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Conserved domains on  [gi|2534146820|ref|WP_291057819|]
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ROK family transcriptional regulator [Herbiconiux sp.]

Protein Classification

ROK family transcriptional regulator( domain architecture ID 20650276)

NagC/ROK (Repressor, ORF, Kinase) family transcriptional regulator is involved in carbohydrate-dependent transcriptional control; contains a DNA-binding helix-turn-helix (HTH) domain

CATH:  3.30.420.40|1.10.10.10
Gene Ontology:  GO:0003700|GO:0006355|GO:0005524|GO:0003677
PubMed:  20512568|17979299|7952186|15808743|2644244|8831795|7781919|8800467
SCOP:  3000034|3000092|4000330

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 77-371 6.76e-92

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24073:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 304  Bit Score: 278.28  E-value: 6.76e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  77 HYFLGIKLTGDAVMAAVTNLRAGVVNYFELALSSTEPETVVERIAAAAGRAGGSYPID-----AIGIGLGGVV-AGDGSV 150
Cdd:cd24073     1 AYVVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSpdrllGIGVGLPGLVdAETGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 151 SSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLV 230
Cdd:cd24073    81 RWSPLLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 231 GHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTAL--DRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANL 308
Cdd:cd24073   161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGlrGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLVNL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534146820 309 VAPSFVVVGGEGVDLAAVSARAVDEGIREQRDPR-ASTVKVELTSGTNESWCRGAAVIALQGYV 371
Cdd:cd24073   241 LDPELIIISGEGVRAGDLLFEPMREALRAHVFPGlASDLELVIHPWGDEAWARGAAALALQEFF 304
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 8-63 3.83e-03

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


:

Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 35.26  E-value: 3.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2534146820   8 DLAQSVALEVLLHGPLARV-ELARRLDLAPATLTRISAELIDVGLLVETPQLAERRA 63
Cdd:pfam12802   4 TPAQFRVLLALARNPGLTVaELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
 
Name Accession Description Interval E-value
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
 77-371 6.76e-92

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: 278.28  E-value: 6.76e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  77 HYFLGIKLTGDAVMAAVTNLRAGVVNYFELALSSTEPETVVERIAAAAGRAGGSYPID-----AIGIGLGGVV-AGDGSV 150
Cdd:cd24073     1 AYVVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSpdrllGIGVGLPGLVdAETGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 151 SSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLV 230
Cdd:cd24073    81 RWSPLLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 231 GHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTAL--DRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANL 308
Cdd:cd24073   161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGlrGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLVNL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534146820 309 VAPSFVVVGGEGVDLAAVSARAVDEGIREQRDPR-ASTVKVELTSGTNESWCRGAAVIALQGYV 371
Cdd:cd24073   241 LDPELIIISGEGVRAGDLLFEPMREALRAHVFPGlASDLELVIHPWGDEAWARGAAALALQEFF 304
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
 73-368 3.15e-55

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: 183.94  E-value: 3.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  73 VAEAHYFLGIKLTGDAVMAAVTNLRAGVVNYFELAL-SSTEPETVVERIAA-----AAGRAGGSYPIDAIGIGLGGVVAG 146
Cdd:COG1940     1 NPDAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTpAGAGPEAVLEAIAElieelLAEAGISRGRILGIGIGVPGPVDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 147 D-GSVSSAPFL-GWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDD 224
Cdd:COG1940    81 EtGVVLNAPNLpGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 225 SGVGLVGHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTAL-DRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIA 303
Cdd:COG1940   161 GNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGgAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534146820 304 AVANLVAPSFVVVGGEGVDLAAVSARAVDEGIREQRDPRAST-VKVELTSGTNESWCRGAAVIALQ 368
Cdd:COG1940   241 NLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREdPRIVPASLGDDAGLLGAAALALE 306
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
 80-368 6.27e-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: 130.15  E-value: 6.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  80 LGIKLTGDAVMAAVTNLrAGVVNYFELALSSTE--PETVVERIAAAAGRAGGS-YPIDAIGIGLGGVVA-GDGSVSSAPF 155
Cdd:pfam00480   1 IGIDIGGTKIAAALFDE-EGEILARERVPTPTTttEETLVDAIAFFVDSAQRKfGELIAVGIGSPGLISpKYGYITNTPN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 156 LGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWPL 235
Cdd:pfam00480  80 IGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 236 DPLGPMCNRGHRGCAESMLTVPAILRDISTALDrPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVAPSFVV 315
Cdd:pfam00480 160 DPNGPKCGCGNHGCLETIASGRALEKRYQQKGE-DLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDPQAIV 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2534146820 316 VGGEGVDlaavsARAVDEGIREQ------RDPRASTVKVELTSGTNESWCRGAAVIALQ 368
Cdd:pfam00480 239 LGGGVSN-----ADGLLEAIRSLvkkylnGYLPVPPVIIVAASLGDNAGALGAAALAKQ 292
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
 80-318 3.14e-24

