|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
357-661 |
0e+00 |
|
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.
Pssm-ID: 466910 [Multi-domain] Cd Length: 305 Bit Score: 571.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 357 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 436
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 516
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 517 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 596
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765945268 597 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 661
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
11-323 |
7.58e-103 |
|
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the combined epimerization and UDP-hydrolysis of UDP-N-acetylglucosamine to N-acetylmannosamine. This is in contrast to the related enzyme WecB (TIGR00236) which retains the UDP moiety. NeuC acts in concert with NeuA and NeuB to synthesize CMP-N5-acetyl-neuraminate.
Pssm-ID: 274654 Cd Length: 364 Bit Score: 317.93 E-value: 7.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDPDL-ELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 91 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 169
Cdd:TIGR03568 80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 170 SMCEDHDRILLAGCPSYDKLLSAK---------------NKDYM------------SIIRMW------------------ 204
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNILSLDllskeeleeklgidlDKPYAlvtfhpvtlekaEAEEQIkellkaldelnkniifty 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 205 ----LGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENV 280
Cdd:TIGR03568 240 pnadAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLRADSV 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1765945268 281 LHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 323
Cdd:TIGR03568 319 IDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIEIL 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
11-324 |
5.73e-83 |
|
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340819 [Multi-domain] Cd Length: 365 Bit Score: 266.38 E-value: 5.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDPGL-ELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 91 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 167
Cdd:cd03786 77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 168 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSII--RMWLGSKEMV---------------------------------- 211
Cdd:cd03786 156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELVlsKLGLLEKKYIlvtlhrrenvdsgerleellealeelaekydliv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 212 ---------RVMRKKGIEH--HPNFRAVKH-VPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIGRETGE 278
Cdd:cd03786 236 vypnhprtrPRIREVGLKFlgGLPNIRLIDpLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTERPERVE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1765945268 279 NVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 324
Cdd:cd03786 315 AGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
358-664 |
3.26e-68 |
|
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: 225.16 E-value: 3.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 435
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 436 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiI----------HQHEL 505
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYL----------TlgtgigggivINGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 506 IHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNA 585
Cdd:COG1940 156 LRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 586 KAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGAAS 660
Cdd:COG1940 223 LALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAA 302
|
....
gi 1765945268 661 MVLD 664
Cdd:COG1940 303 LALE 306
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
37-324 |
2.04e-48 |
|
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.
Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 173.10 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 37 EFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 116
Cdd:pfam02350 6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 117 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLS 191
Cdd:pfam02350 80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 192 AK-------------NKDYM-----------------SIIRMW--LGSKEMVRV---------MRK---KGIEHHPNFRA 227
Cdd:pfam02350 160 SReeieersgilaklGKRYVlvtfhrreneddpealrNILEALraLAERPDVPVvfpvhnnprTRRrlnERLEGYPRVRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 228 VKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKILQALHLQFGK 302
Cdd:pfam02350 240 IEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERIVAALERLLED 314
|
330 340
....*....|....*....|..
gi 1765945268 303 QYPCSKIYGDGNAVPRILKFLK 324
Cdd:pfam02350 315 PASYKNPYGDGNASERIVDILE 336
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
359-618 |
2.17e-35 |
|
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.
Pssm-ID: 395384 [Multi-domain] Cd Length: 292 Bit Score: 135.55 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErinLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVlHS 437
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 438 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 517
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 518 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 597
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260
....*....|....*....|.
gi 1765945268 598 LGLGVVNILHTMNPSLVILSG 618
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGG 241
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
359-618 |
6.88e-35 |
|
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]
Pssm-ID: 273246 [Multi-domain] Cd Length: 318 Bit Score: 135.03 E-value: 6.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHST 438
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 439 KLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 518
Cdd:TIGR00744 81 NL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 519 LVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 597
Cdd:TIGR00744 159 IRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVARW 238
|
250 260
....*....|....*....|.
gi 1765945268 598 LGLGVVNILHTMNPSLVILSG 618
Cdd:TIGR00744 239 AGAGLADLASLFNPSAIVLGG 259
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
24-325 |
4.92e-15 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 77.03 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 24 KLAPIMFGIKTEPEFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 98
Cdd:COG0381 16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 99 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 163
Cdd:COG0381 84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 164 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSII--RMWLGSKEMVRV-------------MR------------- 215
Cdd:COG0381 152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDIleELGLEPKKYILVtlhrrenvddperLEnilealrelaery 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 216 ----------------KKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVINL--GT-RQI 272
Cdd:COG0381 232 dlpvvfpvhprtrkrlEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCLTLrdTTeRPE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1765945268 273 GRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 325
Cdd:COG0381 308 TVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
359-635 |
4.61e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 73.02 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMCVEAAAEAVKlncrilgVGISTGGRVNprEGIVlh 436
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAALAERKfGQGKGLENFVTLITGTGIGGGIIHQHELIHG 508
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQ-ALPDDIRNMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 509 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNAKAQ 588
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1765945268 589 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 635
Cdd:PRK05082 212 ALINRSAQAIARLIADLKATLDCQCVVLGGSvgLAEGYLELVQAYLAQE 260
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
357-661 |
0e+00 |
|
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.
