|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-538 |
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: 946.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDATCS 83
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 84 LVVLDKDGHPLTVSPSGRSEQNIIVWMDHRAISQAERINATHHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAGFFF 163
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPETWAKAGHFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 164 DLPDFLTWRATQDDTRSLCSTVCKWTFMGQEDS---WDASYFRTIGLEDLLHHDAEKIGRYVRMMGEPLGHGLTSGAARE 240
Cdd:cd07782 161 DLPDFLTWKATGSLTRSLCSLVCKWTYLAHEGSeggWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 241 MGLIPGTSVSVSIIDGHAGALGILGA--CGVSGEVADFNRRVALIGGTSTGHMAMSPEPRFINGIWGPYYSAILPAYWLN 318
Cdd:cd07782 241 LGLPEGTPVGVSLIDAHAGGLGTLGAdvGGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 319 EGGQSATGALIDHVIQSHPCYDMLLTQGKTAGKTIYQVLNELLRTMAGE-PESIAFLTKDIHVLPYFHGNRSPRANPTLT 397
Cdd:cd07782 321 EGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEkGLPLAYLTRDLHVLPDFHGNRSPLADPTLR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 398 GAITGLKLSRTPEDMALQYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAM 477
Cdd:cd07782 401 GMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556268182 478 LLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTNsIKQYYDRKYRIFHEMYQDLMKYR 538
Cdd:cd07782 481 LLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEE-LKKYHDRKYEVFLKMYEDQREYR 540
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
4-538 |
0e+00 |
|
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.
Pssm-ID: 273552 [Multi-domain] Cd Length: 541 Bit Score: 688.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDATCS 83
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLAESKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 84 LVVLDKDGHPLTVSPSGRSEQNIIVWMDHRAISQAERINATHHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAGFFF 163
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPELFARCKFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 164 DLPDFLTWRATQDDTRSLCSTVCKWTFM---GQEDSWDASYFRTIGLEDLLHHDAEKIGRYVRMMGEPLGHGLTSGAARE 240
Cdd:TIGR01315 161 DLTDFLTWRATGKEIRSFCSVVCKWGFVpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 241 MGLIPGTSVSVSIIDGHAGALGILGACGV-SGEVADFNRRVALIGGTSTGHMAMSPEPRFINGIWGPYYSAILPAYWLNE 319
Cdd:TIGR01315 241 LGLPAGTAVGSGLIDAHAGWIGTVGAKVAeNGDVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 320 GGQSATGALIDHVIQSHPCYDMLLTQGKTAGKTIYQVLNELLRTMAGEP--ESIAFLTKDIHVLPYFHGNRSPRANPTLT 397
Cdd:TIGR01315 321 GGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHLKEMAAKTnaPSISYLVRHFHVYPDLWGNRSPIADPNMR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 398 GAITGLKLSRTPEDMALQYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAM 477
Cdd:TIGR01315 401 GVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556268182 478 LLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTNSIKQYYDRKYRIFHEMYQDLMKYR 538
Cdd:TIGR01315 481 LHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDPAKKLHDRKYEIFLQLARTQQEYR 541
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
2-538 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 662.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 2 ASYFIGVDVGTGSARAGIFDL-TGRMVGLATRDIEMYR------PKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVK 74
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAaDGEELASAVHPYPRWViglylpPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 75 GIGFDAT-CSLVVLDKDGHPLTVSP--SGRSEQNIIVWMDHRAISQAERIN----ATHHRVLDYVGGTISPEMQTPKLLW 147
Cdd:COG1069 81 GIGVDATgCTPVPVDADGTPLALLPefAENPHAMVILWKDHTAQEEAERINelakARGEDYLRYVGGIISSEWFWPKILH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 148 LKQHMPNTWANAGFFFDLPDFLTWRATQDDTRSLCSTVCKWTFMGQEDSW-DASYFRTIGLedLLHHDAEKIGRYVRMMG 226
Cdd:COG1069 161 LLREDPEVYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAHEGGYpSEEFFAALDP--LLDGLADRLGTEIYPLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 227 EPLGHgLTSGAAREMGLIPGTSVSVSIIDGHAGALGILGACgvsgevadfNRRVALIGGTSTGHMAMSPEPRFINGIWGP 306
Cdd:COG1069 239 EPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVE---------PGTLVKVMGTSTCHMLVSPEERFVPGICGQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 307 YYSAILPAYWLNEGGQSATGALIDHVIQSHPCYDMLLTQGKTAGKTIYQVLNELLrtmagepESIAFLTKDIHVLPYFHG 386
Cdd:COG1069 309 VDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLTEEA-------AKLPPGESGLHALDWFNG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 387 NRSPRANPTLTGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGG-TKNPVFVQEHANATG 465
Cdd:COG1069 382 NRSPLADQRLKGVILGLTLGTDAEDI---YRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIaTKNPLVMQIYADVTG 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556268182 466 CAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMGAMSR-IGKTVTPQTNsIKQYYDRKYRIFHEMYQDLMKYR 538
Cdd:COG1069 459 RPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSgFDKVYTPDPE-NVAVYDALYAEYLQLHDYFGRGR 531
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-533 |
0e+00 |
|
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: 656.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLT-GRMVGLATRDIEMYR-PKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDAT 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYaGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 82 CSLVVLDKDGHPLTVSPSGRSEQNIIVWMDHRAISQAERINAT-HHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAG 160
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQcPQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDKHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 161 FFFDLPDFLTWRATQDDTRSLCSTVCKWTFMGQEDSWDASYFRTIGLEDLlHHDAEKIGRYVRMMGEPLGHGLtSGAARE 240
Cdd:cd07768 161 HIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 241 MGLIPGTSVSVSIIDGHAGALGILGAcgvsgevaDFNRRVALIGGTSTGHMAMSPEPRFINGIWGPYYSAILPAYWLNEG 320
Cdd:cd07768 239 MGLHPGTAVVVSCIDAHASWFAVASP--------HLETSLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 321 GQSATGALIDHVIQSHPCYDMLLtQGKTAGKTIYQVLNELLRTMAGEPesiaFLTKDIHVLPYFHGNRSPRANPTLTGAI 400
Cdd:cd07768 311 GQSATGKLIEHLFESHPCARKFD-EALKKGADIYQVLEQTIRQIEKNN----GLSIHILTLDMFFGNRSEFADPRLKGSF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 401 TGLKLSRTPEDMALQYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLG 480
Cdd:cd07768 386 IGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILG 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 556268182 481 SAMMGTVAAGV---YESLTEAMGAMSRIGKTVTPQTNSIKQYYDRKYRIFHEMYQD 533
Cdd:cd07768 466 AAVLAKVAAGKkqlADSITEADISNDRKSETFEPLAYRLGADYILLYKLLCVKYHI 521
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-531 |
5.42e-156 |
|
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: 455.07 E-value: 5.42e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDL-TGRMVGLATRDIE--MYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDA 80
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLaDGEELASAVVPYPtgYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 81 TCS-LVVLDKDGHPLTvspsgrseqNIIVWMDHRAISQAERINATHHRV----LDYVGGTISPEMQTPKLLWLKQHMPNT 155
Cdd:cd07781 81 TSStVVPVDEDGNPLA---------PAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 156 WANAGFFFDLPDFLTWRATQDDTRSLCSTVCKWTFMGQEDSWDASYFRTIGLEDLLHHDaeKIGRYVRMMGEPLGHgLTS 235
Cdd:cd07781 152 YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGLLKLRE--KLPGEVVPVGEPAGT-LTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 236 GAAREMGLIPGTSVSVSIIDGHAGALGilgaCGVSGEvadfnRRVALIGGTSTGHMAMSPEPRFINGIWGPYYSAILPAY 315
Cdd:cd07781 229 EAAERLGLPAGIPVAQGGIDAHMGAIG----AGVVEP-----GTLALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 316 WLNEGGQSATGALIDHVIqshpcyDMLLTQGKTAGKTIYQVLNEllrtmagEPESIAFLTKDIHVLPYFHGNRSPRANPT 395
Cdd:cd07781 300 YGLEAGQSAVGDIFAWFV------RLFVPPAEERGDSIYALLSE-------EAAKLPPGESGLVALDWFNGNRTPLVDPR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 396 LTGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGT-KNPVFVQEHANATGCAMLLPEES 474
Cdd:cd07781 367 LRGAIVGLTLGTTPAHI---YRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSD 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 556268182 475 EAMLLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTNSiKQYYDRKYRIFHEMY 531
