|
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 ... |
5-520 |
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: 725.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDATCS 84
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 85 LVALDAEGNGLSVSPDSPASQDIIMWMDHRAHEETVRINATRDPALCYVGGEVSIEMELPKLLWLQRHHPETWNQAWRFF 164
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPETWAKAGHFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 165 DLADFLVWKATGQDAASLCTLTCKWNYLAHEA---QFSESLLREVGLETLLT----KIPDTILDVAECVGK-LSPQAAQA 236
Cdd:cd07782 161 DLPDFLTWKATGSLTRSLCSLVCKWTYLAHEGsegGWDDDFFKEIGLEDLVEdnfaKIGSVVLPPGEPVGGgLTAEAAKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 237 LGLPEEVVVASGMIDAHAGGVALTGSHPEG----------TLALISGTSNCHMLASQTEIHTPGVWGPYWSAMLPGYWLT 306
Cdd:cd07782 241 LGLPEGTPVGVSLIDAHAGGLGTLGADVGGlpceadpltrRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 307 EGGQSAAGALVDWTLREHGASADLFAKAEAAQRHPVALLNDWVAALEQEEKYP----TRNLHILADHHGNRSPRSRPDAR 382
Cdd:cd07782 321 EGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKGLPlaylTRDLHVLPDFHGNRSPLADPTLR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 383 GSVVGLTLETGERALARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAV 462
Cdd:cd07782 401 GMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 515952599 463 TLGAAICGAVASGAWATLTDATREMVKAGDIITRRPETAAFHRQKYEAYLMLWTQQQA 520
Cdd:cd07782 481 LLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQRE 538
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-514 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 592.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQ-GERLSFATRPISQFH------ASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSI 77
Cdd:COG1069 3 YVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWViglylpPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 78 GFDAT-CSLVALDAEGNGLSVSP---DSPAsQDIIMWMDHRAHEETVRIN----ATRDPALCYVGGEVSIEMELPKLLWL 149
Cdd:COG1069 83 GVDATgCTPVPVDADGTPLALLPefaENPH-AMVILWKDHTAQEEAERINelakARGEDYLRYVGGIISSEWFWPKILHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 150 QRHHPETWNQAWRFFDLADFLVWKATGQDAASLCTLTCKWNYLAHEAQF-SESLLREVG--LETLLTKIPDTILDVAECV 226
Cdd:COG1069 162 LREDPEVYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAHEGGYpSEEFFAALDplLDGLADRLGTEIYPLGEPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 227 GKLSPQAAQALGLPEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAMLPGYWLT 306
Cdd:COG1069 242 GTLTAEWAARLGLPPGTAVAVGAIDAHAGAVG-AGGVEPGTLVKVMGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 307 EGGQSAAGALVDWTLREHGASADLFAKAEAAQRHPVALLNDWVAALEQEEkyptRNLHILADHHGNRSPRSRPDARGSVV 386
Cdd:COG1069 321 EAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLTEEAAKLPPGE----SGLHALDWFNGNRSPLADQRLKGVIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 387 GLTLETGeraLARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGG-ATHNRLWLREYADATGCDIHLLAEEDAVTLG 465
Cdd:COG1069 397 GLTLGTD---AEDIYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALG 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 515952599 466 AAICGAVASGAWATLTDATREMVKAGD-IITRRPETAAFHRQKYEAYLML 514
Cdd:COG1069 474 AAMFAAVAAGAYPDVEEAMAAMGSGFDkVYTPDPENVAVYDALYAEYLQL 523
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
5-521 |
4.85e-176 |
|
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: 507.12 E-value: 4.85e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDATCS 84
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLAESKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 85 LVALDAEGNGLSVSPDSPASQDIIMWMDHRAHEETVRINATRDPALCYVGGEVSIEMELPKLLWLQRHHPETWNQAWRFF 164
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPELFARCKFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 165 DLADFLVWKATGQDAASLCTLTCKWNYLAHEAQ---FSESLLREVGLETLLT----KIPDTILDVAECVGK-LSPQAAQA 236
Cdd:TIGR01315 161 DLTDFLTWRATGKEIRSFCSVVCKWGFVPVDGSnkgWQEDFYETIGLGELVTdnfiRMGGSWMSPGELVGGgLTAEAAQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 237 LGLPEEVVVASGMIDAHAGGVALTG---------SHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAMLPGYWLTE 307
Cdd:TIGR01315 241 LGLPAGTAVGSGLIDAHAGWIGTVGakvaengdvSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 308 GGQSAAGALVDWTLREHGASADLFAKAEAAQRHPVALLNDWVAALEQEEKYP-----TRNLHILADHHGNRSPRSRPDAR 382
Cdd:TIGR01315 321 GGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHLKEMAAKTNAPsisylVRHFHVYPDLWGNRSPIADPNMR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 383 GSVVGLTLETGERALARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADAtgCDIHLLA--EED 460
Cdd:TIGR01315 401 GVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADA--CDMPVLIpyVNE 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515952599 461 AVTLGAAICGAVASGAWATLTDATREMVKAGDIITRRPETA-AFHRQKYEAYLMLWTQQQAL 521
Cdd:TIGR01315 479 AVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDPAkKLHDRKYEIFLQLARTQQEY 540
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
5-515 |
1.45e-161 |
|
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: 468.55 E-value: 1.45e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLY-SAQGERLSFATRPISQFHASN--ARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDA 81
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVdLADGEELASAVVPYPTGYIPPrpGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 82 TCS-LVALDAEGNglsvsPDSPAsqdiIMWMDHRAHEETVRINATRDPA----LCYVGGEVSIEMELPKLLWLQRHHPET 156
Cdd:cd07781 81 TSStVVPVDEDGN-----PLAPA----ILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 157 WNQAWRFFDLADFLVWKATGQDAASLCTLTCKWNYLAHEAQFSESLLREVGLE--TLLTKIPDTILDVAECVGKLSPQAA 234
Cdd:cd07781 152 YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGllKLREKLPGEVVPVGEPAGTLTAEAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 235 QALGLPEEVVVASGMIDAHAGGVALtGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAMLPGYWLTEGGQSAAG 314
Cdd:cd07781 232 ERLGLPAGIPVAQGGIDAHMGAIGA-GVVEPGTLALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQSAVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 315 ALVDWtLREHgasadLFAKAEAAQRHPVALLNDWVAALEQEEKyptrNLHILADHHGNRSPRSRPDARGSVVGLTLETGE 394
Cdd:cd07781 311 DIFAW-FVRL-----FVPPAEERGDSIYALLSEEAAKLPPGES----GLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 395 ralARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGAT-HNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVA 473
Cdd:cd07781 381 ---AHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVA 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 515952599 474 SGAWATLTDATREMVKAGDIITRRPETAAFHRQKYEAYLMLW 515
Cdd:cd07781 458 AGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKELY 499
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
5-515 |
5.08e-131 |
|
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: 391.22 E-value: 5.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYS-AQGERLSFATRPISQFHASNA-RVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDAT 82
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSSKKSwKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 83 CSLVALDAEGNGLSVSPDSPASQDIIMWMDHRAHEETVRINATRDPALC-YVGGEVSIEMELPKLLWLQRHHPETWNQAW 161
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHLRDKHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 162 RFFDLADFLVWKATGQDAASLCTLTCKWNYLAHEAQFSESLLREVGLETL---LTKIPDTILDVAECVGKLSPQAAQALG 238
Cdd:cd07768 161 HIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLEhltTTKNLPSNVPIGTTSGVALPEMAEKMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 239 LPEEVVVASGMIDAHAGGVALTGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAMLPGYWLTEGGQSAAGALVD 318
