|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
439-743 |
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: 576.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 439 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 518
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 598
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 599 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 678
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190014632 679 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 743
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
42-405 |
7.20e-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: 387.65 E-value: 7.20e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 42 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 121
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDPDL-ELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 122 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 200
Cdd:TIGR03568 80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 201 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDvKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 278
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGID-LDKPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 279 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 358
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 190014632 359 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 405
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 ... |
42-406 |
5.94e-103 |
|
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: 320.69 E-value: 5.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 42 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 121
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDPGL-ELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 122 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 198
Cdd:cd03786 77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 199 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKSKDYIVALQHPVTTDikHSIKMFELTLDALISFNKR- 277
Cdd:cd03786 156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTLHRRENV--DSGERLEELLEALEELAEKy 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 278 -TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIG 355
Cdd:cd03786 232 dLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTER 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 190014632 356 RETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 406
Cdd:cd03786 310 PERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
440-746 |
8.22e-69 |
|
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: 228.63 E-value: 8.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 517
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 518 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiI----------HQHEL 587
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYL----------TlgtgigggivINGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 588 IHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNA 667
Cdd:COG1940 156 LRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 668 KAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGAAS 742
Cdd:COG1940 223 LALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAA 302
|
....
gi 190014632 743 MVLD 746
Cdd:COG1940 303 LALE 306
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
68-406 |
3.90e-61 |
|
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: 208.93 E-value: 3.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 68 EFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 147
Cdd:pfam02350 6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 148 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLs 222
Cdd:pfam02350 80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 223 aknkDYMSIIRMWLG-DDVKSKDYIVALQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKk 299
Cdd:pfam02350 159 ----LSREEIEERSGiLAKLGKRYVLVTFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 300 gIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKI 374
Cdd:pfam02350 231 -LEGYPRVRLIEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERI 304
|
330 340 350
....*....|....*....|....*....|..
gi 190014632 375 LQALHLQFGKQYPCSKIYGDGNAVPRILKFLK 406
Cdd:pfam02350 305 VAALERLLEDPASYKNPYGDGNASERIVDILE 336
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
441-700 |
1.22e-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: 136.70 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErinLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVlHS 519
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 520 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 599
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 600 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 679
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260
....*....|....*....|.
gi 190014632 680 LGLGVVNILHTMNPSLVILSG 700
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGG 241
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
441-700 |
6.00e-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: 135.41 E-value: 6.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHST 520
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 521 KLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 600
Cdd:TIGR00744 81 NL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 601 LVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 679
Cdd:TIGR00744 159 IRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVARW 238
|
250 260
....*....|....*....|.
gi 190014632 680 LGLGVVNILHTMNPSLVILSG 700
Cdd:TIGR00744 239 AGAGLADLASLFNPSAIVLGG 259
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
55-407 |
1.18e-19 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 91.28 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 55 KLAPIMFGIKTEPEFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 129
Cdd:COG0381 16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 130 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 194
Cdd:COG0381 84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 195 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGddVKSKDYIVALQH-PVTTDIKHSIKMFeltLDALIS 273
Cdd:COG0381 152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELG--LEPKKYILVTLHrRENVDDPERLENI---LEALRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 274 FNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVI 347
Cdd:COG0381 227 LAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190014632 348 NL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 407
Cdd:COG0381 298 TLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
441-717 |
2.22e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 74.18 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMCVEAAAEAVKlncrilgVGISTGGRVNprEGIVlh 518
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAALAERKfGQGKGLENFVTLITGTGIGGGIIHQHELIHG 590
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQ-ALPDDIRNMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 591 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNAKAQ 670
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 190014632 671 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 717
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 ... |
439-743 |
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: 576.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 439 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 518
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 598
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 599 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 678
Cdd:cd24060 161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190014632 679 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 743
Cdd:cd24060 241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
42-405 |
7.20e-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: 387.65 E-value: 7.20e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 42 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 121
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDPDL-ELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 122 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 200
Cdd:TIGR03568 80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 201 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDvKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 278
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGID-LDKPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 279 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 358
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 190014632 359 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 405
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 ... |
42-406 |
5.94e-103 |
|
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: 320.69 E-value: 5.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 42 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 121
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDPGL-ELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 122 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 198
Cdd:cd03786 77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 199 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKSKDYIVALQHPVTTDikHSIKMFELTLDALISFNKR- 277
Cdd:cd03786 156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTLHRRENV--DSGERLEELLEALEELAEKy 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 278 -TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIG 355
Cdd:cd03786 232 dLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTER 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 190014632 356 RETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 406
Cdd:cd03786 310 PERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
440-746 |
8.22e-69 |
|
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: 228.63 E-value: 8.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ--FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 517
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIptPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 518 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiI----------HQHEL 587
Cdd:COG1940 87 NAPNL-PGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYL----------TlgtgigggivINGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 588 IHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLGNA 667
Cdd:COG1940 156 LRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAGDP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 668 KAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGAAS 742
Cdd:COG1940 223 LALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGAAA 302
|
....
