|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
83-398 |
2.00e-147 |
|
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: 420.62 E-value: 2.00e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 83 FHSVAVRLGRDYIQLSLYNLGGKELASDYHEFHYSHQTQLIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVV 162
Cdd:cd24075 1 FHILAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEALLSQLIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 163 EYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEI 242
Cdd:cd24075 81 HYMPHIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 243 GHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYESSLaNIESITINDVCEHANLGDELAKQSLIRVGNQLGK 322
Cdd:cd24075 161 GHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQGYASQL-TLQDCTIKDICQAALNGDQLAQDVIKRAGRYLGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447639941 323 AIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQIDKQPTIGAFAMIKRAMLNGVLL 398
Cdd:cd24075 240 VIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQALPDFRQELKIVASQLDHNSAIGAFALVKRALLEGGLL 315
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
84-390 |
1.19e-83 |
|
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: 257.90 E-value: 1.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 84 HSVAVRLGRDYIQLSLYNLGGKELASDYHEFHYSHQTQ-LIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVV 162
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEaVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 163 EYMPNI-AIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGE 241
Cdd:COG1940 86 LNAPNLpGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 242 IGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIaqgyesslaNIESITINDVCEHANLGDELAKQSLIRVGNQLG 321
Cdd:COG1940 166 IGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG---------GAEKLTAEELFAAARAGDPLALEVLDEAARYLG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 322 KAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQI-DKQPTIGAFAMIKR 390
Cdd:COG1940 237 IGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLgDDAGLLGAAALALE 306
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
86-390 |
6.42e-72 |
|
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: 227.22 E-value: 6.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 86 VAVRLGRDYIQLSLYNLGGKELASdyHEFHYShQTQLIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVVEYM 165
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILAR--ERVPTP-TTTTEETLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYITNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 166 PNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGHI 245
Cdd:pfam00480 78 PNIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 246 QIDPLGEQCQCGNFGCLETVAANPAIISRVKKliaQGyesslaniESITINDVCEHANLGDELAKQSLIRVGNQLGKAIA 325
Cdd:pfam00480 158 QLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---KG--------EDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447639941 326 MTINLFNPQKVVIAGQITaAQEIVFPAIQRNVENQSLKTFHTNL--PIVASQIDKQPTIGAFAMIKR 390
Cdd:pfam00480 227 NLINLFDPQAIVLGGGVS-NADGLLEAIRSLVKKYLNGYLPVPPviIVAASLGDNAGALGAAALAKQ 292
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
130-393 |
7.82e-36 |
|
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]
Pssm-ID: 273246 [Multi-domain] Cd Length: 318 Bit Score: 133.49 E-value: 7.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 130 LNTFIKQQQERIEQFIAIGIALPGLVNPETGVVEYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDC 209
Cdd:TIGR00744 44 VDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAVNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 210 QDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGHIQIDPLGE-QCQCGNFGCLETVAANPAIISRVKKLIAQGYESS-- 286
Cdd:TIGR00744 124 RDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHIRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEvl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 287 --LANIESITINDVCEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKT 364
Cdd:TIGR00744 204 laLGDGDGISAKHVFVAARQGDPVAVDSYREVARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGG 283
|
250 260 270
....*....|....*....|....*....|
gi 1447639941 365 FHTNLPIVASQI-DKQPTIGAFAMIKRAML 393
Cdd:TIGR00744 284 ARQVADIIAAQLgNDAGLVGAADLARTYII 313
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
118-356 |
4.69e-20 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 89.66 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 118 HQTQ--LIEGLLFHLNTFIKQQQERIEQFI-AIGIALPGLVNPETGVVEYMPNI---AIDALALGDIIRDNFHVECFVGN 191
Cdd:PRK09698 33 KRTAevIAPDLVSGLGEMIDEYLRRFNARChGIVMGFPALVSKDRRTVISTPNLpltALDLYDLADKLENTLNCPVFFSR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 192 DVRGMAL--AEHYfgaskDCQDSILVSVHRGTGAG--IIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAA 267
Cdd:PRK09698 113 DVNLQLLwdVKEN-----NLTQQLVLGAYLGTGMGfaVWMNGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 268 NPAiISRVkkliaqgYESSLANiesITINDVCEHAnlGDELAKQSLIrvgNQLGKAIAMTINLFNPQKVVIAGQITAAQE 347
Cdd:PRK09698 188 GMA-LRRW-------YEQQPRD---YPLSDLFVHA--GDHPFIQSLL---ENLARAIATSINLFDPDAIILGGGVMDMPA 251
|
250
....*....|....*
gi 1447639941 348 ivFP------AIQRN 356
Cdd:PRK09698 252 --FPretliaMIQKY 264
|
|
| HTH_MARR |
smart00347 |
helix_turn_helix multiple antibiotic resistance protein; |
22-102 |
7.52e-05 |
|
helix_turn_helix multiple antibiotic resistance protein;
Pssm-ID: 197670 [Multi-domain] Cd Length: 101 Bit Score: 41.43 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 22 RLIDLQGPISRIQVADVSQLAPASVTKITRQLLERGLIkevAQQASTGGRRA--ISLTTEVAPFHSVAVRLGRDYIQLSL 99
Cdd:smart00347 17 RILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLV---RREPSPEDRRSvlVSLTEEGRELIEQLLEARSETLAELL 93
|
...