Cdd:cd07768 241 LHPGTAVVVSCIDAHASWFAVASPHLETSLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 319 WtLREHGASADLFAKAEAAQRHPVALLNDwvaALEQEEKYPTRNLHILADH--HGNRSPRSRPDARGSVVGLTLETGERA 396
Cdd:cd07768 321 H-LFESHPCARKFDEALKKGADIYQVLEQ---TIRQIEKNNGLSIHILTLDmfFGNRSEFADPRLKGSFIGESLDTSMLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 397 LARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASGA 476
Cdd:cd07768 397 LTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGK 476
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 515952599 477 ---WATLTDATREMVKAGDIITRRP-ETAAFHRQKYEAYLMLW 515
Cdd:cd07768 477 kqlADSITEADISNDRKSETFEPLAyRLGADYILLYKLLCVKY 519
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-514 |
9.39e-105 |
|
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: 322.94 E-value: 9.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDAT-C 83
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQmH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNGLSvspdsPAsqdiIMWMDHRAHEETVRINATRDPALCY--VGGEVSIEMELPKLLWLQRHHPETWNQAW 161
Cdd:COG1070 82 GLVLLDADGEPLR-----PA----ILWNDTRAAAEAAELREELGEEALYeiTGNPLHPGFTAPKLLWLKENEPEIFARIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 162 RFFDLADFLVWKATGQDA-----ASLCTLtckWNYlaHEAQFSESLLREVGLETLltKIPdTILDVAECVGKLSPQAAQA 236
Cdd:COG1070 153 KVLLPKDYLRYRLTGEFVtdysdASGTGL---LDV--RTRDWSDELLEALGIDRE--LLP-ELVPPGEVAGTLTAEAAAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 237 LGLPEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAMLPGYWLTEGGQSAAGAL 316
Cdd:COG1070 225 TGLPAGTPVVAGAGDNAAAALG-AGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 317 VDWTlrehgasADLFAKAEAAqrhPVALLNDWVAALEQEEK----YPTRNlhiladhhGNRSPRSRPDARGSVVGLTLET 392
Cdd:COG1070 304 LRWF-------RDLFADGELD---DYEELNALAAEVPPGADgllfLPYLS--------GERTPHWDPNARGAFFGLTLSH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 393 GERALARlylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAV 472
Cdd:COG1070 366 TRAHLAR---AVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAV 442
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 515952599 473 ASGAWATLTDATREMVKAGDIITRRPETAAFHRQKYEAYLML 514
Cdd:COG1070 443 GLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYREL 484
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
5-512 |
1.14e-91 |
|
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: 288.65 E-value: 1.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDAT-C 83
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQmQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNGLSvspdspasqDIIMWMDHRAHEETVRINATRDPALCY---VGGEVSIEMELPKLLWLQRHHPETWNQA 160
Cdd:cd07805 81 GVVPVDKDGNPLR---------NAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEIYAKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 161 WRFFDLADFLVWKATGQDAASLCTLTCKWNYLAHEAQFSESLLREVGLEtlLTKIPDtILDVAECVGKLSPQAAQALGLP 240
Cdd:cd07805 152 HKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGID--PDKLPE-LVPSTEVVGELTPEAAAELGLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 241 EEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSN---CH----MLASQTEIHTpgvwgpyWSAMLPGYWLTEGGQSAA 313
Cdd:cd07805 229 AGTPVVGGGGDAAAAALG-AGAVEEGDAHIYLGTSGwvaAHvpkpKTDPDHGIFT-------LASADPGRYLLAAEQETA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 314 GALVDWtlrehgaSADLFAKAEAAQRHPVALLNDWVAALEqeekyPTRN----LHILadhHGNRSPRSRPDARGSVVGLT 389
Cdd:cd07805 301 GGALEW-------ARDNLGGDEDLGADDYELLDELAAEAP-----PGSNgllfLPWL---NGERSPVEDPNARGAFIGLS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 390 LETGERALARlylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAE-EDAVTLGAAI 468
Cdd:cd07805 366 LEHTRADLAR---AVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAAL 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 515952599 469 CGAVASGAWATLTDATrEMVKAGDIITRRPETAAFHRQKYEAYL 512
Cdd:cd07805 443 LAAVGLGLLKSFDEAK-ALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
6-512 |
2.88e-86 |
|
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: 276.59 E-value: 2.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 6 FLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNAR--VEQSSAEIWQQVCAVVREAVDSSgiSPDAICSIGFDATC 83
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISYKQDPKDLwfVTQSSTEIWKAIKTALKELIEEL--SDYIVSGIGVSATC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVAL---DAEGNGLSVSPDSPAS---QDIIMWMDHRAHEETVRIN-ATRDPALCYVGGEVSIEMELPKLLWLQRHHPET 156
Cdd:cd07778 80 SMVVMqrdSDTSYLVPYNVIHEKSnpdQDIIFWMDHRASEETQWLNnILPDDILDYLGGGFIPEMAIPKLKYLIDLIKED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 157 WNQAWRFFDLADFLVWKatgqdaasLCTLTCKWNYLAHEAQ-------------FSESLLREVGLETLLTKIPDTILD-- 221
Cdd:cd07778 160 TFKKLEVFDLHDWISYM--------LATNLGHSNIVPVNAPpsigigidgslkgWSKDFYSKLKISTKVCNVGNTFKEap 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 222 ----VAECVGKLSPQAAQALGLPEEVVVASGMIDAHAG--GVALTGSHPEGTLALISGTSNCHMLASQTEIHTP--GVWG 293
Cdd:cd07778 232 plpyAGIPIGKVNVILASYLGIDKSTVVGHGCIDCYAGwfSTFAAAKTLDTTLFMVAGTSTCFLYATSSSQVGPipGIWG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 294 PYWSaMLPGYWLTEGGQSAAGALVDWTLREHGASADLFAKAEAAQRHPVALLNDWVAALEQEEKYPTRNLHILADHHGNR 373
Cdd:cd07778 312 PFDQ-LLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDANFFETVEEKIDKYERLLGQSIHYLTRHMFFYGDYLGNR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 374 SPRSRPDARGSVVGLTLETGERALARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYAdATGCDI 453
Cdd:cd07778 391 TPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLS-TVLSKI 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515952599 454 HLLAEEDAVTLGAAIcGAVASGAWATLTDATREM----VKAGDII-------TRRPE-----TAAFHRQKYEAYL 512
Cdd:cd07778 470 HIIVPLSDSKYAVVK-GAALLGKAAFLHNQSIEErlisLKNEDQIsicasasIVKLVsdetkLAIILRAKYQIMN 543
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
5-514 |
1.01e-81 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 264.79 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQ-GERLSFATRP-----ISQF-HASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSI 77
Cdd:PRK04123 4 YVIGLDFGTDSVRALLVDCAtGEELATAVVEyphwvKGRYlDLPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAVVGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 78 GFDAT-CSLVALDAEGNGLSVSP---DSPASqDIIMWMDHRAHEETVRINA---TRDPA--LCYVGGEVSIEMELPKLLW 148
Cdd:PRK04123 84 GVDFTgSTPAPVDADGTPLALLPefaENPHA-MVKLWKDHTAQEEAEEINRlahERGEAdlSRYIGGIYSSEWFWAKILH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 149 LQRHHPETWNQAWRFFDLADFLVWKATGQDAA-----SLCTLTCKWNYLAHEAQF-SESLLREV--GLETLL-TKIPDTI 219
Cdd:PRK04123 163 VLREDPAVYEAAASWVEACDWVVALLTGTTDPqdivrSRCAAGHKALWHESWGGLpSADFFDALdpLLARGLrDKLFTET 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 220 LDVAECVGKLSPQAAQALGLPEEVVVASGMIDAHAGGVAlTGSHPeGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAM 299
Cdd:PRK04123 243 WTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVG-AGAEP-GTLVKVMGTSTCDILLADKQRAVPGICGQVDGSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 300 LPGYWLTEGGQSAAGALVDWtLREHGASADLFAKAEAAQRHPVALLNDWVAALEQEEKYPTRnlhiLADHHGNRSPRSRP 379
Cdd:PRK04123 321 VPGLIGYEAGQSAVGDIFAW-FARLLVPPEYKDEAEARGKQLLELLTEAAAKQPPGEHGLVA----LDWFNGRRTPLADQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 380 DARGSVVGLTLETgeRAlARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGG-ATHNRLWLREYADATGCDIHLLAE 458
Cdd:PRK04123 396 RLKGVITGLTLGT--DA-PDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVAS 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 515952599 459 EDAVTLGAAICGAVASGAWATLTDATREMVKA-GDIITRRPETAAFHRQKYEAYLML 514