gi 190014632 743 MVLD 746
Cdd:COG1940 303 LALE 306
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
68-406 |
3.90e-61 |
|
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: 208.93 E-value: 3.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 68 EFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 147
Cdd:pfam02350 6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 148 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLs 222
Cdd:pfam02350 80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 223 aknkDYMSIIRMWLG-DDVKSKDYIVALQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKk 299
Cdd:pfam02350 159 ----LSREEIEERSGiLAKLGKRYVLVTFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 300 gIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKI 374
Cdd:pfam02350 231 -LEGYPRVRLIEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERI 304
|
330 340 350
....*....|....*....|....*....|..
gi 190014632 375 LQALHLQFGKQYPCSKIYGDGNAVPRILKFLK 406
Cdd:pfam02350 305 VAALERLLEDPASYKNPYGDGNASERIVDILE 336
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
440-746 |
1.89e-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: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ-FNPK-TYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 517
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVpLPASdDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 518 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 597
Cdd:cd24076 83 LAPNL--GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 598 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEdlllVEGMSVPKdeavgalhLIQAAKLGNAKAQSILRTAG 677
Cdd:cd24076 161 IGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAG----GEPLSLAE--------LVEAARAGDPAALAALEEVG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190014632 678 TALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLD 746
Cdd:cd24076 229 EYLGIGLANLVNTFNPELVVLGGALAPlgpWLLPPLRAEVARRALPAPARDVRIVVSRlgEDAAALGAAALAID 302
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
440-700 |
3.55e-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: 188.54 E-value: 3.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKY---TQFNpKTYEERINLILQmcveaAAEAVKLNCRILGVGISTGGRVNPREGIV 516
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDsvpTPAS-KGGDAILERLLE-----IIAELKEKYDIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 517 LHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAA 596
Cdd:cd24068 76 IYATDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 597 ELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLlvegmsvpkdeavGALHLIQAAKLGNAKAQSILRTA 676
Cdd:cd24068 156 ELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGI-------------DGREIFDLADAGDPLAKEVVEEF 222
|
250 260
....*....|....*....|....
gi 190014632 677 GTALGLGVVNILHTMNPSLVILSG 700
Cdd:cd24068 223 AEDLATGLANLVHIFDPEVIVIGG 246
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
440-700 |
1.35e-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: 187.37 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYTQ-FNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 518
Cdd:cd24073 3 VVGVKLTEDRITAVLTDLRGNVLASHTLpLDSGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGICRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 STKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 598
Cdd:cd24073 83 SPLL--GWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 599 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 678
Cdd:cd24073 161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAG------------LRGEPLTIEDLLAAARAGDPAARAILRRAGR 228
|
250 260
....*....|....*....|..
