|
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 ... |
11-480 |
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: 777.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTK----------------------- 67
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKevlegagvdpeqvkgigfdatcs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 68 -------------------------------------------------------------------NLREiCWDKAGHF 80
Cdd:cd07782 81 lvvldaegkpvsvspsgddernvilwmdhraveeaerinatghevlkyvggkispemeppkllwlkeNLPE-TWAKAGHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 81 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAAR 156
Cdd:cd07782 160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 157 DLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGF 236
Cdd:cd07782 240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 237 WLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 314
Cdd:cd07782 318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 315 TLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGL 394
Cdd:cd07782 398 TLRGM------------------------ISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 395 SKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLV 474
Cdd:cd07782 454 SKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMY 533
|
....*.
gi 767905023 475 EHQKEY 480
Cdd:cd07782 534 EDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
11-480 |
1.74e-171 |
|
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: 493.64 E-value: 1.74e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKN---------------------- 68
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQvlaeskvdpnsvkgigfdatcs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 69 ---------------------------------------------LR-------------EICWDK---------AGHFF 81
Cdd:TIGR01315 81 lvvlthdgeplpvsknggadqniilwmdhralaeaekinatnhnlLRyvggkmsvemeipKVLWLKnnmppelfaRCKFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 82 DLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARD 157
Cdd:TIGR01315 161 DLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 158 LGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQpvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFW 237
Cdd:TIGR01315 241 LGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAF---TRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 238 LNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLAD 313
Cdd:TIGR01315 318 LAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIAD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 314 LTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 393
Cdd:TIGR01315 397 PNMRGV------------------------IIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 394 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQ-DKKYYDKKYQVFLK 472
Cdd:TIGR01315 453 QCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDpAKKLHDRKYEIFLQ 532
|
....*...
gi 767905023 473 LVEHQKEY 480
Cdd:TIGR01315 533 LARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
9-480 |
2.87e-149 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 436.47 E-value: 2.87e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 9 ERYYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEP---------QFnhhEQSSEDIWAACC--------------- 63
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEaavrealaqagvdpa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 64 ---------------VVTKNLREIC------------------------------------------------------- 73
Cdd:COG1069 78 dvvgigvdatgctpvPVDADGTPLAllpefaenphamvilwkdhtaqeeaerinelakargedylryvggiissewfwpk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 74 -----------WDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIGLE-DFVADnysKIGNQV 139
Cdd:COG1069 158 ilhllredpevYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDPLlDGLAD---RLGTEI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 140 LPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGadvrghglICEGQpvtsrLAVICGTSSCHMGISKDPI 219
Cdd:COG1069 235 YPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGG--------VEPGT-----LVKVMGTSTCHMLVSPEER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 220 FVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNshldliKKAQPVGFLTVDLH 299
Cdd:COG1069 301 FVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESGLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 300 VWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAME 379
Cdd:COG1069 375 ALDWFNGNRSPLADQRLKGV------------------------ILGLTLGTDAED---IYRALVEATAFGTRAIIERFE 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 380 AAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV-GKVVFPRL 457
Cdd:COG1069 428 EEGVPIDEIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDP 507
|
570 580
....*....|....*....|...
gi 767905023 458 QDKKYYDKKYQVFLKLVEHQKEY 480
Cdd:COG1069 508 ENVAVYDALYAEYLQLHDYFGRG 530
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
11-473 |
5.02e-102 |
|
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: 314.47 E-value: 5.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWE--PQFNHHEQSSEDIWAACCVVTKN-LRE----------IC--- 73
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGaLAEagvdpedvvgIGvdt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 74 -----------------------------------------------------------------------WDKAGHFFD 82
Cdd:cd07781 81 tsstvvpvdedgnplapailwmdhraqeeaaeinetahpaleyylayyggvyssewmwpkalwlkrnapevYDAAYTIVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 83 LPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvADNYSKIGNQVLPPGASLGnGLTPEAARDLGLL 161
Cdd:cd07781 161 ACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGL--LKLREKLPGEVVPVGEPAG-TLTAEAAERLGLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 162 PGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEG 241
Cdd:cd07781 238 AGIPVAQGGIDAHMGAIGA--------GVVEPGT-----LALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 242 GQSVTGKLIdhmvqghAAFPELQVKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRSPLADLTLKG 318
Cdd:cd07781 305 GQSAVGDIF-------AWFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRTPLVDPRLRG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 319 MrttgylyipalaalhspssllspqVTGLKLSQDLddlAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KN 397
Cdd:cd07781 370 A------------------------IVGLTLGTTP---AHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKN 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767905023 398 PLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 473
Cdd:cd07781 423 PLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
74-470 |
2.11e-101 |
|
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: 313.79 E-value: 2.11e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 74 WDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDfVADNYSKIGNQVLPPGASLGNGLtP 152
Cdd:cd07768 156 RDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRL-EHLTTTKNLPSNVPIGTTSGVAL-P 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 153 EAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGhglicegqpvtsRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAM 232
Cdd:cd07768 234 EMAEKMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTII 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 233 VPGFWLNEGGQSVTGKLIDHMVQGHAAFPELqVKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLA 312
Cdd:cd07768 302 DPDYSVYEAGQSATGKLIEHLFESHPCARKF-DEALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 313 DLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCG 392
Cdd:cd07768 378 DPRLKGS------------------------FIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASG 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 393 GLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA---SVQEAMAKMSKVGKVVFPRLQD-KKYYDKKYQ 468
Cdd:cd07768 434 GQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEADISNDRKSETFEPLAYRlGADYILLYK 513
|
..