Cdd:cd07781 444 QAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPEN-HAVYEELYALYKELY 499
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
4-534 |
5.92e-104 |
|
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: 321.40 E-value: 5.92e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDAT-C 82
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQmH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLTvspsgrseqNIIVWMDHRAISQAERINATH--HRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAG 160
Cdd:COG1070 82 GLVLLDADGEPLR---------PAILWNDTRAAAEAAELREELgeEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 161 FFFDLPDFLTWRATQD--DTRSLCStvckWTFMG--QEDSWDASYFRTIGLedllhhDAEKIGRyVRMMGEPLGHgLTSG 236
Cdd:COG1070 153 KVLLPKDYLRYRLTGEfvTDYSDAS----GTGLLdvRTRDWSDELLEALGI------DRELLPE-LVPPGEVAGT-LTAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 237 AAREMGLIPGTSVSVSIIDGHAGALGilgacgvSGEVADfnRRVALIGGTSTGHMAMSPEPRFINGIWGPYYSAILPAYW 316
Cdd:COG1070 221 AAAETGLPAGTPVVAGAGDNAAAALG-------AGAVEP--GDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 317 LNEGGQSATGALIDHVIQshpcydmLLTQGktaGKTIYQVLNELLRTMAGEPESIAFLtkdihvlPYFHGNRSPRANPTL 396
Cdd:COG1070 292 LPMGATNNGGSALRWFRD-------LFADG---ELDDYEELNALAAEVPPGADGLLFL-------PYLSGERTPHWDPNA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 397 TGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEA 476
Cdd:COG1070 355 RGAFFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEG 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 556268182 477 MLLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTnSIKQYYDRKYRIFHEMYQDL 534
Cdd:COG1070 432 GALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDP-ENVAAYDELYERYRELYPAL 488
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-529 |
1.33e-84 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 272.49 E-value: 1.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 1 MASYFIGVDVGTGSARAGIFDL-TGRMVG-------LATRDIEMYRPKADFVEQSSDNIwQCVCNAVRDAMSQADINPIQ 72
Cdd:PRK04123 1 MMAYVIGLDFGTDSVRALLVDCaTGEELAtavveypHWVKGRYLDLPPNQALQHPLDYI-ESLEAAIPAVLKEAGVDPAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 73 VKGIGFDAT-CSLVVLDKDGHPLTVSPSGRSEQN--IIVWMDHRAISQAERINATHHR-----VLDYVGGTISPEMQTPK 144
Cdd:PRK04123 80 VVGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 145 LLWLKQHMPNTWANAGFFFDLPDFLTWRAT-----QDDTRSLCSTVCKWTFmgqEDSWD----ASYFRTI--GLEDLLhh 213
Cdd:PRK04123 160 ILHVLREDPAVYEAAASWVEACDWVVALLTgttdpQDIVRSRCAAGHKALW---HESWGglpsADFFDALdpLLARGL-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 214 dAEKIGRYVRMMGEPLGHgLTSGAAREMGLIPGTSVSVSIIDGHAGALGILgacgvsgevADFNRRVALIGgTSTGHMAM 293
Cdd:PRK04123 235 -RDKLFTETWTAGEPAGT-LTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAG---------AEPGTLVKVMG-TSTCDILL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 294 SPEPRFINGIWGPYYSAILPAYWLNEGGQSATG----ALIDHVIQSHpcydmLLTQGKTAGKTIYQVLNELLrtmagepE 369
Cdd:PRK04123 303 ADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGdifaWFARLLVPPE-----YKDEAEARGKQLLELLTEAA-------A 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 370 SIAFLTKDIHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGG 449
Cdd:PRK04123 371 KQPPGEHGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 450 -GTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMGAM-SRIGKTVTPQTNSIKQY---YDRkY 524
Cdd:PRK04123 448 iARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYeqlYQE-Y 526
|
....*
gi 556268182 525 RIFHE 529
Cdd:PRK04123 527 KQLHD 531
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
4-527 |
6.41e-84 |
|
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: 269.00 E-value: 6.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDAT-C 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQmQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLTvspsgrseqNIIVWMDHRAISQAERINATHHRVLDY---VGGTISPEMQTPKLLWLKQHMPNTWANA 159
Cdd:cd07805 81 GVVPVDKDGNPLR---------NAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEIYAKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 160 GFFFDLPDFLTWR-----ATQDDTRSLcstvckwTFMG--QEDSWDASYFRTIGLedllhhDAEKIGRyVRMMGEPLGHg 232
Cdd:cd07805 152 HKFLDAKDYLNFRltgraATDPSTAST-------TGLMdlRKRRWSEELLRAAGI------DPDKLPE-LVPSTEVVGE- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 233 LTSGAAREMGLIPGTSVSVSIIDGHAGALGilgacgvSGEVADFNRRVALigGTStGHMAM-SPEPRFI--NGIwGPYYS 309
Cdd:cd07805 217 LTPEAAAELGLPAGTPVVGGGGDAAAAALG-------AGAVEEGDAHIYL--GTS-GWVAAhVPKPKTDpdHGI-FTLAS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 310 AIlPAYWLNEGGQSATGALIDHVIQshpcydmLLTQGKTAGKTIYQVLNELLRTMAGEPESIAFltkdihvLPYFHGNRS 389
Cdd:cd07805 286 AD-PGRYLLAAEQETAGGALEWARD-------NLGGDEDLGADDYELLDELAAEAPPGSNGLLF-------LPWLNGERS 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 390 PRANPTLTGAITGLKLSRTPEDMAlqyLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAML 469
Cdd:cd07805 351 PVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVE 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 556268182 470 LPEES-EAMLLGSAMMGTVAAGVYESLTEAmGAMSRIGKTVTPQtNSIKQYYDRKYRIF 527
Cdd:cd07805 428 VPENPqEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPD-PENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-519 |
2.26e-77 |
|
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: 250.13 E-value: 2.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDAT-C 82
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLTvspsgrseqNIIVWMDHRaisqaerinaTHHrvldyvggtispemqtpkllwlkqhmpntwanagfF 162
Cdd:cd07779 81 TFVPVDEDGRPLR---------PAISWQDKR----------TAK-----------------------------------F 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 163 FDLPDFLTWRATQD---DTRSLCSTvcKWTFMGQEDsWDASYFRTIGLedllhhDAEKIGRyVRMMGEPLGHgLTSGAAR 239
Cdd:cd07779 107 LTVQDYLLYRLTGEfvtDTTSASRT--GLPDIRTRD-WSDDLLDAFGI------DRDKLPE-LVPPGTVIGT-LTKEAAE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 240 EMGLIPGTSVSVSIIDGHAGALGilgaCGVSGEvadfnRRVALIGGTSTGHMAMSPEPRFINGIWGPYYSAILPAYWLNE 319
Cdd:cd07779 176 ETGLPEGTPVVAGGGDQQCAALG----AGVLEP-----GTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 320 GGQSATGALIDHVIqshpcyDML---LTQGKTAGKTIYQVLNELLrtmagepESIAFLTKDIHVLPYFHGNRSPRANPTL 396
Cdd:cd07779 247 GSINTGGSAVRWFR------DEFgqdEVAEKELGVSPYELLNEEA-------AKSPPGSDGLLFLPYLAGAGTPYWNPEA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 397 TGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEA 476
Cdd:cd07779 314 RGAFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEA 390
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 556268182 477 MLLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTNSIKQY 519
Cdd:cd07779 391 TALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-458 |
1.77e-76 |
|
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: 251.17 E-value: 1.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 5 FIGVDVGTGSARAGIFDLTGRMVGLATRDI--EMYRPKADFVEQSSDNIWqcvcNAVRDAMSQADINPIQ--VKGIGFDA 80
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIW----KAIKTALKELIEELSDyiVSGIGVSA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 81 TCSLVVL---DKDGH--PLTVSP-SGRSEQNIIVWMDHRAISQAERIN-ATHHRVLDYVGGTISPEMQTPKLLWLKQHMP 153
Cdd:cd07778 78 TCSMVVMqrdSDTSYlvPYNVIHeKSNPDQDIIFWMDHRASEETQWLNnILPDDILDYLGGGFIPEMAIPKLKYLIDLIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 154 NTWANAGFFFDLPDFLTWRatqddtrsLCSTVCKW----------TFMGQEDS---WDASYFRTIGLEDLLHHDAEKIGR 220
Cdd:cd07778 158 EDTFKKLEVFDLHDWISYM--------LATNLGHSnivpvnappsIGIGIDGSlkgWSKDFYSKLKISTKVCNVGNTFKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 221 YVRMM--GEPLGHgLTSGAAREMGLIPGTSVSVSIIDGHAGALGilgacgVSGEVADFNRRVALIGGTSTGHMAMSPEP- 297
Cdd:cd07778 230 APPLPyaGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFS------TFAAAKTLDTTLFMVAGTSTCFLYATSSSq 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 298 -RFINGIWGPYySAILPAYWLNEGGQSATGALIDHVIQSHPCYDMLLTQGKTAGKTIYQVLNELLRTMAgepESIAFLTK 376
Cdd:cd07778 303 vGPIPGIWGPF-DQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDANFFETVEEKIDKYERLLG---QSIHYLTR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 377 DIHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMALQYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVF 456
Cdd:cd07778 379 HMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARL 458
|
..