gi 190014632 679 ALGLGVVNILHTMNPSLVILSG 700
Cdd:cd24073 229 ALGLALANLVNLLDPELIIISG 250
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
440-747 |
1.25e-50 |
|
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: 179.32 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIV--KKYTQFNPKTYEERINLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 517
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILarEKYPLDEKENPEEVLEKLYEL-IDRLLEKENIKSKILGIGIGAPGPLDVEKGIIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 518 HSTKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 597
Cdd:cd24059 82 NPPNF-PGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 598 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvEGMSVPKDEavgaLHLIQAAKLGNAKAQSILRTAG 677
Cdd:cd24059 161 IGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARS---------ALGSGRSFQ----LDIVEALQKGDPIADEVIEEAA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190014632 678 TALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGAASMVLDY 747
Cdd:cd24059 228 KYLGIGLVNLINLLNPEAIIIGGELIylgERYLEPIEKEVNSRLFGRNAREVRILKSSlgEDAPLLGAAALVLNK 302
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
440-703 |
7.05e-45 |
|
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: 163.29 E-value: 7.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVklncrILGVGISTGGRVNPREGIVLHS 519
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPPTADGIVDAIVEAVEELREGHD-----VSAVGVAAAGFVDADRATVLFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 520 TKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 599
Cdd:cd24061 76 PNI--AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 600 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDED-----LLLVEGmsvpKDEAVGALHLIQAAKLGNAKAQSILR 674
Cdd:cd24061 154 HIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATpegaaVLLADG----SVDGITGKHISEAARAGDPVALDALR 229
|
250 260
....*....|....*....|....*....
gi 190014632 675 TAGTALGLGVVNILHTMNPSLVILSGVLA 703
Cdd:cd24061 230 ELARWLGAGLASLAALLDPELFVIGGGVS 258
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
440-700 |
5.47e-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: 160.91 E-value: 5.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKyTQF---NPKTYEERINLILQmCVEAAAEAVKLNCRILGVGISTGGRVNPREGIV 516
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEK-TRIpfdHETDPEKVIELIAE-NIKKLIKNKHVEKKLLGIGIAVSGLVDSKKGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 517 LHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAA 596
Cdd:cd24071 81 IRSTIL--GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 597 ELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLvegmSVPKDEAVGALHLIQAAKLGNAKAQSILRTA 676
Cdd:cd24071 159 EIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLS----LLKELEDFEIEKVREAAEEGDSVATELFKKA 234
|
250 260
....*....|....*....|....
gi 190014632 677 GTALGLGVVNILHTMNPSLVILSG 700
Cdd:cd24071 235 GEYLGIGIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
440-716 |
2.10e-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: 156.35 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEER--INLILQMCVEAAAEAVKLNcrILGVGISTGGRVNPREGIVL 517
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGtvSEQVLGLIETLLSKAGKDS--IEGIGVSSAGPLDLRKGTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 518 HSTKLIQEWnsVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 597
Cdd:cd24063 80 NSPNIKGKE--IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 598 LGHLVVSLD-GPDCSCGSHGCIEAYASGMALQREAKKL-HDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRT 675
Cdd:cd24063 158 VGHLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWaEGFSSRTSLKLRNPGGEGITAKEVFSAARKGDPLALKIIEK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 190014632 676 AGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 716
Cdd:cd24063 238 LARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEY 278
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
441-716 |
2.37e-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: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKK--YTQFNPKTYEErinlILQMCVEAAAEAVKLNC-RILGVGISTGGRVNPREGIVL 517
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEfeYRVITLETPEA----LIDEIIDCIDRLLKLWKdRVKGIALAIQGLVDSHKGVSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 518 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 597
Cdd:cd24072 80 WSPGA--PWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 598 LGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAG 677
Cdd:cd24072 158 IGHTKVNPDGARCDCGRRGCLETVASNSALKRNARV------TLKLGPVSADPEKLTMEQLIEALEEGEPIATQIFDRAA 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 190014632 678 TALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 716
Cdd:cd24072 232 NAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRA 270
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
441-715 |
2.71e-39 |
|
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: 145.30 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMcVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLH 518
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPaeEGPEAVLDRIAEL-IEELLAEAGVRERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 STKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLitgtgigggiiH-----------QHEL 587
Cdd:cd23763 80 APNL-PWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYI-----------TlgtgigggiiiDGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 588 IHGSSFCAAELGHLVVsldgpdcscgshgcieayasgmalqreakklhdedlllvegmsvpkdeavgalhliqaaklgna 667
Cdd:cd23763 148 YRGANGAAGEIGHITV---------------------------------------------------------------- 163
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 190014632 668 kaqsiLRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIR 715
Cdd:cd23763 164 -----LEEAARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIRE 206
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
440-700 |
5.39e-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: 146.49 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYTQfnPKTYEERINLILQMCVEAAAEAVKlNCRILGVGISTGGRVNPREGIVLHS 519
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTI--DTKVENGKEDVINRIAETVNELIE-EMELLGIGIGSPGSIDRENGIVRFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 520 TKLiQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 599
Cdd:cd24064 78 PNF-PDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 600 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDE--DLLlvegmsVPKDEAVGALHLIQAAKLGNAKAQSILRTAG 677
Cdd:cd24064 157 HVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRypDSL------AGESEKINAKHVFDAARKNDPLATMVFRRVV 230
|
250 260
....*....|....*....|...