gi 767905023 469 VF 470
Cdd:cd07768 514 LL 515
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
10-479 |
1.25e-62 |
|
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: 211.61 E-value: 1.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 10 RYYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNL-------------------- 69
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELlakagvdpeeiaaigvsgqm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 70 ----------------------------------------REIC-----------------------WDKAGHFFDLPDF 86
Cdd:COG1070 81 hglvlldadgeplrpailwndtraaaeaaelreelgeealYEITgnplhpgftapkllwlkenepeiFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 87 LSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGL-EDFVAdnyskignQVLPPGASLGnGLTPEAARDLGL 160
Cdd:COG1070 161 LRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIdRELLP--------ELVPPGEVAG-TLTAEAAAETGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 161 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNE 240
Cdd:COG1070 228 PAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 241 GGQSVTGKLIDHMVQghaafpelqvKATARCQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDFHGNRSPLADLT 315
Cdd:COG1070 295 GATNNGGSALRWFRD----------LFADGELDDYEELN---ALAAEV-PPGadgllFL-------PYLSGERTPHWDPN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 316 LKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS 395
Cdd:COG1070 354 ARGA------------------------FFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGA 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 396 KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVE 475
Cdd:COG1070 407 RSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYP 486
|
....
gi 767905023 476 HQKE 479
Cdd:COG1070 487 ALKP 490
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
11-463 |
1.52e-59 |
|
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: 201.98 E-value: 1.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLRE------------------- 71
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkagvdpediaaigltsqrs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 72 ---------------ICW-DK-AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvADNYS 133
Cdd:cd07779 81 tfvpvdedgrplrpaISWqDKrTAKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGID---RDKLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 134 KIgnqvLPPGASLGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMG 213
Cdd:cd07779 158 EL----VPPGTVIGT-LTKEAAEETGLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 214 ISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGF 293
Cdd:cd07779 220 VSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 294 LtvDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRF 373
Cdd:cd07779 293 D--GLLFLPYLAGAGTPYWNPEARGA------------------------FIGLTLSHTRAH---LARAILEGIAFELRD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 374 IIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVV 453
Cdd:cd07779 344 NLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTF 423
|
490
....*....|
gi 767905023 454 FPRLQDKKYY 463
Cdd:cd07779 424 EPDPENVAIY 433
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
75-484 |
3.31e-57 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 198.53 E-value: 3.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 75 DKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDFVADnysKIGNQVLPPGAS 145
Cdd:PRK04123 172 EAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD---KLFTETWTAGEP 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 146 LGnGLTPEAARDLGLLPGIAVAASLIDAHAGglgVIGADVRGHGLicegqpvtsrLAVIcGTSSCHMGISKDPIFVPGVW 225
Cdd:PRK04123 249 AG-TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTL----------VKVM-GTSTCDILLADKQRAVPGIC 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 226 GPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSIYAYLNshldliKKA--QPVG---FLTVDlhv 300
Cdd:PRK04123 314 GQVDGSIVPGLIGYEAGQSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT------EAAakQPPGehgLVALD--- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 301 WpdFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEA 380
Cdd:PRK04123 384 W--FNGRRTPLADQRLKGV------------------------ITGLTLGTDAPDI---YRALIEATAFGTRAIMECFED 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 381 AGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKM-SKVGKVVFPRLQ 458
Cdd:PRK04123 435 QGVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPE 514
|
410 420
....*....|....*....|....*..
