|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
408-712 |
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: 567.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 408 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLH 487
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 567
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 568 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 647
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774326 648 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVRDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 712
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
11-374 |
5.95e-129 |
|
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: 386.88 E-value: 5.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 11 RVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDP-DLELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 91 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 169
Cdd:TIGR03568 80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 170 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDVKcKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 247
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGIDLD-KPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 248 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 327
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958774326 328 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 374
Cdd:TIGR03568 315 ADSVIDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIEIL 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
11-375 |
1.21e-101 |
|
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: 316.07 E-value: 1.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 11 RVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDP-GLELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 91 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 167
Cdd:cd03786 77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 168 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKCKDYIVALQHPVTTDikHSIKMFELTLDALISFNKR- 246
Cdd:cd03786 156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTLHRRENV--DSGERLEELLEALEELAEKy 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 247 -TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIG 324
Cdd:cd03786 232 dLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTER 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774326 325 RETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 375
Cdd:cd03786 310 PERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
409-715 |
6.57e-67 |
|
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: 222.85 E-value: 6.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 486
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 487 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLItgtgigggiiHQHELIHGSSFCAAE 566
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTlgtgigggivINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 567 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNVKAQSILRTAG 646
Cdd:COG1940 166 IGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDPLALEVLDEAA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774326 647 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVRDVIRQQALSSVQDVD--VVVSDLVDPALLGAASMVLD 715
Cdd:COG1940 233 RYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAALALE 306
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
37-375 |
2.55e-60 |
|
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: 206.23 E-value: 2.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 37 AFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 116
Cdd:pfam02350 6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 117 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLs 191
Cdd:pfam02350 80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 192 aknkDYMSIIRMWLG-DDVKCKDYIVALQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKk 268
Cdd:pfam02350 159 ----LSREEIEERSGiLAKLGKRYVLVTFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 269 gIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKI 343
Cdd:pfam02350 231 -LEGYPRVRLIEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERI 304
|
330 340 350
....*....|....*....|....*....|..
gi 1958774326 344 LQALHLQFGKQYPCSKIYGDGNAVPRILKFLK 375
Cdd:pfam02350 305 VAALERLLEDPASYKNPYGDGNASERIVDILE 336
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
410-688 |
2.47e-36 |
|
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: 138.63 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErisLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVlHS 488
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 489 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 568
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 569 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNVKAQSILRTAGTA 648
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958774326 649 LGLGVVNILHTMNPSLVILSG--VLASHYIHIVRDVIRQQAL 688
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGGgvSNADGLLEAIRSLVKKYLN 262
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
410-686 |
5.12e-36 |
|
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: 138.49 E-value: 5.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTyEERISLILQMCVEAAAEAV-KLNCRILGVGISTGGRVNPQEGVVLHS 488
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTT-PETIVDAIASAVDSFIQHIaKVGHEIVAIGIGAPGPVNRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 489 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 568
Cdd:TIGR00744 80 VNL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 569 HLVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 647
Cdd:TIGR00744 158 HIRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVAR 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958774326 648 ALGLGVVNILHTMNPSLVILSGVLaSHYIHIVRDVIRQQ 686
Cdd:TIGR00744 238 WAGAGLADLASLFNPSAIVLGGGL-SDAGDLLLDPIRKS 275
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
24-376 |
4.33e-18 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 86.66 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 24 KLAPIMFGIKTEPAFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 98
Cdd:COG0381 16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 99 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 163
Cdd:COG0381 84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 164 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGddVKCKDYIVALQH-PVTTDIKHSIKMFeltLDALIS 242
Cdd:COG0381 152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELG--LEPKKYILVTLHrRENVDDPERLENI---LEALRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 243 FNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVI 316