gi 1447639941 100 YNL 102
Cdd:smart00347 94 AGL 96
|
|
| MarR |
pfam01047 |
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ... |
22-74 |
1.12e-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: 36.76 E-value: 1.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1447639941 22 RLIDLQGPISRIQVADVSQLAPASVTKITRQLLERGLIKevaQQASTGGRRAI 74
Cdd:pfam01047 10 RILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIE---RSRSPEDRREV 59
|
|
| MntR |
COG1321 |
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription]; |
19-79 |
1.55e-03 |
|
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
Pssm-ID: 440932 [Multi-domain] Cd Length: 135 Bit Score: 38.65 E-value: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447639941 19 AVYRLIDLQGPISRIQVADVSQLAPASVTKITRQLLERGLIKEVaqqastgGRRAISLTTE 79
Cdd:COG1321 14 AIYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEYE-------PYGGITLTEE 67
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
83-398 |
2.00e-147 |
|
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: 420.62 E-value: 2.00e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 83 FHSVAVRLGRDYIQLSLYNLGGKELASDYHEFHYSHQTQLIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVV 162
Cdd:cd24075 1 FHILAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEALLSQLIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 163 EYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEI 242
Cdd:cd24075 81 HYMPHIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 243 GHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYESSLaNIESITINDVCEHANLGDELAKQSLIRVGNQLGK 322
Cdd:cd24075 161 GHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQGYASQL-TLQDCTIKDICQAALNGDQLAQDVIKRAGRYLGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447639941 323 AIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQIDKQPTIGAFAMIKRAMLNGVLL 398
Cdd:cd24075 240 VIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQALPDFRQELKIVASQLDHNSAIGAFALVKRALLEGGLL 315
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
83-402 |
2.21e-101 |
|
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: 303.85 E-value: 2.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 83 FHSVAVRLGRDYIQLSLYNLGGKELASDYHEFHYSHQTQLIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVV 162
Cdd:cd24074 2 WQFLSIRIGRGYITLALRDLNGRLLAEERYPLPAKDNDPFLDRLLESISEFFSRHQKKLERLTAIAITLPGIIDPESGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 163 EYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEI 242
Cdd:cd24074 82 HRLPFYDIKNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 243 GHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQgYESSLANIESITINDVCEHANLGDELAKQSLIRVGNQLGK 322
Cdd:cd24074 162 GHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLLEQ-SPDSMLHGQPISIESLCQAALAGDPLAQDIIIQVGRHLGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 323 AIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQIDKQPTIGAFAMIKRAMLNGVLLQKLL 402
Cdd:cd24074 241 ILAILVNLFNPEKILIGSPLNNAAEILFPALSQSIRQQSLPAYSQHLQIESTKFYNDGTMPGAALIKDALYDGSLLLKLL 320
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
84-390 |
1.19e-83 |
|
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: 257.90 E-value: 1.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 84 HSVAVRLGRDYIQLSLYNLGGKELASDYHEFHYSHQTQ-LIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVV 162
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEaVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 163 EYMPNI-AIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGE 241
Cdd:COG1940 86 LNAPNLpGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 242 IGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIaqgyesslaNIESITINDVCEHANLGDELAKQSLIRVGNQLG 321
Cdd:COG1940 166 IGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG---------GAEKLTAEELFAAARAGDPLALEVLDEAARYLG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 322 KAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQI-DKQPTIGAFAMIKR 390
Cdd:COG1940 237 IGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLgDDAGLLGAAALALE 306
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
86-390 |
6.42e-72 |
|
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: 227.22 E-value: 6.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 86 VAVRLGRDYIQLSLYNLGGKELASdyHEFHYShQTQLIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVVEYM 165
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILAR--ERVPTP-TTTTEETLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYITNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 166 PNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGHI 245