gi 767905023 459 DKKYYDKKYQVFLKLVE-HQKEYLAIM 484
Cdd:PRK04123 515 NVARYEQLYQEYKQLHDyFGRGGNAVM 541
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
201-432 |
5.09e-55 |
|
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: 182.52 E-value: 5.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 201 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 279
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 280 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLddlAIL 359
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGS------------------------ITGLSSPTTL---AHL 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767905023 360 YLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 432
Cdd:pfam02782 123 YRAILESLALQLRQILEALTKqEGHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
11-429 |
1.55e-48 |
|
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: 171.59 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLRE-----------IC------ 73
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkagidpsdiaaIGisgqmp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 74 ----WDKAG--------------HFFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGL-EDFVADny 132
Cdd:cd00366 81 gvvlVDADGnplrpaiiwldrraKFLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIpREKLPP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 133 skignqVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHM 212
Cdd:cd00366 158 ------IVESGEVVG-RVTPEAAEETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 213 GISKDPIFVPGVWGPYFSAmVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP-- 290
Cdd:cd00366 218 VCTDEPVPPDPRLLNRCHV-VPGLWLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgs 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 291 --VGFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIA 368
Cdd:cd00366 286 dgLIFL-------PYLSGERSPIWDPAARGV------------------------FFGLTLSHTRAH---LIRAVLEGVA 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767905023 369 LGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLG 429
Cdd:cd00366 332 YALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
54-481 |
9.73e-45 |
|
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: 164.71 E-value: 9.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 54 SSEDIWAACCVVTKNLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDFVAD 130
Cdd:TIGR01234 154 SSEWFWAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 131 NYSK-IGNQVLPPGAslgngLTPEAARDLGLLPGIAVAASLIDAHaggLGVIGADVrghgliceGQPvtSRLAVICGTSS 209
Cdd:TIGR01234 233 KLFTdIWTAGEPAGT-----LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTST 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 210 CHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSiyayLNSHLDLIKKAQ 289
Cdd:TIGR01234 295 CHVLIGDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 290 PV---GFLTVDlhvWpdFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQA 366
Cdd:TIGR01234 370 PSgehGLVALD---W--FNGNRSPLVDQRLKGV------------------------ITGLTLATDAPL---LYRALIEA 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 367 IALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAK 445
Cdd:TIGR01234 418 TAFGTRMIMETFTDSGVPVEELMAAGGIArKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAK 497
|
410 420 430
....*....|....*....|....*....|....*..
gi 767905023 446 MSKVGKVVF-PRLQDKKYYDKKYQVFLKLVEHQKEYL 481
Cdd:TIGR01234 498 MGSAVEKTLtPCSENAQRYEQLYARYQELAMSFGQYN 534
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
11-471 |
3.27e-43 |
|
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: 159.22 E-value: 3.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLRE------------------- 71
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksgidpsdiaaiafsgqmq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 72 --ICWDKAGH---------------------------------------------------------------FFDLPDF 86
Cdd:cd07805 81 gvVPVDKDGNplrnaiiwsdtraaeeaeeiagglggiegyrlgggnppsgkdplakilwlkenepeiyakthkFLDAKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 87 LSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDfvadnySKIgNQVLPPGASLGnGLTPEAARDLGLLPGIA 165
Cdd:cd07805 161 LNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDP------DKL-PELVPSTEVVG-ELTPEAAAELGLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 166 VAASLIDAHAGGLGViGADVRGHGLICegqpvtsrlaviCGTSS---CHmgiSKDPIFVPGvwGPYFS--AMVPGFWLNE 240
Cdd:cd07805 233 VVGGGGDAAAAALGA-GAVEEGDAHIY------------LGTSGwvaAH---VPKPKTDPD--HGIFTlaSADPGRYLLA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 241 GGQSVTGKLIDHMVQgHAAFPELQVKatarcqSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLADLTL 316
Cdd:cd07805 295 AEQETAGGALEWARD-NLGGDEDLGA------DDYELLD---ELAAEAPPgsngLLFL-------PWLNGERSPVEDPNA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 317 KGMrttgylYIpalaalhspssllspqvtGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSK 396
Cdd:cd07805 358 RGA------FI------------------GLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGAR 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767905023 397 NPLFVQMHADITGMPV-VLSQEVESVLVGAAVLGACASGDFASVQEAmAKMSKVGKVVFPRLQDKKYYDKKYQVFL 471
Cdd:cd07805 411 SDLWCQILADVLGRPVeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
12-433 |
5.70e-42 |
|
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: 156.80 E-value: 5.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 12 YVGVDVGTGSVRAALVDQSGVLLAFADQPI--KNWEPQFNHHEQSSEDIWAA-------------------CCV------ 64
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAiktalkelieelsdyivsgIGVsatcsm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 65 VTKNLRE---------------------ICW-DKAG-------------------------------------------- 78
Cdd:cd07778 82 VVMQRDSdtsylvpynviheksnpdqdiIFWmDHRAseetqwlnnilpddildylgggfipemaipklkylidlikedtf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 79 ---HFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDFVAD--NYSKIGNQV 139