Pssm-ID: 466910 [Multi-domain] Cd Length: 305 Bit Score: 571.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 357 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 436
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 516
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 517 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 596
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765945268 597 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 661
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
11-323 |
7.58e-103 |
|
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the combined epimerization and UDP-hydrolysis of UDP-N-acetylglucosamine to N-acetylmannosamine. This is in contrast to the related enzyme WecB (TIGR00236) which retains the UDP moiety. NeuC acts in concert with NeuA and NeuB to synthesize CMP-N5-acetyl-neuraminate.
Pssm-ID: 274654 Cd Length: 364 Bit Score: 317.93 E-value: 7.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDPDL-ELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 91 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 169
Cdd:TIGR03568 80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 170 SMCEDHDRILLAGCPSYDKLLSAK---------------NKDYM------------SIIRMW------------------ 204
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNILSLDllskeeleeklgidlDKPYAlvtfhpvtlekaEAEEQIkellkaldelnkniifty 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 205 ----LGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENV 280
Cdd:TIGR03568 240 pnadAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLRADSV 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1765945268 281 LHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 323
Cdd:TIGR03568 319 IDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIEIL 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
11-324 |
5.73e-83 |
|
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340819 [Multi-domain] Cd Length: 365 Bit Score: 266.38 E-value: 5.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDPGL-ELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 91 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 167
Cdd:cd03786 77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 168 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSII--RMWLGSKEMV---------------------------------- 211
Cdd:cd03786 156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELVlsKLGLLEKKYIlvtlhrrenvdsgerleellealeelaekydliv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 212 ---------RVMRKKGIEH--HPNFRAVKH-VPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIGRETGE 278
Cdd:cd03786 236 vypnhprtrPRIREVGLKFlgGLPNIRLIDpLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTERPERVE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1765945268 279 NVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 324
Cdd:cd03786 315 AGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
358-664 |
3.26e-68 |
|
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: 225.16 E-value: 3.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 435
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 436 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiI----------HQHEL 505
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYL----------TlgtgigggivINGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 506 IHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNA 585
Cdd:COG1940 156 LRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 586 KAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGAAS 660
Cdd:COG1940 223 LALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAA 302
|
....
gi 1765945268 661 MVLD 664
Cdd:COG1940 303 LALE 306
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
358-664 |
8.66e-57 |
|
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Bacillus subtilis xylose repressor (BsXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. BsXylR acts as transcriptional repressor of xylose-utilizing enzymes.
Pssm-ID: 466926 [Multi-domain] Cd Length: 303 Bit Score: 194.71 E-value: 8.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ-FNPK-TYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 435
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVpLPASdDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 436 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 515
Cdd:cd24076 83 LAPNL--GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 516 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEdlllVEGMSVPKdeavgalhLIQAAKLGNAKAQSILRTAG 595
Cdd:cd24076 161 IGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAG----GEPLSLAE--------LVEAARAGDPAALAALEEVG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765945268 596 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLD 664
Cdd:cd24076 229 EYLGIGLANLVNTFNPELVVLGGALAPlgpWLLPPLRAEVARRALPAPARDVRIVVSRlgEDAAALGAAALAID 302
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
358-618 |
5.28e-54 |
|
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and similar proteins; The family includes Fusobacterium nucleatum N-acetylmannosamine kinase (NanK; EC 2.7.1.60) and beta-glucoside kinase (BglK; EC 2.7.1.85) from Klebsiella pneumoniae and Listeria innocua. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. BglK catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. It may have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. The subfamily belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466918 [Multi-domain] Cd Length: 294 Bit Score: 186.99 E-value: 5.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKY---TQFNpKTYEERINLILQmcveaAAEAVKLNCRILGVGISTGGRVNPREGIV 434
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDsvpTPAS-KGGDAILERLLE-----IIAELKEKYDIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 435 LHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAA 514
Cdd:cd24068 76 IYATDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 515 ELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLlvegmsvpkdeavGALHLIQAAKLGNAKAQSILRTA 594
Cdd:cd24068 156 ELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGI-------------DGREIFDLADAGDPLAKEVVEEF 222
|
250 260
....*....|....*....|....
gi 1765945268 595 GTALGLGVVNILHTMNPSLVILSG 618
Cdd:cd24068 223 AEDLATGLANLVHIFDPEVIVIGG 246
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
358-618 |
4.13e-53 |
|
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; CYANR acts as transcriptional repressor of cyclobis-(1-6)-alpha-nigerosyl (CNN) degrading enzymes. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466923 [Multi-domain] Cd Length: 304 Bit Score: 184.68 E-value: 4.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ-FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 436
Cdd:cd24073 3 VVGVKLTEDRITAVLTDLRGNVLASHTLpLDSGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGICRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 STKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 516
Cdd:cd24073 83 SPLL--GWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 517 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 596
Cdd:cd24073 161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAG------------LRGEPLTIEDLLAAARAGDPAARAILRRAGR 228
|
250 260
....*....|....*....|..