Cdd:PRK04123 473 DQCPALGAAIFAAVAAGAYPDIPEAQQAMASPvEKTYQPDPENVARYEQLYQEYKQL 529
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
5-511 |
3.89e-81 |
|
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: 261.32 E-value: 3.89e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDA-TC 83
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNGLSvspdsPAsqdiIMWMDHRAHEETVRINATRDPALCYVGGEVSIE-MELPKLLWLQRHHPETWNQAWR 162
Cdd:cd07808 81 GLVLLDKNGRPLR-----PA----ILWNDQRSAAECEELEARLGDEILIITGNPPLPgFTLPKLLWLKENEPEIFARIRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 163 FFdLA-DFLVWKATGQ------DAASlcTL-----TCKWnylaheaqfSESLLREVGLEtlLTKIPDtILDVAECVGKLS 230
Cdd:cd07808 152 IL-LPkDYLRYRLTGElatdpsDASG--TLlfdveKREW---------SEELLEALGLD--PSILPP-IVESTEIVGTLT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 231 PQAAQALGLPEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTS-NCHMLASQTEI-HTPGVWgpYWSAMLPGYWLTEG 308
Cdd:cd07808 217 PEAAEELGLPEGTPVVAGAGDNAAAALG-AGVVEPGDALISLGTSgVVFAPTDKPVPdPKGRLH--TFPHAVPGKWYAMG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 309 G-QSAAGAL---VDWTLREHGASADLFAKAEAAQR-------HPvallndwvaaleqeekYptrnlhiLAdhhGNRSPRS 377
Cdd:cd07808 294 VtLSAGLSLrwlRDLFGPDRESFDELDAEAAKVPPgsegllfLP----------------Y-------LS---GERTPYW 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 378 RPDARGSVVGLTLETGERALARlylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLA 457
Cdd:cd07808 348 DPNARGSFFGLSLSHTRAHLAR---AVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPA 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 515952599 458 EEDAVTLGAAICGAVASGAWATLTDATREMVKAGDIITRRPETAAFHRQKYEAY 511
Cdd:cd07808 425 EEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARY 478
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
5-475 |
2.05e-79 |
|
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: 255.59 E-value: 2.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGisPDAICSIGFdAT-- 82
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISV-SSqg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 83 CSLVALDAEGNGLSvspdspasqDIIMWMDHRAHEETVRINATRDPALCY--VGGEVSIEMELPKLLWLQRHHPETWNQA 160
Cdd:cd07773 78 ESGVPVDRDGEPLG---------PAIVWFDPRGKEEAEELAERIGAEELYriTGLPPSPMYSLAKLLWLREHEPEIFAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 161 WRFFDLADFLVWKATGQDAASLcTLTCKWNYL-AHEAQFSESLLREVGLETllTKIPDtILDVAECVGKLSPQAAQALGL 239
Cdd:cd07773 149 AKWLSVADYIAYRLTGEPVTDY-SLASRTMLFdIRKRTWSEELLEAAGIDA--SLLPE-LVPSGTVIGTVTPEAAEELGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 240 PEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWS---AMLPGYWLTEGGQSAaGAL 316
Cdd:cd07773 225 PAGTPVVVGGHDHLCAALG-AGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLPG-GAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 317 VDWTLREHGASADLFAKAEAAqrhpvallndwvaaLEQEEKYPTRnLHILADHHGNRSPRSRPDARGSVVGLTLETGERA 396
Cdd:cd07773 303 LEWFRDLFGGDESDLAAADEL--------------AEAAPPGPTG-LLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRAD 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515952599 397 LARlylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASG 475
Cdd:cd07773 368 LLR---AILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
5-468 |
1.68e-72 |
|
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: 235.92 E-value: 1.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDAT-C 83
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNGLSvspdspasqDIIMWMDHRAHeetvrinatrdpalcyvggevsiemelpkllwlqrhhpetwnqawrF 163
Cdd:cd00366 81 GVVLVDADGNPLR---------PAIIWLDRRAK----------------------------------------------F 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 164 FDLADFLVWKATGQDA-----ASLCTLtckwnYLAHEAQFSESLLREVGLEtlLTKIPDtILDVAECVGKLSPQAAQALG 238
Cdd:cd00366 106 LQPNDYIVFRLTGEFAidysnASGTGL-----YDIKTGDWSEELLDALGIP--REKLPP-IVESGEVVGRVTPEAAEETG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 239 LPEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAmLPGYWLTEGGQSAAGALVD 318
Cdd:cd00366 178 LPAGTPVVAGGGDTAAAALG-AGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLWLLEGAINTGGASLR 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 319 WtLRehgasaDLFAKAEAAQRHPVALlndwvAALEQEEKYPTRNLHILADHHGNRSPRSRPDARGSVVGLTLETGERALA 398
Cdd:cd00366 256 W-FR------DEFGEEEDSDAEYEGL-----DELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLI 323
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 399 RlylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAI 468
Cdd:cd00366 324 R---AVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAI 390
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
5-475 |
5.63e-68 |
|
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: 225.51 E-value: 5.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDAT-C 83
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNglsvsPDSPAsqdiIMWMDHRAHEETVRINA--TRDPALCYVGGEVSIEMELPKLLWLQRHHPETWNQAW 161
Cdd:cd07802 81 GLYLVDKDGK-----PVRNA----ILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 162 RFFDLADFLVWKATGQ------DA-ASLCTLtckwnylaHEAQFSESLLREVGLETLLTKIPDtILDVAECVGKLSPQAA 234
Cdd:cd07802 152 TVLFCKDWIRYRLTGEistdytDAgSSLLDL--------DTGEYDDELLDLLGIEELKDKLPP-LVPSTEIAGRVTAEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 235 QALGLPEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGpYWSAMLPGYWLTEGGQSAAG 314
Cdd:cd07802 223 ALTGLPEGTPVAAGAFDVVASALG-AGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLYLIVEASPTSA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 315 ALVDWTLREhgasadLFAKAEAAQRHPVALLNDWVAALEQEEK------YptrnlhiLADHHGNrsprsrPDARGSVVGL 388
Cdd:cd07802 301 SNLDWFLDT------LLGEEKEAGGSDYDELDELIAAVPPGSSgviflpY-------LYGSGAN------PNARGGFFGL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 389 TLETGERALARlylATLQAIAYGTRHIMDTLKHHGHTlSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAI 468
Cdd:cd07802 362 TAWHTRAHLLR---AVYEGIAFSHRDHLERLLVARKP-ETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAI 437
|
....*..
gi 515952599 469 CGAVASG 475
Cdd:cd07802 438 CAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
5-504 |
2.49e-67 |
|
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: 223.55 E-value: 2.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDAT-C 83
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNglsvsPDSPAsqdiIMWMDHRAHeetvrinatrdpalcyvggevsiemelpkllwlqrhhpetwnqawRF 163
Cdd:cd07779 81 TFVPVDEDGR-----PLRPA----ISWQDKRTA---------------------------------------------KF 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 164 FDLADFLVWKATGQ---DAASLCtltckWNYL--AHEAQFSESLLREVGLEtlLTKIPDtILDVAECVGKLSPQAAQALG 238
Cdd:cd07779 107 LTVQDYLLYRLTGEfvtDTTSAS-----RTGLpdIRTRDWSDDLLDAFGID--RDKLPE-LVPPGTVIGTLTKEAAEETG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 239 LPEEVVVASGMIDAHAGGVALTGSHPeGTLALISGT-SNCHMLASQTEIHTPGVWGPYWSAMlPGYWLTEGGQSAAGALV 317
Cdd:cd07779 179 LPEGTPVVAGGGDQQCAALGAGVLEP-GTASLSLGTaAVVIAVSDKPVEDPERRIPCNPSAV-PGKWVLEGSINTGGSAV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 318 DWtLRehgasaDLFAKAEAAQRH----PVALLNdwvaalEQEEKYPTRNLHILADHH--GNRSPRSRPDARGSVVGLTLE 391
Cdd:cd07779 257 RW-FR------DEFGQDEVAEKElgvsPYELLN------EEAAKSPPGSDGLLFLPYlaGAGTPYWNPEARGAFIGLTLS 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 392 TGERALARlylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGA 471
Cdd:cd07779 324 HTRAHLAR---AILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAA 400
|
490 500 510
....*....|....*....|....*....|...
