAKILHVTRQDSAVAQsAASWIELC-DWVPALLSG--TTRPQDirrgrcsaghKSLwheSWGGLPPASFFDELDPILN-- 231
Cdd:cd24121 133 AAQLAWLKENEPERLE-RARTALHCkDWLFYKLTGeiATDPSD----------ASL---TFLDFRTRQYDDEVLDLLGle 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 232 --RHLPSPLFTDTWTadipVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNALVKVIGTSTCDILIADKQSV 308
Cdd:cd24121 199 elRHLLPPIRPGTEV----IGPLTPEAAAATGLPAGTPVVLGPFDVVATALGSGAiEPGDACSILGTTGVHEVVVDEPDL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 309 GERAVKG-ICGQVDGSVVpgfigleagqSAFGDIYA-----WFGRVLGWPLEQLAAQHPELKAQINASQKQLLPALTEAW 382
Cdd:cd24121 275 EPEGVGYtICLGVPGRWL----------RAMANMAGtpnldWFLRELGEVLKEGAEPAGSDLFQDLEELAASSPPGAEGV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 383 AKNPSLDHlpvvldwfNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFgarAIMECFTDQGIAVNNVMALGGIA 462
Cdd:cd24121 345 LYHPYLSP--------AGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVAL---AMRDCYEHMGEDPGELRLSGGGA 413
|
490 500 510
....*....|....*....|....*....|
gi 1412217475 463 RKNQViMQACCDVLNRPLQIVASDQCCALG 492
Cdd:cd24121 414 RSDTW-CQILADALGVPVRVPAGEEFGARG 442
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-530 |
3.24e-05 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 46.56 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 1 MAIAIGLDFGSDSVRALAVDcASGEEIATSvewyprwqkgqfcDAPNN--QFRHHPRDYIESMEAAL-------KTVLAE 71
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVD-RQGKIVARA-------------STPNAsdIAAENSDWHQWSLDAILqrfadccRQINSE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 72 LSVEQraaVVGIGVDSTGSTPAPIDADGNVLalRPefaenpnamFVLWKDHTAVEEAEEITR------LCHAPGNVDYSr 145
Cdd:PRK10331 67 LTECH---IRGITVTTFGVDGALVDKQGNLL--YP---------IISWKCPRTAAVMENIERyisaqqLQQISGVGAFS- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 146 yIGGIYSSEWFwaKILHVTrqdsaVAQSAASWIELCDWVPALLSG--TTrpqdirrGRCSAGHKSLW---HESWGglppa 220
Cdd:PRK10331 132 -FNTLYKLVWL--KENHPQ-----LLEQAHAWLFISSLINHRLTGefTT-------DITMAGTSQMLdiqQRDFS----- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 221 sffdelDPILNR-HLPSPLFTDTWTADIPVGTLCPEWAQRLGLPESV-VISGGaFDCHMGAVGAGAQPNAlvKVIGTSTC 298
Cdd:PRK10331 192 ------PEILQAtGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIpVISAG-HDTQFALFGSGAGQNQ--PVLSSGTW 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 299 DILIADKQsvgeravkgicgQVDGSVVPGFIG----LEAGQSAFGDIYAWFGR-VLGWpleqlaaqhpelkaqinasQKQ 373
Cdd:PRK10331 263 EILMVRSA------------QVDTSLLSQYAGstceLDSQSGLYNPGMQWLASgVLEW-------------------VRK 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 374 LLPALTEAWaknPSLDHlpvvldwfNGRRTPNANQrlkGVITDLNLATDTPLLFGGLIAATAFG--ARAIMECFTDQ--- 448
Cdd:PRK10331 312 LFWTAETPY---QTMIE--------EARAIPPGAD---GVKMQCDLLACQNAGWQGVTLNTTRGhfYRAALEGLTAQlkr 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 449 ---------GIAVNNVMALGGIARkNQVIMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASAVe 519
Cdd:PRK10331 378 nlqvlekigHFKASELLLVGGGSR-NALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQY- 455
|
570
....*....|.