gi 556268182 457 VQ 458
Cdd:cd07778 459 LQ 460
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-490 |
7.29e-75 |
|
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: 244.36 E-value: 7.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDA-TC 82
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGlVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLtvspsgrseQNIIVWMDHRAISQAERINAT--HHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAG 160
Cdd:cd07804 81 ALVPVDENGKPL---------RPAILYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 161 FFFDLPDFLTWRAT----QDDTRSLCSTVCkwtFMGQEDSWDASYFRTIGLedllhhDAEKIGRyVRMMGEPLGHgLTSG 236
Cdd:cd07804 152 KFLGAYDYIVYKLTgeyvIDYSSAGNEGGL---FDIRKRTWDEELLEALGI------DPDLLPE-LVPSTEIVGE-VTKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 237 AAREMGLIPGTSVSVSIIDGHAGALgilgACGV--SGEVAdfnrrVALigGTSTGHMAMSPEPRFINGIWGPYYSaiLPA 314
Cdd:cd07804 221 AAEETGLAEGTPVVAGTVDAAASAL----SAGVvePGDLL-----LML--GTAGDIGVVTDKLPTDPRLWLDYHD--IPG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 315 YWLNEGGQSATGALIDHVIQShpCYDMLLTQGKTAGKTIYQVLNEllrtmagEPESIAFLTKDIHVLPYFHGNRSPRANP 394
Cdd:cd07804 288 TYVLNGGMATSGSLLRWFRDE--FAGEEVEAEKSGGDSAYDLLDE-------EAEKIPPGSDGLIVLPYFMGERTPIWDP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 395 TLTGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEES 474
Cdd:cd07804 359 DARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDT 435
|
490
....*....|....*.
gi 556268182 475 EAMLLGSAMMGTVAAG 490
Cdd:cd07804 436 VGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-531 |
1.51e-73 |
|
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: 241.67 E-value: 1.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDA-TC 82
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLtvspsgRseqNIIVWMDHRAISQAERINATH-HRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAGF 161
Cdd:cd07808 81 GLVLLDKNGRPL------R---PAILWNDQRSAAECEELEARLgDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 162 FFdLP-DFLTWRATQD--------------DTRSLCstvckwtfmgqedsWDASYFRTIGL-EDLL---HHDAEKIGRyv 222
Cdd:cd07808 152 IL-LPkDYLRYRLTGElatdpsdasgtllfDVEKRE--------------WSEELLEALGLdPSILppiVESTEIVGT-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 223 rmmgeplghgLTSGAAREMGLIPGTSVSVSIIDGHAGALGilgaCGV--SGEVAdfnrrVALigGTSTGHMAMSPEPRFI 300
Cdd:cd07808 215 ----------LTPEAAEELGLPEGTPVVAGAGDNAAAALG----AGVvePGDAL-----ISL--GTSGVVFAPTDKPVPD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 301 --NGIWgpYYSAILPAYWLNEGG-QSATGALiDHViqshpcYDMLLTQGKTagktiYQVLNELLRTMAGEPESIAFltkd 377
Cdd:cd07808 274 pkGRLH--TFPHAVPGKWYAMGVtLSAGLSL-RWL------RDLFGPDRES-----FDELDAEAAKVPPGSEGLLF---- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 378 ihvLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMAlqyLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFV 457
Cdd:cd07808 336 ---LPYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWR 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556268182 458 QEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTNSiKQYYDRKYRIFHEMY 531
Cdd:cd07808 410 QILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPER-HEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-490 |
5.56e-73 |
|
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: 238.99 E-value: 5.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDAT-C 82
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLtvspsgrseQNIIVWMDHRAISQAERINA--THHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAG 160
Cdd:cd07802 81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 161 FFFDLPDFLTWRATqdDTRSLCSTVCKWTFMGQED-SWDASYFRTIGLEDL------LHHDAEKIGRyvrmmgeplghgL 233
Cdd:cd07802 152 TVLFCKDWIRYRLT--GEISTDYTDAGSSLLDLDTgEYDDELLDLLGIEELkdklppLVPSTEIAGR------------V 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 234 TSGAAREMGLIPGTSVSVSIIDGHAGALGilgaCGVSGEvadfnRRVALIGGTSTGHMAMSPEPRFINGIWGpYYSAILP 313
Cdd:cd07802 218 TAEAAALTGLPEGTPVAAGAFDVVASALG----AGAVDE-----GQLCVILGTWSINEVVTDEPVVPDSVGS-NSLHADP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 314 AYWLNEGGQSATGALIDHVIqshpcyDMLLTQGKTAGKTIYQVLNELLRTMAGEPESIAFltkdihvLPYFHGnrsPRAN 393
Cdd:cd07802 288 GLYLIVEASPTSASNLDWFL------DTLLGEEKEAGGSDYDELDELIAAVPPGSSGVIF-------LPYLYG---SGAN 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 394 PTLTGAITGLKLSRTPEDMAlqyLATIQAIALGTRHIIETMNQSGySIDTIMATGGGTKNPVFVQEHANATGCAMLLPEE 473
Cdd:cd07802 352 PNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVAR-KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDG 427
|
490
....*....|....*..
gi 556268182 474 SEAMLLGSAMMGTVAAG 490
Cdd:cd07802 428 EELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
4-490 |
5.82e-71 |
|
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: 234.02 E-value: 5.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQAdiNPIQVKGIGFdAT-- 81
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA--GPDPIAAISV-SSqg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 82 CSLVVLDKDGHPLTvspsgrseqNIIVWMDHRAISQAERINATHH--RVLDYVGGTISPeMQT-PKLLWLKQHMPNTWAN 158
Cdd:cd07773 78 ESGVPVDRDGEPLG---------PAIVWFDPRGKEEAEELAERIGaeELYRITGLPPSP-MYSlAKLLWLREHEPEIFAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 159 AGFFFDLPDFLTWR----ATQDDT---RSLCstvckwtFMGQEDSWDASyfrtigLEDLLHHDAEKIGRyVRMMGEPLGH 231
Cdd:cd07773 148 AAKWLSVADYIAYRltgePVTDYSlasRTML-------FDIRKRTWSEE------LLEAAGIDASLLPE-LVPSGTVIGT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 232 gLTSGAAREMGLIPGTSVSVSIIDGHAGALGilgaCGV--SGEVADfnrrvalIGGTSTGHMAMSPEPRFINGIWGPYYS 309
Cdd:cd07773 214 -VTPEAAEELGLPAGTPVVVGGHDHLCAALG----AGViePGDVLD-------STGTAEALLAVVDEPPLDEMLAEGGLS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 310 ---AILPAYWLNEGGQSAtGALIDHVIqshpcyDMLLtqgktAGKTIYQVLNELLRTMAGEPESIAFLtkdihvlPYFHG 386
Cdd:cd07773 282 yghHVPGGYYYLAGSLPG-GALLEWFR------DLFG-----GDESDLAAADELAEAAPPGPTGLLFL-------PHLSG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 387 NRSPRANPTLTGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGC 466
Cdd:cd07773 343 SGTPDFDPDARGAFLGLTLGTTRADL---LRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGR 419
|
490 500
....*....|....*....|....
gi 556268182 467 AMLLPEESEAMLLGSAMMGTVAAG 490
Cdd:cd07773 420 PIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-485 |
3.27e-69 |
|
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: 227.83 E-value: 3.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDAT-C 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLTvspsgrseqNIIVWMDHRaisqaerinathHRVLdyvggtispemqtpkllwlkqhMPNTWANAgff 162
Cdd:cd00366 81 GVVLVDADGNPLR---------PAIIWLDRR------------AKFL----------------------QPNDYIVF--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 163 fdlpdFLTWRATQDDTRSLCSTVCKWtfmgQEDSWDASYFRTIGLedllhhDAEKIGRyVRMMGEPLGHgLTSGAAREMG 242
Cdd:cd00366 115 -----RLTGEFAIDYSNASGTGLYDI----KTGDWSEELLDALGI------PREKLPP-IVESGEVVGR-VTPEAAEETG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 243 LIPGTSVSVSIIDGHAGALGilgaCGVSGEvadfnRRVALIGGTSTGHMAMSPEPRFINGIWGPYYSAIlPAYWLNEGGQ 322
Cdd:cd00366 178 LPAGTPVVAGGGDTAAAALG----AGVVEP-----GDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHVV-PGLWLLEGAI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 323 SATGALIDHVIqshpcyDMLltqgktAGKTIYQVLNELLRTMAGEPESIA----FltkdihvLPYFHGNRSPRANPTLTG 398
Cdd:cd00366 248 NTGGASLRWFR------DEF------GEEEDSDAEYEGLDELAAEVPPGSdgliF-------LPYLSGERSPIWDPAARG 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 399 AITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAML 478
Cdd:cd00366 309 VFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAA 385
|
....*..