Cdd:cd07778 162 kklEVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNvgNTFKEAPPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 140 LPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIgadvrghgliCEGQPVTSRLAVICGTSSCHMGISKDPI 219
Cdd:cd07778 234 PYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 220 --FVPGVWGPyFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATarcqSIYAYLNSHLDLI--KKAQPVGFLT 295
Cdd:cd07778 303 vgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYLT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 296 VDLHVWPDFHGNRSPLADltlkgmrttgylyipalaalhspssllsPQVTG--LKLSQD--LDDLAILYLATVQAIALGT 371
Cdd:cd07778 378 RHMFFYGDYLGNRTPYND----------------------------PNMSGsfIGESTDssLTDLVLKYILILEFLAFQT 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767905023 372 RFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVV---LSQEVESVLVGAAVLGACAS 433
Cdd:cd07778 430 KLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAF 494
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
11-473 |
2.60e-37 |
|
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: 143.06 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLREIC----------------- 73
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAgispsdiaaigltgqmh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 74 -----------------------------------------------------------------WDKAGHFFdLP-DFL 87
Cdd:cd07808 81 glvlldkngrplrpailwndqrsaaeceelearlgdeiliitgnpplpgftlpkllwlkenepeiFARIRKIL-LPkDYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 88 SWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdfvadnyskigNQVLPP---GASLGNGLTPEAAR 156
Cdd:cd07808 160 RYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD-----------PSILPPiveSTEIVGTLTPEAAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 157 DLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPV----TSrlAVICGTSSCHMGISKDPIF-----VPGVW-- 225
Cdd:cd07808 222 ELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfphaVPGKWya 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 226 -GPYFSAmvpGF---WLNE--GGQSVTGKLIDHMVQGHAAfpelqvkatarcqsiyaylnshldlikKAQPVGFLtvdlh 299
Cdd:cd07808 292 mGVTLSA---GLslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSEGLLFL----- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 300 vwPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAME 379
Cdd:cd07808 337 --PYLSGERTPYWDPNARGS------------------------FFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLK 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 380 AAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQD 459
Cdd:cd07808 388 ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPER 467
|
570
....*....|....
gi 767905023 460 KKYYDKKYQVFLKL 473
Cdd:cd07808 468 HEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
11-430 |
1.53e-31 |
|
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: 125.80 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLRE------------------- 71
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAelrprrvvaiavdgtsgtl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 72 ICWDKAGH-------------------------------------FFDLP-----------------------DFLSWKA 91
Cdd:cd07783 81 VLVDREGEplrpaimyndaravaeaeelaeaagavaprtglavspSSSLAkllwlkrhepevlaktakflhqaDWLAGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 92 TGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASL 170
Cdd:cd07783 161 TGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIP-------PDLLPRVVAPGTVIGT-LTAEAAEELGLPAGTPVVAGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 171 IDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPGVwGPYFSAMVPGFWLNEGGQSVTGKLI 250
Cdd:cd07783 233 TDSIAAFLAS--------GAVRPGDAVTS-----LGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 251 DHmvqghaAFPELQVKAtarcqsiyaylnshldLIKKAQPVGflTVDLHVWP-DFHGNRSPLADltlkgmrttgylyipa 329
Cdd:cd07783 299 RW------FFSDDELAE----------------LSAQADPPG--PSGLIYYPlPLRGERFPFWD---------------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 330 laalhspssllsPQVTGLKLSQDLDDlAILYLATVQAIALGTRFIIEAMEAAGHS-ISTLFLCGGLSKNPLFVQMHADIT 408
Cdd:cd07783 339 ------------PDARGFLLPRPHDR-AEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVL 405
|
490 500
....*....|....*....|..
gi 767905023 409 GMPVVLSQEVESVLvGAAVLGA 430
Cdd:cd07783 406 GVPVVIAEEEEAAL-GAALLAA 426
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
11-434 |
2.13e-31 |
|
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: 125.74 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLRE------------------- 71
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksgvdpsdiagvgvtghgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 72 ---------------ICW-------------------------------------------------DKAGHFFDLPDFL 87
Cdd:cd07802 81 glylvdkdgkpvrnaILSndsraadivdrweedgtlekvypltgqplwpgqpvallrwlkeneperyDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 88 SWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDFvadnYSKIGnQVLPPGASLGnGLTPEAARDLGL 160
Cdd:cd07802 161 RYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEEL----KDKLP-PLVPSTEIAG-RVTAEAAALTGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 161 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGpYFSAMVPGFWLNE 240
Cdd:cd07802 228 PEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLYLIV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 241 GGQSVTGKLIDHMVQghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVgfltvdlhvwpdfhgnrspladltlkgmr 320
Cdd:cd07802 294 EASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPG----------------------------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 321 TTGYLYIPALAAlhspsSLLSPQVT----GLKLSQDLDDLAilyLATVQAIALGTRFIIEAMEAAGHsISTLFLCGGLSK 396
Cdd:cd07802 336 SSGVIFLPYLYG-----SGANPNARggffGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGAR 406
|
490 500 510
....*....|....*....|....*....|....*...