Cdd:COG0381 227 LAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774326 317 NL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 376
Cdd:COG0381 298 TLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
410-686 |
1.65e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 74.56 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERISLILQMCVEAAAEAVKlncrilgVGISTGGRVNpqEGVVlh 487
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAAMAERKFGQGKGQeNFVTLITGTGIGGGIIHQHELIHG 559
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQALPDDIR-NMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 560 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNVKAQ 639
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958774326 640 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVRDVIRQQ 686
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 ... |
408-712 |
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: 567.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 408 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLH 487
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 567
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 568 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 647
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774326 648 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVRDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 712
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
11-374 |
5.95e-129 |
|
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: 386.88 E-value: 5.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 11 RVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDP-DLELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 91 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 169
Cdd:TIGR03568 80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 170 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDVKcKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 247
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGIDLD-KPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 248 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 327
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958774326 328 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 374
Cdd:TIGR03568 315 ADSVIDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIEIL 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
11-375 |
1.21e-101 |
|
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: 316.07 E-value: 1.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 11 RVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDP-GLELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 91 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 167
Cdd:cd03786 77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 168 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKCKDYIVALQHPVTTDikHSIKMFELTLDALISFNKR- 246
Cdd:cd03786 156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTLHRRENV--DSGERLEELLEALEELAEKy 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 247 -TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIG 324
Cdd:cd03786 232 dLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTER 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774326 325 RETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 375
Cdd:cd03786 310 PERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
409-715 |
6.57e-67 |
|
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: 222.85 E-value: 6.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 486
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 487 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLItgtgigggiiHQHELIHGSSFCAAE 566
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTlgtgigggivINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 567 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNVKAQSILRTAG 646
Cdd:COG1940 166 IGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDPLALEVLDEAA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774326 647 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVRDVIRQQALSSVQDVD--VVVSDLVDPALLGAASMVLD 715
Cdd:COG1940 233 RYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAALALE 306
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
37-375 |
2.55e-60 |
|
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: 206.23 E-value: 2.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 37 AFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 116
Cdd:pfam02350 6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 117 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLs 191
Cdd:pfam02350 80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 192 aknkDYMSIIRMWLG-DDVKCKDYIVALQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKk 268
Cdd:pfam02350 159 ----LSREEIEERSGiLAKLGKRYVLVTFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 269 gIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKI 343
Cdd:pfam02350 231 -LEGYPRVRLIEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERI 304
|
330 340 350
....*....|....*....|....*....|..
gi 1958774326 344 LQALHLQFGKQYPCSKIYGDGNAVPRILKFLK 375
Cdd:pfam02350 305 VAALERLLEDPASYKNPYGDGNASERIVDILE 336
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
409-715 |
2.16e-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: 197.40 E-value: 2.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ-FNPK-TYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 486
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVpLPASdDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 487 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 566
Cdd:cd24076 83 LAPNL--GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 567 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEdlllVEGMSVPKdeavgalhLIQAAKLGNVKAQSILRTAG 646
Cdd:cd24076 161 IGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAG----GEPLSLAE--------LVEAARAGDPAALAALEEVG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774326 647 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVRDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLD 715
Cdd:cd24076 229 EYLGIGLANLVNTFNPELVVLGGALAPlgpWLLPPLRAEVARRALPAPARDVRIVVSRlgEDAAALGAAALAID 302
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
409-688 |
1.31e-52 |
|
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: 184.29 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ----FNPKTYEERISLILQMCVEAAAEAVKlncRILGVGISTGGRVNPQEGV 484
Cdd:cd24073 3 VVGVKLTEDRITAVLTDLRGNVLASHTLpldsGDPEAVAEAIAEAVAELLAQAGLSPD---RLLGIGVGLPGLVDAETGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 485 VLHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCA 564
Cdd:cd24073 80 CRWSPLL--GWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 565 AELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvPKDEAVGALHLIQAAKLGNVKAQSILRT 644