gi 190014632 678 TALGLGVVNILHTMNPSLVILSG 700
Cdd:cd24064 231 DALAIAIGGFVHIFNPEIIIIGG 253
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
439-717 |
1.43e-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: 142.08 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 439 SALAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKlncRILGVGISTGGRVNPREGIVLH 518
Cdd:cd24065 1 STIGLDLGGTKIAAGVVD-GGRILSRLVVPTPREGGEAVLDALARAVEALQAEAP---GVEAVGLGVPGPLDFRRGRVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 STKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 598
Cdd:cd24065 77 APN-IPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 599 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDlllvegMSVPKdeavgalhLIQAAKLGNAKAQSILRTAGT 678
Cdd:cd24065 156 GHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRP------MSTAE--------LFELAQQGEPKALRIVEQAAA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 190014632 679 ALGLGVVNILHTMNPSLVILSGVLASH---YIHIVKDVIRQQ 717
Cdd:cd24065 222 HLGIGLANLQKALDPEVFVLGGGVAQVgdyYLLPVQEAARRY 263
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
441-700 |
1.22e-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: 136.70 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEErinLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVlHS 519
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTtTTEE---TLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYI-TN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 520 TKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELG 599
Cdd:pfam00480 77 TPNIG-WDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 600 HLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 679
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQGDEVAEEAVERLARY 220
|
250 260
....*....|....*....|.
gi 190014632 680 LGLGVVNILHTMNPSLVILSG 700
Cdd:pfam00480 221 LAKAIANLINLFDPQAIVLGG 241
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
441-700 |
6.00e-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: 135.41 E-value: 6.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHST 520
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 521 KLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 600
Cdd:TIGR00744 81 NL--DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 601 LVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTA 679
Cdd:TIGR00744 159 IRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVARW 238
|
250 260
....*....|....*....|.
