|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
349-653 |
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: 570.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 349 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 428
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 508
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 509 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 588
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765945226 589 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 653
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
2-315 |
1.26e-106 |
|
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: 327.56 E-value: 1.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 2 IEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS- 80
Cdd:TIGR03568 50 IEKDGFDIDEKIEILLDSDSNAGMAKSMGLTIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTe 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 81 GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDvKSKDYIVA 158
Cdd:TIGR03568 130 GAIDESIRHAITKLSHLHFVATEEYRQRVIQMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGID-LDKPYALV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 159 LQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCM 238
Cdd:TIGR03568 206 TFHPVTLEKAEAEEQIKELLKALDELNKNIIFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 239 IGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILK 313
Cdd:TIGR03568 285 IGNSSSGIIEAPSFGVPTINIGTRQKGRLRADSVIDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIE 362
|
..
gi 1765945226 314 FL 315
Cdd:TIGR03568 363 IL 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
4-316 |
1.16e-82 |
|
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: 265.23 E-value: 1.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 4 QDDFDINTRLHTIVRGEDEAAMVESVGLaLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS--- 80
Cdd:cd03786 49 FILFLIKPDYDLDLMGDNQTLGAKTGGL-LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 81 GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKSKDYIVALQ 160
Cdd:cd03786 128 GMPEEENRHRIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 161 HPVTTDikHSIKMFELTLDALISFNKR--TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCM 238
Cdd:cd03786 206 HRRENV--DSGERLEELLEALEELAEKydLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 239 IGNSScGVREVGAF-GTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRIL 312
Cdd:cd03786 283 LTDSG-GIQEEASFlGKPVLVLRDRTERPERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIV 361
|
....
gi 1765945226 313 KFLK 316
Cdd:cd03786 362 DILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
350-656 |
2.39e-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: 225.55 E-value: 2.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 427
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 428 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiI----------HQHEL 497
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYL----------TlgtgigggivINGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 498 IHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNA 577
Cdd:COG1940 156 LRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 578 KAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGAAS 652
Cdd:COG1940 223 LALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAA 302
|
....
gi 1765945226 653 MVLD 656
Cdd:COG1940 303 LALE 306
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
5-316 |
1.89e-55 |
|
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: 191.98 E-value: 1.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 5 DDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---- 80
Cdd:pfam02350 29 EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNETLAGALAAFYLRIPVAHVEAGLRSfdlt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 81 -GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLsaknkDYMSIIRMWLG-DDVKSKDYIVA 158
Cdd:pfam02350 107 ePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL-----LSREEIEERSGiLAKLGKRYVLV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 159 LQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKkgIEHHPNFRAVKHVPFDQFIQLVAHAG 236
Cdd:pfam02350 182 TFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER--LEGYPRVRLIEPLGYLDFLSLLKRAD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 237 CMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKILQALHLQFGKQYPCSKIYGDGNAVPRI 311
Cdd:pfam02350 257 LVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERIVAALERLLEDPASYKNPYGDGNASERI 331
|
....*
gi 1765945226 312 LKFLK 316
Cdd:pfam02350 332 VDILE 336
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
351-610 |
1.99e-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: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErinLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVlHS 429
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 430 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 509
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 510 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 589
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260
....*....|....*....|.
gi 1765945226 590 LGLGVVNILHTMNPSLVILSG 610
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGG 241
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
351-610 |
6.32e-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: 6.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHST 430
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 431 KLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 510
Cdd:TIGR00744 81 NL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 511 LVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 589
Cdd:TIGR00744 159 IRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVARW 238
|
250 260
....*....|....*....|.