Cdd:cd24073 158 GEIGHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAG------------LRGEPLTIEDLLAAARAGDPAARAILRR 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958774326 645 AGTALGLGVVNILHTMNPSLVILSG---VLASHYIHIVRDVIRQQAL 688
Cdd:cd24073 226 AGRALGLALANLVNLLDPELIIISGegvRAGDLLFEPMREALRAHVF 272
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
409-688 |
3.03e-52 |
|
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: 182.76 E-value: 3.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKY---TQFNpKTYEErislILQMCVEAAAEaVKLNCRILGVGISTGGRVNPQEGVV 485
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDsvpTPAS-KGGDA----ILERLLEIIAE-LKEKYDIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 486 LHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAA 565
Cdd:cd24068 76 IYATDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 566 ELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLlvegmsvpkdeavGALHLIQAAKLGNVKAQSILRTA 645
Cdd:cd24068 156 ELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGI-------------DGREIFDLADAGDPLAKEVVEEF 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958774326 646 GTALGLGVVNILHTMNPSLVILSG-VLAS--HYIHIVRDVIRQQAL 688
Cdd:cd24068 223 AEDLATGLANLVHIFDPEVIVIGGgISAQgeLFLEELREELRKLLM 268
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
409-716 |
4.37e-49 |
|
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: 174.70 E-value: 4.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIV--KKYTQFNPKTYEERISLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 486
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILarEKYPLDEKENPEEVLEKLYEL-IDRLLEKENIKSKILGIGIGAPGPLDVEKGIIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 487 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 566
Cdd:cd24059 82 NPPNF-PGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 567 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvEGMSVPKDEavgaLHLIQAAKLGNVKAQSILRTAG 646
Cdd:cd24059 161 IGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARS---------ALGSGRSFQ----LDIVEALQKGDPIADEVIEEAA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774326 647 TALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVRDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLDY 716
Cdd:cd24059 228 KYLGIGLVNLINLLNPEAIIIGGELIylgERYLEPIEKEVNSRLFGRNAREVRILKSSlgEDAPLLGAAALVLNK 302
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
409-672 |
2.45e-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: 161.37 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVklncrILGVGISTGGRVNPQEGVVLHS 488
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPPTADGIVDAIVEAVEELREGHD-----VSAVGVAAAGFVDADRATVLFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 489 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 568
Cdd:cd24061 76 PNI--AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 569 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDED-----LLLVEGmsvpKDEAVGALHLIQAAKLGNVKAQSILR 643
Cdd:cd24061 154 HIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATpegaaVLLADG----SVDGITGKHISEAARAGDPVALDALR 229
|
250 260
....*....|....*....|....*....
gi 1958774326 644 TAGTALGLGVVNILHTMNPSLVILSGVLA 672
Cdd:cd24061 230 ELARWLGAGLASLAALLDPELFVIGGGVS 258
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
409-669 |
1.05e-42 |
|
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: 157.06 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYT-QFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLH 487
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEKTRiPFDHETDPEKVIELIAENIKKLIKNKHVEKKLLGIGIAVSGLVDSKKGIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 STKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 567
Cdd:cd24071 83 STIL--GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 568 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLvegmSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 647
Cdd:cd24071 161 GHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLS----LLKELEDFEIEKVREAAEEGDSVATELFKKAGE 236
|
250 260
....*....|....*....|..
gi 1958774326 648 ALGLGVVNILHTMNPSLVILSG 669
Cdd:cd24071 237 YLGIGIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
409-685 |
7.34e-41 |
|
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: 151.72 E-value: 7.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEER--ISLILQMCVEAAAEAVKLNcrILGVGISTGGRVNPQEGVVL 486
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGtvSEQVLGLIETLLSKAGKDS--IEGIGVSSAGPLDLRKGTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 487 HSTKLIQEWnsVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 566
Cdd:cd24063 80 NSPNIKGKE--IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 567 LGHLVVSLD-GPDCSCGSHGCIEAYASGMALQREAKKL-HDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRT 644
Cdd:cd24063 158 VGHLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWaEGFSSRTSLKLRNPGGEGITAKEVFSAARKGDPLALKIIEK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958774326 645 AGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVRDVIRQ 685
Cdd:cd24063 238 LARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEY 278
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
410-685 |
1.05e-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: 151.41 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKK--YTQFNPKTYEERISLILQMcveaAAEAVKLNC-RILGVGISTGGRVNPQEGVVL 486
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEfeYRVITLETPEALIDEIIDC----IDRLLKLWKdRVKGIALAIQGLVDSHKGVSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 487 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 566
Cdd:cd24072 80 WSPGA--PWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 567 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAG 646
Cdd:cd24072 158 IGHTKVNPDGARCDCGRRGCLETVASNSALKRNARV------TLKLGPVSADPEKLTMEQLIEALEEGEPIATQIFDRAA 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958774326 647 TALGLGVVNILHTMNPSLVILSGVLASHYIHIVRDVIRQ 685
Cdd:cd24072 232 NAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRA 270
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
409-669 |
1.03e-38 |
|
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: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYTQfnPKTYEERISLILQMCVEAAAEAVKlNCRILGVGISTGGRVNPQEGVVLHS 488
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTI--DTKVENGKEDVINRIAETVNELIE-EMELLGIGIGSPGSIDRENGIVRFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 489 TKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 568
Cdd:cd24064 78 PNF-PDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 569 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDE--DLLlvegmsVPKDEAVGALHLIQAAKLGNVKAQSILRTAG 646
Cdd:cd24064 157 HVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRypDSL------AGESEKINAKHVFDAARKNDPLATMVFRRVV 230
|
250 260
....*....|....*....|...