gi 190014632 680 LGLGVVNILHTMNPSLVILSG 700
Cdd:TIGR00744 239 AGAGLADLASLFNPSAIVLGG 259
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
440-719 |
5.98e-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: 132.41 E-value: 5.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT--YEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVL 517
Cdd:cd24062 2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLegGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 518 HSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 597
Cdd:cd24062 82 VAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 598 LGHL-VVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTA 676
Cdd:cd24062 160 IGHItVNPEGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAVVDTV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 190014632 677 GTALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQAL 719
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGGGVSaagEFLLSPVKEYFDRFTF 285
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
440-717 |
1.10e-27 |
|
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: 113.79 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKKYT-QFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREgiVLH 518
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQiKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVDENE--IIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 STKliQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKglENFVTLITgtgigggiiH---------QHELIH 589
Cdd:cd24077 81 TPY--YDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSEDY--DNLISISI---------HsgigagiiiNNQLYR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 590 GSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDedlllVEGMSVPkdeavgalHLIQAAKLGNAKA 669
Cdd:cd24077 148 GYNGFAGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKKG-----LETLTFD--------DLIQLYNEGDPEA 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 190014632 670 QSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDvIRQQ 717
Cdd:cd24077 215 LELIDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELLEK-IKEQ 261
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
440-719 |
2.54e-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: 107.45 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIVKK----YTQFNPKTYEERInlilqmcVEAAAEAVKLNCR----ILGVGISTGGRVNP 511
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAEhtvpLTALNQEALLSQL-------IEEIAQFLKSHRRktqrLIAISITLPGLINP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 512 REGIVlHSTKLIQeWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGS 591
Cdd:cd24075 76 KTGVV-HYMPHIQ-VKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 592 SFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDllLVEGMSvPKDEAVGAlhLIQAAKLGNAKAQS 671
Cdd:cd24075 154 NGNAGEIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQG--YASQLT-LQDCTIKD--ICQAALNGDQLAQD 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 190014632 672 ILRTAGTALGLGVVNILHTMNPSLVILSG--VLASHYIH-IVKDVIRQQAL 719
Cdd:cd24075 229 VIKRAGRYLGKVIAILINLLNPQKIIIAGeiTQADKVLLpVIKKCIQSQAL 279
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
441-700 |
2.58e-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: 106.50 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEERINLILQMcveaaaeAVKLNCRILGVGISTGGRVNPREGIVLHS 519
Cdd:cd24152 3 LVFDIGGTFIKYALVDENGNIIKKGKIPTPKdSLEEFLDYIKKI-------IKRYDEEIDGIAISAPGVIDPETGIIYGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 520 TKLiqEWNS-VDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 598
Cdd:cd24152 76 GAL--PYLKgFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 599 GHLVVSLDGPDCSCGSHgcieaYASGMALQREAKKLHDedlllvegmsvpkDEAVGALHLIQAAKLGNAKAQSILRTAGT 678
Cdd:cd24152 154 SYLLTDDDDKDLLFFSG-----LASMFGLVKRYNKAKG-------------LEPLDGEEIFEKYAKGDEAAKKILDEYIR 215
|
250 260
....*....|....*....|..
gi 190014632 679 ALGLGVVNILHTMNPSLVILSG 700
Cdd:cd24152 216 NLAKLIYNIQYILDPEVIVIGG 237
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
497-719 |
4.78e-21 |
|
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466924 [Multi-domain] Cd Length: 322 Bit Score: 94.69 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 497 RILGVGISTGGRVNPREGIVLHSTKL-IQEWnsvdlrtPLSDTLH----LPVWVDNDGNCAALAERKFGQGKGLENFVTL 571
Cdd:cd24074 62 RLTAIAITLPGIIDPESGIVHRLPFYdIKNL-------PLGEALEqhtgLPVYVQHDISAWTLAERFFGAAKGAKNIIQI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 572 ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKL---HDEDLLLVEGMSVP 648
Cdd:cd24074 135 VIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLleqSPDSMLHGQPISIE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190014632 649 kdeavgalHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVL---ASHYIHIVKDVIRQQAL 719
Cdd:cd24074 215 --------SLCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLnnaAEILFPALSQSIRQQSL 280
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
442-703 |
7.91e-21 |
|
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: 93.84 E-value: 7.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 442 AVDLGGTNLRVAIVSMKGEIVKKYTQFNPKT-YEERINLILQMCVEAAAEAvklNCRiLGVGISTGGRVNPREGIVLhsT 520
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDdYAAFLAAIAELVAEADARF---GVK-GPVGIGIPGVIDPEDGTLI--T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 521 KLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH 600
Cdd:cd24057 78 ANIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 601 LVVSLD----GPD-----CSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNAKAQS 671
Cdd:cd24057 158 GPLPADalllGYDlpvlrCGCGQTGCLETYLSGRGLERLYAHLYGEEL--------------DAPEIIAAWAAGDPQAVA 223
|
250 260 270
....*....|....*....|....*....|..