Cdd:pfam00480 78 PNIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 246 QIDPLGEQCQCGNFGCLETVAANPAIISRVKKliaQGyesslaniESITINDVCEHANLGDELAKQSLIRVGNQLGKAIA 325
Cdd:pfam00480 158 QLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---KG--------EDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447639941 326 MTINLFNPQKVVIAGQITaAQEIVFPAIQRNVENQSLKTFHTNL--PIVASQIDKQPTIGAFAMIKR 390
Cdd:pfam00480 227 NLINLFDPQAIVLGGGVS-NADGLLEAIRSLVKKYLNGYLPVPPviIVAASLGDNAGALGAAALAKQ 292
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
84-387 |
1.35e-68 |
|
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: 218.97 E-value: 1.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 84 HSVAVRLGRDYIQLSLYNLGGKELASdyHEFHYSH---QTQLIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETG 160
Cdd:cd24076 2 AVIGVELGVDYITVVVTDLAGEVLWR--REVPLPAsddPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 161 VVEYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVG 240
Cdd:cd24076 80 VVLLAPNLGWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 241 EIGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYESSLANIEsitindvcEHANLGDELAKQSLIRVGNQL 320
Cdd:cd24076 160 EIGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAGGEPLSLAELV--------EAARAGDPAALAALEEVGEYL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447639941 321 GKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQIDKQPT-IGAFAM 387
Cdd:cd24076 232 GIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAaLGAAAL 299
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
84-372 |
5.77e-62 |
|
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: 202.01 E-value: 5.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 84 HSVAVRLGRDYIQLSLYNLGGKELASDYHEFHYSHQTQLIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVVE 163
Cdd:cd24073 2 YVVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGICR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 164 YMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIG 243
Cdd:cd24073 82 WSPLLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 244 HIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGyesslaniESITINDVCEHANLGDELAKQSLIRVGNQLGKA 323
Cdd:cd24073 162 HTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGLRG--------EPLTIEDLLAAARAGDPAARAILRRAGRALGLA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1447639941 324 IAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIV 372
Cdd:cd24073 234 LANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFPGLASDLELV 282
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
83-387 |
3.11e-61 |
|
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: 200.12 E-value: 3.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 83 FHSVAVRLGRDYIQLSLYNLGGKELASDYHEFH-YSHQTQLIEgLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGV 161
Cdd:cd24059 1 PYVIGVEIGRDLLSAVLCDLSGNILAREKYPLDeKENPEEVLE-KLYELIDRLLEKENIKSKILGIGIGAPGPLDVEKGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 162 VEYMPNI-AIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVG 240
Cdd:cd24059 80 ILNPPNFpGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 241 EIGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYesslaniesITINDVCEHANLGDELAKQSLIRVGNQL 320
Cdd:cd24059 160 EIGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARSALGSGR---------SFQLDIVEALQKGDPIADEVIEEAAKYL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447639941 321 GKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQIDK-QPTIGAFAM 387
Cdd:cd24059 231 GIGLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEdAPLLGAAAL 298
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
84-376 |
2.90e-57 |
|
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: 189.80 E-value: 2.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 84 HSVAVRLGRDYIQLSLYNLGGKELasDYHEFHYSHQTQ---LIEGLLFHLNTFIKQQqERIEQFIAIGIALPGLVNPETG 160
Cdd:cd24071 2 YIIGVKIEEGYLVLALTDLKGKIL--EKTRIPFDHETDpekVIELIAENIKKLIKNK-HVEKKLLGIGIAVSGLVDSKKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 161 VVEYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVG 240
Cdd:cd24071 79 IVIRSTILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 241 EIGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYESSLANIESITINDVCEHANLGDELAKQSLIRVGNQL 320
Cdd:cd24071 159 EIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLSLLKELEDFEIEKVREAAEEGDSVATELFKKAGEYL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447639941 321 GKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQI 376
Cdd:cd24071 239 GIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSL 294
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
146-375 |
1.66e-47 |
|