gi 515952599 472 VASGAWATLTDATREMVKAGDIITRRPETAAFH 504
Cdd:cd07779 401 VGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
5-475 |
3.51e-66 |
|
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: 221.25 E-value: 3.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRP--ISQFHASNArvEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDA- 81
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEhdLLTPKPGWA--EHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 82 TCSLVALDAEGNglsvsPDSPAsqdiIMWMDHRAHEETVRINAT--RDPALCYVGGEVSIEMELPKLLWLQRHHPETWNQ 159
Cdd:cd07804 79 VPALVPVDENGK-----PLRPA----ILYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 160 AWRFFDLADFLVWKATGQ---DAASLCTLTCKWNYLAHEaqFSESLLREVGLETLLtkIPDtILDVAECVGKLSPQAAQA 236
Cdd:cd07804 150 TRKFLGAYDYIVYKLTGEyviDYSSAGNEGGLFDIRKRT--WDEELLEALGIDPDL--LPE-LVPSTEIVGEVTKEAAEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 237 LGLPEEVVVASGMIDAHAGGVALTGSHPeGTLALISGTSNCHMLASQTEIHTPGVWGPYWSamLPGYWLTEGGQSAAGAL 316
Cdd:cd07804 225 TGLAEGTPVVAGTVDAAASALSAGVVEP-GDLLLMLGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVLNGGMATSGSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 317 VDWtLRehgasaDLFAKAE--AAQRHPVALLndwvAALEQE-EKYPTR--NLHILADHHGNRSPRSRPDARGSVVGLTLE 391
Cdd:cd07804 302 LRW-FR------DEFAGEEveAEKSGGDSAY----DLLDEEaEKIPPGsdGLIVLPYFMGERTPIWDPDARGVIFGLTLS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 392 TGeraLARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGA 471
Cdd:cd07804 371 HT---RAHLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAG 447
|
....
gi 515952599 472 VASG 475
Cdd:cd07804 448 VGVG 451
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
5-474 |
3.56e-66 |
|
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: 220.56 E-value: 3.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPdaICSIGFDATC- 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRR--VVAIAVDGTSg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNglsvsPDSPAsqdiIMWMDHRAHEETVRINATRDPALCYVGGEVSIEMELPKLLWLQRHHPETWNQAWRF 163
Cdd:cd07783 79 TLVLVDREGE-----PLRPA----IMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 164 FDLADFLVWKATGQDAASLCTLTCKWNYLAHEAQFSESLLREVGLEtlLTKIPDtILDVAECVGKLSPQAAQALGLPEEV 243
Cdd:cd07783 150 LHQADWLAGRLTGDRGVTDYNNALKLGYDPETGRWPSWLLALLGIP--PDLLPR-VVAPGTVIGTLTAEAAEELGLPAGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 244 VVASGMIDAHAGGVALTGSHPeGTLALISGTSNCHMLASQTEIHTPGVwGPYWSAMLPGYWLTEGGQSAAGALVDWTLRE 323
Cdd:cd07783 227 PVVAGTTDSIAAFLASGAVRP-GDAVTSLGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVLRWFFSD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 324 HGAsADLFAKAEAAQrhPVALLndwvaaleqeeKYPtrnlHILAdhhGNRSPRSRPDARGSVVGLTLETGEralarLYLA 403
Cdd:cd07783 305 DEL-AELSAQADPPG--PSGLI-----------YYP----LPLR---GERFPFWDPDARGFLLPRPHDRAE-----FLRA 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515952599 404 TLQAIAYGTRHIMDTLKHHGHT-LSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAvTLGAAICGAVAS 474
Cdd:cd07783 359 LLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA-ALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
5-512 |
4.27e-64 |
|
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: 216.27 E-value: 4.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGisPDAICSIGFDATC- 83
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG--GGEVDAIGFSSAMh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNGLSvspdspasqDIIMWMDHRAHEETVRINATRDPALCY--VGGEVSIEMELPKLLWLQRHHPETWNQAW 161
Cdd:cd07770 79 SLLGVDEDGEPLT---------PVITWADTRAAEEAERLRKEGDGSELYrrTGCPIHPMYPLAKLLWLKEERPELFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 162 RFFDLADFLVWKATGQDAASLCT---------LTCKWnylaheaqfSESLLREVGLEtlLTKIPdTILDVAECVGKLSPQ 232
Cdd:cd07770 150 KFVSIKEYLLYRLTGELVTDYSTasgtgllniHTLDW---------DEEALELLGID--EEQLP-ELVDPTEVLPGLKPE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 233 AAQALGLPEEVVVASGMIDAHAGGVALTGSHPeGTLALISGTSncHMLASQTEIHTPGVWGPYWSAMLP-GYWLTEGGQS 311
Cdd:cd07770 218 FAERLGLLAGTPVVLGASDGALANLGSGALDP-GRAALTVGTS--GAIRVVSDRPVLDPPGRLWCYRLDeNRWLVGGAIN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 312 AAGALVDWTLREHGASADLFAKAEAAQRhpvallndwvaaleqEEKYPTRNLHILADHHGNRSPRSRPDARGSVVGLTLE 391
Cdd:cd07770 295 NGGNVLDWLRDTLLLSGDDYEELDKLAE---------------AVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 392 TGERALARlylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGA 471
Cdd:cd07770 360 HTRADILR---AVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLAL 436
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 515952599 472 VASGAWATLtdATREMVKAGDIITRRPETAAFHRQKYEAYL 512
Cdd:cd07770 437 EALGLISSL--EADELVKIGKVVEPDPENHAIYAELYERFK 475
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
5-475 |
1.89e-48 |
|
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: 173.96 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDAT-- 82
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 83 -CSLValDAEGNglsvsPDSPAsqdiIMWMDHRAHEETVRINA--TRDPALCYVGGEVSIEMELPKLLWLQRHHPETWNQ 159
Cdd:cd24121 81 gTWLV--DEDGR-----PVRDA----ILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 160 AWRFFDLADFLVWKATGQDAA--SLCTLTCkwnYLAHEAQFSESLLREVGLETLLTKIPDtILDVAECVGKLSPQAAQAL 237
Cdd:cd24121 150 ARTALHCKDWLFYKLTGEIATdpSDASLTF---LDFRTRQYDDEVLDLLGLEELRHLLPP-IRPGTEVIGPLTPEAAAAT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 238 GLPEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSNCHMLASQtEIHTPGVWGPYWSAM-LPGYWLTEGGQSAAGAL 316
Cdd:cd24121 226 GLPAGTPVVLGPFDVVATALG-SGAIEPGDACSILGTTGVHEVVVD-EPDLEPEGVGYTICLgVPGRWLRAMANMAGTPN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 317 VDWTLREhgASADLFAKAEAAQRHPVALLNDWVAALEqeekyPTRN---LHILADHHGNRSPRSRPDARGSVVGLTLETG 393
Cdd:cd24121 304 LDWFLRE--LGEVLKEGAEPAGSDLFQDLEELAASSP-----PGAEgvlYHPYLSPAGERAPFVNPNARAQFTGLSLEHT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 394 ERALARlylATLQAIAYGTRhimDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVA 473
Cdd:cd24121 377 RADLLR---AVYEGVALAMR---DCYEHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVA 450
|
..
gi 515952599 474 SG 475
Cdd:cd24121 451 LG 452
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
268-473 |
2.43e-48 |
|
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: 165.96 E-value: 2.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 268 LALISGTSNCHMLASQTEIH-TPGVWGPYWSAMLPGYWLTEGGQSAAGALVDWTLREHGASADLFAKAEAaqrhpvallN 346
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLsVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAGNV---------E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 347 DWVAALEQEEKYPTRNLHILADHHGNRSPRSRPDARGSVVGLTLETGeraLARLYLATLQAIAYGTRHIMDTL-KHHGHT 425
Cdd:pfam02782 72 SLAELAALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTT---LAHLYRAILESLALQLRQILEALtKQEGHP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515952599 426 LSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVA 473
Cdd:pfam02782 149 IDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
5-475 |
4.79e-45 |
|
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: 164.26 E-value: 4.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQ-GERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDATC 83
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAEtGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 -SLVALDAEGNGLSvspdsPAsqdiIMWMDHRAHEETVRINATRDPALCYVGGEVSIE-MELPKLLWLQRHHPETWNQAW 161
Cdd:cd07809 81 hGLVALDADGKVLR-----PA----KLWCDTRTAPEAEELTEALGGKKCLLVGLNIPArFTASKLLWLKENEPEHYARIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 162 RFFDLADFLVWKATGQ------DAAslCTL-----TCKWNYLAHEAQFSESLLREvgletlltKIPDtILDVAECVGKLS 230
Cdd:cd07809 152 KILLPHDYLNWKLTGEkvtglgDAS--GTFpidprTRDYDAELLAAIDPSRDLRD--------LLPE-VLPAGEVAGRLT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 231 PQAAQALGLPEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSNCHMLASQTEIHTP-GVWGPYWSAMLpGYWLTEGG 309
Cdd:cd07809 221 PEGAEELGLPAGIPVAPGEGDNMTGALG-TGVVNPGTVAVSLGTSGTAYGVSDKPVSDPhGRVATFCDSTG-GMLPLINT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 310 QSAAGALVDWTLREHGASADLFakAEAAQRHP-----VALLNdwvaaleqeekYptrnlhiladHHGNRSPRsRPDARGS 384
Cdd:cd07809 299 TNCLTAWTELFRELLGVSYEEL--DELAAQAPpgaggLLLLP-----------F----------LNGERTPN-LPHGRAS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 385 VVGLTLETGERA-LARlylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVT 463
Cdd:cd07809 355 LVGLTLSNFTRAnLAR---AALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGA 431
|
490
....*....|..