gi 1412217475 520 KTLQPRSEQAQ 530
Cdd:PRK10331 456 RYFYPQTEPEF 466
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-486 |
1.31e-03 |
|
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: 41.44 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 3 IAIGLDFGSDSVRALAVDCASGEEIATSVEWYPRWQKGQfcdapnnqfrhHPRDYIESME---AALKTVLAELSVEQRAA 79
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVSRPTPAPISSD-----------DPGRSEQDPEkilEAVRNLIDELPREYLSD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 80 VVGIGVdsTGstp--apIDADGNvlALRPefaenpnamFVLWKDHTAVEE--------AEEITRLCH---APGNvdysry 146
Cdd:cd07777 70 VTGIGI--TGqmhgivlWDEDGN--PVSP---------LITWQDQRCSEEflgglstyGEELLPKSGmrlKPGY------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 147 igGIYSseWFWakiLHVTRQDSAVAQSAASwieLCDWVPALLSGTTRPqdirrgRCS---AGhkslwheSWGglppasFF 223
Cdd:cd07777 131 --GLAT--LFW---LLRNGPLPSKADRAGT---IGDYIVARLTGLPKP------VMHptnAA-------SWG------LF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 224 DELDPILNRHL------PSPLFTDTWTADIPVGTLCPEwaqrlgLPESVVISGGafdchMG----AV-GAGAQP-NALVK 291
Cdd:cd07777 182 DLETGTWNKDLlealglPVILLPEIVPSGEIVGTLSSA------LPKGIPVYVA-----LGdnqaSVlGSGLNEeNDAVL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 292 VIGTStcdiliadkqsvgeravkgicGQVdGSVVPGFIgleagQSAFGDIYAWF-GRVL--------GWPLEQLAAQHPE 362
Cdd:cd07777 251 NIGTG---------------------AQL-SFLTPKFE-----LSGSVEIRPFFdGRYLlvaaslpgGRALAVLVDFLRE 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 363 LKAQINASQK--QLLPALTEAwAKNPSLDHLPVVLDWFNGRRTPNanqrLKGVITDLNLATDTPllfGGLIAATAFG-AR 439
Cdd:cd07777 304 WLRELGGSLSddEIWEKLDEL-AESEESSDLSVDPTFFGERHDPE----GRGSITNIGESNFTL---GNLFRALCRGiAE 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1412217475 440 AIMECFT---DQGIAVNNVMALGGIARKNQVIMQACCDVLNRPLQIVASD 486
Cdd:cd07777 376 NLHEMLPrldLDLSGIERIVGSGGALRKNPVLRRIIEKRFGLPVVLSEGS 425
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-102 |
1.48e-03 |
|
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: 41.04 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 1 MAIAIGLDFGSDSVRALAVDcASGEEIATSVEWYPRWQKgqfcdapnnqfrhhPRDYIESMEAALKTVLAELSVEqRAAV 80
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVD-LDGEVLARERIPTPAGAG--------------PEAVLEAIAELIEELLAEAGIS-RGRI 67
|
90 100
....*....|....*....|..
gi 1412217475 81 VGIGVdstgSTPAPIDADGNVL 102
Cdd:COG1940 68 LGIGI----GVPGPVDPETGVV 85
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
5-102 |
3.75e-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: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 5 IGLDFGSDSVRALAVDcASGEEIATSVEWYPRwqkgqfcdapnnqfRHHPRDYIESMEAALKTVLAELSVEQRAAVVGIG 84
Cdd:cd23763 1 IGIDIGGTKIRAALVD-LDGEILARERVPTPA--------------EEGPEAVLDRIAELIEELLAEAGVRERILGIGIG 65
|
90
....*....|....*....
gi 1412217475 85 VdstgstPAPIDAD-GNVL 102
Cdd:cd23763 66 V------PGPVDPEtGIVL 78
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
398-540 |
8.64e-03 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 38.80 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412217475 398 FNGRRTPNANQRLKGVITDLNLATDTPLLFGGLIAATAFGARAIMECFT-DQGIAVNNVMALGGIArKNQVIMQACCDVL 476
Cdd:PTZ00294 352 FSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEkDAGIELNSLRVDGGLT-KNKLLMQFQADIL 430
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1412217475 477 NRPLQIVASDQCCALGAAIFAAVAAKVHADIPSaQQKMASAVEKTLQPRSEQAQRfEQLYRRYQ 540
Cdd:PTZ00294 431 GKDIVVPEMAETTALGAALLAGLAVGVWKSLEE-VKKLIRRSNSTFSPQMSAEER-KAIYKEWN 492
|
|
| |