gi 1765945226 590 LGLGVVNILHTMNPSLVILSG 610
Cdd:TIGR00744 239 AGAGLADLASLFNPSAIVLGG 259
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
2-317 |
2.53e-16 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 80.88 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 2 IEQDDFDINtrlhtiVRGEDEAAMVesvGLALVKLPDVLNRLKPDIMIVHGD------------RfdalalatsaalMNI 69
Cdd:COG0381 55 IPKPDYDLG------IGSGSLAEQT---ARILEGLEEVLEEEKPDAVLVHGDtnstlaaalaafK------------LGI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 70 RILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWL 146
Cdd:COG0381 114 PVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTELARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 147 GddVKSKDYIVALQH-PVTTDIKHSIKMFeltLDALISFNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHV 223
Cdd:COG0381 194 G--LEPKKYILVTLHrRENVDDPERLENI---LEALRELAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 224 PFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVINL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGK 294
Cdd:COG0381 264 GYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCLTLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPA 336
|
330 340
....*....|....*....|....*..
gi 1765945226 295 QYPCSK----IYGDGNAVPRILKFLKS 317
Cdd:COG0381 337 AYERMAravnPYGDGNASERIVDILLR 363
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
351-627 |
5.93e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 73.02 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMCVEAAAEAVKlncrilgVGISTGGRVNprEGIVlh 428
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAALAERKfGQGKGLENFVTLITGTGIGGGIIHQHELIHG 500
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQ-ALPDDIRNMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 501 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNAKAQ 580
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1765945226 581 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 627
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 ... |
349-653 |
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: 570.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 349 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 428
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 508
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 509 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 588
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765945226 589 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 653
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
2-315 |
1.26e-106 |
|
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: 327.56 E-value: 1.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 2 IEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS- 80
Cdd:TIGR03568 50 IEKDGFDIDEKIEILLDSDSNAGMAKSMGLTIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTe 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 81 GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDvKSKDYIVA 158
Cdd:TIGR03568 130 GAIDESIRHAITKLSHLHFVATEEYRQRVIQMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGID-LDKPYALV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 159 LQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCM 238
Cdd:TIGR03568 206 TFHPVTLEKAEAEEQIKELLKALDELNKNIIFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 239 IGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILK 313
Cdd:TIGR03568 285 IGNSSSGIIEAPSFGVPTINIGTRQKGRLRADSVIDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIE 362
|
..
gi 1765945226 314 FL 315
Cdd:TIGR03568 363 IL 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
4-316 |
1.16e-82 |
|
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: 265.23 E-value: 1.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 4 QDDFDINTRLHTIVRGEDEAAMVESVGLaLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS--- 80
Cdd:cd03786 49 FILFLIKPDYDLDLMGDNQTLGAKTGGL-LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 81 GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKSKDYIVALQ 160
Cdd:cd03786 128 GMPEEENRHRIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 161 HPVTTDikHSIKMFELTLDALISFNKR--TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCM 238
Cdd:cd03786 206 HRRENV--DSGERLEELLEALEELAEKydLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 239 IGNSScGVREVGAF-GTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRIL 312
Cdd:cd03786 283 LTDSG-GIQEEASFlGKPVLVLRDRTERPERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIV 361
|
....
gi 1765945226 313 KFLK 316
Cdd:cd03786 362 DILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
350-656 |
2.39e-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: 225.55 E-value: 2.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 427
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 428 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiI----------HQHEL 497
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYL----------TlgtgigggivINGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 498 IHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNA 577
Cdd:COG1940 156 LRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 578 KAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGAAS 652
Cdd:COG1940 223 LALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAA 302
|
....