gi 190014632 672 ILRTAGTALGLGVVNILHTMNPSLVILSGVLA 703
Cdd:cd24057 224 HVDRWLDLLAGCLANILTALDPDVVVLGGGLS 255
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
441-711 |
3.28e-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: 91.58 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSmKGEIVKKYTQFNPKTYEerinliLQMCVEAAAE-AVKLNCRILGVGISTGGRVnpREGIVLH- 518
Cdd:cd24069 1 LAIDIGGTKIAAALIG-NGQIIDRRQIPTPRSGT------PEALADALASlLADYQGQFDRVAVASTGII--RDGVLTAl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 STKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAEL 598
Cdd:cd24069 72 NPKNLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 599 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAkklhdedlllvegmSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 678
Cdd:cd24069 152 GHTLADPPGPVCGCGRRGCVEAIASGTAIAAAA--------------SEILGEPVDAKDVFERARSGDEEAARLIDRAAR 217
|
250 260 270
....*....|....*....|....*....|....*
gi 190014632 679 ALGLGVVNILHTMNPSLVILSGV--LASHYIHIVK 711
Cdd:cd24069 218 ALADLIADLKATLDLDCVVIGGSvgLAEGFLERVE 252
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
55-407 |
1.18e-19 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 91.28 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 55 KLAPIMFGIKTEPEFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 129
Cdd:COG0381 16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 130 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 194
Cdd:COG0381 84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 195 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGddVKSKDYIVALQH-PVTTDIKHSIKMFeltLDALIS 273
Cdd:COG0381 152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELG--LEPKKYILVTLHrRENVDDPERLENI---LEALRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 274 FNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVI 347
Cdd:COG0381 227 LAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190014632 348 NL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 407
Cdd:COG0381 298 TLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
441-700 |
2.17e-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: 89.19 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNPK-TYEERINLILQMcVEAAAEAVKLNCRilgVGISTGGRVNPREGIVLHS 519
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRgDYEATLDAIADL-VEEAEEELGAPAT---VGIGTPGSISPRTGLVKNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 520 tkliqewNSV-----DLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFC 594
Cdd:cd24066 78 -------NSTwlngkPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 595 AAELGHLVV------SLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLIQAAKLGNAK 668
Cdd:cd24066 151 AGEWGHNPLpwpdedELPGPPCYCGKRGCVETFLSGPALERDYARLTGKTL--------------SAEEIVALARAGDAA 216
|
250 260 270
....*....|....*....|....*....|..
gi 190014632 669 AQSILRTAGTALGLGVVNILHTMNPSLVILSG 700
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. ... |
441-633 |
4.27e-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: 88.38 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIV---KKYTQfNPKTYEERINLILQMcVEAAAEAVKLNCRilGVGISTGGRVNPREGIVL 517
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLdfeKVPSK-DLLRAGDPVEVLADL-IREYIEEAGLKPA--AIVIGVPGTVDKDRRTVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 518 HSTKlIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQ------------GKGLENFVTLItgtgigggiihqH 585
Cdd:cd24070 80 STPN-IPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNlddegvvlgfyiGTGIGNAILIN------------G 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 190014632 586 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 633
Cdd:cd24070 147 KPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEE 194
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
441-717 |
2.22e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 74.18 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMCVEAAAEAVKlncrilgVGISTGGRVNprEGIVlh 518
Cdd:PRK05082 4 LAIDIGGTKIAAALVGEDGQIRQRRQIPTPasQTPEALRQALSALVSPLQAQADR-------VAVASTGIIN--DGIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 sTKLiqewNSVDL----RTPLSDTLH----LPVWVDNDGNCAALAERKfGQGKGLENFVTLITGTGIGGGIIHQHELIHG 590