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: 163.88 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 146 AIGIALPGLVNPETGVVEYM-PNI-AIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGA 223
Cdd:cd24068 59 GIGISSAGQVDPKTGEVIYAtDNLpGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 224 GIIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIaqgyesslaNIESITINDVCEHAN 303
Cdd:cd24068 139 AIILDGRLYRGANGSAGELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEAL---------GEPGIDGREIFDLAD 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447639941 304 LGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQ 375
Cdd:cd24068 210 AGDPLAKEVVEEFAEDLATGLANLVHIFDPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAK 281
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
142-372 |
1.02e-45 |
|
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: 159.76 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 142 EQFIAIGIALPGLVNPETGVVEYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGT 221
Cdd:cd24062 60 EDLIGIGVGVPGPVDVETGTVEVAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 222 GAGIIVNGQVFLGYNRNVGEIGHIQIDP-LGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYESSLANI----ESITIN 296
Cdd:cd24062 140 GGGVIANGKIVHGANGAAGEIGHITVNPeGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRIlalgGELTAK 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447639941 297 DVCEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIV 372
Cdd:cd24062 220 DVFEAAKAGDELALAVVDTVARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIV 295
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
86-387 |
8.17e-45 |
|
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: 154.93 E-value: 8.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 86 VAVRLGRDYIQLSLYNLGGKELASDYHEFHYSHQTQ-LIEGLLFHLNTFIKQQQERiEQFIAIGIALPGLVNPETGVVEY 164
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEaVLDRIAELIEELLAEAGVR-ERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 165 MPNI-AIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIG 243
Cdd:cd23763 80 APNLpWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 244 HIQIdplgeqcqcgnfgcletvaanpaiisrvkkliaqgyesslaniesitINDVCEHanlgdelakqslirvgnqLGKA 323
Cdd:cd23763 160 HITV-----------------------------------------------LEEAARY------------------LGIG 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447639941 324 IAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQI-DKQPTIGAFAM 387
Cdd:cd23763 175 LANLINLLNPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELgDDAGLLGAAAL 239
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
84-355 |
1.17e-43 |
|
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: 154.11 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 84 HSVAVRLGRDYIQLSLYNLGGKELASD-YHEFHYSHQTQLIEGLLFHLNTFIKQQQERIEQfiaIGIALPGLVNPETGVV 162
Cdd:cd24072 2 WVLGIVVSPNSLRAQVGNACGELLGEFeYRVITLETPEALIDEIIDCIDRLLKLWKDRVKG---IALAIQGLVDSHKGVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 163 EYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEI 242
Cdd:cd24072 79 LWSPGAPWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 243 GHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYESslANIESITINDVCEHANLGDELAKQSLIRVGNQLGK 322
Cdd:cd24072 159 GHTKVNPDGARCDCGRRGCLETVASNSALKRNARVTLKLGPVS--ADPEKLTMEQLIEALEEGEPIATQIFDRAANAIGR 236
|
250 260 270
....*....|....*....|....*....|...
gi 1447639941 323 AIAMTINLFNPQKVVIAGQITAAQEIVFPAIQR 355
Cdd:cd24072 237 SLANILNLLNPEQVLLYGRGCRAGDLLLPAIRR 269
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
84-388 |
3.72e-43 |
|
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: 152.31 E-value: 3.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 84 HSVAVRLGRDYIQLSLYNLGGKELASDYHEFHYSHQTQLIEGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETgvVE 163
Cdd:cd24077 2 YSIGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVDENE--II 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 164 YMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFgaSKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIG 243
Cdd:cd24077 80 FTPYYDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTF--SEDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 244 HIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIaqgyesslaNIESITINDVCEHANLGDELAKQSLIRVGNQLGKA 323
Cdd:cd24077 158 HMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKK---------GLETLTFDDLIQLYNEGDPEALELIDQFIKYLAIG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447639941 324 IAMTINLFNPQKVVIAGQITAaqeiVFPAIQRNVENQSLKTFHTNLPIVASQIDKQPT-IGAFAMI 388
Cdd:cd24077 229 INNIINTFNPEIIIINSSLIN----EIPELLEKIKEQLSSSFNKYVEILISTLGKNATlLGGAAVA 290
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
142-376 |
1.60e-40 |
|