gi 1765945226 653 MVLD 656
Cdd:COG1940 303 LALE 306
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
350-656 |
4.30e-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: 195.48 E-value: 4.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ-FNPK-TYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 427
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVpLPASdDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 428 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 507
Cdd:cd24076 83 LAPNL--GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 508 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEdlllVEGMSVPKdeavgalhLIQAAKLGNAKAQSILRTAG 587
Cdd:cd24076 161 IGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAG----GEPLSLAE--------LVEAARAGDPAALAALEEVG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765945226 588 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLD 656
Cdd:cd24076 229 EYLGIGLANLVNTFNPELVVLGGALAPlgpWLLPPLRAEVARRALPAPARDVRIVVSRlgEDAAALGAAALAID 302
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
5-316 |
1.89e-55 |
|
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: 191.98 E-value: 1.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 5 DDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---- 80
Cdd:pfam02350 29 EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNETLAGALAAFYLRIPVAHVEAGLRSfdlt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 81 -GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLsaknkDYMSIIRMWLG-DDVKSKDYIVA 158
Cdd:pfam02350 107 ePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL-----LSREEIEERSGiLAKLGKRYVLV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 159 LQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKkgIEHHPNFRAVKHVPFDQFIQLVAHAG 236
Cdd:pfam02350 182 TFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER--LEGYPRVRLIEPLGYLDFLSLLKRAD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 237 CMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKILQALHLQFGKQYPCSKIYGDGNAVPRI 311
Cdd:pfam02350 257 LVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERIVAALERLLEDPASYKNPYGDGNASERI 331
|
....*
gi 1765945226 312 LKFLK 316
Cdd:pfam02350 332 VDILE 336
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
350-610 |
3.76e-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: 187.38 E-value: 3.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKY---TQFNpKTYEERINLILQmcveaAAEAVKLNCRILGVGISTGGRVNPREGIV 426
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDsvpTPAS-KGGDAILERLLE-----IIAELKEKYDIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 427 LHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAA 506
Cdd:cd24068 76 IYATDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 507 ELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLlvegmsvpkdeavGALHLIQAAKLGNAKAQSILRTA 586
Cdd:cd24068 156 ELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGI-------------DGREIFDLADAGDPLAKEVVEEF 222
|
250 260
....*....|....*....|....
gi 1765945226 587 GTALGLGVVNILHTMNPSLVILSG 610
Cdd:cd24068 223 AEDLATGLANLVHIFDPEVIVIGG 246
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
350-610 |
3.70e-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: 3.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ-FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 428
Cdd:cd24073 3 VVGVKLTEDRITAVLTDLRGNVLASHTLpLDSGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGICRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 STKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 508
Cdd:cd24073 83 SPLL--GWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 509 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 588
Cdd:cd24073 161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAG------------LRGEPLTIEDLLAAARAGDPAARAILRRAGR 228
|
250 260
....*....|....*....|..
gi 1765945226 589 ALGLGVVNILHTMNPSLVILSG 610
Cdd:cd24073 229 ALGLALANLVNLLDPELIIISG 250
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
350-657 |
5.24e-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: 178.93 E-value: 5.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIV--KKYTQFNPKTYEERINLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 427
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILarEKYPLDEKENPEEVLEKLYEL-IDRLLEKENIKSKILGIGIGAPGPLDVEKGIIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 428 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 507
Cdd:cd24059 82 NPPNF-PGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 508 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvEGMSVPKDEavgaLHLIQAAKLGNAKAQSILRTAG 587
Cdd:cd24059 161 IGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARS---------ALGSGRSFQ----LDIVEALQKGDPIADEVIEEAA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765945226 588 TALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLDY 657
Cdd:cd24059 228 KYLGIGLVNLINLLNPEAIIIGGELIylgERYLEPIEKEVNSRLFGRNAREVRILKSSlgEDAPLLGAAALVLNK 302
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
350-613 |
1.06e-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: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVklncrILGVGISTGGRVNPREGIVLHS 429
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPPTADGIVDAIVEAVEELREGHD-----VSAVGVAAAGFVDADRATVLFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 430 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 509
Cdd:cd24061 76 PNI--AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 510 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDED-----LLLVEGmsvpKDEAVGALHLIQAAKLGNAKAQSILR 584
Cdd:cd24061 154 HIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATpegaaVLLADG----SVDGITGKHISEAARAGDPVALDALR 229
|
250 260
....*....|....*....|....*....
gi 1765945226 585 TAGTALGLGVVNILHTMNPSLVILSGVLA 613
Cdd:cd24061 230 ELARWLGAGLASLAALLDPELFVIGGGVS 258
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
350-610 |
3.54e-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: 3.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKyTQF---NPKTYEERINLILQmCVEAAAEAVKLNCRILGVGISTGGRVNPREGIV 426
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEK-TRIpfdHETDPEKVIELIAE-NIKKLIKNKHVEKKLLGIGIAVSGLVDSKKGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 427 LHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAA 506
Cdd:cd24071 81 IRSTIL--GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 507 ELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLvegmSVPKDEAVGALHLIQAAKLGNAKAQSILRTA 586
Cdd:cd24071 159 EIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLS----LLKELEDFEIEKVREAAEEGDSVATELFKKA 234
|
250 260
....*....|....*....|....