gi 1765945268 597 ALGLGVVNILHTMNPSLVILSG 618
Cdd:cd24073 229 ALGLALANLVNLLDPELIIISG 250
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
358-665 |
8.06e-51 |
|
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to N-acetylglucosamine kinase (Tm1224; EC 2.7.1.59) from Thermotoga maritima, which belongs to kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Tm1224 lacks the cysteine-rich zinc-binding motif, which presents in other family members.
Pssm-ID: 466909 [Multi-domain] Cd Length: 305 Bit Score: 178.55 E-value: 8.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIV--KKYTQFNPKTYEERINLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 435
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILarEKYPLDEKENPEEVLEKLYEL-IDRLLEKENIKSKILGIGIGAPGPLDVEKGIIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 436 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 515
Cdd:cd24059 82 NPPNF-PGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 516 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvEGMSVPKDEavgaLHLIQAAKLGNAKAQSILRTAG 595
Cdd:cd24059 161 IGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARS---------ALGSGRSFQ----LDIVEALQKGDPIADEVIEEAA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765945268 596 TALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLDY 665
Cdd:cd24059 228 KYLGIGLVNLINLLNPEAIIIGGELIylgERYLEPIEKEVNSRLFGRNAREVRILKSSlgEDAPLLGAAALVLNK 302
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
37-324 |
2.04e-48 |
|
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.
Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 173.10 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 37 EFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 116
Cdd:pfam02350 6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 117 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLS 191
Cdd:pfam02350 80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 192 AK-------------NKDYM-----------------SIIRMW--LGSKEMVRV---------MRK---KGIEHHPNFRA 227
Cdd:pfam02350 160 SReeieersgilaklGKRYVlvtfhrreneddpealrNILEALraLAERPDVPVvfpvhnnprTRRrlnERLEGYPRVRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 228 VKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKILQALHLQFGK 302
Cdd:pfam02350 240 IEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERIVAALERLLED 314
|
330 340
....*....|....*....|..
gi 1765945268 303 QYPCSKIYGDGNAVPRILKFLK 324
Cdd:pfam02350 315 PASYKNPYGDGNASERIVDILE 336
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
358-621 |
1.41e-44 |
|
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466911 [Multi-domain] Cd Length: 306 Bit Score: 161.75 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVklncrILGVGISTGGRVNPREGIVLHS 437
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPPTADGIVDAIVEAVEELREGHD-----VSAVGVAAAGFVDADRATVLFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 438 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 517
Cdd:cd24061 76 PNI--AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 518 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDED-----LLLVEGmsvpKDEAVGALHLIQAAKLGNAKAQSILR 592
Cdd:cd24061 154 HIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATpegaaVLLADG----SVDGITGKHISEAARAGDPVALDALR 229
|
250 260
....*....|....*....|....*....
gi 1765945268 593 TAGTALGLGVVNILHTMNPSLVILSGVLA 621
Cdd:cd24061 230 ELARWLGAGLASLAALLDPELFVIGGGVS 258
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
358-618 |
3.58e-44 |
|
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Listeria monocytogenes Lmo0178 protein, which is a predicted transcription repressor belonging to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466921 [Multi-domain] Cd Length: 312 Bit Score: 160.53 E-value: 3.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKyTQF---NPKTYEERINLILQmCVEAAAEAVKLNCRILGVGISTGGRVNPREGIV 434
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEK-TRIpfdHETDPEKVIELIAE-NIKKLIKNKHVEKKLLGIGIAVSGLVDSKKGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 435 LHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAA 514
Cdd:cd24071 81 IRSTIL--GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 515 ELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLvegmSVPKDEAVGALHLIQAAKLGNAKAQSILRTA 594
Cdd:cd24071 159 EIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLS----LLKELEDFEIEKVREAAEEGDSVATELFKKA 234
|
250 260
....*....|....*....|....