gi 556268182 479 LGSAMMG 485
Cdd:cd00366 386 LGAAILA 392
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-531 |
3.80e-68 |
|
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: 227.44 E-value: 3.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINpiQVKGIGFDATC- 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFSSAMh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLTvspsgrseqNIIVWMDHRAISQAERINATH--HRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAG 160
Cdd:cd07770 79 SLLGVDEDGEPLT---------PVITWADTRAAEEAERLRKEGdgSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 161 FFFDLPDFLTWRATQD---DTrSLCStvckWT-FMGQED-SWDasyfrtiglEDLLHH---DAEKIGRyVRMMGEPLGhG 232
Cdd:cd07770 150 KFVSIKEYLLYRLTGElvtDY-STAS----GTgLLNIHTlDWD---------EEALELlgiDEEQLPE-LVDPTEVLP-G 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 233 LTSGAAREMGLIPGTSVSVSIIDGhagALGILGACGVSGevadfnRRVALIGGTStGHM-AMSPEPRfIN---GIWgPYY 308
Cdd:cd07770 214 LKPEFAERLGLLAGTPVVLGASDG---ALANLGSGALDP------GRAALTVGTS-GAIrVVSDRPV-LDppgRLW-CYR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 309 saILPAYWL-----NEGGqsatgALIDHVIqshpcyDMLLTQGktagkTIYQVLNELLRTMAGEPESIAFLtkdihvlPY 383
Cdd:cd07770 282 --LDENRWLvggaiNNGG-----NVLDWLR------DTLLLSG-----DDYEELDKLAEAVPPGSHGLIFL-------PY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 384 FHGNRSPRANPTLTGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANA 463
Cdd:cd07770 337 LAGERAPGWNPDARGAFFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556268182 464 TGCAMLLPEESEAMLLGSAMMGTVAAGVYESLteAMGAMSRIGKTVTPQTNSiKQYYDRKYRIFHEMY 531
Cdd:cd07770 414 LGRPVLVPEEEEASALGAALLALEALGLISSL--EADELVKIGKVVEPDPEN-HAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
4-489 |
4.87e-62 |
|
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: 209.77 E-value: 4.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINpiQVKGIGFDATC- 82
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTSg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLTvspsgrseqNIIVWMDHRAISQAERINATHHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAGFF 162
Cdd:cd07783 79 TLVLVDREGEPLR---------PAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 163 FDLPDFLTWRATQDDTRSLCSTVCKWTFMGQEDSWDAsyfrtiGLEDLLHHDAEKIGRyVRMMGEPLGHgLTSGAAREMG 242
Cdd:cd07783 150 LHQADWLAGRLTGDRGVTDYNNALKLGYDPETGRWPS------WLLALLGIPPDLLPR-VVAPGTVIGT-LTAEAAEELG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 243 LIPGTSVSVSIIDGHAGALGiLGACGVsGEVADfnrrvalIGGTSTGHMAMSPEPRFINGiwGPYYSAILPA-YWLNEGG 321
Cdd:cd07783 222 LPAGTPVVAGTTDSIAAFLA-SGAVRP-GDAVT-------SLGTTLVLKLLSDKRVPDPG--GGVYSHRHGDgYWLVGGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 322 QSATGALIDHVIQSHPcydmlltqgktagktiyqvLNELLRTMAGEPESiafltkDIHVLPY-FHGNRSPRANPTLTGAI 400
Cdd:cd07783 291 SNTGGAVLRWFFSDDE-------------------LAELSAQADPPGPS------GLIYYPLpLRGERFPFWDPDARGFL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 401 TGLKLSRtpEDMalqYLATIQAIALGTRHIIETMNQSGYS-IDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAmLL 479
Cdd:cd07783 346 LPRPHDR--AEF---LRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA-AL 419
|
490
....*....|
gi 556268182 480 GSAMMGTVAA 489
Cdd:cd07783 420 GAALLAAAGL 429
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
280-489 |
1.34e-55 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 185.22 E-value: 1.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 280 VALIGGTSTGHMAMSPEP-RFINGIWGPYYSAILPAYWLNEGGQSATGALIDHVIQSHPCYDMLLTQGKTagktiyqvlN 358
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAGNV---------E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 359 ELLRTMAGEPESIAFLtkdIHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQS- 437
Cdd:pfam02782 72 SLAELAALAAVAPAGG---LLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHL---YRAILESLALQLRQILEALTKQe 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556268182 438 GYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAA 489
Cdd:pfam02782 146 GHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
4-490 |
5.02e-40 |
|
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: 150.85 E-value: 5.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDAT-- 81
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 82 -CSLVvlDKDGHPLtvspsgrseQNIIVWMDHRAISQAERINA--THHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWAN 158
Cdd:cd24121 81 gTWLV--DEDGRPV---------RDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 159 AGFFFDLPDF----LTWRATQDDTRSLcstvckWTFMG-QEDSWDASYFRTIGLEDLLH-----HDAEKIGRYvrmmgep 228
Cdd:cd24121 150 ARTALHCKDWlfykLTGEIATDPSDAS------LTFLDfRTRQYDDEVLDLLGLEELRHllppiRPGTEVIGP------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 229 lghgLTSGAAREMGLIPGTSVSVSIIDGHAGALGilgaCGVsgevadFNRRVAL-IGGTSTGHMAMSPEPRfINGIWGPY 307
Cdd:cd24121 217 ----LTPEAAAATGLPAGTPVVLGPFDVVATALG----SGA------IEPGDACsILGTTGVHEVVVDEPD-LEPEGVGY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 308 YSAI-LPAYWLNEGGQSATGALIDHVIQShpCYDMLLTQGKTAGKTIYQVLNELLRtmAGEPESIAFLtkdihVLPYFH- 385
Cdd:cd24121 282 TICLgVPGRWLRAMANMAGTPNLDWFLRE--LGEVLKEGAEPAGSDLFQDLEELAA--SSPPGAEGVL-----YHPYLSp 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 386 -GNRSPRANPTLTGAITGLKLSRTPEDMAlqyLATIQAIALGTRHIIETMnqsGYSIDTIMATGGGTKNPVFVQEHANAT 464
Cdd:cd24121 353 aGERAPFVNPNARAQFTGLSLEHTRADLL---RAVYEGVALAMRDCYEHM---GEDPGELRLSGGGARSDTWCQILADAL 426
|
490 500
....*....|....*....|....*.