Cdd:PRK05082 73 -TAL----NPHNLggllHFPLVQTLEqltdLPTIALNDAQAAAWAEYQ-ALPDDIRNMVFITVSTGVGGGIVLNGKLLTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 591 SSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAKlGNAKAQ 670
Cdd:PRK05082 147 PGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ-GDEQAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 190014632 671 SILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 717
Cdd:PRK05082 212 ALINRSAQAIARLIADLKATLDCQCVVLGGSvgLAEGYLELVQAYLAQE 260
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
442-638 |
2.53e-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: 74.12 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 442 AVDLGGTNLRVAIVSMKGEIVKKyTQFNPKTYEErinlILQMCVEAAAEAVKlncRILGVGISTGGRVNPRE-----GIV 516
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIER-TEFPTTTPEE----TLQAVIDFFREQEE---PIDAIGIASFGPIDLNPtsptyGYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 517 LHSTKLiqEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFcaA 596
Cdd:cd24067 75 TTTPKP--GWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLH--P 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 190014632 597 ELGHLVVSLDGPDC----SCGSHG-CIEAYASGMAL----QREAKKLHDED 638
Cdd:cd24067 151 EMGHIRVPRHPDDDgfpgVCPFHGdCLEGLASGPAIaarwGIPAEELPDDH 201
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
41-406 |
4.42e-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: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 41 LRVCVATCNRADYSKLAPIMFGIKTEPeFFELDVVVLGSHliddygntYRMIEQ--DDFDINTRlHTIVRGEDEAAMVES 118
Cdd:TIGR00236 1 LKVMIVLGTRPEAIKMAPLIRALKKYP-EIDSYVIVTAQH--------REMLDQvlDLFHLPPD-YDLNIMSPGQTLGEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 119 VGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSI-----RHAITKLAHYHVCCTR 193
Cdd:TIGR00236 71 TSNMLEGLEELLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMpeeinRQLTGHIADLHFAPTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 194 SAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDvksKDYIVALQHPVTT------DIKHSIKmfelt 267
Cdd:TIGR00236 151 QAKDNLLRENVKADSIFVTGNTVIDALLTNVEIAYSSPVLSEFGED---KRMILLTLHRRENvgepleNIFKAIR----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 268 ldALISFNKRTLVLFPnidAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVI 347
Cdd:TIGR00236 223 --EIVEEFEDVQIVYP---VHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190014632 348 NL---GTRQIGRETGENVLHvrdADTQDKILQALHLQFGKQYPCSKI------YGDGNAVPRILKFLK 406
Cdd:TIGR00236 298 VLrdtTERPETVEAGTNKLV---GTDKENITKAAKRLLTDPDEYKKMsnasnpYGDGEASERIVEELL 362
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
441-633 |
3.36e-10 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 61.92 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIV---KKYTQ--FNPKTYEERINLILQMCVEAAAeavklncRILGVGISTGGRVNPREGI 515
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILhceKKRTAevIAPDLVSGLGEMIDEYLRRFNA-------RCHGIVMGFPALVSKDRRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 516 VLHSTKL-IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERK-----------FGQGKGLENFVTLitgtgigggiih 583
Cdd:PRK09698 80 VISTPNLpLTALDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKennltqqlvlgAYLGTGMGFAVWM------------ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 190014632 584 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 633
Cdd:PRK09698 148 NGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQ 197
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
444-709 |
5.32e-10 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 61.16 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 444 DLGGTNLRVAIVSMKGEIVKKYTQFNPKT-YEERINLILQMCVEAAAeavKLNCRilG-VGISTGGRVNPREGIVLhsTK 521
Cdd:PRK13310 6 DIGGTKIELGVFNEKLELQWEERVPTPRDsYDAFLDAVCELVAEADQ---RFGCK--GsVGIGIPGMPETEDGTLY--AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 522 LIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHL 601
Cdd:PRK13310 79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 602 --------VVSLDGP--DCSCGSHGCIEAYASGMALQreakklhdedlLLVEGMsvpKDEAVGALHLIQAAKLGNAKAQS 671
Cdd:PRK13310 159 rlpvdaltLLGWDAPlrRCGCGQKGCIENYLSGRGFE-----------WLYQHY---YGEPLQAPEIIALYYQGDEQAVA 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 190014632 672 ILRTAGTALGLGVVNILHTMNPSLVILSGVLaSHYIHI 709