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: 101.52  E-value: 3.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  80 LGIKLTGDAVMAAVTNLRAGVVNYFELAlSSTEPETVVERIA-----AAAGRAGGSYPIDAIGIGLGGVV-AGDGSVSSA 153
Cdd:TIGR00744   1 IGVDIGGTTIKLGVVDEEGNILSKWKVP-TDTTPETIVDAIAsavdsFIQHIAKVGHEIVAIGIGAPGPVnRQRGTVYFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 154 PFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHW 233
Cdd:TIGR00744  80 VNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 234 PLDPLGPM-CNRGHRGCAESMLTVPAILRDISTALDRPVDWTEFLSLV--------------RAGQPAATGIATSSGRAL 298
Cdd:TIGR00744 160 RMVPDGRLlCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGdgdgisakhvfvaaRQGDPVAVDSYREVARWA 239

                         250       260
                  ....*....|....*....|
gi 2534146820 299 GRLIAAVANLVAPSFVVVGG 318
Cdd:TIGR00744 240 GAGLADLASLFNPSAIVLGG 259
PRK05082 PRK05082
N-acetylmannosamine kinase; Provisional
 157-324 3.91e-15

N-acetylmannosamine kinase; Provisional


Pssm-ID: 235338 [Multi-domain]  Cd Length: 291  Bit Score: 74.95  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 157 GWTDVPLARLVQQATGIPAFAANDLTA--FMEAQHwfgLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWP 234
Cdd:PRK05082   82 GLLHFPLVQTLEQLTDLPTIALNDAQAaaWAEYQA---LPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHTL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 235 LDPLGPMCNRGHRGCAESMLTVPAILRDiSTALDRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVAPSFV 314
Cdd:PRK05082  159 ADPHGPVCGCGRRGCVEAIASGRAIAAA-AQGWLAGCDAKTIFERAGQGDEQAQALINRSAQAIARLIADLKATLDCQCV 237

                         170
                  ....*....|
gi 2534146820 315 VVGGeGVDLA 324
Cdd:PRK05082  238 VLGG-SVGLA 246
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 8-63 3.83e-03

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 35.26  E-value: 3.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2534146820   8 DLAQSVALEVLLHGPLARV-ELARRLDLAPATLTRISAELIDVGLLVETPQLAERRA 63
Cdd:pfam12802   4 TPAQFRVLLALARNPGLTVaELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
COG3355 COG3355
Predicted transcriptional regulator [Transcription];
27-75 6.73e-03

Predicted transcriptional regulator [Transcription];


Pssm-ID: 442583 [Multi-domain]  Cd Length: 131  Bit Score: 36.48  E-value: 6.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2534146820  27 ELARRLDLAPATLTRISAELIDVGLLVETpQLAERRAGRP----SIPLDVVAE 75
Cdd:COG3355    47 ELAEALDRSRSTVYRSLQKLLEAGLVERE-KRNLEGGGYPyvyyAIDPEELKE 98
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
20-63 9.19e-03

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 35.65  E-value: 9.19e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2534146820   20 HGPLARVELARRLDLAPATLTRISAELIDVGLLVETPQLAERRA 63
Cdd:smart00347  22 EGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRS 65
 
Name Accession Description Interval E-value
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
 77-371 6.76e-92

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: 278.28  E-value: 6.76e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  77 HYFLGIKLTGDAVMAAVTNLRAGVVNYFELALSSTEPETVVERIAAAAGRAGGSYPID-----AIGIGLGGVV-AGDGSV 150
Cdd:cd24073     1 AYVVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSpdrllGIGVGLPGLVdAETGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 151 SSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLV 230
Cdd:cd24073    81 RWSPLLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 231 GHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTAL--DRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANL 308
Cdd:cd24073   161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGlrGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLVNL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534146820 309 VAPSFVVVGGEGVDLAAVSARAVDEGIREQRDPR-ASTVKVELTSGTNESWCRGAAVIALQGYV 371
Cdd:cd24073   241 LDPELIIISGEGVRAGDLLFEPMREALRAHVFPGlASDLELVIHPWGDEAWARGAAALALQEFF 304
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
 73-368 3.15e-55

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: 183.94  E-value: 3.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  73 VAEAHYFLGIKLTGDAVMAAVTNLRAGVVNYFELAL-SSTEPETVVERIAA-----AAGRAGGSYPIDAIGIGLGGVVAG 146
Cdd:COG1940     1 NPDAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTpAGAGPEAVLEAIAElieelLAEAGISRGRILGIGIGVPGPVDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 147 D-GSVSSAPFL-GWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDD 224
Cdd:COG1940    81 EtGVVLNAPNLpGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 225 SGVGLVGHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTAL-DRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIA 303
Cdd:COG1940   161 GNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGgAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534146820 304 AVANLVAPSFVVVGGEGVDLAAVSARAVDEGIREQRDPRAST-VKVELTSGTNESWCRGAAVIALQ 368
Cdd:COG1940   241 NLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREdPRIVPASLGDDAGLLGAAALALE 306
ASKHA_ATPase_ROK_Lmo0178-like cd24071
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ...
 78-320 2.03e-41

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: 147.82  E-value: 2.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  78 YFLGIKLTGDAVMAAVTNLRAGVVNYFELALSS-TEPETVVERIAAAAGRAGGSYPIDA----IGIGLGGVVAGD-GSVS 151
Cdd:cd24071     2 YIIGVKIEEGYLVLALTDLKGKILEKTRIPFDHeTDPEKVIELIAENIKKLIKNKHVEKkllgIGIAVSGLVDSKkGIVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 152 SAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVG 231
Cdd:cd24071    82 RSTILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 232 HWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTALDR----PVDWTEFLS------LVRAGQPAATGIATSSGRALGRL 301
Cdd:cd24071   162 HMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESyplsLLKELEDFEiekvreAAEEGDSVATELFKKAGEYLGIG 241