gi 767905023 397 NPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 434
Cdd:cd07802 407 SPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
11-434 |
1.04e-30 |
|
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: 123.47 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLRE------------------- 71
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAqagpdpiaaisvssqgesg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 72 -------------ICW-------------------------------------------------DKAGHFFDLPDFLSW 89
Cdd:cd07773 81 vpvdrdgeplgpaIVWfdprgkeeaeelaerigaeelyritglppspmyslakllwlrehepeifAKAAKWLSVADYIAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 90 KATGVTARSLcSLVCKWTY--SAEKGWDDSFWKMIGLEdfvADNYSkignQVLPPGASLGNgLTPEAARDLGLLPGIAVA 167
Cdd:cd07773 161 RLTGEPVTDY-SLASRTMLfdIRKRTWSEELLEAAGID---ASLLP----ELVPSGTVIGT-VTPEAAEELGLPAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 168 ASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFS---AMVPGFWLNEGGQS 244
Cdd:cd07773 232 VGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 245 vTGKLIDHMVQGHAAFPELQVKATARCQSIYAylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMrttgy 324
Cdd:cd07773 299 -GGALLEWFRDLFGGDESDLAAADELAEAAPP----------GPTGLLFL-------PHLSGSGTPDFDPDARGA----- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 325 lyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMH 404
Cdd:cd07773 356 -------------------FLGLTLGTTRADL---LRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLK 413
|
490 500 510
....*....|....*....|....*....|
gi 767905023 405 ADITGMPVVLSQEVESVLVGAAVLGACASG 434
Cdd:cd07773 414 ADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
11-434 |
2.98e-28 |
|
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: 116.86 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQP--IKNwePQFNHHEQSSEDIWAACCVVTKNL------------------- 69
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEhdLLT--PKPGWAEHDPEVWWGAVCEIIRELlakagispkeiaaigvsgl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 70 -----------------------------------------REIC-----------------------WDKAGHFFDLPD 85
Cdd:cd07804 79 vpalvpvdengkplrpailygdrrateeiewlnenigedriFEITgnpldsqsvgpkllwikrnepevFKKTRKFLGAYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 86 FLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGLEdfvadnySKIGNQVLPPGASLGnGLTPEAARDL 158
Cdd:cd07804 159 YIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGID-------PDLLPELVPSTEIVG-EVTKEAAEET 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 159 GLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVPGVWGPYFSamVPGFWL 238
Cdd:cd07804 226 GLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 239 NEGGQSVTGKLIDHMVQGHAafPELQVKATARCQSIYAYLNshldliKKAQ--PVGfltVD-LHVWPDFHGNRSPLADLT 315
Cdd:cd07804 291 LNGGMATSGSLLRWFRDEFA--GEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIVLPYFMGERTPIWDPD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 316 LKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS 395
Cdd:cd07804 360 ARGV------------------------IFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGA 412
|
490 500 510
....*....|....*....|....*....|....*....
gi 767905023 396 KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 434
Cdd:cd07804 413 KSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
11-474 |
7.08e-28 |
|
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: 116.12 E-value: 7.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLRE------------------- 71
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAklgggevdaigfssamhsl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 72 -------------ICW-------------------------------------------------DKAGHFFDLPDFLSW 89
Cdd:cd07770 81 lgvdedgepltpvITWadtraaeeaerlrkegdgselyrrtgcpihpmyplakllwlkeerpelfAKAAKFVSIKEYLLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 90 KATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEdfvADNYSKIgnqvLPPGASLGnGLTPEAARDLGLLPGI 164
Cdd:cd07770 161 RLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGID---EEQLPEL----VDPTEVLP-GLKPEFAERLGLLAGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 165 AVAASLIDahaGGLGVIGAdvrghGLICEGqpvtsRLAVICGTSschmG----ISKDPIFVP--GVWgPYFSAmvPGFWL 238
Cdd:cd07770 229 PVVLGASD---GALANLGS-----GALDPG-----RAALTVGTS----GairvVSDRPVLDPpgRLW-CYRLD--ENRWL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 239 -----NEGGqSVTGKLIDHMVQGHAAFPELQVKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPDFHGNRSPLAD 313
Cdd:cd07770 289 vggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PYLAGERAPGWN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 314 LTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG 393
Cdd:cd07770 347 PDARGA------------------------FFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGG 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 394 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEamAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 473
Cdd:cd07770 400 FLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKL 477
|
.