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466914 [Multi-domain] Cd Length: 301 Bit Score: 145.72 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 142 EQFIAIGIALPGLVNPETGVVEYMPNIA-IDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRG 220
Cdd:cd24064 54 MELLGIGIGSPGSIDRENGIVRFSPNFPdWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 221 TGAGIIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQgYESSLA-NIESITINDVC 299
Cdd:cd24064 134 VGSGVICHGQLLTGYDGIAAELGHVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKR-YPDSLAgESEKINAKHVF 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447639941 300 EHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKTFHTNLPIVASQI 376
Cdd:cd24064 213 DAARKNDPLATMVFRRVVDALAIAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNL 289
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
86-386 |
4.22e-37 |
|
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: 136.70 E-value: 4.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 86 VAVRLGRDYIQLSLYNLGGKELASDYHEF-HYSHQTQLIEGLLFHLNTFIKQqqERIEQFIAIGIALPGLVNPETGVVEY 164
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLKIRQPTpKTGDPGTVSEQVLGLIETLLSK--AGKDSIEGIGVSSAGPLDLRKGTIVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 165 MPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGH 244
Cdd:cd24063 81 SPNIKGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 245 IQIDP-LGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYESSLANI-----ESITINDVCEHANLGDELAKQSLIRVGN 318
Cdd:cd24063 161 LVVDTeSGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTSLKLrnpggEGITAKEVFSAARKGDPLALKIIEKLAR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 319 QLGKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLktfHTNLP-IVASQI-DKQPTIGAFA 386
Cdd:cd24063 241 YNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEKNPA---ISKGPeIVLSELgDDVGLIGALA 307
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
130-393 |
7.82e-36 |
|
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]
Pssm-ID: 273246 [Multi-domain] Cd Length: 318 Bit Score: 133.49 E-value: 7.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 130 LNTFIKQQQERIEQFIAIGIALPGLVNPETGVVEYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDC 209
Cdd:TIGR00744 44 VDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAVNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 210 QDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGHIQIDPLGE-QCQCGNFGCLETVAANPAIISRVKKLIAQGYESS-- 286
Cdd:TIGR00744 124 RDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHIRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEvl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 287 --LANIESITINDVCEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQSLKT 364
Cdd:TIGR00744 204 laLGDGDGISAKHVFVAARQGDPVAVDSYREVARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGG 283
|
250 260 270
....*....|....*....|....*....|
gi 1447639941 365 FHTNLPIVASQI-DKQPTIGAFAMIKRAML 393
Cdd:TIGR00744 284 ARQVADIIAAQLgNDAGLVGAADLARTYII 313
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
144-354 |
1.83e-35 |
|
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: 132.48 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 144 FIAIGIALPGLVNPETGVVEYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGA 223
Cdd:cd24061 54 VSAVGVAAAGFVDADRATVLFAPNIAWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 224 GIIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGYESS-----LANIESITINDV 298
Cdd:cd24061 134 GIVIGGKLLRGAFGIAGEFGHIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATPEGAavllaDGSVDGITGKHI 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447639941 299 CEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQ 354
Cdd:cd24061 214 SEAARAGDPVALDALRELARWLGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIR 269
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
147-387 |
8.29e-30 |
|
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: 117.13 E-value: 8.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 147 IGIALPGLVNPETGVVEYMPNIAID--ALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAG 224
Cdd:cd24060 63 VGISTGGRVNPREGIVLHSTKLIQEwsSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 225 IIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAANPAIISRVKKLIAQGY----ESSLANIESITINDVCE 300
Cdd:cd24060 143 IILNHELIHGSSFCAAELGHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLllveGMSVTNDEEVTAKHLIQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 301 HANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQE-IVFPAIQRnvenQSLKTFhTNLPIVASQIDKQ 379
Cdd:cd24060 223 AAKLGNAKAQKILRTAGTALGLGIVNILHTLNPSLVILSGVLASHYEnIVKDVIAQ----RALPSV-QNVDVVVSDLVDP 297
|
....*...