gi 1765945226 587 GTALGLGVVNILHTMNPSLVILSG 610
Cdd:cd24071 235 GEYLGIGIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
350-626 |
2.37e-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: 155.57 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEER--INLILQMCVEAAAEAVKLNcrILGVGISTGGRVNPREGIVL 427
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGtvSEQVLGLIETLLSKAGKDS--IEGIGVSSAGPLDLRKGTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 428 HSTKLIQEWnsVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 507
Cdd:cd24063 80 NSPNIKGKE--IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 508 LGHLVVSLD-GPDCSCGSHGCIEAYASGMALQREAKKL-HDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRT 585
Cdd:cd24063 158 VGHLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWaEGFSSRTSLKLRNPGGEGITAKEVFSAARKGDPLALKIIEK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1765945226 586 AGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 626
Cdd:cd24063 238 LARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEY 278
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
351-626 |
2.38e-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: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKK--YTQFNPKTYEErinlILQMCVEAAAEAVKLNC-RILGVGISTGGRVNPREGIVL 427
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEfeYRVITLETPEA----LIDEIIDCIDRLLKLWKdRVKGIALAIQGLVDSHKGVSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 428 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 507
Cdd:cd24072 80 WSPGA--PWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 508 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAG 587
Cdd:cd24072 158 IGHTKVNPDGARCDCGRRGCLETVASNSALKRNARV------TLKLGPVSADPEKLTMEQLIEALEEGEPIATQIFDRAA 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1765945226 588 TALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 626
Cdd:cd24072 232 NAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRA 270
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
350-610 |
4.92e-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: 146.10 E-value: 4.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYTQfnPKTYEERINLILQMCVEAAAEAVKlNCRILGVGISTGGRVNPREGIVLHS 429
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTI--DTKVENGKEDVINRIAETVNELIE-EMELLGIGIGSPGSIDRENGIVRFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 430 TKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 509
Cdd:cd24064 78 PNF-PDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 510 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDE--DLLlvegmsVPKDEAVGALHLIQAAKLGNAKAQSILRTAG 587
Cdd:cd24064 157 HVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRypDSL------AGESEKINAKHVFDAARKNDPLATMVFRRVV 230
|
250 260
....*....|....*....|...
gi 1765945226 588 TALGLGVVNILHTMNPSLVILSG 610
Cdd:cd24064 231 DALAIAIGGFVHIFNPEIIIIGG 253
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
351-625 |
1.30e-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: 142.60 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 428
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPaeEGPEAVLDRIAEL-IEELLAEAGVRERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 STKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiiH-----------QHEL 497
Cdd:cd23763 80 APNL-PWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYI-----------TlgtgigggiiiDGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 498 IHGSSFCAAELGHLVVsldgpdcscgshgcieayasgmalqreakklhdedlllvegmsvpkdeavgalhliqaaklgna 577
Cdd:cd23763 148 YRGANGAAGEIGHITV---------------------------------------------------------------- 163
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1765945226 578 kaqsiLRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIR 625
Cdd:cd23763 164 -----LEEAARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIRE 206
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
349-627 |
1.70e-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: 141.31 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 349 SALAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKlncRILGVGISTGGRVNPREGIVLH 428
Cdd:cd24065 1 STIGLDLGGTKIAAGVVD-GGRILSRLVVPTPREGGEAVLDALARAVEALQAEAP---GVEAVGLGVPGPLDFRRGRVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 STKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 508
Cdd:cd24065 77 APN-IPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 509 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDlllvegMSVPKdeavgalhLIQAAKLGNAKAQSILRTAGT 588
Cdd:cd24065 156 GHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRP------MSTAE--------LFELAQQGEPKALRIVEQAAA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1765945226 589 ALGLGVVNILHTMNPSLVILSGVLASH---YIHIVKDVIRQQ 627
Cdd:cd24065 222 HLGIGLANLQKALDPEVFVLGGGVAQVgdyYLLPVQEAARRY 263
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
351-610 |
1.99e-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: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErinLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVlHS 429
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 430 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 509
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 510 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 589
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260
....*....|....*....|.