gi 1765945268 595 GTALGLGVVNILHTMNPSLVILSG 618
Cdd:cd24071 235 GEYLGIGIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
358-634 |
3.73e-42 |
|
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466913 [Multi-domain] Cd Length: 308 Bit Score: 154.80 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEER--INLILQMCVEAAAEAVKLNcrILGVGISTGGRVNPREGIVL 435
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGtvSEQVLGLIETLLSKAGKDS--IEGIGVSSAGPLDLRKGTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 436 HSTKLIQEWnsVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 515
Cdd:cd24063 80 NSPNIKGKE--IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 516 LGHLVVSLD-GPDCSCGSHGCIEAYASGMALQREAKKL-HDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRT 593
Cdd:cd24063 158 VGHLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWaEGFSSRTSLKLRNPGGEGITAKEVFSAARKGDPLALKIIEK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1765945268 594 AGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 634
Cdd:cd24063 238 LARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEY 278
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
359-634 |
2.41e-40 |
|
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YphH that belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466922 [Multi-domain] Cd Length: 308 Bit Score: 149.87 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKK--YTQFNPKTYEErinlILQMCVEAAAEAVKLNC-RILGVGISTGGRVNPREGIVL 435
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEfeYRVITLETPEA----LIDEIIDCIDRLLKLWKdRVKGIALAIQGLVDSHKGVSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 436 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 515
Cdd:cd24072 80 WSPGA--PWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 516 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAG 595
Cdd:cd24072 158 IGHTKVNPDGARCDCGRRGCLETVASNSALKRNARV------TLKLGPVSADPEKLTMEQLIEALEEGEPIATQIFDRAA 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1765945268 596 TALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 634
Cdd:cd24072 232 NAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRA 270
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
358-618 |
6.25e-39 |
|
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466914 [Multi-domain] Cd Length: 301 Bit Score: 145.72 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYTQfnPKTYEERINLILQMCVEAAAEAVKlNCRILGVGISTGGRVNPREGIVLHS 437
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTI--DTKVENGKEDVINRIAETVNELIE-EMELLGIGIGSPGSIDRENGIVRFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 438 TKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 517
Cdd:cd24064 78 PNF-PDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 518 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDE--DLLlvegmsVPKDEAVGALHLIQAAKLGNAKAQSILRTAG 595
Cdd:cd24064 157 HVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRypDSL------AGESEKINAKHVFDAARKNDPLATMVFRRVV 230
|
250 260
....*....|....*....|...
gi 1765945268 596 TALGLGVVNILHTMNPSLVILSG 618
Cdd:cd24064 231 DALAIAIGGFVHIFNPEIIIIGG 253
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
359-633 |
1.21e-38 |
|
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: 142.99 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 436
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPaeEGPEAVLDRIAEL-IEELLAEAGVRERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 STKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiiH-----------QHEL 505
Cdd:cd23763 80 APNL-PWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYI-----------TlgtgigggiiiDGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 506 IHGSSFCAAELGHLVVsldgpdcscgshgcieayasgmalqreakklhdedlllvegmsvpkdeavgalhliqaaklgna 585
Cdd:cd23763 148 YRGANGAAGEIGHITV---------------------------------------------------------------- 163
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1765945268 586 kaqsiLRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIR 633
Cdd:cd23763 164 -----LEEAARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIRE 206
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
357-635 |
2.28e-37 |
|
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; HK (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). Thermus thermophilus HK possesses significant enzymatic activity against glucose and mannose. However, it shows little catalytic capacity for galactose and fructose. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466915 [Multi-domain] Cd Length: 289 Bit Score: 140.93 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 357 SALAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKlncRILGVGISTGGRVNPREGIVLH 436
Cdd:cd24065 1 STIGLDLGGTKIAAGVVD-GGRILSRLVVPTPREGGEAVLDALARAVEALQAEAP---GVEAVGLGVPGPLDFRRGRVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 STKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 516
Cdd:cd24065 77 APN-IPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 517 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDlllvegMSVPKdeavgalhLIQAAKLGNAKAQSILRTAGT 596
Cdd:cd24065 156 GHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRP------MSTAE--------LFELAQQGEPKALRIVEQAAA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1765945268 597 ALGLGVVNILHTMNPSLVILSGVLASH---YIHIVKDVIRQQ 635
Cdd:cd24065 222 HLGIGLANLQKALDPEVFVLGGGVAQVgdyYLLPVQEAARRY 263
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
359-618 |
2.17e-35 |
|
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.
Pssm-ID: 395384 [Multi-domain] Cd Length: 292 Bit Score: 135.55 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErinLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVlHS 437
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 438 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 517
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 518 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 597
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260
....*....|....*....|.
gi 1765945268 598 LGLGVVNILHTMNPSLVILSG 618
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGG 241
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
359-618 |
6.88e-35 |
|
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]
Pssm-ID: 273246 [Multi-domain] Cd Length: 318 Bit Score: 135.03 E-value: 6.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHST 438
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 439 KLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 518
Cdd:TIGR00744 81 NL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 519 LVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 597
Cdd:TIGR00744 159 IRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVARW 238
|
250 260
....*....|....*....|.
gi 1765945268 598 LGLGVVNILHTMNPSLVILSG 618
Cdd:TIGR00744 239 AGAGLADLASLFNPSAIVLGG 259
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
358-637 |
1.09e-33 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466912 [Multi-domain] Cd Length: 311 Bit Score: 131.26 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT--YEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 435
Cdd:cd24062 2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLegGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 436 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 515
Cdd:cd24062 82 VAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 516 LGHL-VVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTA 594
Cdd:cd24062 160 IGHItVNPEGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAVVDTV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1765945268 595 GTALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQAL 637
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGGGVSaagEFLLSPVKEYFDRFTF 285
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
358-635 |
6.54e-28 |
|
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Staphylococcus aureus xylose repressor (SaXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. SaXylR acts as a transcriptional repressor of xylose-utilizing enzymes. It lacks the cysteine-rich zinc-binding motif, which presents in other family members.
