|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
433-737 |
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: 570.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 433 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLH 512
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 592
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 593 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 672
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568927006 673 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 737
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
36-399 |
4.32e-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: 388.04 E-value: 4.32e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 36 RVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 115
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDP-DLELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 116 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 194
Cdd:TIGR03568 80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 195 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDVKcKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 272
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGIDLD-KPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 273 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 352
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568927006 353 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 399
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 ... |
36-400 |
8.11e-102 |
|
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: 317.23 E-value: 8.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 36 RVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 115
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDP-GLELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 116 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 192
Cdd:cd03786 77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 193 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKCKDYIVALQHPVTTDikHSIKMFELTLDALISFNKR- 271
Cdd:cd03786 156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTLHRRENV--DSGERLEELLEALEELAEKy 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 272 -TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIG 349
Cdd:cd03786 232 dLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTER 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 568927006 350 RETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 400
Cdd:cd03786 310 PERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
434-740 |
2.64e-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: 224.39 E-value: 2.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 511
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 512 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLItgtgigggiiHQHELIHGSSFCAAE 591
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTlgtgigggivINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 592 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNVKAQSILRTAG 671
Cdd:COG1940 166 IGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDPLALEVLDEAA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568927006 672 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGAASMVLD 740
Cdd:COG1940 233 RYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAALALE 306
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
62-400 |
1.48e-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: 207.39 E-value: 1.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 62 AFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 141
Cdd:pfam02350 6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 142 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLs 216
Cdd:pfam02350 80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 217 aknkDYMSIIRMWLG-DDVKCKDYIVALQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKk 293
Cdd:pfam02350 159 ----LSREEIEERSGiLAKLGKRYVLVTFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 294 gIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKI 368
Cdd:pfam02350 231 -LEGYPRVRLIEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERI 304
|
330 340 350
....*....|....*....|....*....|..
gi 568927006 369 LQALHLQFGKQYPCSKIYGDGNAVPRILKFLK 400
Cdd:pfam02350 305 VAALERLLEDPASYKNPYGDGNASERIVDILE 336
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
435-694 |
2.56e-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: 2.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErisLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVlHS 513
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 514 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 593
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 594 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNVKAQSILRTAGTA 673
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260
....*....|....*....|.
gi 568927006 674 LGLGVVNILHTMNPSLVILSG 694
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGG 241
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
435-694 |
1.34e-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: 137.34 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTyEERISLILQMCVEAAAEAV-KLNCRILGVGISTGGRVNPQEGVVLHS 513
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTT-PETIVDAIASAVDSFIQHIaKVGHEIVAIGIGAPGPVNRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 514 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 593
Cdd:TIGR00744 80 VNL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 594 HLVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 672
Cdd:TIGR00744 158 HIRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVAR 237
|
250 260
....*....|....*....|..