gi 1765945226 590 LGLGVVNILHTMNPSLVILSG 610
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGG 241
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
351-610 |
6.32e-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: 6.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHST 430
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 431 KLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 510
Cdd:TIGR00744 81 NL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 511 LVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 589
Cdd:TIGR00744 159 IRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVARW 238
|
250 260
....*....|....*....|.
gi 1765945226 590 LGLGVVNILHTMNPSLVILSG 610
Cdd:TIGR00744 239 AGAGLADLASLFNPSAIVLGG 259
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
350-629 |
1.05e-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: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT--YEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 427
Cdd:cd24062 2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLegGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 428 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 507
Cdd:cd24062 82 VAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 508 LGHL-VVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTA 586
Cdd:cd24062 160 IGHItVNPEGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAVVDTV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1765945226 587 GTALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQAL 629
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGGGVSaagEFLLSPVKEYFDRFTF 285
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
350-627 |
9.80e-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: 113.40 E-value: 9.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKKYT-QFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREgiVLH 428
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQiKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVDENE--IIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 STKliQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKglENFVTLITgtgigggiiH---------QHELIH 499
Cdd:cd24077 81 TPY--YDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSEDY--DNLISISI---------HsgigagiiiNNQLYR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 500 GSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDedlllVEGMSVPkdeavgalHLIQAAKLGNAKA 579
Cdd:cd24077 148 GYNGFAGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKKG-----LETLTFD--------DLIQLYNEGDPEA 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1765945226 580 QSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDvIRQQ 627
Cdd:cd24077 215 LELIDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELLEK-IKEQ 261
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
351-610 |
1.82e-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: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEERINLILQMcveaaaeAVKLNCRILGVGISTGGRVNPREGIVLHS 429
Cdd:cd24152 3 LVFDIGGTFIKYALVDENGNIIKKGKIPTPKdSLEEFLDYIKKI-------IKRYDEEIDGIAISAPGVIDPETGIIYGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 430 TKLiqEWNS-VDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 508
Cdd:cd24152 76 GAL--PYLKgFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 509 GHLVVSLDGPDCSCGSHgcieaYASGMALQREAKKLHDedlllvegmsvpkDEAVGALHLIQAAKLGNAKAQSILRTAGT 588
Cdd:cd24152 154 SYLLTDDDDKDLLFFSG-----LASMFGLVKRYNKAKG-------------LEPLDGEEIFEKYAKGDEAAKKILDEYIR 215
|
250 260
....*....|....*....|..
gi 1765945226 589 ALGLGVVNILHTMNPSLVILSG 610
Cdd:cd24152 216 NLAKLIYNIQYILDPEVIVIGG 237
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
350-629 |
5.36e-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: 105.91 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIVKK----YTQFNPKTYEERInlilqmcVEAAAEAVKLNCR----ILGVGISTGGRVNP 421
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAEhtvpLTALNQEALLSQL-------IEEIAQFLKSHRRktqrLIAISITLPGLINP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 422 REGIVlHSTKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGS 501
Cdd:cd24075 76 KTGVV-HYMPHIQ-VKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 502 SFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDllLVEGMSvPKDEAVGAlhLIQAAKLGNAKAQS 581
Cdd:cd24075 154 NGNAGEIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQG--YASQLT-LQDCTIKD--ICQAALNGDQLAQD 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1765945226 582 ILRTAGTALGLGVVNILHTMNPSLVILSG--VLASHYIH-IVKDVIRQQAL 629
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 ... |
407-629 |
6.72e-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: 94.30 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 407 RILGVGISTGGRVNPREGIVLHSTKL-IQEWnsvdlrtPLSDTLH----LPVWVDNDGNCAALAERKFGQGKGLENFVTL 481
Cdd:cd24074 62 RLTAIAITLPGIIDPESGIVHRLPFYdIKNL-------PLGEALEqhtgLPVYVQHDISAWTLAERFFGAAKGAKNIIQI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 482 ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKL---HDEDLLLVEGMSVP 558
Cdd:cd24074 135 VIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLleqSPDSMLHGQPISIE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765945226 559 kdeavgalHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVL---ASHYIHIVKDVIRQQAL 629
Cdd:cd24074 215 --------SLCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLnnaAEILFPALSQSIRQQSL 280
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
352-613 |
1.52e-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: 92.68 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 352 AVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT-YEERINLILQMCVEAAAEAvklNCRiLGVGISTGGRVNPREGIVLhsT 430
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDdYAAFLAAIAELVAEADARF---GVK-GPVGIGIPGVIDPEDGTLI--T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 431 KLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 510
Cdd:cd24057 78 ANIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 511 LVVSLD----GPD-----CSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNAKAQS 581
Cdd:cd24057 158 GPLPADalllGYDlpvlrCGCGQTGCLETYLSGRGLERLYAHLYGEEL--------------DAPEIIAAWAAGDPQAVA 223
|
250 260 270
....*....|....*....|....*....|..