                         250
                  ....*....|....*....
gi 2534146820 302 IAAVANLVAPSFVVVGGEG 320
Cdd:cd24071   242 IKNLINIFNPEAIIIGGEG 260
ASKHA_ATPase_ROK_BsXylR-like cd24076
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ...
 78-369 6.42e-41

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: 146.56  E-value: 6.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  78 YFLGIKLTGDAVMAAVTNLRAGVVNYFELALS-STEPETVVERIA-----AAAGRAGGSYPIDAIGIGLGGVV-AGDGSV 150
Cdd:cd24076     2 AVIGVELGVDYITVVVTDLAGEVLWRREVPLPaSDDPDEVLAQLAalireALAAAPDSPLGILGIGVGVPGLVdSEDGVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 151 SSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLV 230
Cdd:cd24076    82 LLAPNLGWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGEI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 231 GHWPLDPLGPMCNRGHRGCAESMLTVPAILR--DISTALDRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANL 308
Cdd:cd24076   162 GHMTVDPDGPPCSCGNRGCWETYASERALLRaaGRLGAGGEPLSLAELVEAARAGDPAALAALEEVGEYLGIGLANLVNT 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534146820 309 VAPSFVVVGGEGVDLAAVSARAVDEGIREQR-DPRASTVKVELTSGTNESWCRGAAVIALQG 369
Cdd:cd24076   242 FNPELVVLGGALAPLGPWLLPPLRAEVARRAlPAPARDVRIVVSRLGEDAAALGAAALAIDH 303
ASKHA_NBD_ROK_TM1224-like cd24059
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ...
 78-371 1.44e-39

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: 142.72  E-value: 1.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  78 YFLGIKLTGDAVMAAVTNLRAGVVNYFELALSSTE-PETVVERIAAAAGRAGGSYPID----AIGIG-LGGVVAGDGSVS 151
Cdd:cd24059     2 YVIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKEnPEEVLEKLYELIDRLLEKENIKskilGIGIGaPGPLDVEKGIIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 152 SAP-FLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLV 230
Cdd:cd24059    82 NPPnFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 231 GHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTALDRPVDWTEFL-SLVRAGQPAATGIATSSGRALGRLIAAVANLV 309
Cdd:cd24059   162 GHTSIDINGPRCSCGNRGCLELYASIPAIEKKARSALGSGRSFQLDIvEALQKGDPIADEVIEEAAKYLGIGLVNLINLL 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534146820 310 APSFVVVGGEGVDLAAVSARAVDEGIREQRDPRAST-VKVELTSGTNESWCRGAAVIALQGYV 371
Cdd:cd24059   242 NPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAReVRILKSSLGEDAPLLGAAALVLNKYF 304
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
 80-368 6.27e-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: 130.15  E-value: 6.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  80 LGIKLTGDAVMAAVTNLrAGVVNYFELALSSTE--PETVVERIAAAAGRAGGS-YPIDAIGIGLGGVVA-GDGSVSSAPF 155
Cdd:pfam00480   1 IGIDIGGTKIAAALFDE-EGEILARERVPTPTTttEETLVDAIAFFVDSAQRKfGELIAVGIGSPGLISpKYGYITNTPN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 156 LGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWPL 235
Cdd:pfam00480  80 IGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 236 DPLGPMCNRGHRGCAESMLTVPAILRDISTALDrPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVAPSFVV 315
Cdd:pfam00480 160 DPNGPKCGCGNHGCLETIASGRALEKRYQQKGE-DLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDPQAIV 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2534146820 316 VGGEGVDlaavsARAVDEGIREQ------RDPRASTVKVELTSGTNESWCRGAAVIALQ 368
Cdd:pfam00480 239 LGGGVSN-----ADGLLEAIRSLvkkylnGYLPVPPVIIVAASLGDNAGALGAAALAKQ 292
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
 78-318 1.36e-34

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: 129.21  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  78 YFLGIKLTGdavmaavTNLRAGVVN----YFELALSSTE----PETVVERIAAAAGRAGGSYPIDAIGIGLGGVV-AGDG 148
Cdd:cd24068     1 KILGIDIGG-------TKIKYGLVDadgeILEKDSVPTPaskgGDAILERLLEIIAELKEKYDIEGIGISSAGQVdPKTG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 149 SV--SSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSG 226
Cdd:cd24068    74 EViyATDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 227 VGLVGHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTAL-DRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAV 305
Cdd:cd24068   154 AGELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALgEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANL 233

                         250
                  ....*....|...
gi 2534146820 306 ANLVAPSFVVVGG 318
Cdd:cd24068   234 VHIFDPEVIVIGG 246
ASKHA_NBD_ROK_TmGLK-like cd24064
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ...
 114-365 2.02e-31