gi 1447639941 380 PTIGAFAM 387
Cdd:cd24060 298 ALLGAASM 305
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
122-344 |
2.80e-28 |
|
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: 112.64 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 122 LIEGLLFHLNTFIKQQQERIEqfiAIGIALPGLVNPETGVVEYMPNI-AIDALALGDIIRDNFHVECFVGNDVRGMALAE 200
Cdd:cd24070 41 PVEVLADLIREYIEEAGLKPA---AIVIGVPGTVDKDRRTVISTPNIpGLDGVNLADILENKLGIPVILERDVNLLLLYD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 201 HYFGASKDcqDSILVSVHRGTGAG--IIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAANPAIisrvKKL 278
Cdd:cd24070 118 MRAGNLDD--EGVVLGFYIGTGIGnaILINGKPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRAL----EEI 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447639941 279 IAQGYesslaniESITINDVCEHANLGDELakQSLIRvgnQLGKAIAMTINLFNPQKVVIAGQITA 344
Cdd:cd24070 192 AEEHY-------PDTPILDIFVDHGDEPEL--DEFVE---DLALAIATEINILDPDAVILGGGVID 245
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
124-361 |
9.97e-28 |
|
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: 110.88 E-value: 9.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 124 EGLLFHLNTFIKQQQERIEQFIAIGIALPGLVNPETGVVEYMPNI-AIDALALGDIIRDNFHVECFVGNDVRGMALAEHY 202
Cdd:cd24065 36 EAVLDALARAVEALQAEAPGVEAVGLGVPGPLDFRRGRVRFAPNIpGLTDFPIRRGLAERLGLPVVLENDANAAALAEHH 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 203 FGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAANPAIISrvkkliaqg 282
Cdd:cd24065 116 YGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHTTVLPGGPMCGCGLVGCLEALASGRALAR--------- 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447639941 283 yESSLANIESITINDVCEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEIVFPAIQRNVENQS 361
Cdd:cd24065 187 -DASFAYGRPMSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARRYT 264
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
134-358 |
2.11e-24 |
|
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: 101.49 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 134 IKQQQERIEqfiAIGIALPGLVNPETGVVEYM-PNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDS 212
Cdd:cd24152 47 IKRYDEEID---GIAISAPGVIDPETGIIYGGgALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 213 ILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQcgNFGCLetvAANPAIISRVKKliaqgyessLANIES 292
Cdd:cd24152 124 AVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYLLTDDDDKDLL--FFSGL---ASMFGLVKRYNK---------AKGLEP 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447639941 293 ITINDVCEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITaAQEIVFPAIQRNVE 358
Cdd:cd24152 190 LDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIYNIQYILDPEVIVIGGGIS-EQPLFIEDLKKEVN 254
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
118-356 |
4.69e-20 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 89.66 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 118 HQTQ--LIEGLLFHLNTFIKQQQERIEQFI-AIGIALPGLVNPETGVVEYMPNI---AIDALALGDIIRDNFHVECFVGN 191
Cdd:PRK09698 33 KRTAevIAPDLVSGLGEMIDEYLRRFNARChGIVMGFPALVSKDRRTVISTPNLpltALDLYDLADKLENTLNCPVFFSR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 192 DVRGMAL--AEHYfgaskDCQDSILVSVHRGTGAG--IIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAA 267
Cdd:PRK09698 113 DVNLQLLwdVKEN-----NLTQQLVLGAYLGTGMGfaVWMNGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 268 NPAiISRVkkliaqgYESSLANiesITINDVCEHAnlGDELAKQSLIrvgNQLGKAIAMTINLFNPQKVVIAGQITAAQE 347
Cdd:PRK09698 188 GMA-LRRW-------YEQQPRD---YPLSDLFVHA--GDHPFIQSLL---ENLARAIATSINLFDPDAIILGGGVMDMPA 251
|
250
....*....|....*
gi 1447639941 348 ivFP------AIQRN 356
Cdd:PRK09698 252 --FPretliaMIQKY 264
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
147-349 |
3.54e-18 |
|