gi 568927006 673 ALGLGVVNILHTMNPSLVILSG 694
Cdd:TIGR00744 238 WAGAGLADLASLFNPSAIVLGG 259
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
49-401 |
2.63e-18 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 87.43 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 49 KLAPIMFGIKTEPAFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 123
Cdd:COG0381 16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 124 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 188
Cdd:COG0381 84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 189 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGddVKCKDYIVALQH-PVTTDIKHSIKMFeltLDALIS 267
Cdd:COG0381 152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELG--LEPKKYILVTLHrRENVDDPERLENI---LEALRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 268 FNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVI 341
Cdd:COG0381 227 LAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568927006 342 NL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 401
Cdd:COG0381 298 TLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
435-711 |
2.65e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 74.18 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERISLILQMCVEAAAEAVKlncrilgVGISTGGRVNpqEGVVlh 512
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAAMAERKFGQGKGQeNFVTLITGTGIGGGIIHQHELIHG 584
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQALPDDIR-NMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 585 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNVKAQ 664
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568927006 665 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 711
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 ... |
433-737 |
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: 570.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 433 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLH 512
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 592
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 593 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 672
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568927006 673 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 737
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
36-399 |
4.32e-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: 388.04 E-value: 4.32e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 36 RVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 115
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDP-DLELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 116 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 194
Cdd:TIGR03568 80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 195 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDVKcKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 272
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGIDLD-KPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 273 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 352
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568927006 353 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 399
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 ... |
36-400 |
8.11e-102 |
|
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: 317.23 E-value: 8.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 36 RVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 115
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDP-GLELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 116 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 192
Cdd:cd03786 77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 193 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKCKDYIVALQHPVTTDikHSIKMFELTLDALISFNKR- 271
Cdd:cd03786 156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTLHRRENV--DSGERLEELLEALEELAEKy 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 272 -TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIG 349
Cdd:cd03786 232 dLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTER 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 568927006 350 RETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 400
Cdd:cd03786 310 PERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
434-740 |
2.64e-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: 224.39 E-value: 2.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 511
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 512 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLItgtgigggiiHQHELIHGSSFCAAE 591
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTlgtgigggivINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 592 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNVKAQSILRTAG 671
Cdd:COG1940 166 IGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDPLALEVLDEAA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568927006 672 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGAASMVLD 740
Cdd:COG1940 233 RYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAALALE 306
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
62-400 |
1.48e-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: 207.39 E-value: 1.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 62 AFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 141
Cdd:pfam02350 6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 142 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLs 216
Cdd:pfam02350 80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 217 aknkDYMSIIRMWLG-DDVKCKDYIVALQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKk 293
Cdd:pfam02350 159 ----LSREEIEERSGiLAKLGKRYVLVTFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 294 gIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKI 368
Cdd:pfam02350 231 -LEGYPRVRLIEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERI 304
|
330 340 350
....*....|....*....|....*....|..
gi 568927006 369 LQALHLQFGKQYPCSKIYGDGNAVPRILKFLK 400
Cdd:pfam02350 305 VAALERLLEDPASYKNPYGDGNASERIVDILE 336
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
434-740 |
1.74e-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: 197.79 E-value: 1.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ-FNPK-TYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 511
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVpLPASdDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 512 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 591
Cdd:cd24076 83 LAPNL--GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 592 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEdlllVEGMSVPKdeavgalhLIQAAKLGNVKAQSILRTAG 671
Cdd:cd24076 161 IGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAG----GEPLSLAE--------LVEAARAGDPAALAALEEVG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568927006 672 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLD 740
Cdd:cd24076 229 EYLGIGLANLVNTFNPELVVLGGALAPlgpWLLPPLRAEVARRALPAPARDVRIVVSRlgEDAAALGAAALAID 302
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
434-694 |
1.49e-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: 183.91 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKY---TQFNpKTYEErislILQMCVEAAAEaVKLNCRILGVGISTGGRVNPQEGVV 510
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDsvpTPAS-KGGDA----ILERLLEIIAE-LKEKYDIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 511 LHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAA 590
Cdd:cd24068 76 IYATDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 591 ELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLlvegmsvpkdeavGALHLIQAAKLGNVKAQSILRTA 670
Cdd:cd24068 156 ELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGI-------------DGREIFDLADAGDPLAKEVVEEF 222
|
250 260
....*....|....*....|....