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: 121.06  E-value: 2.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 114 ETVVERIAAAAGRAGGSYPIDAIGIGL-GGVVAGDGSVSSAP-FLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWF 191
Cdd:cd24064    37 EDVINRIAETVNELIEEMELLGIGIGSpGSIDRENGIVRFSPnFPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 192 GLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTALDR-- 269
Cdd:cd24064   117 GNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRyp 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 270 --------PVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVAPSFVVVGGeGVdlaavsARAVD---EGIREQ 338
Cdd:cd24064   197 dslageseKINAKHVFDAARKNDPLATMVFRRVVDALAIAIGGFVHIFNPEIIIIGG-GI------SRAGSfllDPIREK 269

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2534146820 339 RDPR-----ASTVKVELTSGTNESWCRGAAVI 365
Cdd:cd24064   270 TKKYvmlsfQDTYSIELSNLVEDAGILGAASI 301
ASKHA_ATPase_ROK_YphH-like cd24072
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ...
 80-337 1.49e-28

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: 113.28  E-value: 1.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  80 LGIKLTGDAVMAAVTNLRAGVVNYFELALSSTE-PETVVERIAAAAGRAGGSYPIDAIGIGL---GGVVAGDGSVSSAPF 155
Cdd:cd24072     4 LGIVVSPNSLRAQVGNACGELLGEFEYRVITLEtPEALIDEIIDCIDRLLKLWKDRVKGIALaiqGLVDSHKGVSLWSPG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 156 LGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWPL 235
Cdd:cd24072    84 APWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGHTKV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 236 DPLGPMCNRGHRGCAESMLTVPAILRDIST-------ALDRPVDWTE-FLSLVRAGQPAATGIATSSGRALGRLIAAVAN 307
Cdd:cd24072   164 NPDGARCDCGRRGCLETVASNSALKRNARVtlklgpvSADPEKLTMEqLIEALEEGEPIATQIFDRAANAIGRSLANILN 243

                         250       260       270
                  ....*....|....*....|....*....|
gi 2534146820 308 LVAPSFVVVGGEGVDLAAVSARAVDEGIRE 337
Cdd:cd24072   244 LLNPEQVLLYGRGCRAGDLLLPAIRRAIAE 273
ASKHA_ATPase_ROK_Mlc cd24074
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ...
 135-365 1.30e-27

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: 110.86  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 135 AIGIGLGGVV-AGDGSVSSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGC 213
Cdd:cd24074    65 AIAITLPGIIdPESGIVHRLPFYDIKNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGV 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 214 VANGRLLANDDSGVGLVGHWPLDPLGPMCNRGHRGCAESMLTVPAILRDI---------STALDRPVDWTEFLSLVRAGQ 284
Cdd:cd24074   145 ITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQAnqlleqspdSMLHGQPISIESLCQAALAGD 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 285 PAATGIATSSGRALGRLIAAVANLVAPSFVVVGGEGVDLAAVSARAVDEGIREQRDPR-ASTVKVELTSGTNESWCRGAA 363
Cdd:cd24074   225 PLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLNNAAEILFPALSQSIRQQSLPAySQHLQIESTKFYNDGTMPGAA 304


                  ..
gi 2534146820 364 VI 365
Cdd:cd24074   305 LI 306
ASKHA_NBD_ROK_TtHK-like cd24065
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ...
 80-325 9.66e-27

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: 107.80  E-value: 9.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  80 LGIKLTGdavmaavTNLRAGVVNYFELALSSTEP------ETVVERIAAAAGRAGGSYP-IDAIGIGLGG-VVAGDGSVS 151
Cdd:cd24065     3 IGLDLGG-------TKIAAGVVDGGRILSRLVVPtpreggEAVLDALARAVEALQAEAPgVEAVGLGVPGpLDFRRGRVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 152 SAPFL-GWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLV 230
Cdd:cd24065    76 FAPNIpGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 231 GHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTALDRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVA 310
Cdd:cd24065   156 GHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRPMSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALD 235

                         250
                  ....*....|....*
gi 2534146820 311 PSFVVVGGeGVDLAA 325
Cdd:cd24065   236 PEVFVLGG-GVAQVG 249
ASKHA_ATPase_ROK cd23763
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ...
 80-365 2.74e-26

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: 105.24  E-value: 2.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  80 LGIKLTGDAVMAAVTNLRAGVVNYFELALSSTE-PETVVERIAAA----AGRAGGSYPIDAIGIGLGGVV-AGDGSVSSA 153
Cdd:cd23763     1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEgPEAVLDRIAELieelLAEAGVRERILGIGIGVPGPVdPETGIVLFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 154 PFL-GWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLanddsgvglvgh 232
Cdd:cd23763    81 PNLpWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLY------------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 233 wpldplgpmcnRGHRGCAesmltvpailrdistaldrpvdwTEF--LSLVRagqpaatgiatSSGRALGRLIAAVANLVA 310
Cdd:cd23763   149 -----------RGANGAA-----------------------GEIghITVLE-----------EAARYLGIGLANLINLLN 183

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2534146820 311 PSFVVVGGEGVDLAAVSARAVDEGIREQR-DPRASTVKVELTSGTNESWCRGAAVI 365
Cdd:cd23763   184 PELIVLGGGVAEAGDLLLEPIREAVRRRAlPPLRRRVRIVPSELGDDAGLLGAAAL 239
ASKHA_NBD_ROK_BsGLK-like cd24062
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ...
 134-325 1.02e-24