gi 1958774326 647 TALGLGVVNILHTMNPSLVILSG 669
Cdd:cd24064 231 DALAIAIGGFVHIFNPEIIIIGG 253
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
410-688 |
6.79e-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: 141.06 E-value: 6.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERISLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLH 487
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPaeEGPEAVLDRIAEL-IEELLAEAGVRERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 STKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLitgtgigggiiH-----------QHEL 556
Cdd:cd23763 80 APNL-PWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYI-----------TlgtgigggiiiDGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 557 IHGSSFCAAELGHLVVsldgpdcscgshgcieayasgmalqreakklhdedlllvegmsvpkdeavgalhliqaaklgnv 636
Cdd:cd23763 148 YRGANGAAGEIGHITV---------------------------------------------------------------- 163
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958774326 637 kaqsiLRTAGTALGLGVVNILHTMNPSLVILSGVLASH---YIHIVRDVIRQQAL 688
Cdd:cd23763 164 -----LEEAARYLGIGLANLINLLNPELIVLGGGVAEAgdlLLEPIREAVRRRAL 213
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
408-686 |
1.05e-36 |
|
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: 139.39 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 408 SALAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKlncRILGVGISTGGRVNPQEGVVLH 487
Cdd:cd24065 1 STIGLDLGGTKIAAGVVD-GGRILSRLVVPTPREGGEAVLDALARAVEALQAEAP---GVEAVGLGVPGPLDFRRGRVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 STKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 567
Cdd:cd24065 77 APN-IPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 568 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDlllvegMSVPKdeavgalhLIQAAKLGNVKAQSILRTAGT 647
Cdd:cd24065 156 GHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRP------MSTAE--------LFELAQQGEPKALRIVEQAAA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958774326 648 ALGLGVVNILHTMNPSLVILSGVLASH---YIHIVRDVIRQQ 686
Cdd:cd24065 222 HLGIGLANLQKALDPEVFVLGGGVAQVgdyYLLPVQEAARRY 263
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
410-688 |
2.47e-36 |
|
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: 138.63 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErisLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVlHS 488
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 489 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 568
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 569 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNVKAQSILRTAGTA 648
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958774326 649 LGLGVVNILHTMNPSLVILSG--VLASHYIHIVRDVIRQQAL 688
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGGgvSNADGLLEAIRSLVKKYLN 262
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
410-686 |
5.12e-36 |
|
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: 138.49 E-value: 5.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTyEERISLILQMCVEAAAEAV-KLNCRILGVGISTGGRVNPQEGVVLHS 488
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTT-PETIVDAIASAVDSFIQHIaKVGHEIVAIGIGAPGPVNRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 489 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 568
Cdd:TIGR00744 80 VNL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 569 HLVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 647
Cdd:TIGR00744 158 HIRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVAR 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958774326 648 ALGLGVVNILHTMNPSLVILSGVLaSHYIHIVRDVIRQQ 686
Cdd:TIGR00744 238 WAGAGLADLASLFNPSAIVLGGGL-SDAGDLLLDPIRKS 275
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
409-688 |
2.96e-34 |
|
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: 133.18 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT--YEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 486
Cdd:cd24062 2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLegGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 487 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 566