gi 515952599 464 LGAAICGAVASG 475
Cdd:cd07809 432 LGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
5-475 |
6.85e-43 |
|
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: 158.54 E-value: 6.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNA--RVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIgfdAT 82
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYpdAKEFDPEELWEKICEAIREALKKAGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 83 CS----LVALDAEGNGLSVSPDspasqdiimwMDHRAHEETVRINATRDPALCYVGGEVSIEMELP-KLLWLQRHHPETW 157
Cdd:cd07798 78 TSqregIVFLDKDGRELYAGPN----------IDARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEIF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 158 NQAWRFFDLADFLVWKATGQDAASLCTLTCKWNYLAHEAQFSESLLREVGLETLLTkiPDtILDVAECVGKLSPQAAQAL 237
Cdd:cd07798 148 ERIATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEIL--PE-IVPSGTVLGTVSEEAAREL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 238 GLPEEVVVASGMIDAHAGGVAlTGSHPEGTLALISGTSN-CHMLASQTEIHTPG-VW-GPYwsaMLPGYWLTEGGQSAAG 314
Cdd:cd07798 225 GLPEGTPVVVGGADTQCALLG-SGAIEPGDIGIVAGTTTpVQMVTDEPIIDPERrLWtGCH---LVPGKWVLESNAGVTG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 315 ALVDWTLR----EHGASADLFAKaEAAQRHPVAllNDWVAALE----QEEKYPTRNLHILADHHGNRSPRSRPDargsvv 386
Cdd:cd07798 301 LNYQWLKEllygDPEDSYEVLEE-EASEIPPGA--NGVLAFLGpqifDARLSGLKNGGFLFPTPLSASELTRGD------ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 387 gltletgeraLARlylATLQAIAYGTRHIMDTLKH-HGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLG 465
Cdd:cd07798 372 ----------FAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALG 438
|
490
....*....|
gi 515952599 466 AAICGAVASG 475
Cdd:cd07798 439 AAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
5-511 |
1.45e-32 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 130.53 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISqfHASNARVEQS----SAEIWQQVCAVVREAVDSSGISPDAICSIgfd 80
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWR--HKEVPDVPGSmdfdTEKNWKLICECIREALKKAGIAPKSIAAI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 81 ATCS----LVALDAEGNGLSVSPDspasqdiimwMDHRAHEETVRINATR---DPALCYVGGEVSIEMELPKLLWLQRHH 153
Cdd:cd07775 76 STTSmregIVLYDNEGEEIWACAN----------VDARAAEEVSELKELYntlEEEVYRISGQTFALGAIPRLLWLKNNR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 154 PETWNQAWRFFDLADFLVWKATGQDAA--SLCTLTCKWNylAHEAQFSESLLREVGLEtlltkiPDTILDVAEC---VGK 228
Cdd:cd07775 146 PEIYRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD--LKTRDWDPEILEMAGLK------ADILPPVVESgtvIGK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 229 LSPQAAQALGLPEEVVVASGMIDAHAGGVALtGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAMLPGYWLTEG 308
Cdd:cd07775 218 VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL-GVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIPDMWQAEG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 309 GQSAAGALVDWtLREhGASADLFAKAEAAQRHPVALLNDWVAALeqeekyPTRNLHILA--------DHHGNRSPrsrpd 380
Cdd:cd07775 297 ISFFPGLVMRW-FRD-AFCAEEKEIAERLGIDAYDLLEEMAKDV------PPGSYGIMPifsdvmnyKNWRHAAP----- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 381 argSVVGLTLETGERALARLYLATLQAIAYGTRHIMDTLKH-HGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEE 459
Cdd:cd07775 364 ---SFLNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEfSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVK 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 515952599 460 DAVTLGAAICGAVASGAWATLTDATREMVKAGDIITRRPETAAFHRQKYEAY 511
Cdd:cd07775 441 EATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYEKW 492
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
5-255 |
1.09e-27 |
|
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: 111.28 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFDATC- 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 SLVALDAEGNGLSvspdspasqDIIMWMDHRAHEETVRINATRDPALCYVGGEVSIEM--ELPKLLWLQRHHPETWNQAW 161
Cdd:pfam00370 81 GTVLLDKNDKPLY---------NAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPgfTLSKLRWIKENEPEVFEKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 162 RFFDLADFLVWKATGQDAASLcTLTCKWNYL-AHEAQFSESLLREVGLEtlLTKIPDtILDVAECVGKLSPQAAQALGLP 240
Cdd:pfam00370 152 KFLTIHDYLRWRLTGVFVTDH-TNASRSMMFnIHKLDWDPELLAALGIP--RDHLPP-LVESSEIYGELNPELAAMWGLD 227
|
250
....*....|....*
gi 515952599 241 EEVVVASGMIDAHAG 255
Cdd:pfam00370 228 EGVPVVGGGGDQQAA 242
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
6-482 |
1.02e-22 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 101.20 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 6 FLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDS---SGISPDAICSIGFDAT 82
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQhslQDVKALGIAGQMHGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 83 CslvaLDAEGNGLSvspdsPAsqdiIMWMDHRAHEETVRINAtRDPALCYVGGEVSIE-MELPKLLWLQRHHPETWNQAW 161
Cdd:PRK15027 82 L----LDAQQRVLR-----PA----ILWNDGRCAQECALLEA-RVPQSRVITGNLMMPgFTAPKLLWVQRHEPEIFRQID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 162 RFFDLADFLVWKATGQDAASLCTLT-CKWNYLAHEaQFSESLLREVGLETllTKIPdTILDVAECVGKLSPQAAQALGLP 240
Cdd:PRK15027 148 KVLLPKDYLRLRMTGEFASDMSDAAgTMWLDVAKR-DWSDVMLQACHLSR--DQMP-ALYEGSEITGALLPEVAKAWGMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 241 EEVVVASGMiDAHAGGVALtGSHPEGTLALISGTSNCHMLASQTEIHTPGVWGPYWSAMLPGYWLTEGGQSAAGALVDWT 320
Cdd:PRK15027 224 TVPVVAGGG-DNAAGAVGV-GMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 321 LREHGAsADLFAKAEAAQRhpvallndwvaalEQEEKYPTRNLHILAdhhGNRSPRSRPDARGSVVGLTLETGERALARl 400
Cdd:PRK15027 302 AKLTGL-SNVPALIAAAQQ-------------ADESAEPVWFLPYLS---GERTPHNNPQAKGVFFGLTHQHGPNELAR- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 401 ylATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEED-AVTLGAAICGAVASGAWAT 479
Cdd:PRK15027 364 --AVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDvGPALGAARLAQIAANPEKS 441
|
...