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: 102.75  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 134 DAIGIGLG--GVV-AGDGSVSSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVG 210
Cdd:cd24062    61 DLIGIGVGvpGPVdVETGTVEVAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 211 FGCVANGRLLANDDSGVGLVGHWPLDPLGPM-CNRGHRGCAESMLTVPAILRDI--------STALDRPVDWTEFLS--- 278
Cdd:cd24062   141 GGVIANGKIVHGANGAAGEIGHITVNPEGGApCNCGKTGCLETVASATGIVRIAreeleegkGSSALRILALGGELTakd 220

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2534146820 279 ---LVRAGQPAATGIATSSGRALGRLIAAVANLVAPSFVVVGGeGVDLAA 325
Cdd:cd24062   221 vfeAAKAGDELALAVVDTVARYLGLALANLANTLNPEKIVIGG-GVSAAG 269
ASKHA_NBD_ROK_SgGLK-like cd24061
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ...
 94-318 1.66e-24

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: 102.05  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  94 TNLRAGVVNYFELALSS------TEPETVVERIAAAAGRAGGSYPIDAIGIGLGGVVAGD-GSVSSAPFLGWTDVPLARL 166
Cdd:cd24061     9 TKIAAGVVDEEGEILATervptpPTADGIVDAIVEAVEELREGHDVSAVGVAAAGFVDADrATVLFAPNIAWRNEPLKDL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 167 VQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWPLDPLGPMCNRGH 246
Cdd:cd24061    89 LEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRVVPDGLLCGCGS 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 247 RGCAESMLTVPAILR---------------DISTALDRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVAP 311
Cdd:cd24061   169 RGCWEQYASGRALVRyakeaanatpegaavLLADGSVDGITGKHISEAARAGDPVALDALRELARWLGAGLASLAALLDP 248


                  ....*..
gi 2534146820 312 SFVVVGG 318
Cdd:cd24061   249 ELFVIGG 255
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
 80-318 3.14e-24

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: 101.52  E-value: 3.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  80 LGIKLTGDAVMAAVTNLRAGVVNYFELAlSSTEPETVVERIA-----AAAGRAGGSYPIDAIGIGLGGVV-AGDGSVSSA 153
Cdd:TIGR00744   1 IGVDIGGTTIKLGVVDEEGNILSKWKVP-TDTTPETIVDAIAsavdsFIQHIAKVGHEIVAIGIGAPGPVnRQRGTVYFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 154 PFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHW 233
Cdd:TIGR00744  80 VNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 234 PLDPLGPM-CNRGHRGCAESMLTVPAILRDISTALDRPVDWTEFLSLV--------------RAGQPAATGIATSSGRAL 298
Cdd:TIGR00744 160 RMVPDGRLlCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGdgdgisakhvfvaaRQGDPVAVDSYREVARWA 239

                         250       260
                  ....*....|....*....|
gi 2534146820 299 GRLIAAVANLVAPSFVVVGG 318
Cdd:TIGR00744 240 GAGLADLASLFNPSAIVLGG 259
ASKHA_ATPase_ROK_NagC cd24075
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ...
 77-319 6.36e-23

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: 97.82  E-value: 6.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  77 HYFLGIKLTGDAVMAAVTNLRAGVVNYFELALSSTEPETVVERIAAAAGRAGGSYP-----IDAIGIGLGGVVAGD-GSV 150
Cdd:cd24075     1 FHILAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEALLSQLIEEIAQFLKSHRrktqrLIAISITLPGLINPKtGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 151 SSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLV 230
Cdd:cd24075    81 HYMPHIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 231 GHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTALDR------PVDWTEFLSLVRA---GQPAATGIATSSGRALGRL 301
Cdd:cd24075   161 GHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQgyasqlTLQDCTIKDICQAalnGDQLAQDVIKRAGRYLGKV 240

                         250
                  ....*....|....*...
gi 2534146820 302 IAAVANLVAPSFVVVGGE 319
Cdd:cd24075   241 IAILINLLNPQKIIIAGE 258
ASKHA_NBD_ROK_ApGLK-like cd24063
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ...
 94-318 4.05e-22

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: 95.48  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  94 TNLRAGVVNYFELALS--------STEPETVVERIAAAAGRAGGSYPIDAI-GIGL---GGVVAGDGSVSSAPFLGWTDV 161
Cdd:cd24063    10 TWIRAGLVDEDGRILLkirqptpkTGDPGTVSEQVLGLIETLLSKAGKDSIeGIGVssaGPLDLRKGTIVNSPNIKGKEI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 162 PLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWPLDP-LGP 240
Cdd:cd24063    90 PLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHLVVDTeSGL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 241 MCNRGHRGCAESMLTVPAILRDISTALDRPVDWT---------------EFLSLVRAGQPAATGIATSSGRALGRLIAAV 305
Cdd:cd24063   170 KCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTslklrnpggegitakEVFSAARKGDPLALKIIEKLARYNGRGIANV 249

                         250
                  ....*....|...
gi 2534146820 306 ANLVAPSFVVVGG 318
Cdd:cd24063   250 INAYDPELIVIGG 262
ASKHA_NBD_ROK_EcNanK-like cd24069
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ...
 132-324 1.94e-21