Pssm-ID: 466927 [Multi-domain] Cd Length: 295 Bit Score: 114.17 E-value: 6.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKKYT-QFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREgiVLH 436
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQiKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVDENE--IIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 STKliQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKglENFVTLITgtgigggiiH---------QHELIH 507
Cdd:cd24077 81 TPY--YDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSEDY--DNLISISI---------HsgigagiiiNNQLYR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 508 GSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDedlllVEGMSVPkdeavgalHLIQAAKLGNAKA 587
Cdd:cd24077 148 GYNGFAGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKKG-----LETLTFD--------DLIQLYNEGDPEA 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1765945268 588 QSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDvIRQQ 635
Cdd:cd24077 215 LELIDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELLEK-IKEQ 261
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
359-618 |
1.79e-25 |
|
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This subfamily is composed of uncharacterized proteins belonging to the the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466988 [Multi-domain] Cd Length: 286 Bit Score: 106.88 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEERINLILQMcveaaaeAVKLNCRILGVGISTGGRVNPREGIVLHS 437
Cdd:cd24152 3 LVFDIGGTFIKYALVDENGNIIKKGKIPTPKdSLEEFLDYIKKI-------IKRYDEEIDGIAISAPGVIDPETGIIYGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 438 TKLiqEWNS-VDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 516
Cdd:cd24152 76 GAL--PYLKgFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 517 GHLVVSLDGPDCSCGSHgcieaYASGMALQREAKKLHDedlllvegmsvpkDEAVGALHLIQAAKLGNAKAQSILRTAGT 596
Cdd:cd24152 154 SYLLTDDDDKDLLFFSG-----LASMFGLVKRYNKAKG-------------LEPLDGEEIFEKYAKGDEAAKKILDEYIR 215
|
250 260
....*....|....*....|..
gi 1765945268 597 ALGLGVVNILHTMNPSLVILSG 618
Cdd:cd24152 216 NLAKLIYNIQYILDPEVIVIGG 237
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
358-637 |
3.28e-25 |
|
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as a repressor of the nagEBACD operon involved in the uptake and degradation of the amino sugars, N-acetyl-D-glucosamine (GlcNAc) and glucosamine (GlcN). It acts both as an activator and a repressor for the transcription of the glmSU operon, encoding proteins necessary for the synthesis of GlcN (glmS) and the formation of UDP-GlcNAc (glmU). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466925 [Multi-domain] Cd Length: 315 Bit Score: 106.68 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIVKK----YTQFNPKTYEERInlilqmcVEAAAEAVKLNCR----ILGVGISTGGRVNP 429
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAEhtvpLTALNQEALLSQL-------IEEIAQFLKSHRRktqrLIAISITLPGLINP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 430 REGIVlHSTKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGS 509
Cdd:cd24075 76 KTGVV-HYMPHIQ-VKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 510 SFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDllLVEGMSvPKDEAVGAlhLIQAAKLGNAKAQS 589
Cdd:cd24075 154 NGNAGEIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQG--YASQLT-LQDCTIKD--ICQAALNGDQLAQD 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1765945268 590 ILRTAGTALGLGVVNILHTMNPSLVILSG--VLASHYIH-IVKDVIRQQAL 637
Cdd:cd24075 229 VIKRAGRYLGKVIAILINLLNPQKIIIAGeiTQADKVLLpVIKKCIQSQAL 279
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
415-637 |
4.33e-21 |
|
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466924 [Multi-domain] Cd Length: 322 Bit Score: 94.69 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 415 RILGVGISTGGRVNPREGIVLHSTKL-IQEWnsvdlrtPLSDTLH----LPVWVDNDGNCAALAERKFGQGKGLENFVTL 489
Cdd:cd24074 62 RLTAIAITLPGIIDPESGIVHRLPFYdIKNL-------PLGEALEqhtgLPVYVQHDISAWTLAERFFGAAKGAKNIIQI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 490 ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKL---HDEDLLLVEGMSVP 566
Cdd:cd24074 135 VIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLleqSPDSMLHGQPISIE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765945268 567 kdeavgalHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVL---ASHYIHIVKDVIRQQAL 637
Cdd:cd24074 215 --------SLCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLnnaAEILFPALSQSIRQQSL 280
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
360-621 |
1.83e-20 |
|
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called GlcNAc kinase, catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466907 [Multi-domain] Cd Length: 298 Bit Score: 92.30 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 360 AVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT-YEERINLILQMCVEAAAEAvklNCRiLGVGISTGGRVNPREGIVLhsT 438
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDdYAAFLAAIAELVAEADARF---GVK-GPVGIGIPGVIDPEDGTLI--T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 439 KLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 518
Cdd:cd24057 78 ANIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 519 LVVSLD----GPD-----CSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNAKAQS 589
Cdd:cd24057 158 GPLPADalllGYDlpvlrCGCGQTGCLETYLSGRGLERLYAHLYGEEL--------------DAPEIIAAWAAGDPQAVA 223
|
250 260 270
....*....|....*....|....*....|..