gi 568927006 671 GTALGLGVVNILHTMNPSLVILSG 694
Cdd:cd24068 223 AEDLATGLANLVHIFDPEVIVIGG 246
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
434-694 |
1.98e-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: 183.91 E-value: 1.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ----FNPKTYEERISLILQMCVEAAAEAVKlncRILGVGISTGGRVNPQEGV 509
Cdd:cd24073 3 VVGVKLTEDRITAVLTDLRGNVLASHTLpldsGDPEAVAEAIAEAVAELLAQAGLSPD---RLLGIGVGLPGLVDAETGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 510 VLHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCA 589
Cdd:cd24073 80 CRWSPLL--GWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 590 AELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvPKDEAVGALHLIQAAKLGNVKAQSILRT 669
Cdd:cd24073 158 GEIGHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAG------------LRGEPLTIEDLLAAARAGDPAARAILRR 225
|
250 260
....*....|....*....|....*
gi 568927006 670 AGTALGLGVVNILHTMNPSLVILSG 694
Cdd:cd24073 226 AGRALGLALANLVNLLDPELIIISG 250
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
434-741 |
2.61e-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: 175.47 E-value: 2.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIV--KKYTQFNPKTYEERISLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 511
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILarEKYPLDEKENPEEVLEKLYEL-IDRLLEKENIKSKILGIGIGAPGPLDVEKGIIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 512 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 591
Cdd:cd24059 82 NPPNF-PGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 592 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvEGMSVPKDEavgaLHLIQAAKLGNVKAQSILRTAG 671
Cdd:cd24059 161 IGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARS---------ALGSGRSFQ----LDIVEALQKGDPIADEVIEEAA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568927006 672 TALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLDY 741
Cdd:cd24059 228 KYLGIGLVNLINLLNPEAIIIGGELIylgERYLEPIEKEVNSRLFGRNAREVRILKSSlgEDAPLLGAAALVLNK 302
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
434-697 |
1.54e-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: 162.14 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVklncrILGVGISTGGRVNPQEGVVLHS 513
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPPTADGIVDAIVEAVEELREGHD-----VSAVGVAAAGFVDADRATVLFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 514 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 593
Cdd:cd24061 76 PNI--AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 594 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDED-----LLLVEGmsvpKDEAVGALHLIQAAKLGNVKAQSILR 668
Cdd:cd24061 154 HIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATpegaaVLLADG----SVDGITGKHISEAARAGDPVALDALR 229
|
250 260
....*....|....*....|....*....
gi 568927006 669 TAGTALGLGVVNILHTMNPSLVILSGVLA 697
Cdd:cd24061 230 ELARWLGAGLASLAALLDPELFVIGGGVS 258
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
434-694 |
1.04e-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: 157.45 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYT-QFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLH 512
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEKTRiPFDHETDPEKVIELIAENIKKLIKNKHVEKKLLGIGIAVSGLVDSKKGIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 STKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 592
Cdd:cd24071 83 STIL--GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 593 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLvegmSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 672
Cdd:cd24071 161 GHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLS----LLKELEDFEIEKVREAAEEGDSVATELFKKAGE 236
|
250 260
....*....|....*....|..
gi 568927006 673 ALGLGVVNILHTMNPSLVILSG 694
Cdd:cd24071 237 YLGIGIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
434-710 |
5.70e-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: 152.49 E-value: 5.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEER--ISLILQMCVEAAAEAVKLNcrILGVGISTGGRVNPQEGVVL 511
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGtvSEQVLGLIETLLSKAGKDS--IEGIGVSSAGPLDLRKGTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 512 HSTKLIQEWnsVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 591
Cdd:cd24063 80 NSPNIKGKE--IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 592 LGHLVVSLD-GPDCSCGSHGCIEAYASGMALQREAKKL-HDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRT 669
Cdd:cd24063 158 VGHLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWaEGFSSRTSLKLRNPGGEGITAKEVFSAARKGDPLALKIIEK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568927006 670 AGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 710
Cdd:cd24063 238 LARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEY 278
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
435-710 |
2.39e-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: 150.64 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKK--YTQFNPKTYEERISLILQMcveaAAEAVKLNC-RILGVGISTGGRVNPQEGVVL 511
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEfeYRVITLETPEALIDEIIDC----IDRLLKLWKdRVKGIALAIQGLVDSHKGVSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 512 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 591
Cdd:cd24072 80 WSPGA--PWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 592 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAG 671
Cdd:cd24072 158 IGHTKVNPDGARCDCGRRGCLETVASNSALKRNARV------TLKLGPVSADPEKLTMEQLIEALEEGEPIATQIFDRAA 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 568927006 672 TALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 710
Cdd:cd24072 232 NAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRA 270
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
434-694 |
8.13e-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: 8.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYTQfnPKTYEERISLILQMCVEAAAEAVKlNCRILGVGISTGGRVNPQEGVVLHS 513
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTI--DTKVENGKEDVINRIAETVNELIE-EMELLGIGIGSPGSIDRENGIVRFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 514 TKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 593
Cdd:cd24064 78 PNF-PDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 594 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDE--DLLlvegmsVPKDEAVGALHLIQAAKLGNVKAQSILRTAG 671
Cdd:cd24064 157 HVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRypDSL------AGESEKINAKHVFDAARKNDPLATMVFRRVV 230
|
250 260
....*....|....*....|...