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: 93.12  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 132 PIDAIGIGLGGVVaGDGSVSSA---PFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVG 208
Cdd:cd24069    51 QFDRVAVASTGII-RDGVLTALnpkNLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 209 VGFGCVANGRLLANDDSGVGLVGHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTALDRPVDWTEFLSLVRAGQPAAT 288
Cdd:cd24069   130 VGGGLVLNGQLLTGPNGLAGHIGHTLADPPGPVCGCGRRGCVEAIASGTAIAAAASEILGEPVDAKDVFERARSGDEEAA 209

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2534146820 289 GIATSSGRALGRLIAAVANLVAPSFVVVGGeGVDLA 324
Cdd:cd24069   210 RLIDRAARALADLIADLKATLDLDCVVIGG-SVGLA 244
ASKHA_NBD_ROK_GNE cd24060
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ...
 133-348 8.73e-20

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: 88.63  E-value: 8.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 133 IDAIGIGLGGVV-AGDGSV--SSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGV 209
Cdd:cd24060    60 ILGVGISTGGRVnPREGIVlhSTKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGI 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 210 GFGCVANGRLLANDDSGVGLVGHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTALD--------RPVDWTEFLSLVR 281
Cdd:cd24060   140 GGGIILNHELIHGSSFCAAELGHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDedlllvegMSVTNDEEVTAKH 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534146820 282 AGQPAATG------IATSSGRALGRLIAAVANLVAPSFVVVGGEgvdLAAVSARAVDEGIREQRDPRASTVKV 348
Cdd:cd24060   220 LIQAAKLGnakaqkILRTAGTALGLGIVNILHTLNPSLVILSGV---LASHYENIVKDVIAQRALPSVQNVDV 289
PRK05082 PRK05082
N-acetylmannosamine kinase; Provisional
 157-324 3.91e-15

N-acetylmannosamine kinase; Provisional


Pssm-ID: 235338 [Multi-domain]  Cd Length: 291  Bit Score: 74.95  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 157 GWTDVPLARLVQQATGIPAFAANDLTA--FMEAQHwfgLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWP 234
Cdd:PRK05082   82 GLLHFPLVQTLEQLTDLPTIALNDAQAaaWAEYQA---LPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHTL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 235 LDPLGPMCNRGHRGCAESMLTVPAILRDiSTALDRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVAPSFV 314
Cdd:PRK05082  159 ADPHGPVCGCGRRGCVEAIASGRAIAAA-AQGWLAGCDAKTIFERAGQGDEQAQALINRSAQAIARLIADLKATLDCQCV 237

                         170
                  ....*....|
gi 2534146820 315 VVGGeGVDLA 324
Cdd:PRK05082  238 VLGG-SVGLA 246
ASKHA_NBD_ROK_EcFRK-like cd24066
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ...
 162-318 1.53e-14

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: 73.39  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 162 PLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLVGHWPLDPL--- 238
Cdd:cd24066    86 PLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGHNPLPWPded 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 239 ---GPMCNRGHRGCAESMLTVPAILRDISTALDRPVDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVAPSFVV 315
Cdd:cd24066   166 elpGPPCYCGKRGCVETFLSGPALERDYARLTGKTLSAEEIVALARAGDAAAVATLDRFLDRLGRALANVINILDPDVIV 245


                  ...
gi 2534146820 316 VGG 318
Cdd:cd24066   246 LGG 248
ASKHA_NBD_ROK_NAGK cd24057
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
 136-365 2.08e-14

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: 73.04  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 136 IGIGLGGVV-AGDGSVSSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCV 214
Cdd:cd24057    60 VGIGIPGVIdPEDGTLITANIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLV 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 215 ANGRLLANDDSGVGLVGHWPL--DPLGPM-------CNRGHRGCAESMLTVPAILRDISTALDRPVDWTEFLSLVRAGQP 285
Cdd:cd24057   140 VNGRLVGGRSGIAGEWGHGPLpaDALLLGydlpvlrCGCGQTGCLETYLSGRGLERLYAHLYGEELDAPEIIAAWAAGDP 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 286 AATGIATSSGRALGRLIAAVANLVAPSFVVVGGeGVDLAAVSARAVDEGIREQRDPRASTVKVELTSGTNESWCRGAAVI 365
Cdd:cd24057   220 QAVAHVDRWLDLLAGCLANILTALDPDVVVLGG-GLSNFPALIAELPAALPAHLLSGARTPRIVPARHGDAGGVRGAAFL 298
ASKHA_ATPase_ROK_SaXylR-like cd24077
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ...
 78-368 2.41e-14

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: 72.96  E-value: 2.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  78 YFLGIKLTGDAVMAAVTNLRAGVVNYFELALSSTEPETVVERIAAAAGRAGGSYP---IDAIGIGLG--GVVaGDGSVSS 152
Cdd:cd24077     2 YSIGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENILEILKSIIQELISQAPktpYGLVGIGIGihGIV-DENEIIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 153 APFLGWTDVPLARLVQQATGIPAFAAND--LTAFmeAQHWFglGAGHDNFAALTLGVGVGFGCVANGRLLANDDSGVGLV 230
Cdd:cd24077    81 TPYYDLEDIDLKEKLEEKFNVPVYLENEanLSAL--AERTF--SEDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 231 GHWPLDPLGPMCNRGHRGCAESMLTVPAILRDISTALDRP-VDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLV 309
Cdd:cd24077   157 GHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKKGLEtLTFDDLIQLYNEGDPEALELIDQFIKYLAIGINNIINTF 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 310 APSFVVVGGEgvdLAAVSARAVDEgIREQ-RDPRASTVKVELTSGTNESWCRGAAVIALQ 368
Cdd:cd24077   237 NPEIIIINSS---LINEIPELLEK-IKEQlSSSFNKYVEILISTLGKNATLLGGAAVAIK 292
PRK09698 PRK09698
D-allose kinase; Provisional
 131-368 3.23e-13