gi 767905023 474 V 474
Cdd:cd07770 478 Y 478
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
11-434 |
1.44e-22 |
|
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: 99.99 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHH--EQSSEDIWAACCVVTKNL------------------- 69
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREAlkkagispedisavsstsq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 70 RE--ICWDKAGH-FFDLPDF-----------------LSWKATGVT-----------------------ARSLCSL---- 102
Cdd:cd07798 81 REgiVFLDKDGReLYAGPNIdargveeaaeiddefgeEIYTTTGHWptelfpaarllwfkenrpeiferIATVLSIsdwi 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 103 --------VCKWTYSAEKG--------WDDSFWKMIGLEDfvadnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAV 166
Cdd:cd07798 161 gyrltgelVSEPSQASETQlfdikkreWSQELLEALGLPP-------EILPEIVPSGTVLGT-VSEEAARELGLPEGTPV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 167 AASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDPIFVP--GVW-GPYfsaMVPGFWLNEGGQ 243
Cdd:cd07798 233 VVGGADTQCALLGS--------GAIEPGD-----IGIVAGTTTPVQMVTDEPIIDPerRLWtGCH---LVPGKWVLESNA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 244 SVTGKLIDHMVQGHAAFPELQvkatarcqsiYAYLNSHLDLIKKAQP--VGFLTvdlhvwpdfhgnrSPLADLTLKGMRT 321
Cdd:cd07798 297 GVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLG-------------PQIFDARLSGLKN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 322 TGYLYipalaalhspSSLLSPQVTGLKlsqdldDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLF 400
Cdd:cd07798 354 GGFLF----------PTPLSASELTRG------DFAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALL 414
|
490 500 510
....*....|....*....|....*....|....
gi 767905023 401 VQMHADITGMPVVLSQEVESVLVGAAVLGACASG 434
Cdd:cd07798 415 CQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
11-434 |
5.44e-21 |
|
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: 95.31 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNLRE------------------ 71
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKdagaelrdvaaigisgqm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 72 ---ICWDKAG------------------------------------------------------------HFFDLP-DFL 87
Cdd:cd07809 81 hglVALDADGkvlrpaklwcdtrtapeaeeltealggkkcllvglniparftaskllwlkenepehyariAKILLPhDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 88 SWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDFVADNYSKIGnQVLPPGASLGnGLTPEAARDLGL 160
Cdd:cd07809 161 NWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLP-EVLPAGEVAG-RLTPEGAEELGL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 161 LPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDPIFVPgvwgpyfSAMVPGF---- 236
Cdd:cd07809 230 PAGIPVAPGEGDNMTGALGT--------GVVNPGTVAVS-----LGTSGTAYGVSDKPVSDP-------HGRVATFcdst 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 237 ----WLNEG---GQSVTGKLIDHMVQGHAAFPELQVKATARCQSI--YAYLNshldlikkaqpvgfltvdlhvwpdfhgn 307
Cdd:cd07809 290 ggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLllLPFLN---------------------------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 308 rspladltlkGMRTTGYlyipalaalhspssllsPQVTGLKLSQDLDD--LAILYLATVQAIALGTRFIIEAMEAAGHSI 385
Cdd:cd07809 342 ----------GERTPNL-----------------PHGRASLVGLTLSNftRANLARAALEGATFGLRYGLDILRELGVEI 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 767905023 386 STLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 434
Cdd:cd07809 395 DEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
362-475 |
1.67e-15 |
|
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: 78.66 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 362 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGdFASVQ 440
Cdd:cd07769 374 AALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVG-FWKDL 452
|
90 100 110
....*....|....*....|....*....|....*
gi 767905023 441 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 475
Cdd:cd07769 453 DELASLWQVDKRFEPSMDEEE-RERLYRGWKKAVE 486
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
362-475 |
2.10e-15 |
|
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: 78.33 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 362 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 440
Cdd:cd07792 384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463
|
90 100 110
....*....|....*....|....*....|....*
gi 767905023 441 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 475
Cdd:cd07792 464 ELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
362-475 |
2.79e-15 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 78.18 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 362 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 440
Cdd:COG0554 377 AALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLE 456
|
90 100 110
....*....|....*....|....*....|....*
gi 767905023 441 EaMAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 475
Cdd:COG0554 457 E-LAALWKVDRRFEPQM-DEEERERLYAGWKKAVE 489
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
65-468 |
3.51e-15 |
|
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: 77.76 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 65 VTKNLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDFvadnyskIGNQVLPP 142
Cdd:cd07775 141 LKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKAD-------ILPPVVES 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 143 GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrlAVICGTSSCHMGI-SKDPIFV 221
Cdd:cd07775 212 GTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 222 PGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFPELQVKATARCQSIYAYLNshldliKKAQ--PVGFltvdlh 299
Cdd:cd07775 277 PAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCAEEKEIAERLGIDAYDLLE------EMAKdvPPGS------ 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 300 vwpdfHGNRSPLADLtlkgMRTTGYlYIPAlaalhspssllsPQVTGLKLSQDLDDLAILYLATVQAIALGTRFIIEAME 379
Cdd:cd07775 343 -----YGIMPIFSDV----MNYKNW-RHAA------------PSFLNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 380 AA-GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQ 458
Cdd:cd07775 401 EFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPE 480
|
410
....*....|
gi 767905023 459 DKKYYDKKYQ 468
Cdd:cd07775 481 NHEVYQDLYE 490
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
362-462 |
1.60e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 75.78 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 362 ATVQAIALGTRFIIEAME-AAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 440
Cdd:PTZ00294 383 AALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462
|
90 100
....*....|....*....|..