gi 568927006 672 TALGLGVVNILHTMNPSLVILSG 694
Cdd:cd24064 231 DALAIAIGGFVHIFNPEIIIIGG 253
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
435-709 |
2.23e-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: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERISLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLH 512
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPaeEGPEAVLDRIAEL-IEELLAEAGVRERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 STKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLitgtgigggiiH-----------QHEL 581
Cdd:cd23763 80 APNL-PWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYI-----------TlgtgigggiiiDGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 582 IHGSSFCAAELGHLVVsldgpdcscgshgcieayasgmalqreakklhdedlllvegmsvpkdeavgalhliqaaklgnv 661
Cdd:cd23763 148 YRGANGAAGEIGHITV---------------------------------------------------------------- 163
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568927006 662 kaqsiLRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIR 709
Cdd:cd23763 164 -----LEEAARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIRE 206
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
435-694 |
2.56e-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: 2.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErisLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVlHS 513
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 514 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 593
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 594 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNVKAQSILRTAGTA 673
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260
....*....|....*....|.
gi 568927006 674 LGLGVVNILHTMNPSLVILSG 694
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGG 241
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
433-711 |
3.53e-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: 138.23 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 433 SALAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKlncRILGVGISTGGRVNPQEGVVLH 512
Cdd:cd24065 1 STIGLDLGGTKIAAGVVD-GGRILSRLVVPTPREGGEAVLDALARAVEALQAEAP---GVEAVGLGVPGPLDFRRGRVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 STKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 592
Cdd:cd24065 77 APN-IPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 593 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDlllvegMSVPKdeavgalhLIQAAKLGNVKAQSILRTAGT 672
Cdd:cd24065 156 GHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRP------MSTAE--------LFELAQQGEPKALRIVEQAAA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568927006 673 ALGLGVVNILHTMNPSLVILSGVLASH---YIHIVKDVIRQQ 711
Cdd:cd24065 222 HLGIGLANLQKALDPEVFVLGGGVAQVgdyYLLPVQEAARRY 263
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
435-694 |
1.34e-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: 137.34 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTyEERISLILQMCVEAAAEAV-KLNCRILGVGISTGGRVNPQEGVVLHS 513
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTT-PETIVDAIASAVDSFIQHIaKVGHEIVAIGIGAPGPVNRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 514 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 593
Cdd:TIGR00744 80 VNL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 594 HLVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 672
Cdd:TIGR00744 158 HIRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVAR 237
|
250 260
....*....|....*....|..