gi 556268182 465 GCAMLLPEESEAMLLGSAMMGTVAAG 490
Cdd:cd24121 427 GVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-490 |
5.49e-39 |
|
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: 148.14 E-value: 5.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADF--VEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIgfdAT 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPdaKEFDPEELWEKICEAIREALKKAGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 82 CS----LVVLDKDGHPLTVSPsgrseqNIivwmDHRAISQAERINATHHRVLDYVGGTISPEMQTP-KLLWLKQHMPNTW 156
Cdd:cd07798 78 TSqregIVFLDKDGRELYAGP------NI----DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEIF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 157 ANAGFFFDLPDFLTWR----ATQDDTrSLCST----VCKwtfmgqeDSWDASYFRTIGLEDLLHHDaekigryVRMMGEP 228
Cdd:cd07798 148 ERIATVLSISDWIGYRltgeLVSEPS-QASETqlfdIKK-------REWSQELLEALGLPPEILPE-------IVPSGTV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 229 LGhGLTSGAAREMGLIPGTSVSVSIIDGHAGALGilgaCGVSgEVADfnrrVALIGGTSTGHMAMSPEPRFI--NGIW-G 305
Cdd:cd07798 213 LG-TVSEEAARELGLPEGTPVVVGGADTQCALLG----SGAI-EPGD----IGIVAGTTTPVQMVTDEPIIDpeRRLWtG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 306 PYysaILPAYWLNEGGQSATGALIDHVIqshpcyDMLLtqgkTAGKTIYQVLNELLRT-MAGEPESIAFLTKDIhvlpyf 384
Cdd:cd07798 283 CH---LVPGKWVLESNAGVTGLNYQWLK------ELLY----GDPEDSYEVLEEEASEiPPGANGVLAFLGPQI------ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 385 hgnrsprANPTLTGAITGLKLSRTP--------EDMAlqyLATIQAIALGTRHIIETMNQ-SGYSIDTIMATGGGTKNPV 455
Cdd:cd07798 344 -------FDARLSGLKNGGFLFPTPlsaseltrGDFA---RAILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSAL 413
|
490 500 510
....*....|....*....|....*....|....*
gi 556268182 456 FVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAG 490
Cdd:cd07798 414 LCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-490 |
1.24e-37 |
|
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: 144.23 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDL-TGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDATC 82
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAeTGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 -SLVVLDKDGHPLtvSPSgrseqniIVWMDHRAISQAERI-NATHHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAG 160
Cdd:cd07809 81 hGLVALDADGKVL--RPA-------KLWCDTRTAPEAEELtEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 161 FFFDLPDFLTWRATQDdtrslcstvckwTFMGQEDS----WDASYFRTIGlEDLLHHDAEKIGRY-----VRMMGEPLGH 231
Cdd:cd07809 152 KILLPHDYLNWKLTGE------------KVTGLGDAsgtfPIDPRTRDYD-AELLAAIDPSRDLRdllpeVLPAGEVAGR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 232 gLTSGAAREMGLIPGTSVSVSIIDGHAGALGilgacgvSGEVADfnRRVALIGGTSTGHMAMSPEPRF-----INGiwgp 306
Cdd:cd07809 219 -LTPEGAEELGLPAGIPVAPGEGDNMTGALG-------TGVVNP--GTVAVSLGTSGTAYGVSDKPVSdphgrVAT---- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 307 yysailPAywlneggqSATGALIdHVIQSHPCYDMLLTQGKTAGKTIYQVLNELLRTMAGEPESIAFltkdihvLPYFHG 386
Cdd:cd07809 285 ------FC--------DSTGGML-PLINTTNCLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLL-------LPFLNG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 387 NRSPRaNPTLTGAITGLKLSR-TPEDMAlqyLATIQAIALGTRHIIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATG 465
Cdd:cd07809 343 ERTPN-LPHGRASLVGLTLSNfTRANLA---RAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFG 418
|
490 500
....*....|....*....|....*
gi 556268182 466 CAMLLPEESEAMLLGSAMMGTVAAG 490
Cdd:cd07809 419 VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-525 |
7.30e-36 |
|
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: 140.16 E-value: 7.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRdiEMYRPKADFVEQSSD----NIWQCVCNAVRDAMSQADINPIQVKGIgfd 79
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQR--EWRHKEVPDVPGSMDfdteKNWKLICECIREALKKAGIAPKSIAAI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 80 ATCS----LVVLDKDGHPLtvspsgrseqniivW----MDHRAISQAERINATHHrvldyvggTISPEM-----QT---- 142
Cdd:cd07775 76 STTSmregIVLYDNEGEEI--------------WacanVDARAAEEVSELKELYN--------TLEEEVyrisgQTfalg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 143 --PKLLWLKQHMPNTWANAGFFFDLPDFLTWRATQD---DTrSLCSTVCkwTFMGQEDSWDASYFRTIGLEDLLHHDaek 217
Cdd:cd07775 134 aiPRLLWLKNNRPEIYRKAAKITMLSDWIAYKLSGElavEP-SNGSTTG--LFDLKTRDWDPEILEMAGLKADILPP--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 218 igryVRMMGEPLGHgLTSGAAREMGLIPGTSVSVSIIDGHAGALGIlgacGVSGEvadfnRRVALIGGTSTGHMAMSPEP 297
Cdd:cd07775 208 ----VVESGTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL----GVVRP-----GQTAVLGGSFWQQEVNTAAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 298 RF-------INgiwgpyySAILPAYWLNEGGQSATGALIDHVIQSHPCYDMLLTqgKTAGKTIYQVLNELLRTM-AGEPE 369
Cdd:cd07775 274 VTdpamnirVN-------CHVIPDMWQAEGISFFPGLVMRWFRDAFCAEEKEIA--ERLGIDAYDLLEEMAKDVpPGSYG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 370 SIAFLTKDIHVLPYFHgnrsprANPTLTG-AITGLKLSRtpedmALQYLATIQAIALGTRHIIETM-NQSGYSIDTIMAT 447
Cdd:cd07775 345 IMPIFSDVMNYKNWRH------AAPSFLNlDIDPEKCNK-----ATFFRAIMENAAIVSAGNLERIaEFSGIFPDSLVFA 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556268182 448 GGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTNSiKQYYDRKYR 525
Cdd:cd07775 414 GGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPEN-HEVYQDLYE 490
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-262 |
3.38e-33 |
|
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: 126.68 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFDATC- 82
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 SLVVLDKDGHPLTvspsgrseqNIIVWMDHRAISQAERINA--THHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAG 160
Cdd:pfam00370 81 GTVLLDKNDKPLY---------NAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 161 FFFDLPDFLTWRATQDDT--RSLCSTVcKWTFMGQEDsWDASYFRTIGL-EDLL---HHDAEKIGRyvrmmgeplghgLT 234
Cdd:pfam00370 152 KFLTIHDYLRWRLTGVFVtdHTNASRS-MMFNIHKLD-WDPELLAALGIpRDHLpplVESSEIYGE------------LN 217
|
250 260
....*....|....*....|....*...
gi 556268182 235 SGAAREMGLIPGTSVSVSIIDGHAGALG 262
Cdd:pfam00370 218 PELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
4-522 |
1.66e-29 |
|
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: 121.42 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFdaTC- 82
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGI--TNq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 --SLVVLDKD-GHPLTvspsgrseqNIIVWMDHRAISQAERINATHH--RVLDYVGGTISPEMQTPKLLWLKQHMPN--- 154
Cdd:cd07769 79 reTTVVWDKKtGKPLY---------NAIVWQDRRTADICEELKAKGLeeRIREKTGLPLDPYFSATKIKWILDNVPGare 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 155 -------------TWanagfffdlpdfLTWRATQD----------------DTRSLCstvckwtfmgqedsWDasyfrti 205
Cdd:cd07769 150 raergellfgtidTW------------LIWKLTGGkvhvtdvtnasrtmlfNIHTLE--------------WD------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 206 glEDLLhhdaEKIGRYVRMMGEPLGHGLTSGAAREMGLIPGTSVSVSIIDGHAgALgiLG-ACGVSGEV-ADFnrrvali 283
Cdd:cd07769 197 --DELL----ELFGIPRSMLPEVRPSSEVFGYTDPEGLGAGIPIAGILGDQQA-AL--FGqGCFEPGMAkNTY------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 284 gGT------STGHMAMSPEPRFINGI-WG----PYYsAIlpaywlnEGGQSATGALIdhviqshpcydmlltqgktagkt 352
Cdd:cd07769 261 -GTgcfllmNTGEKPVPSKNGLLTTIaWQiggkVTY-AL-------EGSIFIAGAAI----------------------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 353 iyQVLNELLRTM--AGEPESIAFLTKD---IHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMAlqyLATIQAIALGT 427
Cdd:cd07769 309 --QWLRDNLGLIedAAETEELARSVEDnggVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQT 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 428 RHIIETMNQ-SGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLtEAMGAMSRIG 506
Cdd:cd07769 384 RDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDL-DELASLWQVD 462
|
570
....*....|....*...
gi 556268182 507 KTVTPQ--TNSIKQYYDR 522
Cdd:cd07769 463 KRFEPSmdEEERERLYRG 480
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-525 |
5.33e-29 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 120.17 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 1 MASYFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFD- 79
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 80 --ATCslVVLDKD-GHPLTvspsgrseqNIIVWMDHRAISQAERINATHH--RVLDYVGGTISPEMQTPKLLWLKQHMPN 154
Cdd:COG0554 81 qrETT--VVWDRKtGKPLY---------NAIVWQDRRTADICEELKADGLedLIREKTGLVLDPYFSATKIKWILDNVPG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 155 TW--ANAG-FFFDLPD-FLTWRATQ------DDT----------RSLCstvckwtfmgqedsWDasyfrtiglEDLLhhD 214
Cdd:COG0554 150 ARerAEAGeLLFGTIDsWLIWKLTGgkvhvtDVTnasrtmlfniHTLD--------------WD---------DELL--E 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 215 AEKI------------GRYVRMMGEPLGHGltsgaaremglIPgtsVSVSIIDGHAGALGIlgACGVSGEV--------- 273
Cdd:COG0554 205 LFGIprsmlpevrpssEVFGETDPDLFGAE-----------IP---IAGIAGDQQAALFGQ--ACFEPGMAkntygtgcf 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 274 ADFNrrvaliggtsTGHMAMSPEPRFINGI-WG----PYYsAIlpaywlnEGGQSATGALID------HVIQShpcydml 342
Cdd:COG0554 269 LLMN----------TGDEPVRSKNGLLTTIaWGlggkVTY-AL-------EGSIFVAGAAVQwlrdglGLIDS------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 343 ltqgktagktiyqvlnellrtmAGEPESIAFLTKD---IHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMAlqyLAT 419
Cdd:COG0554 324 ----------------------AAESEALARSVEDnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA---RAA 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 420 IQAIALGTRHIIETMNQ-SGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEa 498
Cdd:COG0554 379 LESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEE- 457
|
570 580
....*....|....*....|....*..