D-allose kinase; Provisional


Pssm-ID: 182034 [Multi-domain]  Cd Length: 302  Bit Score: 69.63  E-value: 3.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 131 YPIDAIGIGLGGVVAGDG-SVSSAPFL---GWTDVPLARLVQQATGIPAFAANDLTAFM--EAQHwfgLGAGHDNFAALT 204
Cdd:PRK09698   60 ARCHGIVMGFPALVSKDRrTVISTPNLpltALDLYDLADKLENTLNCPVFFSRDVNLQLlwDVKE---NNLTQQLVLGAY 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 205 LGVGVGFGCVANGRLLANDDSGVGLVGHWPLDPLGPMCNRGHRGCAESMLTVPAiLRDISTALDRPVDWTEFlsLVRAGQ 284
Cdd:PRK09698  137 LGTGMGFAVWMNGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMA-LRRWYEQQPRDYPLSDL--FVHAGD 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 285 -PAATGIATSsgraLGRLIAAVANLVAPSFVVVGGEGVDLAAVSARAVDEGIRE--QRDPRASTVKVELTSGTNESWCRG 361
Cdd:PRK09698  214 hPFIQSLLEN----LARAIATSINLFDPDAIILGGGVMDMPAFPRETLIAMIQKylRKPLPYEVVRFIYASSSDFNGAQG 289


                  ....*..
gi 2534146820 362 AAVIALQ 368
Cdd:PRK09698  290 AAILAHQ 296
ASKHA_NBD_ROK_AlsK cd24070
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ...
 77-366 1.17e-11

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: 64.88  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  77 HYFLGIKLTGdavmaavTNLRAGVVN-----YFELALSSTEP---ETVVERIAAA--AGRAGGSYPIDAIGIGLGGVVAG 146
Cdd:cd24070     1 KYVLGIDIGG-------TNIRIGLVDedgklLDFEKVPSKDLlraGDPVEVLADLirEYIEEAGLKPAAIVIGVPGTVDK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 147 DGS-VSSAPFL-GWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVGFGCVANGRLLANDD 224
Cdd:cd24070    74 DRRtVISTPNIpGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 225 SGVGLVGHWPLDPLGPMCNRGHRGCAE---SMLTVPAILRD--ISTA-LDRPVDWT------EFLslvragqpaatgiat 292
Cdd:cd24070   154 GVAGELGHIPVYGNGKPCGCGNTGCLEtyaSGRALEEIAEEhyPDTPiLDIFVDHGdepeldEFV--------------- 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534146820 293 ssgRALGRLIAAVANLVAPSFVVVGGeGV-DLAAVSARAVDEGIREQ-RDPR-ASTVKVELTSGTNESWCRGAAVIA 366
Cdd:cd24070   219 ---EDLALAIATEINILDPDAVILGG-GViDMKGFPRETLEEYIRKHlRKPYpADNLKIIYAELGPEAGVIGAAIYA 291
ASKHA_NBD_ROK-like cd24152
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ...
 133-318 7.19e-10

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: 59.50  E-value: 7.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 133 IDAIGIGLGGVV-AGDGSV-SSAPFLGWTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFAALTLGVGVG 210
Cdd:cd24152    54 IDGIAISAPGVIdPETGIIyGGGALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 211 FGCVANGRLLANDDSGVGLVGHWPLDPLGPMCNRGHRgcaesMLTVPAILRDISTALDR-PVDWTEFLSLVRAGQPAATG 289
Cdd:cd24152   134 GAIIIDGKLYRGSHFFAGEFSYLLTDDDDKDLLFFSG-----LASMFGLVKRYNKAKGLePLDGEEIFEKYAKGDEAAKK 208

                         170       180
                  ....*....|....*....|....*....
gi 2534146820 290 IATSSGRALGRLIAAVANLVAPSFVVVGG 318
Cdd:cd24152   209 ILDEYIRNLAKLIYNIQYILDPEVIVIGG 237
ASKHA_NBD_ROK_BsFRK-like cd24067
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ...
 79-321 1.53e-08

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: 55.24  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  79 FLGIKLTGDAVMAAVTNLRAGVVNYFELAlsSTEPETVVERIAAAAGRAggSYPIDAIGIGLGGVVAGD------GSVSS 152
Cdd:cd24067     1 FGGIEAGGTKFVCAVGTGDGNIIERTEFP--TTTPEETLQAVIDFFREQ--EEPIDAIGIASFGPIDLNptsptyGYITT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 153 APFLGWTDVPLARLVQQATGIP-AF-----AAndltAFMEAQHwfGLGAGHDNFAALTLGVGVGFGCVANGRLLanddsg 226
Cdd:cd24067    77 TPKPGWRNFDILGALKRAFPVPvGFdtdvnAA----ALAEYRW--GAAKGLDSLAYITVGTGIGVGLVVNGKPV------ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 227 VGLV----GHWPL------DPLGPMCnRGHRGCAESMLTVPAILRdistaldrpvdwteflslvRAGQPAATG-----IA 291
Cdd:cd24067   145 HGLLhpemGHIRVprhpddDGFPGVC-PFHGDCLEGLASGPAIAA-------------------RWGIPAEELpddhpAW 204