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: 84.21 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 147 IGIALPGLVNPETGVVeYMPNI-AIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDcQDSIL-VSVHRGTGAG 224
Cdd:cd24057 60 VGIGIPGVIDPEDGTL-ITANIpAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRG-YPSVFgLILGTGVGGG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 225 IIVNGQVFLGYNRNVGEIGH--IQIDPLGEQ-------CQCGNFGCLETVAANPAiisrVKKLIAQGYESSLANIESIti 295
Cdd:cd24057 138 LVVNGRLVGGRSGIAGEWGHgpLPADALLLGydlpvlrCGCGQTGCLETYLSGRG----LERLYAHLYGEELDAPEII-- 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1447639941 296 ndvcEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEIV 349
Cdd:cd24057 212 ----AAWAAGDPQAVAHVDRWLDLLAGCLANILTALDPDVVVLGGGLSNFPALI 261
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
141-342 |
1.14e-17 |
|
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: 82.33 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 141 IEQFIAIGIALPGLVNpeTGVVEYMPNIAI---DALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSV 217
Cdd:cd24069 49 QGQFDRVAVASTGIIR--DGVLTALNPKNLgglSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 218 HRGTGAGIIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVAANPAIisrvkkliaqGYESSLANIESITIND 297
Cdd:cd24069 127 STGVGGGLVLNGQLLTGPNGLAGHIGHTLADPPGPVCGCGRRGCVEAIASGTAI----------AAAASEILGEPVDAKD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447639941 298 VCEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQI 342
Cdd:cd24069 197 VFERARSGDEEAARLIDRAARALADLIADLKATLDLDCVVIGGSV 241
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
116-340 |
2.84e-17 |
|
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: 81.48 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 116 YSHQTQLIEGLlfhlntfIKQQQERIEQFIAIGIALPGLVNPETGVVEYMPNIAIDALALGDIIRDNFHVECFVGNDVRG 195
Cdd:cd24066 35 YEATLDAIADL-------VEEAEEELGAPATVGIGTPGSISPRTGLVKNANSTWLNGKPLKADLEARLGRPVRIENDANC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 196 MALAEHYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGHIQIDPL------GEQCQCGNFGCLETVAANP 269
Cdd:cd24066 108 FALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGHNPLPWPdedelpGPPCYCGKRGCVETFLSGP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447639941 270 AIISRVKKLIAqgyesslaniESITINDVCEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAG 340
Cdd:cd24066 188 ALERDYARLTG----------KTLSAEEIVALARAGDAAAVATLDRFLDRLGRALANVINILDPDVIVLGG 248
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
147-348 |
2.42e-14 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 73.14 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 147 IGIALPGLVNPETGVVEYMPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGTGAGII 226
Cdd:PRK09557 60 VGVGIPGSISPYTGLVKNANSTWLNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 227 VNGQVFLGYNRNVGEIGHiqiDPL------------GEQCQCGNFGCLETVAANPAIISRVKKLIAQgyesSLANIESIT 294
Cdd:PRK09557 140 INGRVHIGGNGIAGEWGH---NPLpwmdedelryrnEVPCYCGKQGCIETFISGTGFATDYRRLSGK----ALKGSEIIR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1447639941 295 INDVcehanlGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAGQITAAQEI 348
Cdd:PRK09557 213 LVEE------GDPVAELAFRRYEDRLAKSLAHVINILDPDVIVLGGGMSNVDRL 260
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
187-342 |
3.08e-13 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 69.56 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 187 CFVGNDVRGMALAEhYFGASKDCQDSILVSVHRGTGAGIIVNGQVFLGYNRNVGEIGHIQIDPLGEQCQCGNFGCLETVA 266
Cdd:PRK05082 100 TIALNDAQAAAWAE-YQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHTLADPHGPVCGCGRRGCVEAIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 267 ANPAiisrvkklIAQGYESSLANIESitiNDVCEHANLGDELAkQSLIrvgNQLGKAIA-----MTINLfNPQKVVIAGQ 341
Cdd:PRK05082 179 SGRA--------IAAAAQGWLAGCDA---KTIFERAGQGDEQA-QALI---NRSAQAIArliadLKATL-DCQCVVLGGS 242
|
.