Cdd:cd24062 82 VAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 567 LGHL-VVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTA 645
Cdd:cd24062 160 IGHItVNPEGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAVVDTV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958774326 646 GTALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVRDVIRQQAL 688
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGGGVSaagEFLLSPVKEYFDRFTF 285
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
409-686 |
1.86e-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: 115.72 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKKYT-QFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEgvVLH 487
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQiKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVDENE--IIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 STKliQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGkgQENFVTLITgtgigggiiH---------QHELIH 558
Cdd:cd24077 81 TPY--YDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSED--YDNLISISI---------HsgigagiiiNNQLYR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 559 GSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDedlllVEGMSVPkdeavgalHLIQAAKLGNVKA 638
Cdd:cd24077 148 GYNGFAGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKKG-----LETLTFD--------DLIQLYNEGDPEA 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958774326 639 QSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVrDVIRQQ 686
Cdd:cd24077 215 LELIDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELL-EKIKEQ 261
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
410-669 |
3.90e-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: 106.11 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEErisLILQMCVEAAAEAVKLncrILGVGISTGGRVNPQEGVVLHST 489
Cdd:cd24152 3 LVFDIGGTFIKYALVDENGNIIKKGKIPTPKDSLE---EFLDYIKKIIKRYDEE---IDGIAISAPGVIDPETGIIYGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 490 KLiqEWNS-VDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 568
Cdd:cd24152 77 AL--PYLKgFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 569 HLVVSLDGPDCSCGSHgcieaYASGMALQREAKKLHDedlllvegmsvpkDEAVGALHLIQAAKLGNVKAQSILRTAGTA 648
Cdd:cd24152 155 YLLTDDDDKDLLFFSG-----LASMFGLVKRYNKAKG-------------LEPLDGEEIFEKYAKGDEAAKKILDEYIRN 216
|
250 260
....*....|....*....|.
gi 1958774326 649 LGLGVVNILHTMNPSLVILSG 669
Cdd:cd24152 217 LAKLIYNIQYILDPEVIVIGG 237
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
409-688 |
7.62e-24 |
|
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: 102.83 E-value: 7.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIVKK----YTQFNPKTYEERISLILQMCVEAaaEAVKLNcRILGVGISTGGRVNPQEGV 484
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAEhtvpLTALNQEALLSQLIEEIAQFLKS--HRRKTQ-RLIAISITLPGLINPKTGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 485 VlHSTKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCA 564
Cdd:cd24075 80 V-HYMPHIQ-VKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 565 AELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDllLVEGMSvPKDEAVGAlhLIQAAKLGNVKAQSILRT 644
Cdd:cd24075 158 GEIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQG--YASQLT-LQDCTIKD--ICQAALNGDQLAQDVIKR 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958774326 645 AGTALGLGVVNILHTMNPSLVILSG--VLASHYIH-IVRDVIRQQAL 688
Cdd:cd24075 233 AGRYLGKVIAILINLLNPQKIIIAGeiTQADKVLLpVIKKCIQSQAL 279
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
466-688 |
4.86e-22 |
|
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: 97.77 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 466 RILGVGISTGGRVNPQEGVVLHSTKL-IQEWnsvdlrtPLSDTLH----LPVWVDNDGNCAAMAERKFGQGKGQENFVTL 540
Cdd:cd24074 62 RLTAIAITLPGIIDPESGIVHRLPFYdIKNL-------PLGEALEqhtgLPVYVQHDISAWTLAERFFGAAKGAKNIIQI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 541 ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKL---HDEDLLLVEGMSVP 617