gi 568927006 673 ALGLGVVNILHTMNPSLVILSG 694
Cdd:TIGR00744 238 WAGAGLADLASLFNPSAIVLGG 259
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
434-713 |
1.35e-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: 134.34 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT--YEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVL 511
Cdd:cd24062 2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLegGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 512 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 591
Cdd:cd24062 82 VAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 592 LGHL-VVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTA 670
Cdd:cd24062 160 IGHItVNPEGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAVVDTV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568927006 671 GTALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQAL 713
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGGGVSaagEFLLSPVKEYFDRFTF 285
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
434-711 |
3.95e-29 |
|
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: 118.03 E-value: 3.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKKYT-QFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEgvVLH 512
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQiKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVDENE--IIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 STKliQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGkgQENFVTLITgtgigggiiH---------QHELIH 583
Cdd:cd24077 81 TPY--YDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSED--YDNLISISI---------HsgigagiiiNNQLYR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 584 GSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDedlllVEGMSVPkdeavgalHLIQAAKLGNVKA 663
Cdd:cd24077 148 GYNGFAGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKKG-----LETLTFD--------DLIQLYNEGDPEA 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568927006 664 QSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDvIRQQ 711
Cdd:cd24077 215 LELIDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELLEK-IKEQ 261
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
435-694 |
3.39e-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: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEErisLILQMCVEAAAEAVKLncrILGVGISTGGRVNPQEGVVLHST 514
Cdd:cd24152 3 LVFDIGGTFIKYALVDENGNIIKKGKIPTPKDSLE---EFLDYIKKIIKRYDEE---IDGIAISAPGVIDPETGIIYGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 515 KLiqEWNS-VDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 593
Cdd:cd24152 77 AL--PYLKgFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 594 HLVVSLDGPDCSCGSHgcieaYASGMALQREAKKLHDedlllvegmsvpkDEAVGALHLIQAAKLGNVKAQSILRTAGTA 673
Cdd:cd24152 155 YLLTDDDDKDLLFFSG-----LASMFGLVKRYNKAKG-------------LEPLDGEEIFEKYAKGDEAAKKILDEYIRN 216
|
250 260
....*....|....*....|.
gi 568927006 674 LGLGVVNILHTMNPSLVILSG 694
Cdd:cd24152 217 LAKLIYNIQYILDPEVIVIGG 237
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
434-713 |
4.43e-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: 103.60 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIVKK----YTQFNPKTYEERISLILQMCVEAaaEAVKLNcRILGVGISTGGRVNPQEGV 509
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAEhtvpLTALNQEALLSQLIEEIAQFLKS--HRRKTQ-RLIAISITLPGLINPKTGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 510 VlHSTKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCA 589
Cdd:cd24075 80 V-HYMPHIQ-VKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 590 AELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDllLVEGMSvPKDEAVGAlhLIQAAKLGNVKAQSILRT 669
Cdd:cd24075 158 GEIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQG--YASQLT-LQDCTIKD--ICQAALNGDQLAQDVIKR 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568927006 670 AGTALGLGVVNILHTMNPSLVILSG--VLASHYIH-IVKDVIRQQAL 713
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 ... |
491-713 |
1.34e-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: 96.61 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 491 RILGVGISTGGRVNPQEGVVLHSTKL-IQEWnsvdlrtPLSDTLH----LPVWVDNDGNCAAMAERKFGQGKGQENFVTL 565
Cdd:cd24074 62 RLTAIAITLPGIIDPESGIVHRLPFYdIKNL-------PLGEALEqhtgLPVYVQHDISAWTLAERFFGAAKGAKNIIQI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 566 ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKL---HDEDLLLVEGMSVP 642
Cdd:cd24074 135 VIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLleqSPDSMLHGQPISIE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568927006 643 kdeavgalHLIQAAKLGNVKAQSILRTAGTALGlgvvNILHTM----NPSLVILSGVL---ASHYIHIVKDVIRQQAL 713
Cdd:cd24074 215 --------SLCQAALAGDPLAQDIIIQVGRHLG----RILAILvnlfNPEKILIGSPLnnaAEILFPALSQSIRQQSL 280
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
435-694 |
1.85e-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: 92.61 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIV---KKYTQfNPKTYEERISLILQMcVEAAAEAVKLNCRilGVGISTGGRVNPQEGVVL 511
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLdfeKVPSK-DLLRAGDPVEVLADL-IREYIEEAGLKPA--AIVIGVPGTVDKDRRTVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 512 HSTKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQE------------NFVTLItgtgigggiihqH 579
Cdd:cd24070 80 STPN-IPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGvvlgfyigtgigNAILIN------------G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 580 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlHDEDlllvegmsVPkDEAVGALHlIQAAKLG 659
Cdd:cd24070 147 KPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEE-HYPD--------TP-ILDIFVDH-GDEPELD 215
|
250 260 270
....*....|....*....|....*....|....*.