gi 1765945226 582 ILRTAGTALGLGVVNILHTMNPSLVILSGVLA 613
Cdd:cd24057 224 HVDRWLDLLAGCLANILTALDPDVVVLGGGLS 255
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
351-621 |
9.33e-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: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEerinliLQMCVEAAAE-AVKLNCRILGVGISTGGRVnpREGIVLH- 428
Cdd:cd24069 1 LAIDIGGTKIAAALIG-NGQIIDRRQIPTPRSGT------PEALADALASlLADYQGQFDRVAVASTGII--RDGVLTAl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 508
Cdd:cd24069 72 NPKNLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 509 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAkklhdedlllvegmSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 588
Cdd:cd24069 152 GHTLADPPGPVCGCGRRGCVEAIASGTAIAAAA--------------SEILGEPVDAKDVFERARSGDEEAARLIDRAAR 217
|
250 260 270
....*....|....*....|....*....|....*
gi 1765945226 589 ALGLGVVNILHTMNPSLVILSGV--LASHYIHIVK 621
Cdd:cd24069 218 ALADLIADLKATLDLDCVVIGGSvgLAEGFLERVE 252
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
351-610 |
3.30e-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: 88.42 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEERINLILQMcVEAAAEAVKLNCRilgVGISTGGRVNPREGIVLHS 429
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRgDYEATLDAIADL-VEEAEEELGAPAT---VGIGTPGSISPRTGLVKNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 430 tkliqewNSV-----DLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFC 504
Cdd:cd24066 78 -------NSTwlngkPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 505 AAELGHLVV------SLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNAK 578
Cdd:cd24066 151 AGEWGHNPLpwpdedELPGPPCYCGKRGCVETFLSGPALERDYARLTGKTL--------------SAEEIVALARAGDAA 216
|
250 260 270
....*....|....*....|....*....|..
gi 1765945226 579 AQSILRTAGTALGLGVVNILHTMNPSLVILSG 610
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. ... |
351-543 |
5.43e-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: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIV---KKYTQfNPKTYEERINLILQMcVEAAAEAVKLNCRilGVGISTGGRVNPREGIVL 427
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLdfeKVPSK-DLLRAGDPVEVLADL-IREYIEEAGLKPA--AIVIGVPGTVDKDRRTVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 428 HSTKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQ------------GKGLENFVTLItgtgigggiihqH 495
Cdd:cd24070 80 STPN-IPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNlddegvvlgfyiGTGIGNAILIN------------G 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1765945226 496 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 543
Cdd:cd24070 147 KPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEE 194
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
2-317 |
2.53e-16 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 80.88 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 2 IEQDDFDINtrlhtiVRGEDEAAMVesvGLALVKLPDVLNRLKPDIMIVHGD------------RfdalalatsaalMNI 69
Cdd:COG0381 55 IPKPDYDLG------IGSGSLAEQT---ARILEGLEEVLEEEKPDAVLVHGDtnstlaaalaafK------------LGI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 70 RILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWL 146
Cdd:COG0381 114 PVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTELARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 147 GddVKSKDYIVALQH-PVTTDIKHSIKMFeltLDALISFNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHV 223
Cdd:COG0381 194 G--LEPKKYILVTLHrRENVDDPERLENI---LEALRELAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 224 PFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVINL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGK 294
Cdd:COG0381 264 GYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCLTLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPA 336
|
330 340
....*....|....*....|....*..