gi 1765945268 590 ILRTAGTALGLGVVNILHTMNPSLVILSGVLA 621
Cdd:cd24057 224 HVDRWLDLLAGCLANILTALDPDVVVLGGGLS 255
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
359-629 |
8.40e-20 |
|
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar proteins; N-acetylmannosamine kinase (NanK; EC 2.7.1.60), also called ManNAc kinase, or N-acetyl-D-mannosamine kinase, catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. It has also low level glucokinase activity in vitro. This subfamily also contains Brucella melitensis bifunctional enzyme NanE/NanK (EC 5.1.3.9/EC 2.7.1.60), which also converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466919 [Multi-domain] Cd Length: 283 Bit Score: 90.04 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEerinliLQMCVEAAAE-AVKLNCRILGVGISTGGRVnpREGIVLH- 436
Cdd:cd24069 1 LAIDIGGTKIAAALIG-NGQIIDRRQIPTPRSGT------PEALADALASlLADYQGQFDRVAVASTGII--RDGVLTAl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 516
Cdd:cd24069 72 NPKNLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 517 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAkklhdedlllvegmSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 596
Cdd:cd24069 152 GHTLADPPGPVCGCGRRGCVEAIASGTAIAAAA--------------SEILGEPVDAKDVFERARSGDEEAARLIDRAAR 217
|
250 260 270
....*....|....*....|....*....|....*
gi 1765945268 597 ALGLGVVNILHTMNPSLVILSGV--LASHYIHIVK 629
Cdd:cd24069 218 ALADLIADLKATLDLDCVVIGGSvgLAEGFLERVE 252
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
359-618 |
4.45e-19 |
|
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; Escherichia coli FRK (EC 2.7.1.4), also called D-fructose kinase, manno(fructo)kinase, or MAK, catalyzes the phosphorylation of fructose to fructose-6-phosphate. It has also low level glucokinase activity in vitro. It is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466916 [Multi-domain] Cd Length: 294 Bit Score: 88.03 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEERINLILQMcVEAAAEAVKLNCRilgVGISTGGRVNPREGIVLHS 437
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRgDYEATLDAIADL-VEEAEEELGAPAT---VGIGTPGSISPRTGLVKNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 438 tkliqewNSV-----DLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFC 512
Cdd:cd24066 78 -------NSTwlngkPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 513 AAELGHLVV------SLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNAK 586
Cdd:cd24066 151 AGEWGHNPLpwpdedELPGPPCYCGKRGCVETFLSGPALERDYARLTGKTL--------------SAEEIVALARAGDAA 216
|
250 260 270
....*....|....*....|....*....|..
gi 1765945268 587 AQSILRTAGTALGLGVVNILHTMNPSLVILSG 618
Cdd:cd24066 217 AVATLDRFLDRLGRALANVINILDPDVIVLGG 248
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
359-551 |
5.74e-19 |
|
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1.55), also called allokinase, catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. It has also low level glucokinase activity in vitro. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466920 [Multi-domain] Cd Length: 293 Bit Score: 87.99 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIV---KKYTQfNPKTYEERINLILQMcVEAAAEAVKLNCRilGVGISTGGRVNPREGIVL 435
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLdfeKVPSK-DLLRAGDPVEVLADL-IREYIEEAGLKPA--AIVIGVPGTVDKDRRTVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 436 HSTKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQ------------GKGLENFVTLItgtgigggiihqH 503
Cdd:cd24070 80 STPN-IPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNlddegvvlgfyiGTGIGNAILIN------------G 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1765945268 504 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 551
Cdd:cd24070 147 KPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEE 194
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
24-325 |
4.92e-15 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 77.03 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 24 KLAPIMFGIKTEPEFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 98
Cdd:COG0381 16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 99 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 163
Cdd:COG0381 84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 164 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSII--RMWLGSKEMVRV-------------MR------------- 215
Cdd:COG0381 152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDIleELGLEPKKYILVtlhrrenvddperLEnilealrelaery 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 216 ----------------KKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVINL--GT-RQI 272
Cdd:COG0381 232 dlpvvfpvhprtrkrlEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCLTLrdTTeRPE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1765945268 273 GRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 325
Cdd:COG0381 308 TVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