gi 568927006 660 N-VKAQSIlrTAGTAlglgvVNILhtmNPSLVILSG 694
Cdd:cd24070 216 EfVEDLAL--AIATE-----INIL---DPDAVILGG 241
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
436-697 |
7.72e-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: 90.75 E-value: 7.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 436 AVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT-YEERISLILQMCVEAAAEAvklNCRiLGVGISTGGRVNPQEGVVLhsT 514
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDdYAAFLAAIAELVAEADARF---GVK-GPVGIGIPGVIDPEDGTLI--T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 515 KLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 594
Cdd:cd24057 78 ANIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 595 LVVSLD----GPD-----CSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNVKAQS 665
Cdd:cd24057 158 GPLPADalllGYDlpvlrCGCGQTGCLETYLSGRGLERLYAHLYGEEL--------------DAPEIIAAWAAGDPQAVA 223
|
250 260 270
....*....|....*....|....*....|..
gi 568927006 666 ILRTAGTALGLGVVNILHTMNPSLVILSGVLA 697
Cdd:cd24057 224 HVDRWLDLLAGCLANILTALDPDVVVLGGGLS 255
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
435-705 |
1.11e-19 |
|
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: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEerisliLQMCVEAAAE-AVKLNCRILGVGISTGGRVNpqEGVVLH- 512
Cdd:cd24069 1 LAIDIGGTKIAAALIG-NGQIIDRRQIPTPRSGT------PEALADALASlLADYQGQFDRVAVASTGIIR--DGVLTAl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 592
Cdd:cd24069 72 NPKNLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 593 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAkklhdedlllvegmSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGT 672
Cdd:cd24069 152 GHTLADPPGPVCGCGRRGCVEAIASGTAIAAAA--------------SEILGEPVDAKDVFERARSGDEEAARLIDRAAR 217
|
250 260 270
....*....|....*....|....*....|....*
gi 568927006 673 ALGLGVVNILHTMNPSLVILSGV--LASHYIHIVK 705
Cdd:cd24069 218 ALADLIADLKATLDLDCVVIGGSvgLAEGFLERVE 252
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
435-694 |
1.75e-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: 89.57 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEERISLILQMcVEAAAEAVKLNCRilgVGISTGGRVNPQEGVVLHS 513
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRgDYEATLDAIADL-VEEAEEELGAPAT---VGIGTPGSISPRTGLVKNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 514 tkliqewNSV-----DLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFC 588
Cdd:cd24066 78 -------NSTwlngkPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 589 AAELGHLVV------SLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNVK 662
Cdd:cd24066 151 AGEWGHNPLpwpdedELPGPPCYCGKRGCVETFLSGPALERDYARLTGKTL--------------SAEEIVALARAGDAA 216
|
250 260 270
....*....|....*....|....*....|..