gi 515952599 480 LTD 482
Cdd:PRK15027 442 LIE 444
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
5-509 |
8.63e-22 |
|
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: 98.40 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFdAT-- 82
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 83 CSLVALDAEgNGLSVSPdspasqdIIMWMDHRAHEETVRINA-----------------TRDPalCYVGGEV---SIEME 142
Cdd:cd07793 80 NTFLTWDKK-TGKPLHN-------FITWQDLRAAELCESWNRslllkalrggskflhflTRNK--RFLAASVlkfSTAHV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 143 LPKLLWLQRHHPETWNQA----WRFFDLADFLVWKATGQDA-------ASLCTL----TCKWNylaheaqfsesllrevG 207
Cdd:cd07793 150 SIRLLWILQNNPELKEAAekgeLLFGTIDTWLLWKLTGGKVhatdysnASATGLfdpfTLEWS----------------P 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 208 LETLLTKIPDTIL----DVAECVGKLSPQAAQAlGLPEEVVVA--------SGMIDahAGGVALTgshpEGTLALISgts 275
Cdd:cd07793 214 ILLSLFGIPSSILpevkDTSGDFGSTDPSIFGA-EIPITAVVAdqqaalfgECCFD--KGDVKIT----MGTGTFID--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 276 nchmlasqteIHTpgvwGPYWSAMLPGY-----W--------LTEGGQSAAGALVDWtlrehGASADLFakAEAAQRHPV 342
Cdd:cd07793 284 ----------INT----GSKPHASVKGLyplvgWkiggeityLAEGNASDTGTVIDW-----AKSIGLF--DDPSETEDI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 343 AL-LND-----WVAALeqeekyptrnlhiladhHGNRSPRSRPDARGSVVGLTLETGERALARlylATLQAIAYGTRHIM 416
Cdd:cd07793 343 AEsVEDtngvyFVPAF-----------------SGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 417 DTL-KHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASGAWATLTDaTREMVKAGDIIT 495
Cdd:cd07793 403 ETMeKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEE-LKKLRKIEKIFE 481
|
570
....*....|....
gi 515952599 496 RRPEtaafhRQKYE 509
Cdd:cd07793 482 PKMD-----NEKRE 490
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
2-521 |
2.36e-21 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 97.38 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 2 SDGYFLGVDVGSASVRAGLYSAQGERLSFATRPISqfHASNARVEQSS----AEIWQQVCAVVREAVDSSGISPDAICSI 77
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWR--HLAVPDVPGSMefdlEKNWQLACQCIRQALQKAGIPASDIAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 78 gfdATCSL----VALDAEGNGLsvspdspasqdiimW----MDHRAHEETVRINATRD---PALCYVGGEVSIEMELPKL 146
Cdd:PRK10939 79 ---SATSMregiVLYDRNGTEI--------------WacanVDARASREVSELKELHNnfeEEVYRCSGQTLALGALPRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 147 LWLQRHHPETWNQAWRFFDLADFLVWKATGQ---DAASLCT-----LTCKwnylaheaQFSESLLREVGLETlltKIPDT 218
Cdd:PRK10939 142 LWLAHHRPDIYRQAHTITMISDWIAYMLSGElavDPSNAGTtglldLVTR--------DWDPALLEMAGLRA---DILPP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 219 ILDVAECVGKLSPQAAQALGLPEEVVVASGMIDAHAGGVALtGSHPEGTLALISGTsnchmlASQTEIHTP-GVWGPYWS 297
Cdd:PRK10939 211 VKETGTVLGHVTAKAAAETGLRAGTPVVMGGGDVQLGCLGL-GVVRPGQTAVLGGT------FWQQVVNLPaPVTDPNMN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 298 -----AMLPGYWLTEGGQSAAGALVDWtLRehgasaDLFAKAE--AAQRHPVallnDWVAALEQE-EKYPTRNLHIL--- 366
Cdd:PRK10939 284 irinpHVIPGMVQAESISFFTGLTMRW-FR------DAFCAEEklLAERLGI----DAYSLLEEMaSRVPVGSHGIIpif 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 367 --ADHHGNRSprsrpDARGSVVGLTLETGERALARLYLATLQAIAYGTRHIMDTL-KHHGHTLSRIVICGGATHNRLWLR 443
Cdd:PRK10939 353 sdVMRFKSWY-----HAAPSFINLSIDPEKCNKATLFRALEENAAIVSACNLQQIaAFSGVFPSSLVFAGGGSKGKLWSQ 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515952599 444 EYADATGCDIHLLAEEDAVTLGAAICGAVASGAWATLTDATREMVKAGDIITRRPETAAFHRQKYEAYLMLWTQQQAL 521
Cdd:PRK10939 428 ILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEAKEKWQAVYADQLGL 505
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-469 |
3.44e-21 |
|
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: 96.14 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGER-LSFATRPISQF--HASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICsI---- 77
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRiLESVSRPTPAPisSDDPGRSEQDPEKILEAVRNLIDELPREYLSDVTGIG-Itgqm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 78 -GFdatcslVALDAEGNGLSvspdspasqDIIMWMDHRA---HEETVRINATRDPALCyvGGEVSIEMELPKLLWLQRHH 153
Cdd:cd07777 80 hGI------VLWDEDGNPVS---------PLITWQDQRCseeFLGGLSTYGEELLPKS--GMRLKPGYGLATLFWLLRNG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 154 PETwNQAWRFFDLADFLVWKATG--------QDAAS--LCTLTCK-WNYlaheaqfseSLLREVGLETLLtkIPDtILDV 222
Cdd:cd07777 143 PLP-SKADRAGTIGDYIVARLTGlpkpvmhpTNAASwgLFDLETGtWNK---------DLLEALGLPVIL--LPE-IVPS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 223 AECVGKLSPQAAQalGLPeeVVVASGmiDaHAGGVALTGSHPEGTLALISGTSnchmlaSQTEIHTPgvwGPYWSAML-- 300
Cdd:cd07777 210 GEIVGTLSSALPK--GIP--VYVALG--D-NQASVLGSGLNEENDAVLNIGTG------AQLSFLTP---KFELSGSVei 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 301 -----PGYWLTE----GGQSAAgALVDwTLREHGASADLfakaeaaqRHPVALLNDWVAALEQEEKYPTrnLHILADHHG 371
Cdd:cd07777 274 rpffdGRYLLVAaslpGGRALA-VLVD-FLREWLRELGG--------SLSDDEIWEKLDELAESEESSD--LSVDPTFFG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 372 NrspRSRPDARGSVVGLTLEtgERALARLYLATLQAIAYGTRHIMDTLKHHGHTLSRIVICGGA-THNRlWLREY-ADAT 449
Cdd:cd07777 342 E---RHDPEGRGSITNIGES--NFTLGNLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGAlRKNP-VLRRIiEKRF 415
|
490 500
....*....|....*....|
gi 515952599 450 GCDIHLLAEEDAVTLGAAIC 469
Cdd:cd07777 416 GLPVVLSEGSEEAAVGAALL 435
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
5-485 |
5.06e-20 |
|
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: 92.91 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFdaTC- 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGI--TNq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 84 --SLVALDAEGnGLSVSPdspAsqdiIMWMDHRAHEETVRINATrdpalcyvGGEVSIEME--LP--------KLLWLQR 151
Cdd:cd07769 79 reTTVVWDKKT-GKPLYN---A----IVWQDRRTADICEELKAK--------GLEERIREKtgLPldpyfsatKIKWILD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 152 HHPETWNQA----WRFFDLADFLVWKATGQDA-------AS---LCTLtckwnylaHEAQFSESLLREVGletlltkIPD 217
Cdd:cd07769 143 NVPGARERAergeLLFGTIDTWLIWKLTGGKVhvtdvtnASrtmLFNI--------HTLEWDDELLELFG-------IPR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 218 TIL----DVAECVGKLSPqaaqaLGLPEEVVVAsGMI-DAHAggvALTG--SHPEGTLALISGTSnCHML--------AS 282
Cdd:cd07769 208 SMLpevrPSSEVFGYTDP-----EGLGAGIPIA-GILgDQQA---ALFGqgCFEPGMAKNTYGTG-CFLLmntgekpvPS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 283 Q----TEIHtpgvwgpyWSAMLPGYWLTEGGQSAAGALVDWtLR------EHGA-SADLFAKAEAAQRhpVALlndwVAA 351
Cdd:cd07769 278 KngllTTIA--------WQIGGKVTYALEGSIFIAGAAIQW-LRdnlgliEDAAeTEELARSVEDNGG--VYF----VPA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 352 LeqeekyptrnlhiladhHGNRSPRSRPDARGSVVGLTLETGERALARlylATLQAIAYGTRHIMDTLKHH-GHTLSRIV 430
Cdd:cd07769 343 F-----------------SGLGAPYWDPDARGAIVGLTRGTTKAHIVR---AALESIAYQTRDVLEAMEKDsGIKLKELR 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 515952599 431 ICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASGAWATLTDATR 485