360-556 |
3.22e-14 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; Bacillus subtilis FRK (EC 2.7.1.4), also called glucomannan utilization protein E, catalyzes the phosphorylation of fructose to fructose-6-P. It seems to be involved in the degradation of glucomannan. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466917 [Multi-domain] Cd Length: 285 Bit Score: 73.73 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 360 AVDLGGTNLRVAIVSMKGEIVKKyTQFNPKTYEErinlILQMCVEAAAEAVKlncRILGVGISTGGRVNPRE-----GIV 434
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIER-TEFPTTTPEE----TLQAVIDFFREQEE---PIDAIGIASFGPIDLNPtsptyGYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 435 LHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFcaA 514
Cdd:cd24067 75 TTTPKP--GWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLH--P 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1765945268 515 ELGHLVVSLDGPDC----SCGSHG-CIEAYASGMAL----QREAKKLHDED 556
Cdd:cd24067 151 EMGHIRVPRHPDDDgfpgVCPFHGdCLEGLASGPAIaarwGIPAEELPDDH 201
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
359-635 |
4.61e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 73.02 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMCVEAAAEAVKlncrilgVGISTGGRVNprEGIVlh 436
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAALAERKfGQGKGLENFVTLITGTGIGGGIIHQHELIHG 508
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQ-ALPDDIRNMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 509 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNAKAQ 588
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1765945268 589 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 635
Cdd:PRK05082 212 ALINRSAQAIARLIADLKATLDCQCVVLGGSvgLAEGYLELVQAYLAQE 260
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
10-324 |
2.84e-10 |
|
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 272978 Cd Length: 365 Bit Score: 62.47 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 10 LRVCVATCNRADYSKLAPIMFGIKTEPeFFELDVVVLGSHliddygntYRMIEQ--DDFDINTRlHTIVRGEDEAAMVES 87
Cdd:TIGR00236 1 LKVMIVLGTRPEAIKMAPLIRALKKYP-EIDSYVIVTAQH--------REMLDQvlDLFHLPPD-YDLNIMSPGQTLGEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 88 VGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSI-----RHAITKLAHYHVCCTR 162
Cdd:TIGR00236 71 TSNMLEGLEELLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMpeeinRQLTGHIADLHFAPTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 163 SAEQHLISMCEDHDRILLAGCPSYDKLLS----AKNKDYMSII----RMWL-----------GSKEMVRVMRKKGIEH-- 221
Cdd:TIGR00236 151 QAKDNLLRENVKADSIFVTGNTVIDALLTnveiAYSSPVLSEFgedkRMILltlhrrenvgePLENIFKAIREIVEEFed 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 222 -------HPN-------FRAVKHVP---------FDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINL---GTRQIGRE 275
Cdd:TIGR00236 231 vqivypvHLNpvvreplHKHLGDSKrvhliepleYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVLVLrdtTERPETVE 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1765945268 276 TGENVLHvrdADTQDKILQALHLQFGKQYPCSKI------YGDGNAVPRILKFLK 324
Cdd:TIGR00236 311 AGTNKLV---GTDKENITKAAKRLLTDPDEYKKMsnasnpYGDGEASERIVEELL 362
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
359-551 |
3.21e-10 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 61.92 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIV---KKYTQ--FNPKTYEERINLILQMCVEAAAeavklncRILGVGISTGGRVNPREGI 433
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILhceKKRTAevIAPDLVSGLGEMIDEYLRRFNA-------RCHGIVMGFPALVSKDRRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 434 VLHSTKL-IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERK-----------FGQGKGLENFVTLitgtgigggiih 501
Cdd:PRK09698 80 VISTPNLpLTALDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKennltqqlvlgAYLGTGMGFAVWM------------ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1765945268 502 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 551
Cdd:PRK09698 148 NGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQ 197
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
362-627 |
6.08e-10 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 60.77 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 362 DLGGTNLRVAIVSMKGEIVKKYTQFNPKT-YEERINLILQMCVEAAAeavKLNCRilG-VGISTGGRVNPREGIVLhsTK 439
Cdd:PRK13310 6 DIGGTKIELGVFNEKLELQWEERVPTPRDsYDAFLDAVCELVAEADQ---RFGCK--GsVGIGIPGMPETEDGTLY--AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 440 LIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHL 519
Cdd:PRK13310 79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 520 --------VVSLDGP--DCSCGSHGCIEAYASGMALQreakklhdedlLLVEGMsvpKDEAVGALHLIQAAKLGNAKAQS 589
Cdd:PRK13310 159 rlpvdaltLLGWDAPlrRCGCGQKGCIENYLSGRGFE-----------WLYQHY---YGEPLQAPEIIALYYQGDEQAVA 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1765945268 590 ILRTAGTALGLGVVNILHTMNPSLVILSGVLaSHYIHI 627