gi 1765945226 295 QYPCSK----IYGDGNAVPRILKFLKS 317
Cdd:COG0381 337 AYERMAravnPYGDGNASERIVDILLR 363
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
352-548 |
3.54e-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: 73.35 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 352 AVDLGGTNLRVAIVSMKGEIVKKyTQFNPKTYEErinlILQMCVEAAAEAVKlncRILGVGISTGGRVNPRE-----GIV 426
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIER-TEFPTTTPEE----TLQAVIDFFREQEE---PIDAIGIASFGPIDLNPtsptyGYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 427 LHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFcaA 506
Cdd:cd24067 75 TTTPKP--GWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLH--P 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1765945226 507 ELGHLVVSLDGPDC----SCGSHG-CIEAYASGMAL----QREAKKLHDED 548
Cdd:cd24067 151 EMGHIRVPRHPDDDgfpgVCPFHGdCLEGLASGPAIaarwGIPAEELPDDH 201
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
351-627 |
5.93e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 73.02 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMCVEAAAEAVKlncrilgVGISTGGRVNprEGIVlh 428
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAALAERKfGQGKGLENFVTLITGTGIGGGIIHQHELIHG 500
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQ-ALPDDIRNMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 501 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNAKAQ 580
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1765945226 581 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 627
Cdd:PRK05082 212 ALINRSAQAIARLIADLKATLDCQCVVLGGSvgLAEGYLELVQAYLAQE 260
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
351-543 |
3.48e-10 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 61.54 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIV---KKYTQ--FNPKTYEERINLILQMCVEAAAeavklncRILGVGISTGGRVNPREGI 425
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILhceKKRTAevIAPDLVSGLGEMIDEYLRRFNA-------RCHGIVMGFPALVSKDRRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 426 VLHSTKL-IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERK-----------FGQGKGLENFVTLitgtgigggiih 493
Cdd:PRK09698 80 VISTPNLpLTALDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKennltqqlvlgAYLGTGMGFAVWM------------ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1765945226 494 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 543
Cdd:PRK09698 148 NGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQ 197
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
354-619 |
5.27e-10 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 61.16 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 354 DLGGTNLRVAIVSMKGEIVKKYTQFNPKT-YEERINLILQMCVEAAAeavKLNCRilG-VGISTGGRVNPREGIVLhsTK 431
Cdd:PRK13310 6 DIGGTKIELGVFNEKLELQWEERVPTPRDsYDAFLDAVCELVAEADQ---RFGCK--GsVGIGIPGMPETEDGTLY--AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 432 LIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHL 511
Cdd:PRK13310 79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 512 --------VVSLDGP--DCSCGSHGCIEAYASGMALQreakklhdedlLLVEGMsvpKDEAVGALHLIQAAKLGNAKAQS 581
Cdd:PRK13310 159 rlpvdaltLLGWDAPlrRCGCGQKGCIENYLSGRGFE-----------WLYQHY---YGEPLQAPEIIALYYQGDEQAVA 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1765945226 582 ILRTAGTALGLGVVNILHTMNPSLVILSGVLaSHYIHI 619
Cdd:PRK13310 225 HVERYLDLLAICLGNILTIVDPHLVVLGGGL-SNFDAI 261
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
6-316 |
2.98e-09 |
|
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: 59.39 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 6 DFDINTrlhtivrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDD 85
Cdd:TIGR00236 55 DYDLNI-------MSPGQTLGEITSNMLEGLEELLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 86 SI-----RHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDvksKDYIVALQ 160
Cdd:TIGR00236 128 PMpeeinRQLTGHIADLHFAPTEQAKDNLLRENVKADSIFVTGNTVIDALLTNVEIAYSSPVLSEFGED---KRMILLTL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 161 HPVTT------DIKHSIKmfeltldALISFNKRTLVLFPnidAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAH 234
Cdd:TIGR00236 205 HRRENvgepleNIFKAIR-------EIVEEFEDVQIVYP---VHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAAN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 235 AGCMIGNSSCGVREVGAFGTPVINL---GTRQIGRETGENVLHvrdADTQDKILQALHLQFGKQYPCSKI------YGDG 305
Cdd:TIGR00236 275 SHLILTDSGGVQEEAPSLGKPVLVLrdtTERPETVEAGTNKLV---GTDKENITKAAKRLLTDPDEYKKMsnasnpYGDG 351
|
330
....*....|.