gi 568927006 663 AQSILRTAGTALGLGVVNILHTMNPSLVILSG 694
Cdd:cd24066 217 AVATLDRFLDRLGRALANVINILDPDVIVLGG 248
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
49-401 |
2.63e-18 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 87.43 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 49 KLAPIMFGIKTEPAFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 123
Cdd:COG0381 16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 124 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 188
Cdd:COG0381 84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 189 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGddVKCKDYIVALQH-PVTTDIKHSIKMFeltLDALIS 267
Cdd:COG0381 152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELG--LEPKKYILVTLHrRENVDDPERLENI---LEALRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 268 FNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVI 341
Cdd:COG0381 227 LAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568927006 342 NL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 401
Cdd:COG0381 298 TLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
435-711 |
2.65e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 74.18 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERISLILQMCVEAAAEAVKlncrilgVGISTGGRVNpqEGVVlh 512
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAAMAERKFGQGKGQeNFVTLITGTGIGGGIIHQHELIHG 584
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQALPDDIR-NMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 585 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNVKAQ 664
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568927006 665 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 711
Cdd:PRK05082 212 ALINRSAQAIARLIADLKATLDCQCVVLGGSvgLAEGYLELVQAYLAQE 260
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
35-400 |
4.45e-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: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 35 LRVCVATCNRADYSKLAPIMFGIKTEPaFFELDVVVLGSHliddygntYRMIEQ--DDFDINTRlHTIVRGEDEAAMVES 112
Cdd:TIGR00236 1 LKVMIVLGTRPEAIKMAPLIRALKKYP-EIDSYVIVTAQH--------REMLDQvlDLFHLPPD-YDLNIMSPGQTLGEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 113 VGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSI-----RHAITKLAHYHVCCTR 187
Cdd:TIGR00236 71 TSNMLEGLEELLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMpeeinRQLTGHIADLHFAPTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 188 SAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDvkcKDYIVALQHPVTT------DIKHSIKmfelt 261
Cdd:TIGR00236 151 QAKDNLLRENVKADSIFVTGNTVIDALLTNVEIAYSSPVLSEFGED---KRMILLTLHRRENvgepleNIFKAIR----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 262 ldALISFNKRTLVLFPnidAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVI 341
Cdd:TIGR00236 223 --EIVEEFEDVQIVYP---VHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568927006 342 NL---GTRQIGRETGENVLHvrdADTQDKILQALHLQFGKQYPCSKI------YGDGNAVPRILKFLK 400
Cdd:TIGR00236 298 VLrdtTERPETVEAGTNKLV---GTDKENITKAAKRLLTDPDEYKKMsnasnpYGDGEASERIVEELL 362
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
436-632 |
1.51e-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: 71.81 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 436 AVDLGGTNLRVAIVSMKGEIVKKyTQFNPKTYEErislILQMCVEAAAEAVKlncRILGVGISTGG-----RVNPQEGVV 510
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIER-TEFPTTTPEE----TLQAVIDFFREQEE---PIDAIGIASFGpidlnPTSPTYGYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 511 LHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFcaA 590
Cdd:cd24067 75 TTTPKP--GWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLH--P 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568927006 591 ELGHLVVSLDGPDC----SCGSHG-CIEAYASGMAL----QREAKKLHDED 632
Cdd:cd24067 151 EMGHIRVPRHPDDDgfpgVCPFHGdCLEGLASGPAIaarwGIPAEELPDDH 201
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
435-627 |
5.01e-10 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 61.54 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIV---KKYTQ--FNPktyeERISLILQMCVEAAAEavkLNCRILGVGISTGGRVNPQEGV 509
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILhceKKRTAevIAP----DLVSGLGEMIDEYLRR---FNARCHGIVMGFPALVSKDRRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 510 VLHSTKL-IQEWNSVDLRTPLSDTLHLPVWVDNDGNCA----AMAERKFGQ-------GKGQENFVTLitgtgigggiih 577
Cdd:PRK09698 80 VISTPNLpLTALDLYDLADKLENTLNCPVFFSRDVNLQllwdVKENNLTQQlvlgaylGTGMGFAVWM------------ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568927006 578 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 627