Cdd:PRK13310 225 HVERYLDLLAICLGNILTIVDPHLVVLGGGL-SNFDAI 261
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
441-571 |
6.72e-08 |
|
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK (EC 2.7.1.63/EC 2.7.1.2), also called poly(P)/ATP-glucomannokinase (GMK), poly(P) glucokinase, ATP-dependent glucokinase, or polyphosphate--glucose phosphotransferase, catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in Mycobacterium tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor. PPGK belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this family lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466908 [Multi-domain] Cd Length: 239 Bit Score: 54.11 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSM-KGEIVkkytqfnpktyEERINLIL-QMCV-EAAAEAVKLNCRILG----VGISTGGRVnpRE 513
Cdd:cd24058 2 LGIDIGGSGIKGAIVDTdTGELL-----------SERIRIPTpQPATpEAVADVVAELVAHFPwfgpVGVGFPGVV--RR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190014632 514 GIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGK---GLENFVTL 571
Cdd:cd24058 69 GVVRTAANLDKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKgekGVVLVLTL 129
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
444-628 |
1.37e-06 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 50.41 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 444 DLGGTNLRVAIVSmkgEIVKKYTQFNPKTYEERINLILQMCVEAAAEAvKLNCRILG-VGISTGGRVNPREGIVLhsTKL 522
Cdd:PRK13311 6 DMGGTKIELGVFD---ENLQRIWHKRVPTPREDYPQLLQILRDLTEEA-DTYCGVQGsVGIGIPGLPNADDGTVF--TAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 523 IQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLV 602
Cdd:PRK13311 80 VPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFR 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 190014632 603 VSLDGPD----------CSCGSHGCIEAYASGMALQ 628
Cdd:PRK13311 160 LPVDALDilgadiprvpCGCGHRGCIENYISGRGFE 195
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
443-634 |
1.71e-05 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 47.33 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 443 VDLGGTNLRVAIVSMKG-EIVKKYTQFNPKTYEERINLILQMCVEAAAEavkLNCR-ILGVGIStgGRVNPREGIV--LH 518
Cdd:PRK09557 5 IDLGGTKIEVIALDDAGeELFRKRLPTPRDDYQQTIEAIATLVDMAEQA---TGQRgTVGVGIP--GSISPYTGLVknAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 519 STkliqeW-NSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAE 597
Cdd:PRK09557 80 ST-----WlNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 190014632 598 LGHLVVSLDGPD---------CSCGSHGCIEAYASGMALQREAKKL 634
Cdd:PRK09557 155 WGHNPLPWMDEDelryrnevpCYCGKQGCIETFISGTGFATDYRRL 200
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
441-517 |
7.99e-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: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIVK------KYTQ---------FNPKTYEERinlILQMCVEAAAEAVKLNCRILGVGiST 505
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAiayrewEYYTdddypdakeFDPEELWEK---ICEAIREALKKAGISPEDISAVS-ST 78
|
90
....*....|..
gi 190014632 506 GgrvnPREGIVL 517
Cdd:cd07798 79 S----QREGIVF 86
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
440-507 |
3.72e-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: 3.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190014632 440 ALAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPK--TYEERINLILQMCVEAAAEAVK----LNCRILGVGISTGG 507
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. ... |
441-505 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190014632 441 LAVDLGGTNLRVAIVSMKGEIV----KKYTQFNPKTY--EERINLILQMCVEAAAEAVKL--NCRILGVGIST 505
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) ... |
427-460 |
2.42e-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: 2.42e-03
10 20 30
....*....|....*....|....*....|....
gi 190014632 427 ISQDIDHiLETLSALAVDLGGTNLRVAIVSMKGE 460
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) ... |
436-460 |
4.49e-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: 4.49e-03
10 20
....*....|....*....|....*
gi 190014632 436 ETLSALAVDLGGTNLRVAIVSMKGE 460
Cdd:cd24087 41 ETGDYLALDLGGTNLRVCLVKLGGN 65
|
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