                         250       260       270
                  ....*....|....*....|....*....|
gi 2534146820 292 TSSGRALGRLIAAVANLVAPSFVVVGGeGV 321
Cdd:cd24067   205 DLEAYYLAQACANLTLTLSPERIVLGG-GV 233
PRK09557 PRK09557
fructokinase; Reviewed
 136-318 3.84e-08

fructokinase; Reviewed


Pssm-ID: 236565 [Multi-domain]  Cd Length: 301  Bit Score: 54.26  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 136 IGIGLGGVVAgdgsvssaPFLG--------WT-----DVPLARLVQQATGIpafaANDLTAFMEAQHWFGLGAGHDNFAA 202
Cdd:PRK09557   60 VGVGIPGSIS--------PYTGlvknanstWLngqplDKDLSARLNREVRL----ANDANCLAVSEAVDGAAAGKQTVFA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 203 LTLGVGVGFGCVANGRLLAnddSGVGLVGHWPLDPLGPM------------CNRGHRGCAESMLTVPAILRDISTALDRP 270
Cdd:PRK09557  128 VIIGTGCGAGVAINGRVHI---GGNGIAGEWGHNPLPWMdedelryrnevpCYCGKQGCIETFISGTGFATDYRRLSGKA 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2534146820 271 VDWTEFLSLVRAGQPAATGIATSSGRALGRLIAAVANLVAPSFVVVGG 318
Cdd:PRK09557  205 LKGSEIIRLVEEGDPVAELAFRRYEDRLAKSLAHVINILDPDVIVLGG 252
PRK13311 PRK13311
N-acetyl-D-glucosamine kinase; Provisional
 135-289 1.18e-07

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 106271 [Multi-domain]  Cd Length: 256  Bit Score: 52.34  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 135 AIGIGLGGVV-AGDGSVSSAPFLGWTDVPL----ARLVQQATGIPafaaNDLTAFMEAQHWFGLGAGHDNFAALTLGVGV 209
Cdd:PRK13311   59 SVGIGIPGLPnADDGTVFTANVPSAMGQPLqadlSRLIQREVRID----NDANCFALSEAWDPEFRTYPTVLGLILGTGV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820 210 GFGCVANGRLLANDDSGVGLVGHW--PLDPLGPM--------CNRGHRGCAESMLTVPAILRDISTALDRPVDWTEFLSL 279
Cdd:PRK13311  135 GGGLIVNGSIVSGRNHITGEFGHFrlPVDALDILgadiprvpCGCGHRGCIENYISGRGFEWMYSHFYQHTLPATDIIAH 214

                         170
                  ....*....|
gi 2534146820 280 VRAGQPAATG 289
Cdd:PRK13311  215 YAAGEPKAVA 224
ASKHA_NBD_ROK_PPGK cd24058
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ...
 80-222 8.63e-06

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: 46.41  E-value: 8.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534146820  80 LGIKLTGDAVMAAVTNLRAGVVNYFELALSS---TEPETVVERIAAAAGRAGGSypiDAIGIGLGGVVAgDGSVSSAPFL 156
Cdd:cd24058     2 LGIDIGGSGIKGAIVDTDTGELLSERIRIPTpqpATPEAVADVVAELVAHFPWF---GPVGVGFPGVVR-RGVVRTAANL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534146820 157 G--WTDVPLARLVQQATGIPAFAANDLTAFMEAQHWFGLGAGHDNFA-ALTLGVGVGFGCVANGRLLAN 222
Cdd:cd24058    78 DksWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVlVLTLGTGIGSALFVDGHLVPN 146
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 8-63 3.83e-03

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 35.26  E-value: 3.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2534146820   8 DLAQSVALEVLLHGPLARV-ELARRLDLAPATLTRISAELIDVGLLVETPQLAERRA 63
Cdd:pfam12802   4 TPAQFRVLLALARNPGLTVaELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
COG3355 COG3355
Predicted transcriptional regulator [Transcription];
27-75 6.73e-03

Predicted transcriptional regulator [Transcription];


Pssm-ID: 442583 [Multi-domain]  Cd Length: 131  Bit Score: 36.48  E-value: 6.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2534146820  27 ELARRLDLAPATLTRISAELIDVGLLVETpQLAERRAGRP----SIPLDVVAE 75
Cdd:COG3355    47 ELAEALDRSRSTVYRSLQKLLEAGLVERE-KRNLEGGGYPyvyyAIDPEELKE 98
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 20-63 7.15e-03

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 34.45  E-value: 7.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2534146820  20 HGPLARVELARRLDLAPATLTRISAELIDVGLLVETPQLAERRA 63
Cdd:pfam01047  15 HGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRRE 58
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
20-63 9.19e-03

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 35.65  E-value: 9.19e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2534146820   20 HGPLARVELARRLDLAPATLTRISAELIDVGLLVETPQLAERRA 63
Cdd:smart00347  22 EGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRS 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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