Cdd:PRK09698 148 NGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQ 197
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
438-703 |
2.48e-08 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 56.15 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 438 DLGGTNLRVAIVSMKGEivKKYTQFNPkTYEERISLILQMCVEAAAEA-VKLNCRilG-VGISTGGRVNPQEGVVLhsTK 515
Cdd:PRK13310 6 DIGGTKIELGVFNEKLE--LQWEERVP-TPRDSYDAFLDAVCELVAEAdQRFGCK--GsVGIGIPGMPETEDGTLY--AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 516 LIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHL 595
Cdd:PRK13310 79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 596 --------VVSLDGP--DCSCGSHGCIEAYASGMALQreakklhdedlLLVEGMsvpKDEAVGALHLIQAAKLGNVKAQS 665
Cdd:PRK13310 159 rlpvdaltLLGWDAPlrRCGCGQKGCIENYLSGRGFE-----------WLYQHY---YGEPLQAPEIIALYYQGDEQAVA 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 568927006 666 ILRTAGTALGLGVVNILHTMNPSLVILSGVLaSHYIHI 703
Cdd:PRK13310 225 HVERYLDLLAICLGNILTIVDPHLVVLGGGL-SNFDAI 261
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
435-563 |
4.06e-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: 51.80 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSM-KGEIVkkytqfnpktyEERISLIL-QMCV-EAAAEAVKLNCRILG----VGISTGGRVnpQE 507
Cdd:cd24058 2 LGIDIGGSGIKGAIVDTdTGELL-----------SERIRIPTpQPATpEAVADVVAELVAHFPwfgpVGVGFPGVV--RR 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568927006 508 GVVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFV 563
Cdd:cd24058 69 GVVRTAANLDKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVV 124
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
438-622 |
9.94e-07 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 50.80 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 438 DLGGTNLRVAIVSmkgEIVKKYTQFNPKTYEERISLILQMCVEAAAEAvKLNCRILG-VGISTGGRVNPQEGVVLhsTKL 516
Cdd:PRK13311 6 DMGGTKIELGVFD---ENLQRIWHKRVPTPREDYPQLLQILRDLTEEA-DTYCGVQGsVGIGIPGLPNADDGTVF--TAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 517 IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLV 596
Cdd:PRK13311 80 VPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFR 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 568927006 597 VSLDGPD----------CSCGSHGCIEAYASGMALQ 622
Cdd:PRK13311 160 LPVDALDilgadiprvpCGCGHRGCIENYISGRGFE 195
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
437-628 |
1.03e-05 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 48.10 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 437 VDLGGTNLRVAIVSMKG-EIVKKYTQFNPKTYEERISLILQMCVEAAAEavkLNCR-ILGVGIStgGRVNPQEGVV--LH 512
Cdd:PRK09557 5 IDLGGTKIEVIALDDAGeELFRKRLPTPRDDYQQTIEAIATLVDMAEQA---TGQRgTVGVGIP--GSISPYTGLVknAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 513 STkliqeW-NSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 591
Cdd:PRK09557 80 ST-----WlNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568927006 592 LGHLVVSLDGPD---------CSCGSHGCIEAYASGMALQREAKKL 628
Cdd:PRK09557 155 WGHNPLPWMDEDelryrnevpCYCGKQGCIETFISGTGFATDYRRL 200
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
435-511 |
5.12e-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: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIVK------KYTQ---------FNPKTYEERislILQMCVEAAAEAVKLNCRILGVGiST 499
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAiayrewEYYTdddypdakeFDPEELWEK---ICEAIREALKKAGISPEDISAVS-ST 78
|
90
....*....|..
gi 568927006 500 GGRvnpqEGVVL 511
Cdd:cd07798 79 SQR----EGIVF 86
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
434-501 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568927006 434 ALAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPK--TYEERISLILQMCVEAAAEAVK----LNCRILGVGISTGG 501
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) ... |
421-454 |
2.18e-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: 41.11 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|....
gi 568927006 421 ISQDIDHiLETLSALAVDLGGTNLRVAIVSMKGE 454
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. ... |
435-499 |
3.36e-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: 3.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568927006 435 LAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPKTY--EERISLILQMCVEAAAEAVKL--NCRILGVGIST 499
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) ... |
430-454 |
4.44e-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: 4.44e-03
10 20
....*....|....*....|....*
gi 568927006 430 ETLSALAVDLGGTNLRVAIVSMKGE 454
Cdd:cd24087 41 ETGDYLALDLGGTNLRVCLVKLGGN 65
|
|
| |