gi 556268182 499 MGAMSRIGKTVTPQTNsiKQYYDRKYR 525
Cdd:COG0554 458 LAALWKVDRRFEPQMD--EEERERLYA 482
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-525 |
2.36e-27 |
|
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: 115.35 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFdAT-- 81
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 82 CSLVVLDKD-GHPLTvspsgrseqNIIVWMDHRAISQAERINA-THHRVLDYVGG-----------------TISPEMQT 142
Cdd:cd07793 80 NTFLTWDKKtGKPLH---------NFITWQDLRAAELCESWNRsLLLKALRGGSKflhfltrnkrflaasvlKFSTAHVS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 143 PKLLWLKQHMPN----------------TWanagfffdlpdfLTWRATQD-----DTRSLCSTVCKWTFMGQEDSWDASY 201
Cdd:cd07793 151 IRLLWILQNNPElkeaaekgellfgtidTW------------LLWKLTGGkvhatDYSNASATGLFDPFTLEWSPILLSL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 202 FRtIGLEDLLHhdaekigryVRMMGEPLGHGLTS--GAAremglIPGTSVsvsIIDGHAgalGILGACGVS-GEVadfnr 278
Cdd:cd07793 219 FG-IPSSILPE---------VKDTSGDFGSTDPSifGAE-----IPITAV---VADQQA---ALFGECCFDkGDV----- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 279 RVALigGTSTghmamspeprFINgiwgpyysailpaywLNEGGQ---SATGA--LIDHVIQSHPCYdMLLTQGKTAGKTI 353
Cdd:cd07793 273 KITM--GTGT----------FID---------------INTGSKphaSVKGLypLVGWKIGGEITY-LAEGNASDTGTVI 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 354 yqvlnELLRTMAG-----EPESIAFLTKD---IHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMAlqyLATIQAIAL 425
Cdd:cd07793 325 -----DWAKSIGLfddpsETEDIAESVEDtngVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLV---RAILESIAF 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 426 GTRHIIETM-NQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMgAMSR 504
Cdd:cd07793 397 RVKQLLETMeKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELK-KLRK 475
|
570 580
....*....|....*....|.
gi 556268182 505 IGKTVTPQTNSIKqyYDRKYR 525
Cdd:cd07793 476 IEKIFEPKMDNEK--REELYK 494
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-533 |
2.61e-26 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 112.41 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 1 MASYFIGVDVGTGSARAGIFDLTGRMVGLATRdiEMYRPKADFVEQSSD----NIWQCVCNAVRDAMSQADINPIQVKGI 76
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQA--EWRHLAVPDVPGSMEfdleKNWQLACQCIRQALQKAGIPASDIAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 77 gfdATCSL----VVLDKDGHPLtvspsgrseqniivW----MDHRAISQA----ERINATHHRVLDYVGGTISPEmQTPK 144
Cdd:PRK10939 79 ---SATSMregiVLYDRNGTEI--------------WacanVDARASREVselkELHNNFEEEVYRCSGQTLALG-ALPR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 145 LLWLKQHMPNTWANAGFFFDLPDFLTWRAT---QDDTRSLCSTvckWTFMGQEDSWDASYFRTIGLEDllhhdaeKIGRY 221
Cdd:PRK10939 141 LLWLAHHRPDIYRQAHTITMISDWIAYMLSgelAVDPSNAGTT---GLLDLVTRDWDPALLEMAGLRA-------DILPP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 222 VRMMGEPLGHgLTSGAAREMGLIPGTSVSVSIIDGHAGALGI----LGACGVSGevADFNRRVALIGGTSTG-HMAMSPE 296
Cdd:PRK10939 211 VKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDVQLGCLGLgvvrPGQTAVLG--GTFWQQVVNLPAPVTDpNMNIRIN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 297 PRFINGIWgpYYSAI-----LPAYWLNEggqsATGALidhviqshpcyDMLLTQGKtaGKTIYQVLNEL-LRTMAGEPES 370
Cdd:PRK10939 288 PHVIPGMV--QAESIsfftgLTMRWFRD----AFCAE-----------EKLLAERL--GIDAYSLLEEMaSRVPVGSHGI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 371 IAFLTKDIHVLPYFHgnrsprANPTLtgaitgLKLSRTPED-------MALQYLATIqaIALGTRHIIEtmNQSGYSIDT 443
Cdd:PRK10939 349 IPIFSDVMRFKSWYH------AAPSF------INLSIDPEKcnkatlfRALEENAAI--VSACNLQQIA--AFSGVFPSS 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 444 IMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTNSiKQYYDRK 523
Cdd:PRK10939 413 LVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPEN-HELYQEA 491
|
570
....*....|
gi 556268182 524 YRIFHEMYQD 533
Cdd:PRK10939 492 KEKWQAVYAD 501
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
4-512 |
7.24e-21 |
|
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: 95.64 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGFD---A 80
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITnqrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 81 TCslVVLDKD-GHPLTvspsgrseqNIIVWMDHRAISQAERINATHHR---------VLD-YVGGTispemqtpKLLWLK 149
Cdd:cd07786 81 TT--VVWDREtGKPVY---------NAIVWQDRRTADICEELKAEGHEemirektglVLDpYFSAT--------KIRWIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 150 QHMPNTW--ANAG--FFFDLPDFLTWRATQ------DDT---RSLcstvckwTFMGQEDSWDasyfrtiglEDLLhhdae 216
Cdd:cd07786 142 DNVPGARerAERGelAFGTIDSWLIWKLTGgkvhatDVTnasRTM-------LFNIHTLEWD---------DELL----- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 217 kigryvRMMGEPlghgltsgaareMGLIPGTSVSVSIIdGHAGAlGILGA----CGVSGEvadfnRRVALIG-------- 284
Cdd:cd07786 201 ------ELFGIP------------ASMLPEVKPSSEVF-GYTDP-DLLGAeipiAGIAGD-----QQAALFGqacfepgm 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 285 -----GTS------TGHMAMSPEPRFINGIwgpyysailpAYWLN-------EGGQSATGALID------HVIQShpcyd 340
Cdd:cd07786 256 akntyGTGcfmlmnTGEKPVRSKNGLLTTI----------AWQLGgkvtyalEGSIFIAGAAVQwlrdglGLIES----- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 341 mlltqgktagktiyqvlnellrtmAGEPESIAFLTKD---IHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMAlqyL 417
Cdd:cd07786 321 ------------------------AAETEALARSVPDnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA---R 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 418 ATIQAIALGTRHIIETMNQ-SGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLT 496
Cdd:cd07786 374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453
|
570
....*....|....*.
gi 556268182 497 EAmGAMSRIGKTVTPQ 512
Cdd:cd07786 454 EL-AKLWQVDRRFEPS 468
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-518 |
6.81e-20 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 92.73 E-value: 6.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 3 SYFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQadinpIQVKGIGFDATC 82
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKK-----LREKGPSFKIKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 83 --------SLVVLDKD-GHPLtvspsgrseQNIIVWMDHRAISQAERINATHHRVLDY---VGGTISPEMQTPKLLWLKQ 150
Cdd:PTZ00294 77 igitnqreTVVAWDKVtGKPL---------YNAIVWLDTRTYDIVNELTKKYGGSNFFqkiTGLPISTYFSAFKIRWMLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 151 HMPntwanagfffdlpdfltwrATQDDTRSlcSTVCkwtfMGQEDSW----------------DASyfRTIgLEDLlhhd 214
Cdd:PTZ00294 148 NVP-------------------AVKDAVKE--GTLL----FGTIDTWliwnltggkshvtdvtNAS--RTF-LMNI---- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 215 aeKIGRYVRMMGEPLGhgltsgaaremglIPGTSVSVsiidghagalgILGACGVSGEVAdfNRRVALIGGTStghmams 294
Cdd:PTZ00294 196 --KTLKWDEELLNKFG-------------IPKETLPE-----------IKSSSENFGTIS--GEAVPLLEGVP------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 295 peprfINGIWGPYYSAILPAYWLNEGGQS---ATGALI------DHVIQSH-----PCYdmlltQGKTAGKTIY------ 354
Cdd:PTZ00294 241 -----ITGCIGDQQAALIGHGCFEKGDAKntyGTGCFLlmntgtEIVFSKHgllttVCY-----QLGPNGPTVYalegsi 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 355 ----QVLNELLRTM-----AGEPESIAFLTKD---IHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMALqylATIQA 422
Cdd:PTZ00294 311 avagAGVEWLRDNMglishPSEIEKLARSVKDtggVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVR---AALEA 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 423 IALGTRHIIETMNQ-SGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMGA 501
Cdd:PTZ00294 388 IALQTNDVIESMEKdAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKL 467
|
570
....*....|....*..