Cdd:cd24074 135 VIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLleqSPDSMLHGQPISIE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774326 618 kdeavgalHLIQAAKLGNVKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVL---ASHYIHIVRDVIRQQAL 688
Cdd:cd24074 215 --------SLCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLnnaAEILFPALSQSIRQQSL 280
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
410-669 |
3.75e-20 |
|
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: 91.46 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIV---KKYTQfNPKTYEERISLILQMcVEAAAEAVKLNCRilGVGISTGGRVNPQEGVVL 486
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLdfeKVPSK-DLLRAGDPVEVLADL-IREYIEEAGLKPA--AIVIGVPGTVDKDRRTVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 487 HSTKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQE------------NFVTLItgtgigggiihqH 554
Cdd:cd24070 80 STPN-IPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGvvlgfyigtgigNAILIN------------G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 555 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlHDEDlllvegmsVPkDEAVGALHlIQAAKLG 634
Cdd:cd24070 147 KPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEE-HYPD--------TP-ILDIFVDH-GDEPELD 215
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958774326 635 N-VKAQSIlrTAGTAlglgvVNILhtmNPSLVILSG 669
Cdd:cd24070 216 EfVEDLAL--AIATE-----INIL---DPDAVILGG 241
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
410-680 |
9.58e-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: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEerisliLQMCVEAAAE-AVKLNCRILGVGISTGGRVNpqEGVVLH- 487
Cdd:cd24069 1 LAIDIGGTKIAAALIG-NGQIIDRRQIPTPRSGT------PEALADALASlLADYQGQFDRVAVASTGIIR--DGVLTAl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 567
Cdd:cd24069 72 NPKNLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 568 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAkklhdedlllvegmSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 647
Cdd:cd24069 152 GHTLADPPGPVCGCGRRGCVEAIASGTAIAAAA--------------SEILGEPVDAKDVFERARSGDEEAARLIDRAAR 217
|
250 260 270
....*....|....*....|....*....|....*
gi 1958774326 648 ALGLGVVNILHTMNPSLVILSGV--LASHYIHIVR 680
Cdd:cd24069 218 ALADLIADLKATLDLDCVVIGGSvgLAEGFLERVE 252
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
411-672 |
1.40e-19 |
|
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: 89.98 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 411 AVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT-YEERISLILQMCVEAAAEAvklNCRiLGVGISTGGRVNPQEGVVLhsT 489
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDdYAAFLAAIAELVAEADARF---GVK-GPVGIGIPGVIDPEDGTLI--T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 490 KLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 569
Cdd:cd24057 78 ANIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 570 LVVSLD----GPD-----CSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNVKAQS 640
Cdd:cd24057 158 GPLPADalllGYDlpvlrCGCGQTGCLETYLSGRGLERLYAHLYGEEL--------------DAPEIIAAWAAGDPQAVA 223
|
250 260 270
....*....|....*....|....*....|..
gi 1958774326 641 ILRTAGTALGLGVVNILHTMNPSLVILSGVLA 672
Cdd:cd24057 224 HVDRWLDLLAGCLANILTALDPDVVVLGGGLS 255
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
410-669 |
3.27e-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: 88.80 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEERISLILQMcVEAAAEAVKLNCRilgVGISTGGRVNPQEGVVLHS 488
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRgDYEATLDAIADL-VEEAEEELGAPAT---VGIGTPGSISPRTGLVKNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 489 tkliqewNSV-----DLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFC 563
Cdd:cd24066 78 -------NSTwlngkPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 564 AAELGHLVV------SLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNVK 637
Cdd:cd24066 151 AGEWGHNPLpwpdedELPGPPCYCGKRGCVETFLSGPALERDYARLTGKTL--------------SAEEIVALARAGDAA 216
|
250 260 270
....*....|....*....|....*....|..