Cdd:cd07769 403 VDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELAS 457
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
5-482 |
1.07e-19 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 92.05 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFD---A 81
Cdd:COG0554 4 YILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITnqrE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 82 TCslVALDAEgNGLSVSPdspasqdIIMWMDHRA-----------HEETVR------InatrDPalcYVGGevsiemelP 144
Cdd:COG0554 84 TT--VVWDRK-TGKPLYN-------AIVWQDRRTadiceelkadgLEDLIRektglvL----DP---YFSA--------T 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 145 KLLWLQRHHPETWNQAWR---FFDLAD-FLVWKATGQ-----DA--ASLcTL-----TCKWnylaheaqfSESLLREVGl 208
Cdd:COG0554 139 KIKWILDNVPGARERAEAgelLFGTIDsWLIWKLTGGkvhvtDVtnASR-TMlfnihTLDW---------DDELLELFG- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 209 etlltkIPDTIL----DVAECVGKLSPQaaqalGLPEEVVVAsGMI-DAHA-------------------GGVAL--TGS 262
Cdd:COG0554 208 ------IPRSMLpevrPSSEVFGETDPD-----LFGAEIPIA-GIAgDQQAalfgqacfepgmakntygtGCFLLmnTGD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 263 HP----EGTLALIsgtsnCHMLASQTEihtpgvwgpywsamlpgYWLtEGGQSAAGALVDWtLREH----GASADLFAKA 334
Cdd:COG0554 276 EPvrskNGLLTTI-----AWGLGGKVT-----------------YAL-EGSIFVAGAAVQW-LRDGlgliDSAAESEALA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 335 EAAQ-RHPVALlndwVAALEqeekyptrnlhiladhhGNRSPRSRPDARGSVVGLTLETGERALARlylATLQAIAYGTR 413
Cdd:COG0554 332 RSVEdNGGVYF----VPAFT-----------------GLGAPYWDPDARGAIFGLTRGTTRAHIAR---AALESIAYQTR 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 414 HIMDTL-KHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASGAWATLTD 482
Cdd:COG0554 388 DVLDAMeADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEE 457
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
5-482 |
1.30e-17 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 85.80 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAV---DSSGISPDaICSIGFda 81
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIkklREKGPSFK-IKAIGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 82 TC---SLVALDAE-GNGLsvspdspasQDIIMWMDHRAHEETVRINATrdpalcYVGGEVSIEME-LP--------KLLW 148
Cdd:PTZ00294 80 TNqreTVVAWDKVtGKPL---------YNAIVWLDTRTYDIVNELTKK------YGGSNFFQKITgLPistyfsafKIRW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 149 LQRHHPE----------------TWnqawrffdladfLVWKATGQD-------AASLCTL----TCKWnylaheaqfSES 201
Cdd:PTZ00294 145 MLENVPAvkdavkegtllfgtidTW------------LIWNLTGGKshvtdvtNASRTFLmnikTLKW---------DEE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 202 LLREVGletlltkIPDTILDV----AECVGKLSPQAAQAL-GLPeevvvASGMI-DAHAggvALTG--SHPEGTLALISG 273
Cdd:PTZ00294 204 LLNKFG-------IPKETLPEikssSENFGTISGEAVPLLeGVP-----ITGCIgDQQA---ALIGhgCFEKGDAKNTYG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 274 TSnCHMLAS--QTEIHTPGvwgpywsAML-----------PGYWLTEGGQSAAGALVDWTlrehgasadlfakaeaaqRH 340
Cdd:PTZ00294 269 TG-CFLLMNtgTEIVFSKH-------GLLttvcyqlgpngPTVYALEGSIAVAGAGVEWL------------------RD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 341 PVALLNDWVAALEQEEKYP-TRNLHILADHHGNRSPRSRPDARGSVVGLTLETGERALARlylATLQAIAYGTRHIMDTL 419
Cdd:PTZ00294 323 NMGLISHPSEIEKLARSVKdTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVR---AALEAIALQTNDVIESM 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515952599 420 -KHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASGAWATLTD 482
Cdd:PTZ00294 400 eKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEE 463
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
5-485 |
1.31e-17 |
|
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: 85.62 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGFD---A 81
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITnqrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 82 TCslVALDAEgNGLSVspdSPAsqdiIMWMDHRA-----------HEETVR------InatrDPalcYVGGevsiemelP 144
Cdd:cd07786 81 TT--VVWDRE-TGKPV---YNA----IVWQDRRTadiceelkaegHEEMIRektglvL----DP---YFSA--------T 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 145 KLLWLQRHHPETWNQAWR---FFDLAD-FLVWKATG-----QDA--ASLCTLtckwnYLAHEAQFSESLLRevgletlLT 213
Cdd:cd07786 136 KIRWILDNVPGARERAERgelAFGTIDsWLIWKLTGgkvhaTDVtnASRTML-----FNIHTLEWDDELLE-------LF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 214 KIPDTIL-DVAECVGKLSpqAAQALGLPEEVVVAsGMI-DAHAggvALTGS--HPEGTLALISGTSnCHML--------A 281
Cdd:cd07786 204 GIPASMLpEVKPSSEVFG--YTDPDLLGAEIPIA-GIAgDQQA---ALFGQacFEPGMAKNTYGTG-CFMLmntgekpvR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 282 SQTEIHTPGVWGpywsamLPG---YWLtEGGQSAAGALVDWtLR------EHGASADLFAKAeAAQRHPVALlndwVAAL 352
Cdd:cd07786 277 SKNGLLTTIAWQ------LGGkvtYAL-EGSIFIAGAAVQW-LRdglgliESAAETEALARS-VPDNGGVYF----VPAF 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 353 EqeekyptrnlhiladhhGNRSPRSRPDARGSVVGLTLETGERALARlylATLQAIAYGTRHIMDTL-KHHGHTLSRIVI 431
Cdd:cd07786 344 T-----------------GLGAPYWDPDARGAIFGLTRGTTRAHIAR---AALESIAYQTRDLLEAMeADSGIPLKELRV 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 515952599 432 CGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASGAWATLTDATR 485
Cdd:cd07786 404 DGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAK 457
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
9-468 |
1.19e-16 |
|
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: 82.31 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 9 VDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEqSSAEIWQQVCAVVREAVDSSGIspDAICSIGFDATCslVAL 88
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEIEEDGYPCE-DVEAIWEWLLDSLAELAKRHRI--DAINFTTHGATF--ALL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 89 DAEGNgLSVSP---DSPASQDIIMwmdhraheetvRINATRDPAL----CYVGGEVSIEMELpklLWLQRHHPETWNQAW 161
Cdd:cd07772 80 DENGE-LALPVydyEKPIPDEINE-----------AYYAERGPFEetgsPPLPGGLNLGKQL---YWLKREKPELFARAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 162 RFFDLADFLVWKATGQDAASLCTLTCK---WNYlaHEAQFSeSLLREVGLEtlltKIPDTILDVAECVGKLSPQAAQALG 238
Cdd:cd07772 145 TILPLPQYWAWRLTGKAASEITSLGCHtdlWDF--EKNEYS-SLVKKEGWD----KLFPPLRKAWEVLGPLRPDLARRTG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 239 LPEEVVVASGMIDAHAGGVALTGSHPEGTLALISGT------SNCHMLASQTEIHTpgvwgpywsAMLpgYWLTEGGQSA 312
Cdd:cd07772 218 LPKDIPVGCGIHDSNAALLPYLAAGKEPFTLLSTGTwciamnPGNDLPLTELDLAR---------DCL--YNLDVFGRPV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 313 AGAlvdwTL---REHGASADLFAKAEAAQrhpvALLNDwVAALEQEEKYPTRNLHiladhhgnRSPRSRPDARGSVVGLT 389
Cdd:cd07772 287 KTA----RFmggREYERLVERIAKSFPQL----PSLAD-LAKLLARGTFALPSFA--------PGGGPFPGSGGRGVLSA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 390 LETGE--RALARLYLATLQAIAygtrhimdtLKHHGHTLSRIVICGGATHNRLWLREYADA-TGCDIHLLAEEDAVTLGA 466
Cdd:cd07772 350 FPSAEeaYALAILYLALMTDYA---------LDLLGSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGA 420
|
..