gi 556268182 502 MSRIGKTVTPQTNSIKQ 518
Cdd:PTZ00294 468 IRRSNSTFSPQMSAEER 484
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-512 |
3.11e-18 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 87.57 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 1 MASYFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIGF-- 78
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGItn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 79 --DATcslVVLDKD-GHPLtvspsgrseQNIIVWMDHRAISQAERINATHH--RVLDYVGGTISPEMQTPKLLWLKQHMP 153
Cdd:PRK00047 83 qrETT---VVWDKEtGRPI---------YNAIVWQDRRTADICEELKRDGYedYIREKTGLVIDPYFSGTKIKWILDNVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 154 NTW--ANAG-FFFDLPD-FLTWRATQ------DDT---RSLcstvckwtFMGQED-SWDasyfrtiglEDLLhhDAEKIG 219
Cdd:PRK00047 151 GARerAEKGeLLFGTIDtWLVWKLTGgkvhvtDYTnasRTM--------LFNIHTlDWD---------DELL--ELLDIP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 220 RY----VRMMGEPLGHGLTSGAAremglipGTSVSVSiidghagalGILG---------ACGVSGEVADfnrrvalIGGT 286
Cdd:PRK00047 212 RSmlpeVRPSSEVYGKTNPYGFF-------GGEVPIA---------GIAGdqqaalfgqLCFEPGMAKN-------TYGT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 287 ------STGHMAMSPEprfiNGI-----WGPYYSailPAYWLnEGGQSATGALIdhviqshpcydmlltqgktagktiyQ 355
Cdd:PRK00047 269 gcfmlmNTGEKAVKSE----NGLlttiaWGIDGK---VVYAL-EGSIFVAGSAI-------------------------Q 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 356 VLNELLRTMAGEPESIAFLTK-----DIHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMAlqyLATIQAIALGTRHI 430
Cdd:PRK00047 316 WLRDGLKIISDASDSEALARKvedndGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHII---RATLESIAYQTRDV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 431 IETMNQ-SGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEaMGAMSRIGKTV 509
Cdd:PRK00047 393 LDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDE-LKEQWKIDRRF 471
|
...
gi 556268182 510 TPQ 512
Cdd:PRK00047 472 EPQ 474
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-484 |
4.60e-18 |
|
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: 86.51 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARAGIFDL-TGRMVGLATRDIEMYRPKAD--FVEQSSDNIWQCVCNAVRDAMSQADINpiqVKGIGFda 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLeSGRILESVSRPTPAPISSDDpgRSEQDPEKILEAVRNLIDELPREYLSD---VTGIGI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 81 TC---SLVVLDKDGHPLTvspsgrseqNIIVWMDHRAISQ-AERINATHHRVLDYVGGTISPEMQTPKLLWLKQHMPNTw 156
Cdd:cd07777 76 TGqmhGIVLWDEDGNPVS---------PLITWQDQRCSEEfLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGPLP- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 157 ANAGFFFDLPDFLTWRATQDDtrslcSTVCKWTF---MG----QEDSWDASYFRTIGLEDLLH----HDAEKIGRYVRMM 225
Cdd:cd07777 146 SKADRAGTIGDYIVARLTGLP-----KPVMHPTNaasWGlfdlETGTWNKDLLEALGLPVILLpeivPSGEIVGTLSSAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 226 GEplghgltsgaaremglipGTSVSVSIIDgHagalgilgACGVSGEVADFNRRVALIGGTStGHMAMSPEPRFINGIW- 304
Cdd:cd07777 221 PK------------------GIPVYVALGD-N--------QASVLGSGLNEENDAVLNIGTG-AQLSFLTPKFELSGSVe 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 305 -----GPYYSAILPAywLNeGGQSatgalidhviqshpcYDML---LTQ------GKTAGKTIYQVLNELLRtmagepes 370
Cdd:cd07777 273 irpffDGRYLLVAAS--LP-GGRA---------------LAVLvdfLREwlrelgGSLSDDEIWEKLDELAE-------- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 371 iAFLTKDIHVLPYFHGNRSpraNPTLTGAITGLKLS-RTPEDMAlqyLATIQAIALGTRHIIETMNQSGYSIDTIMATGG 449
Cdd:cd07777 327 -SEESSDLSVDPTFFGERH---DPEGRGSITNIGESnFTLGNLF---RALCRGIAENLHEMLPRLDLDLSGIERIVGSGG 399
|
490 500 510
....*....|....*....|....*....|....*.
gi 556268182 450 G-TKNPVFVQEHANATGCAMLLPEESEAMLLGSAMM 484
Cdd:cd07777 400 AlRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALL 435
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-525 |
1.25e-17 |
|
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: 85.65 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 5 FIG-VDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQA---DINPIQVKGIGFda 80
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLkalGISPSDIKAIGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 81 TC---SLVVLDKD-GHPLTvspsgrseqNIIVWMDHRAISQAERINATHHRVLDYV----GGTISPEMQTPKLLWLKQHM 152
Cdd:cd07792 80 TNqreTTVVWDKStGKPLY---------NAIVWLDTRTSDTVEELSAKTPGGKDHFrkktGLPISTYFSAVKLRWLLDNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 153 PNTwanagfffdlpdfltwRATQDDTRSLCSTVckwtfmgqeDSW-------------------DASyfRTIgLEDL--L 211
Cdd:cd07792 151 PEV----------------KKAVDDGRLLFGTV---------DSWliwnltggknggvhvtdvtNAS--RTM-LMNLrtL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 212 HHDAE-------------KIgryvRMMGEPLGHgLTSGAaremglIPGTSVSVSIIDGHAgalgilgacgvsgevadfnr 278
Cdd:cd07792 203 QWDPElceffgipmsilpEI----RSSSEVYGK-IASGP------LAGVPISGCLGDQQA-------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 279 rvALIggtstGHMAMSPeprfingiwgpyysailpaywlnegGQS----ATGALI------DHVIQSH-----PCYDMll 343
Cdd:cd07792 252 --ALV-----GQGCFKP-------------------------GEAkntyGTGCFLlyntgeEPVFSKHgllttVAYKL-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 344 tqGKTAgKTIY----------QVLNELLRTM-----AGEPESIAFLTKD---IHVLPYFHGNRSPRANPTLTGAITGLKL 405
Cdd:cd07792 298 --GPDA-PPVYalegsiaiagAAVQWLRDNLgiissASEVETLAASVPDtggVYFVPAFSGLFAPYWRPDARGTIVGLTQ 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 406 SRTPEDMAlqyLATIQAIALGTRHIIETMNQ-SGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMM 484
Cdd:cd07792 375 FTTKAHIA---RAALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIA 451
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 556268182 485 GTVAAGVYESLTEAMGAMSRIGKTVTPQTNSIKqyYDRKYR 525
Cdd:cd07792 452 AGLAVGVWKSLDELKSLNEGGRTVFEPQISEEE--RERRYK 490
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
9-515 |
1.31e-16 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 82.38 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 9 DVGTGSARAGIFDLTGRMVGLAT------RDIEmyrpKADFVEQSSDNIWQ----CvCNAVRDAMSQADINPIQVKGIGF 78
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARAStpnasdIAAE----NSDWHQWSLDAILQrfadC-CRQINSELTECHIRGITVTTFGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 79 DATcslvVLDKDGHPLTvsPsgrseqnIIVWMDHRAISqaerinathhrVLDYVGGTISPE-MQTP------------KL 145
Cdd:PRK10331 83 DGA----LVDKQGNLLY--P-------IISWKCPRTAA-----------VMENIERYISAQqLQQIsgvgafsfntlyKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 146 LWLKQHMPNTWANAGFFFDLPDFLTWRATQDDT--RSLCSTvckwTFMG--QEDSWDASYFRTIGL-EDLLHHdaekigr 220
Cdd:PRK10331 139 VWLKENHPQLLEQAHAWLFISSLINHRLTGEFTtdITMAGT----SQMLdiQQRDFSPEILQATGLsRRLFPR------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 221 yVRMMGEPLGHgLTSGAAREMGLIPGTSVsvsIIDGHAGALGILGacgvSGevADFNRRVaLIGGTSTGHMAMSPEPrfi 300
Cdd:PRK10331 208 -LVEAGEQIGT-LQPSAAALLGLPVGIPV---ISAGHDTQFALFG----SG--AGQNQPV-LSSGTWEILMVRSAQV--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 301 NGIWGPYYSAI------LPAYwLNEGGQSATGALIDHVIQshpcydMLLTQGktagkTIYQvlnellrTMAGEPESIAFL 374