gi 1958774326 638 AQSILRTAGTALGLGVVNILHTMNPSLVILSG 669
Cdd:cd24066 217 AVATLDRFLDRLGRALANVINILDPDVIVLGG 248
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
24-376 |
4.33e-18 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 86.66 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 24 KLAPIMFGIKTEPAFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 98
Cdd:COG0381 16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 99 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 163
Cdd:COG0381 84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 164 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGddVKCKDYIVALQH-PVTTDIKHSIKMFeltLDALIS 242
Cdd:COG0381 152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELG--LEPKKYILVTLHrRENVDDPERLENI---LEALRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 243 FNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVI 316
Cdd:COG0381 227 LAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774326 317 NL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 376
Cdd:COG0381 298 TLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
410-686 |
1.65e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 74.56 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERISLILQMCVEAAAEAVKlncrilgVGISTGGRVNpqEGVVlh 487
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAAMAERKFGQGKGQeNFVTLITGTGIGGGIIHQHELIHG 559
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQALPDDIR-NMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 560 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNVKAQ 639
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958774326 640 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVRDVIRQQ 686
Cdd:PRK05082 212 ALINRSAQAIARLIADLKATLDCQCVVLGGSvgLAEGYLELVQAYLAQE 260
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
10-375 |
4.27e-14 |
|
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: 74.41 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 10 LRVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHliddygntYRMIEQ--DDFDINTRlHTIVRGEDEAAMVES 87
Cdd:TIGR00236 1 LKVMIVLGTRPEAIKMAPLIRALKKYP-EIDSYVIVTAQH--------REMLDQvlDLFHLPPD-YDLNIMSPGQTLGEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 88 VGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSI-----RHAITKLAHYHVCCTR 162
Cdd:TIGR00236 71 TSNMLEGLEELLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMpeeinRQLTGHIADLHFAPTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 163 SAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDvkcKDYIVALQHPVTT------DIKHSIKmfelt 236
Cdd:TIGR00236 151 QAKDNLLRENVKADSIFVTGNTVIDALLTNVEIAYSSPVLSEFGED---KRMILLTLHRRENvgepleNIFKAIR----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 237 ldALISFNKRTLVLFPnidAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVI 316
Cdd:TIGR00236 223 --EIVEEFEDVQIVYP---VHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774326 317 NL---GTRQIGRETGENVLHvrdADTQDKILQALHLQFGKQYPCSKI------YGDGNAVPRILKFLK 375
Cdd:TIGR00236 298 VLrdtTERPETVEAGTNKLV---GTDKENITKAAKRLLTDPDEYKKMsnasnpYGDGEASERIVEELL 362
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
411-607 |
2.15e-13 |
|
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: 71.42 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 411 AVDLGGTNLRVAIVSMKGEIVKKyTQFNPKTYEErislILQMCVEAAAEAVKlncRILGVGISTGG-----RVNPQEGVV 485
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIER-TEFPTTTPEE----TLQAVIDFFREQEE---PIDAIGIASFGpidlnPTSPTYGYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 486 LHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFcaA 565
Cdd:cd24067 75 TTTPKP--GWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLH--P 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958774326 566 ELGHLVVSLDGPDC----SCGSHG-CIEAYASGMAL----QREAKKLHDED 607
Cdd:cd24067 151 EMGHIRVPRHPDDDgfpgVCPFHGdCLEGLASGPAIaarwGIPAEELPDDH 201
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
410-602 |
6.17e-10 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 61.15 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIV---KKYTQ--FNPktyeERISLILQMCVEAAAEavkLNCRILGVGISTGGRVNPQEGV 484
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILhceKKRTAevIAP----DLVSGLGEMIDEYLRR---FNARCHGIVMGFPALVSKDRRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 485 VLHSTKL-IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERK-----------FGQGKGQENFVTLitgtgigggiih 552
Cdd:PRK09698 80 VISTPNLpLTALDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKennltqqlvlgAYLGTGMGFAVWM------------ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958774326 553 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 602
Cdd:PRK09698 148 NGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQ 197
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