gi 767905023 441 EAMAKMSKVGKVVFPRLQDKKY 462
Cdd:PTZ00294 463 EVKKLIRRSNSTFSPQMSAEER 484
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
362-475 |
1.81e-14 |
|
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: 75.61 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 362 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 440
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
90 100 110
....*....|....*....|....*....|....*
gi 767905023 441 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 475
Cdd:cd07786 454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
362-476 |
4.58e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 67.93 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 362 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 440
Cdd:PRK00047 380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459
|
90 100 110
....*....|....*....|....*....|....*.
gi 767905023 441 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 476
Cdd:PRK00047 460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
11-434 |
1.66e-11 |
|
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: 66.11 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKNL--------REI---------- 72
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVvakldvlpDRVaaigvtgqgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 73 -CW--DKAGHffdlP-------------DFL-SWKATGVT-------------------------------ARSLCSLVC 104
Cdd:cd24121 81 gTWlvDEDGR----PvrdailwldgraaDIVeRWQADGIAeavfeitgtglfpgsqaaqlawlkeneperlERARTALHC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 105 K-WTYS--------------------AEKGWDDSFWKMIGLEDFVAdnyskignqVLPP-GASLGNG--LTPEAARDLGL 160
Cdd:cd24121 157 KdWLFYkltgeiatdpsdasltfldfRTRQYDDEVLDLLGLEELRH---------LLPPiRPGTEVIgpLTPEAAAATGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 161 LPGIAVAASLIDAHAGGLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLne 240
Cdd:cd24121 228 PAGTPVVLGPFDVVATALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWL-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 241 ggqsvtgklidHMVQGHAAFPELQvkatarcqsiyaYLnshLDLIKKAQPVGFLTVDLHVWPDFHG--NRSPLAdltlkg 318
Cdd:cd24121 293 -----------RAMANMAGTPNLD------------WF---LRELGEVLKEGAEPAGSDLFQDLEElaASSPPG------ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 319 mrTTGYLYIPALaalhSPSSLLSP--------QVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMeaaGHSISTLFL 390
Cdd:cd24121 341 --AEGVLYHPYL----SPAGERAPfvnpnaraQFTGLSLEHTRADLL---RAVYEGVALAMRDCYEHM---GEDPGELRL 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 767905023 391 CGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 434
Cdd:cd24121 409 SGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
321-475 |
5.56e-11 |
|
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: 64.51 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 321 TTGYLYIPALAALHSP--SSLLSPQVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKN 397
Cdd:cd07793 349 TNGVYFVPAFSGLQAPynDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNN 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767905023 398 PLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 475
Cdd:cd07793 426 DFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
359-462 |
3.04e-08 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 55.80 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 359 LYLATVQAIALGTRFIIEAMEAAGH-SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA 437
Cdd:PRK10331 363 FYRAALEGLTAQLKRNLQVLEKIGHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFS 442
|
90 100
....*....|....*....|....*
gi 767905023 438 SVQEAMAKMSKVGKVVFPRLQDKKY 462
Cdd:PRK10331 443 SPEQARAQMKYQYRYFYPQTEPEFI 467
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
367-442 |
3.30e-08 |
|
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: 55.61 E-value: 3.30e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767905023 367 IALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAVLGACASGDFASVQEA 442
Cdd:cd07771 378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
362-475 |
2.31e-07 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 53.16 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 362 ATVQAIALGTRFIIEAM------EAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 435
Cdd:PLN02295 384 AVLESMCFQVKDVLDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767905023 436 FASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 475
Cdd:PLN02295 464 WTEEEIFASEKWKNTTTFRPKLDEEE-RAKRYASWCKAVE 502