Cdd:PRK10331 273 DTSLLSQYAGStceldsQSGL-YNPGMQWLASGVLEWVRK------LFWTAE-----TPYQ-------TMIEEARAIPPG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 375 TKDIHVLPYFHGNRspranptlTGAITGLKLSRTPEDMalqYLATIQAIALGTRHIIETMNQ-SGYSIDTIMATGGGTKN 453
Cdd:PRK10331 334 ADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHF---YRAALEGLTAQLKRNLQVLEKiGHFKASELLLVGGGSRN 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556268182 454 PVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTNS 515
Cdd:PRK10331 403 ALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYPQTEP 464
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-535 |
1.22e-13 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 73.08 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 5 FIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIWQCVCNAVRDAMSQADINPIQVKGIG---FDAT 81
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAgqmHGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 82 cslvVLDKDGHPLtvSPSgrseqniIVWMDHRAISQAERINATHHRVLDYVGGTISPEMQTPKLLWLKQHMPNTWANAGF 161
Cdd:PRK15027 82 ----LLDAQQRVL--RPA-------ILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 162 FFDLPDFLTWRATQD---DTRSLCSTVckWTFMGQEDSWDAsyfrtigLEDLLHHDAEKIGRYVRmmGEPLGHGLTSGAA 238
Cdd:PRK15027 149 VLLPKDYLRLRMTGEfasDMSDAAGTM--WLDVAKRDWSDV-------MLQACHLSRDQMPALYE--GSEITGALLPEVA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 239 REMGLiPGTSVSVSIIDGHAGALGIlgacgvsgEVADFNRRVaLIGGTSTGHMAMSpeprfiNGIWGPYYSAI------L 312
Cdd:PRK15027 218 KAWGM-ATVPVVAGGGDNAAGAVGV--------GMVDANQAM-LSLGTSGVYFAVS------EGFLSKPESAVhsfchaL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 313 PAYWlneggqsatgALIDHVIQSHPCYDMlltQGKTAGKTIYQVLNELLRTMAGEPESIAFltkdihvLPYFHGNRSPRA 392
Cdd:PRK15027 282 PQRW----------HLMSVMLSAASCLDW---AAKLTGLSNVPALIAAAQQADESAEPVWF-------LPYLSGERTPHN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 393 NPTLTGAITGLKLSRTPEDMALQYLATI-QAIALGtrhiIETMNQSGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLP 471
Cdd:PRK15027 342 NPQAKGVFFGLTHQHGPNELARAVLEGVgYALADG----MDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYR 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556268182 472 EESE-AMLLGSAMMGTVAAGVYESLTEAMGAMSrIGKTVTPQTNSIKQYYDRKyRIFHEMYQDLM 535
Cdd:PRK15027 418 TGGDvGPALGAARLAQIAANPEKSLIELLPQLP-LEQSHLPDAQRYAAYQPRR-ETFRRLYQQLL 480
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
5-514 |
1.88e-09 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 60.10 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 5 FIG-VDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQSSDNIW----QCVCNAVRDAMSQADINPIQVKGIGFD 79
Cdd:PLN02295 1 FVGaIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILesvlTCIAKALEKAAAKGHNVDSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 80 ATCSLVVL--DKDGHPLtvspsgrseQNIIVWMDHRAISQAERINATHH----RVLDYVGGTISPEMQTPKLLWLKQHMP 153
Cdd:PLN02295 81 NQRETTVAwsKSTGRPL---------YNAIVWMDSRTSSICRRLEKELSggrkHFVETCGLPISTYFSATKLLWLLENVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 154 NTWA----NAGFFFDLPDFLTWRATQDDTRSL----CSTVCKWTFMGQED-SWDASYFRTIGLEdllHHDAEKIGRYVRM 224
Cdd:PLN02295 152 AVKEavksGDALFGTIDSWLIWNLTGGASGGVhvtdVTNASRTMLMNLKTlDWDKPTLEALGIP---AEILPKIVSNSEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 225 MGEpLGHGltsgaaremGLIPGTSVSVSIIDGHAGALGilGACGVsGEVADfnrrvaligGTSTGHMAMspeprfingiw 304
Cdd:PLN02295 229 IGT-IAKG---------WPLAGVPIAGCLGDQHAAMLG--QRCRP-GEAKS---------TYGTGCFIL----------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 305 gpyysailpaywLNEGgqsatgaliDHVIQS-HPcydmLLTQ-----GKT-------------AGKTIyQVLNELLRTM- 364
Cdd:PLN02295 276 ------------LNTG---------EEVVPSkHG----LLTTvayklGPDaptnyalegsvaiAGAAV-QWLRDNLGIIk 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 365 -AGEPESIAFLTKD---IHVLPYFHGNRSPRANPTLTGAITGLKLSRTPEDMAlqyLATIQAIALGTRHIIETMNQ---- 436
Cdd:PLN02295 330 sASEIEALAATVDDtggVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIA---RAVLESMCFQVKDVLDAMRKdage 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 437 --SGYSIDTIMATGGGTKNPVFVQEHANATGCAMLLPEESEAMLLGSAMMGTVAAGVYESLTEAMGAMSRIGKTVTPQTN 514
Cdd:PLN02295 407 ekSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPKLD 486
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-78 |
6.58e-07 |
|
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: 51.05 E-value: 6.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556268182 1 MASYFIGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQssdniwqcVCNAVRDAMSQADINPIQVKGIGF 78
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEA--------IAELIEELLAEAGISRGRILGIGI 72
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
4-498 |
9.46e-07 |
|
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: 51.37 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 4 YFIGVDVGTGSARA--GIFDlTGRmvgLATRdiEMYRPKADFVEQSS------DNIWQCVCNAVRDAMSQADinpiQVKG 75
Cdd:cd07771 1 NYLAVDLGASSGRVilGSLD-GGK---LELE--EIHRFPNRPVEINGhlywdiDRLFDEIKEGLKKAAEQGG----DIDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 76 IGFDAT-CSLVVLDKDGHPLtvspsgrseQNIIVWMDHRaisqaerinatHHRVLDYVGGTISPE---MQT--------- 142
Cdd:cd07771 71 IGIDTWgVDFGLLDKNGELL---------GNPVHYRDPR-----------TEGMMEELFEKISKEelyERTgiqfqpint 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 143 -PKLLWLKQHMPNTWANAGFFFDLPDFLTWRatqddtrsLC-STVCKWTF--------MGQEDsWDASYFRTIGLEDllh 212
Cdd:cd07771 131 lYQLYALKKEGPELLERADKLLMLPDLLNYL--------LTgEKVAEYTIasttqlldPRTKD-WSEELLEKLGLPR--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 213 hdaekigryvRMMGEPLGHG-----LTSGAAREmGLIPGTSVsvsiidgHAGAlgilG---ACGVSGeVADFNRRVALIg 284
Cdd:cd07771 199 ----------DLFPPIVPPGtvlgtLKPEVAEE-LGLKGIPV-------IAVA----ShdtASAVAA-VPAEDEDAAFI- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 285 gtSTGHMAM----SPEPrFINgiwgpyySAILPAYWLNEGGqsatgalIDHVIqshpcydMLLtqgktagKTI--YQVLN 358
Cdd:cd07771 255 --SSGTWSLigveLDEP-VIT-------EEAFEAGFTNEGG-------ADGTI-------RLL-------KNItgLWLLQ 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556268182 359 ELLRTMA--GEPESIAFLTKDIHVLPYFHG----NrSPR-ANPT-LTGAI------TGLKLSRTPEDMALqylATIQAIA 424
Cdd:cd07771 304 ECRREWEeeGKDYSYDELVALAEEAPPFGAfidpD-DPRfLNPGdMPEAIraycreTGQPVPESPGEIAR---CIYESLA 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556268182 425 LGTRHIIETMNQ-SGYSIDTIMATGGGTKNPVFVQEHANATGCAMLL-PeeSEAMLLGSAMMGTVAAGVYESLTEA 498
Cdd:cd07771 380 LKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAgP--VEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
6-77 |
8.94e-04 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 40.91 E-value: 8.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556268182 6 IGVDVGTGSARAGIFDLTGRMVGLATRDIEMYRPKADFVEQssdniwqcVCNAVRDAMSQADINPiQVKGIG 77
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDR--------IAELIEELLAEAGVRE-RILGIG 63
|
|
| |