gi 1447639941 342 I 342
Cdd:PRK05082 243 V 243
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
147-340 |
1.13e-11 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 65.01 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 147 IGIALPGLVNPETGVVeYMPNIAIdalALGDIIRDNFHV----ECFVGNDVRGMALAEHYfgASKDCQDSILVSVHRGTG 222
Cdd:PRK13310 60 VGIGIPGMPETEDGTL-YAANVPA---ASGKPLRADLSArlgrDVRLDNDANCFALSEAW--DDEFTQYPLVMGLILGTG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 223 --AGIIVNGQVFLGYNRNVGEIGHIQI-----DPLGE-----QCQCGNFGCLETVaanpaiisrvkkLIAQGYESSLANI 290
Cdd:PRK13310 134 vgGGLVFNGKPISGRSYITGEFGHMRLpvdalTLLGWdaplrRCGCGQKGCIENY------------LSGRGFEWLYQHY 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1447639941 291 --ESITINDVCEHANLGDELAKQSLIRVGNQLGKAIAMTINLFNPQKVVIAG 340
Cdd:PRK13310 202 ygEPLQAPEIIALYYQGDEQAVAHVERYLDLLAICLGNILTIVDPHLVVLGG 253
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
133-357 |
2.91e-09 |
|
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: 57.55 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 133 FIKQQQERIEqfiAIGIALPGLVNPETGVVEY-----MPNIAIDALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASK 207
Cdd:cd24067 43 FFREQEEPID---AIGIASFGPIDLNPTSPTYgyittTPKPGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 208 DCQDSILVSVHRGTGAGIIVNGQVFLGynRNVGEIGHIQIDPLGEQ------CQCGNfGCLETVAANPAIISRVKKliaq 281
Cdd:cd24067 120 GLDSLAYITVGTGIGVGLVVNGKPVHG--LLHPEMGHIRVPRHPDDdgfpgvCPFHG-DCLEGLASGPAIAARWGI---- 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447639941 282 gyesslaniesitindvcehanLGDELAKQSLIR--VGNQLGKAIAMTINLFNPQKVVIAGQItAAQEIVFPAIQRNV 357
Cdd:cd24067 193 ----------------------PAEELPDDHPAWdlEAYYLAQACANLTLTLSPERIVLGGGV-MQRPGLFPRIREKF 247
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
146-263 |
2.62e-07 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 51.57 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 146 AIGIALPGLVNPETGVVeYMPNIAIdalALGDIIRDNF----HVECFVGNDVRGMALAEHYFGASKDCQDSILVSVHRGT 221
Cdd:PRK13311 59 SVGIGIPGLPNADDGTV-FTANVPS---AMGQPLQADLsrliQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGV 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1447639941 222 GAGIIVNGQVFLGYNRNVGEIGHIQ-----IDPLGEQ-----CQCGNFGCLE 263
Cdd:PRK13311 135 GGGLIVNGSIVSGRNHITGEFGHFRlpvdaLDILGADiprvpCGCGHRGCIE 186
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
134-248 |
2.08e-05 |
|
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: 45.64 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 134 IKQQQERIEQFIAIGIALPGLVnpETGVVEYMPNIAID--ALALGDIIRDNFHVECFVGNDVRGMALAEHYFGASKDCQD 211
Cdd:cd24058 45 VAELVAHFPWFGPVGVGFPGVV--RRGVVRTAANLDKSwiGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKG 122
|
90 100 110
....*....|....*....|....*....|....*....
gi 1447639941 212 SILVsVHRGTGAG--IIVNGQvfLGYNRnvgEIGHIQID 248
Cdd:cd24058 123 VVLV-LTLGTGIGsaLFVDGH--LVPNT---ELGHLEIR 155
|
|
| HTH_MARR |
smart00347 |
helix_turn_helix multiple antibiotic resistance protein; |
22-102 |
7.52e-05 |
|
helix_turn_helix multiple antibiotic resistance protein;
Pssm-ID: 197670 [Multi-domain] Cd Length: 101 Bit Score: 41.43 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447639941 22 RLIDLQGPISRIQVADVSQLAPASVTKITRQLLERGLIkevAQQASTGGRRA--ISLTTEVAPFHSVAVRLGRDYIQLSL 99
Cdd:smart00347 17 RILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLV---RREPSPEDRRSvlVSLTEEGRELIEQLLEARSETLAELL 93
|
...
gi 1447639941 100 YNL 102
Cdd:smart00347 94 AGL 96
|
|
| MarR |
pfam01047 |
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ... |
22-74 |
1.12e-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: 36.76 E-value: 1.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1447639941 22 RLIDLQGPISRIQVADVSQLAPASVTKITRQLLERGLIKevaQQASTGGRRAI 74
Cdd:pfam01047 10 RILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIE---RSRSPEDRREV 59
|
|
| MntR |
COG1321 |
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription]; |
19-79 |
1.55e-03 |
|
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
Pssm-ID: 440932 [Multi-domain] Cd Length: 135 Bit Score: 38.65 E-value: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447639941 19 AVYRLIDLQGPISRIQVADVSQLAPASVTKITRQLLERGLIKEVaqqastgGRRAISLTTE 79
Cdd:COG1321 14 AIYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEYE-------PYGGITLTEE 67
|
|
|