413-678 |
3.08e-08 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 55.76 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 413 DLGGTNLRVAIVSMKGEivKKYTQFNPkTYEERISLILQMCVEAAAEA-VKLNCRilG-VGISTGGRVNPQEGVVLhsTK 490
Cdd:PRK13310 6 DIGGTKIELGVFNEKLE--LQWEERVP-TPRDSYDAFLDAVCELVAEAdQRFGCK--GsVGIGIPGMPETEDGTLY--AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 491 LIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHL 570
Cdd:PRK13310 79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 571 --------VVSLDGP--DCSCGSHGCIEAYASGMALQreakklhdedlLLVEGMsvpKDEAVGALHLIQAAKLGNVKAQS 640
Cdd:PRK13310 159 rlpvdaltLLGWDAPlrRCGCGQKGCIENYLSGRGFE-----------WLYQHY---YGEPLQAPEIIALYYQGDEQAVA 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958774326 641 ILRTAGTALGLGVVNILHTMNPSLVILSGVLaSHYIHI 678
Cdd:PRK13310 225 HVERYLDLLAICLGNILTIVDPHLVVLGGGL-SNFDAI 261
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
410-538 |
4.99e-07 |
|
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: 51.42 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSM-KGEIVkkytqfnpktyEERISLIL-QMCV-EAAAEAVKLNCRILG----VGISTGGRVnpQE 482
Cdd:cd24058 2 LGIDIGGSGIKGAIVDTdTGELL-----------SERIRIPTpQPATpEAVADVVAELVAHFPwfgpVGVGFPGVV--RR 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774326 483 GVVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFV 538
Cdd:cd24058 69 GVVRTAANLDKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVV 124
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
413-597 |
9.44e-07 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 50.80 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 413 DLGGTNLRVAIVSmkgEIVKKYTQFNPKTYEERISLILQMCVEAAAEAvKLNCRILG-VGISTGGRVNPQEGVVLhsTKL 491
Cdd:PRK13311 6 DMGGTKIELGVFD---ENLQRIWHKRVPTPREDYPQLLQILRDLTEEA-DTYCGVQGsVGIGIPGLPNADDGTVF--TAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 492 IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLV 571
Cdd:PRK13311 80 VPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFR 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958774326 572 VSLDGPD----------CSCGSHGCIEAYASGMALQ 597
Cdd:PRK13311 160 LPVDALDilgadiprvpCGCGHRGCIENYISGRGFE 195
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
412-603 |
9.52e-06 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 48.10 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 412 VDLGGTNLRVAIVSMKG-EIVKKYTQFNPKTYEERISLILQMCVEAAAEavkLNCR-ILGVGIStgGRVNPQEGVV--LH 487
Cdd:PRK09557 5 IDLGGTKIEVIALDDAGeELFRKRLPTPRDDYQQTIEAIATLVDMAEQA---TGQRgTVGVGIP--GSISPYTGLVknAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 488 STkliqeW-NSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 566
Cdd:PRK09557 80 ST-----WlNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958774326 567 LGHLVVSLDGPD---------CSCGSHGCIEAYASGMALQREAKKL 603
Cdd:PRK09557 155 WGHNPLPWMDEDelryrnevpCYCGKQGCIETFISGTGFATDYRRL 200
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
410-486 |
4.90e-04 |
|
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: 43.37 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIVK------KYTQ---------FNPKTYEERislILQMCVEAAAEAVKLNCRILGVGiST 474
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAiayrewEYYTdddypdakeFDPEELWEK---ICEAIREALKKAGISPEDISAVS-ST 78
|
90
....*....|..
gi 1958774326 475 GGRvnpqEGVVL 486
Cdd:cd07798 79 SQR----EGIVF 86
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
409-476 |
1.58e-03 |
|
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: 40.78 E-value: 1.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774326 409 ALAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPK--TYEERISLILQMCVEAAAEAVK----LNCRILGVGISTGG 476
Cdd:pfam00370 2 YLGIDCGTTSTKAILFNEQGKIIavaqLENPQITPHpgWAEQDPDEIWQAVAQCIAKTLSqlgiSLKQIKGIGISNQG 79
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
396-429 |
2.32e-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: 2.32e-03
10 20 30
....*....|....*....|....*....|....
gi 1958774326 396 ISQDIDHiLETLSALAVDLGGTNLRVAIVSMKGE 429
Cdd:cd24000 33 VSPLPTG-LESGEFLAIDLGGTNLRVALVSLDGK 65
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
410-474 |
3.22e-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: 40.62 E-value: 3.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774326 410 LAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPKTY--EERISLILQMCVEAAAEAVKL--NCRILGVGIST 474
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVasssAEYPLIRPEPGwaEQDPEEILEAVLEALKEVLAKlgGGEVDAIGFSS 75
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
405-429 |
4.26e-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: 4.26e-03
10 20
....*....|....*....|....*
gi 1958774326 405 ETLSALAVDLGGTNLRVAIVSMKGE 429
Cdd:cd24087 41 ETGDYLALDLGGTNLRVCLVKLGGN 65
|
|
| |