gi 1765945226 306 NAVPRILKFLK 316
Cdd:TIGR00236 352 EASERIVEELL 362
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
351-481 |
1.14e-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: 53.34 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSM-KGEIVkkytqfnpktyEERINLIL-QMCV-EAAAEAVKLNCRILG----VGISTGGRVnpRE 423
Cdd:cd24058 2 LGIDIGGSGIKGAIVDTdTGELL-----------SERIRIPTpQPATpEAVADVVAELVAHFPwfgpVGVGFPGVV--RR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1765945226 424 GIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGK---GLENFVTL 481
Cdd:cd24058 69 GVVRTAANLDKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKgekGVVLVLTL 129
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
354-538 |
1.08e-06 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 50.41 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 354 DLGGTNLRVAIVSmkgEIVKKYTQFNPKTYEERINLILQMCVEAAAEAvKLNCRILG-VGISTGGRVNPREGIVLhsTKL 432
Cdd:PRK13311 6 DMGGTKIELGVFD---ENLQRIWHKRVPTPREDYPQLLQILRDLTEEA-DTYCGVQGsVGIGIPGLPNADDGTVF--TAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 433 IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLV 512
Cdd:PRK13311 80 VPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFR 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1765945226 513 VSLDGPD----------CSCGSHGCIEAYASGMALQ 538
Cdd:PRK13311 160 LPVDALDilgadiprvpCGCGHRGCIENYISGRGFE 195
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
353-544 |
1.32e-05 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 47.71 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 353 VDLGGTNLRVAIVSMKG-EIVKKYTQFNPKTYEERINLILQMCVEAAAEavkLNCR-ILGVGIStgGRVNPREGIV--LH 428
Cdd:PRK09557 5 IDLGGTKIEVIALDDAGeELFRKRLPTPRDDYQQTIEAIATLVDMAEQA---TGQRgTVGVGIP--GSISPYTGLVknAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 429 STkliqeW-NSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 507
Cdd:PRK09557 80 ST-----WlNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1765945226 508 LGHLVVSLDGPD---------CSCGSHGCIEAYASGMALQREAKKL 544
Cdd:PRK09557 155 WGHNPLPWMDEDelryrnevpCYCGKQGCIETFISGTGFATDYRRL 200
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
351-427 |
6.76e-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: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIVK------KYTQ---------FNPKTYEERinlILQMCVEAAAEAVKLNCRILGVGiST 415
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAiayrewEYYTdddypdakeFDPEELWEK---ICEAIREALKKAGISPEDISAVS-ST 78
|
90
....*....|..
gi 1765945226 416 GgrvnPREGIVL 427
Cdd:cd07798 79 S----QREGIVF 86
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
350-417 |
3.19e-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: 3.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765945226 350 ALAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPK--TYEERINLILQMCVEAAAEAVK----LNCRILGVGISTGG 417
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. ... |
351-415 |
1.10e-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: 1.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765945226 351 LAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPKTY--EERINLILQMCVEAAAEAVKL--NCRILGVGIST 415
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) ... |
337-370 |
2.25e-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: 2.25e-03
10 20 30
....*....|....*....|....*....|....
gi 1765945226 337 ISQDIDHiLETLSALAVDLGGTNLRVAIVSMKGE 370
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) ... |
346-370 |
3.83e-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: 3.83e-03
10 20
....*....|....*....|....*
gi 1765945226 346 ETLSALAVDLGGTNLRVAIVSMKGE 370
Cdd:cd24087 41 ETGDYLALDLGGTNLRVCLVKLGGN 65
|
|
| |