gi 515952599 467 AI 468
Cdd:cd07772 421 AL 422
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
143-487 |
3.55e-15 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 77.76 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 143 LPKLLWLQRHHPETWNQAWRFFDLADFLVWKATGQDA-----ASLCTLTCkwnylAHEAQFSESLLREVGLETLLtkIPd 217
Cdd:PRK10331 135 LYKLVWLKENHPQLLEQAHAWLFISSLINHRLTGEFTtditmAGTSQMLD-----IQQRDFSPEILQATGLSRRL--FP- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 218 TILDVAECVGKLSPQAAQALGLPEEV-VVASGmidaHAGGVALTGSHPE-GTLALISGTSNCHMLASQTeihtpgvwgpy 295
Cdd:PRK10331 207 RLVEAGEQIGTLQPSAAALLGLPVGIpVISAG----HDTQFALFGSGAGqNQPVLSSGTWEILMVRSAQ----------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 296 wsamlpgywlteggqsaagALVDWTLREHGASADLFAKAeaaqrhpvALLN-----------DWVAAL--EQEEKYPTRN 362
Cdd:PRK10331 272 -------------------VDTSLLSQYAGSTCELDSQS--------GLYNpgmqwlasgvlEWVRKLfwTAETPYQTMI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 363 LHILADHHGNRSPRSRPD----ARGSVVGLTLETGERALARlylATLQAIAYGTRHIMDTLKHHGHTLSRIVIC-GGATH 437
Cdd:PRK10331 325 EEARAIPPGADGVKMQCDllacQNAGWQGVTLNTTRGHFYR---AALEGLTAQLKRNLQVLEKIGHFKASELLLvGGGSR 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 515952599 438 NRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASGAWATLTDATREM 487
Cdd:PRK10331 402 NALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQM 451
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
6-477 |
2.14e-13 |
|
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: 72.56 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 6 FLG-VDVGSASVRAGLYSAQGERLSFATRPISQFHASNARVEQSSAEIWQQVCAVVREAVD---SSGISPDAICSIGFda 81
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEklkALGISPSDIKAIGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 82 TC---SLVALDAEgnglSVSPDSPAsqdiIMWMDHRAhEETVR--INATRDPALCYV---GgevsiemeLP--------K 145
Cdd:cd07792 80 TNqreTTVVWDKS----TGKPLYNA----IVWLDTRT-SDTVEelSAKTPGGKDHFRkktG--------LPistyfsavK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 146 LLWLQRHHPE----------------TWnqawrffdladfLVWKATGQ-DAASLCT-------------LTCKWnylahe 195
Cdd:cd07792 143 LRWLLDNVPEvkkavddgrllfgtvdSW------------LIWNLTGGkNGGVHVTdvtnasrtmlmnlRTLQW------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 196 aqfSESLLREVGLEtlLTKIPdTILDVAECVGKLSpqAAQALGLPeevvvASGMI-DAHAggvALTGSH--PEGTLALIS 272
Cdd:cd07792 205 ---DPELCEFFGIP--MSILP-EIRSSSEVYGKIA--SGPLAGVP-----ISGCLgDQQA---ALVGQGcfKPGEAKNTY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 273 GTSnCHMLASQ-TEI----H----TPGVW-GPywSAmlPGYWLTEGGQSAAGALVDWtLREHGASADLFAKAE--AAQrh 340
Cdd:cd07792 269 GTG-CFLLYNTgEEPvfskHglltTVAYKlGP--DA--PPVYALEGSIAIAGAAVQW-LRDNLGIISSASEVEtlAAS-- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 341 pvalLND-----WVAALEqeekyptrnlhiladhhGNRSPRSRPDARGSVVGLTLETGERALARlylATLQAIAYGTRHI 415
Cdd:cd07792 341 ----VPDtggvyFVPAFS-----------------GLFAPYWRPDARGTIVGLTQFTTKAHIAR---AALEAVCFQTREI 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515952599 416 MDTL-KHHGHTLSRIVICGGATHNRLWLREYADATGCDIHLLAEEDAVTLGAAICGAVASGAW 477
Cdd:cd07792 397 LDAMnKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVW 459
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
5-490 |
1.61e-11 |
|
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: 66.40 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 5 YFLGVDVGSASVRAGLYSAQGERLSFatRPISQFhaSNARVEQSS------AEIWQQVCAVVREAVDSSGispdAICSIG 78
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKLEL--EEIHRF--PNRPVEINGhlywdiDRLFDEIKEGLKKAAEQGG----DIDSIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 79 FDAT-CSLVALDAEGN--GLSVSPDSPASQDIIMWMDHRAHEETV---------RINAtrdpalcyvggevsiemeLPKL 146
Cdd:cd07771 73 IDTWgVDFGLLDKNGEllGNPVHYRDPRTEGMMEELFEKISKEELyertgiqfqPINT------------------LYQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 147 LWLQRHHPETWNQAWRFFDLADFLVWKATGQDAA--SLCTLTCKWNylAHEAQFSESLLREVGLET-LLTKipdtILDVA 223
Cdd:cd07771 135 YALKKEGPELLERADKLLMLPDLLNYLLTGEKVAeyTIASTTQLLD--PRTKDWSEELLEKLGLPRdLFPP----IVPPG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 224 ECVGKLSPQAAQALGLPEEVVVASGmidAH--AGGVALTGSHPEGTLALISGTSNCHMLASQTEIHTPGV--------WG 293
Cdd:cd07771 209 TVLGTLKPEVAEELGLKGIPVIAVA---SHdtASAVAAVPAEDEDAAFISSGTWSLIGVELDEPVITEEAfeagftneGG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 294 PYWSAML----PGYWLTEggqsaaGALVDWTLREHGAS-ADLFAKAEAAqRHPVALLNdwvaaLEQEEKYPTRNLHILAD 368
Cdd:cd07771 286 ADGTIRLlkniTGLWLLQ------ECRREWEEEGKDYSyDELVALAEEA-PPFGAFID-----PDDPRFLNPGDMPEAIR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 369 HHGNRSPRSRPDARGSVVGLTLETgeraLARLYLATLQAIAYGTrhimdtlkhhGHTLSRIVICGGATHNRLwLREY-AD 447
Cdd:cd07771 354 AYCRETGQPVPESPGEIARCIYES----LALKYAKTIEELEELT----------GKRIDRIHIVGGGSRNAL-LCQLtAD 418
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 515952599 448 ATGCDIHLLAEEdAVTLGAAICGAVASGAWATLTDAtREMVKA 490
Cdd:cd07771 419 ATGLPVIAGPVE-ATAIGNLLVQLIALGEIKSLEEG-RELVRN 459
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
375-507 |
1.96e-11 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 66.26 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 375 PRSRPDARGSVVGLTLETGERALARlylATLQAIAYGTRHIMDTLK------HHGHTLSRIVICGGATHNRLWLREYADA 448
Cdd:PLN02295 359 PRWRDDARGVCVGITRFTNKAHIAR---AVLESMCFQVKDVLDAMRkdageeKSHKGLFLLRVDGGATANNLLMQIQADL 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 515952599 449 TGCDIHLLAEEDAVTLGAAICGAVASGAWATLTDATREMVKAgdIITRRPETAAFHRQK 507
Cdd:PLN02295 436 LGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKN--TTTFRPKLDEEERAK 492
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
375-480 |
2.61e-09 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 59.45 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952599 375 PRSRPDARGSVVGLTLETGERALARlylATLQAIAYGTRHIMDTL-KHHGHTLSRIVICGGATHNRLWLREYADATGCDI 453
Cdd:PRK00047 355 PYWDSDARGAIFGLTRGTTKEHIIR---ATLESIAYQTRDVLDAMqADSGIRLKELRVDGGAVANNFLMQFQADILGVPV 431
|
90 100
....*....|....*....|....*....
gi 515952599 454 H--LLAEEDAvtLGAAICGAVASGAWATL 480
Cdd:PRK00047 432 ErpVVAETTA--LGAAYLAGLAVGFWKDL 458
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
4-79 |
7.11e-05 |
|
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: 44.89 E-value: 7.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515952599 4 GYFLGVDVGSASVRAGLYSAQGERLSFATRPIsqfhasnaRVEQSSAEIWQQVCAVVREAVDSSGISPDAICSIGF 79
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPT--------PAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| |