Cdd:PRK13310 225 HVERYLDLLAICLGNILTIVDPHLVVLGGGL-SNFDAI 261
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
359-489 |
9.85e-08 |
|
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK (EC 2.7.1.63/EC 2.7.1.2), also called poly(P)/ATP-glucomannokinase (GMK), poly(P) glucokinase, ATP-dependent glucokinase, or polyphosphate--glucose phosphotransferase, catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in Mycobacterium tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor. PPGK belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this family lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466908 [Multi-domain] Cd Length: 239 Bit Score: 53.34 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSM-KGEIVkkytqfnpktyEERINLIL-QMCV-EAAAEAVKLNCRILG----VGISTGGRVnpRE 431
Cdd:cd24058 2 LGIDIGGSGIKGAIVDTdTGELL-----------SERIRIPTpQPATpEAVADVVAELVAHFPwfgpVGVGFPGVV--RR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1765945268 432 GIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGK---GLENFVTL 489
Cdd:cd24058 69 GVVRTAANLDKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKgekGVVLVLTL 129
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
362-546 |
1.13e-06 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 50.41 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 362 DLGGTNLRVAIVSmkgEIVKKYTQFNPKTYEERINLILQMCVEAAAEAvKLNCRILG-VGISTGGRVNPREGIVLhsTKL 440
Cdd:PRK13311 6 DMGGTKIELGVFD---ENLQRIWHKRVPTPREDYPQLLQILRDLTEEA-DTYCGVQGsVGIGIPGLPNADDGTVF--TAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 441 IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLV 520
Cdd:PRK13311 80 VPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFR 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1765945268 521 VSLDGPD----------CSCGSHGCIEAYASGMALQ 546
Cdd:PRK13311 160 LPVDALDilgadiprvpCGCGHRGCIENYISGRGFE 195
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
361-552 |
1.33e-05 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 47.71 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 361 VDLGGTNLRVAIVSMKG-EIVKKYTQFNPKTYEERINLILQMCVEAAAEavkLNCR-ILGVGIStgGRVNPREGIV--LH 436
Cdd:PRK09557 5 IDLGGTKIEVIALDDAGeELFRKRLPTPRDDYQQTIEAIATLVDMAEQA---TGQRgTVGVGIP--GSISPYTGLVknAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 437 STkliqeW-NSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 515
Cdd:PRK09557 80 ST-----WlNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1765945268 516 LGHLVVSLDGPD---------CSCGSHGCIEAYASGMALQREAKKL 552
Cdd:PRK09557 155 WGHNPLPWMDEDelryrnevpCYCGKQGCIETFISGTGFATDYRRL 200
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
359-435 |
6.87e-05 |
|
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: 45.68 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVK------KYTQ---------FNPKTYEERinlILQMCVEAAAEAVKLNCRILGVGiST 423
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAiayrewEYYTdddypdakeFDPEELWEK---ICEAIREALKKAGISPEDISAVS-ST 78
|
90
....*....|..
gi 1765945268 424 GgrvnPREGIVL 435
Cdd:cd07798 79 S----QREGIVF 86
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
358-425 |
3.23e-04 |
|
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: 42.71 E-value: 3.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765945268 358 ALAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPK--TYEERINLILQMCVEAAAEAVK----LNCRILGVGISTGG 425
Cdd:pfam00370 2 YLGIDCGTTSTKAILFNEQGKIIavaqLENPQITPHpgWAEQDPDEIWQAVAQCIAKTLSqlgiSLKQIKGIGISNQG 79
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
359-423 |
1.12e-03 |
|
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: 42.16 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPKTY--EERINLILQMCVEAAAEAVKL--NCRILGVGIST 423
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVasssAEYPLIRPEPGwaEQDPEEILEAVLEALKEVLAKlgGGEVDAIGFSS 75
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
345-378 |
2.12e-03 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases 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: 466850 [Multi-domain] Cd Length: 357 Bit Score: 40.72 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|....
gi 1765945268 345 ISQDIDHiLETLSALAVDLGGTNLRVAIVSMKGE 378
Cdd:cd24000 33 VSPLPTG-LESGEFLAIDLGGTNLRVALVSLDGK 65
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
354-378 |
3.88e-03 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.
Pssm-ID: 466937 [Multi-domain] Cd Length: 428 Bit Score: 40.05 E-value: 3.88e-03
10 20
....*....|....*....|....*
gi 1765945268 354 ETLSALAVDLGGTNLRVAIVSMKGE 378
Cdd:cd24087 41 ETGDYLALDLGGTNLRVCLVKLGGN 65
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
359-385 |
9.24e-03 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.
Pssm-ID: 459774 [Multi-domain] Cd Length: 197 Bit Score: 37.87 E-value: 9.24e-03
10 20
....*....|....*....|....*..
gi 1765945268 359 LAVDLGGTNLRVAIVSMKGEIVKKYTQ 385
Cdd:pfam00349 59 LALDLGGTNFRVCLVELGGDGKFEITQ 85
|
|
| |