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
11-426 |
3.64e-07 |
|
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: 52.22 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 11 YYVGVDVGTGSVRAALVD-QSGVLLAFADQPIKNWEPQ--FNHHEQSSEDIWAAccvVTKNLREIC-------------- 73
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA---VRNLIDELPreylsdvtgigitg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 74 -------WDKAGhfFDLPDFLSW---------------------KATGVTARS---LCSLvckWTYSAEKGWDDSFWKMI 122
Cdd:cd07777 78 qmhgivlWDEDG--NPVSPLITWqdqrcseeflgglstygeellPKSGMRLKPgygLATL---FWLLRNGPLPSKADRAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 123 GLEDFVAdnySKIGNQVLPP-----GASLG------NGLTPEAARDLG----LLPGIAVAASLI-----DAHAG-----G 177
Cdd:cd07777 153 TIGDYIV---ARLTGLPKPVmhptnAASWGlfdletGTWNKDLLEALGlpviLLPEIVPSGEIVgtlssALPKGipvyvA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 178 LG-----VIGADVRGHGlicegqpvtsRLAVICGTSScHMGISKDPIFVPGVWG--PYFSamvpGFWLNeggqSVT---- 246
Cdd:cd07777 230 LGdnqasVLGSGLNEEN----------DAVLNIGTGA-QLSFLTPKFELSGSVEirPFFD----GRYLL----VAAslpg 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 247 GKLIDHMVQ-----GHAAFPELQVkatarcQSIYAYLNShLDLIKKAQPvgfLTVDlhvwPDFHGNRspladltlkgmrt 321
Cdd:cd07777 291 GRALAVLVDflrewLRELGGSLSD------DEIWEKLDE-LAESEESSD---LSVD----PTFFGER------------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 322 tgylyipalaalHSPSSLLSpqVTGLklsqDLDDLAI--LYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG-LSKNP 398
Cdd:cd07777 344 ------------HDPEGRGS--ITNI----GESNFTLgnLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNP 405
|
490 500
....*....|....*....|....*...
gi 767905023 399 LFVQMHADITGMPVVLSQEVESVLVGAA 426
Cdd:cd07777 406 VLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
11-62 |
4.35e-06 |
|
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: 48.10 E-value: 4.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAAC 62
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAV 52
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
381-476 |
2.27e-05 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 46.92 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 381 AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDK 460
Cdd:PRK10939 406 SGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENH 485
|
90 100
....*....|....*....|...
gi 767905023 461 KYYDKK-------YQVFLKLVEH 476
Cdd:PRK10939 486 ELYQEAkekwqavYADQLGLVDH 508
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
74-428 |
4.09e-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: 42.63 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 74 WDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledfvadnyskignqvLPP 142
Cdd:cd07772 140 FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------------RKA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 143 GASLGNgLTPEAARDLGLLPGIAVAASLIDAHAgglgvigadvrghglicegqpvtSRLAvicgtsscHMGISKDPiFV- 221
Cdd:cd07772 202 WEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP--------YLAAGKEP-FTl 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 222 --PGVWgpyFSAMVPGF-----WLNEG-----GQSVTGKLIdhmvqGHAAFP-----ELQVKataRCQSIYAYLNSHLDL 284
Cdd:cd07772 249 lsTGTW---CIAMNPGNdlpltELDLArdclyNLDVFGRPV-----KTARFMggreyERLVE---RIAKSFPQLPSLADL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 285 IKkaqpvgFLTVDLHVWPDFHGNRSPladltlkgmrttgylyIPALAALHSPSSLLSPQvtglklsqDLDDLAILYLATV 364
Cdd:cd07772 318 AK------LLARGTFALPSFAPGGGP----------------FPGSGGRGVLSAFPSAE--------EAYALAILYLALM 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767905023 365 QAIALgtrfiieamEAAGHSISTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAVL 428
Cdd:cd07772 368 TDYAL---------DLLGSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
382-465 |
1.85e-03 |
|
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: 40.62 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905023 382 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV----GKVVFPRL 457
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 767905023 458 QDKKYYDK 465
Cdd:cd07776 503 EAAEVYDK 510
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
11-62 |
1.97e-03 |
|
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: 40.62 E-value: 1.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767905023 11 YYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAAC 62
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQF 52
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