|
Name |
Accession |
Description |
Interval |
E-value |
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
5-340 |
4.93e-148 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 418.73 E-value: 4.93e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLR 84
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 85 YTvfqttgsvpiatviineasgsrtilyydsflvadfrrrgvdvsqvaWQSKGDTPSSCCIINNSNGNRTIVLHDTSLPD 164
Cdd:cd01939 81 HC----------------------------------------------YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 165 VSATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPpEQKIRVSVEVEKPREELFQLFGYGDVVFVSKDVAKHL 244
Cdd:cd01939 115 VTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIRITISVEVEKPREELLELAAYCDVVFVSKDWAQSR 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 245 GFQSAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSQG-RSVQEAL 323
Cdd:cd01939 194 GYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEAL 273
|
330
....*....|....*..
gi 1034613839 324 RFGCQVAGKKCGLQGFD 340
Cdd:cd01939 274 DFGNRVASQKCTGVGFD 290
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-334 |
1.33e-37 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 136.17 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYsvdlr 84
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 85 ytvfqttgsvpiatviineasgsrtilyydsflvadfrrrGVDVSQVAwQSKGDTPSSCCIINNSNGNRTIVLHDTSLPD 164
Cdd:COG0524 76 ----------------------------------------GVDTSGVR-RDPGAPTGLAFILVDPDGERTIVFYRGANAE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 165 VSATDFEKVDLTQFKWIHIEG------RNASEQVKMLQRIDAHNtrqppeqkIRVSVEV-------EKPREELFQLFGYG 231
Cdd:COG0524 115 LTPEDLDEALLAGADILHLGGitlasePPREALLAALEAARAAG--------VPVSLDPnyrpalwEPARELLRELLALV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 232 DVVFVSKDVAKHL-GFQSAEEALRGLYGRVRKGAVLVCAwaEEGADALGpDGKLLHSDAFPPpRVVDTLGAGDTFNASVI 310
Cdd:COG0524 187 DILFPNEEEAELLtGETDPEEAAAALLARGVKLVVVTLG--AEGALLYT-GGEVVHVPAFPV-EVVDTTGAGDAFAAGFL 262
|
330 340
....*....|....*....|....
gi 1034613839 311 FSLSQGRSVQEALRFGCQVAGKKC 334
Cdd:COG0524 263 AGLLEGLDLEEALRFANAAAALVV 286
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-341 |
1.20e-27 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 109.31 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 5 QILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLR 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 85 YTVfQTTGSVPIATVIINEASGSRTILYYDsflvadfrrrgvdvsqvawqskGDTPsscciinnsngnrtivLHDTSLPD 164
Cdd:cd01945 81 FIV-VAPGARSPISSITDITGDRATISITA----------------------IDTQ----------------AAPDSLPD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 165 vsatdfekVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPpeqkirVSVEVEKPR--EELFQLfgyGDVVFVSKDVAK 242
Cdd:cd01945 122 --------AILGGADAVLVDGRQPEAALHLAQEARARGIPIP------LDLDGGGLRvlEELLPL---ADHAICSENFLR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 243 HLGFQSAEEALRGLYGRVRKgAVLVCAwAEEGADALGPDGKLLHSDAFpPPRVVDTLGAGDTFNASVIFSLSQGRSVQEA 322
Cdd:cd01945 185 PNTGSADDEALELLASLGIP-FVAVTL-GEAGCLWLERDGELFHVPAF-PVEVVDTTGAGDVFHGAFAHALAEGMPLREA 261
|
330
....*....|....*....
gi 1034613839 323 LRFGCQVAGKKCglQGFDG 341
Cdd:cd01945 262 LRFASAAAALKC--RGLGG 278
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-338 |
2.07e-24 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 100.88 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLRY 85
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 86 TVFQTTGSVPIATVIINEAsGSRTILYYDSfLVADFRRRGVDVSQVAwqskgdtpsscciinnsNGNRTIVLHDTSLPDV 165
Cdd:pfam00294 80 VVIDEDTRTGTALIEVDGD-GERTIVFNRG-AAADLTPEELEENEDL-----------------LENADLLYISGSLPLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 166 SATDfekvDLTQFKWIhiegrnASEQVKMLQRIDAHntrqppeqkirvsveVEKPREELFQLFGYGDVVFVSKDVAKHLG 245
Cdd:pfam00294 141 LPEA----TLEELIEA------AKNGGTFDPNLLDP---------------LGAAREALLELLPLADLLKPNEEELEALT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 246 FQ---SAEEALRGLYGRVRKGA-VLVCAWAEEGADALGPDGKLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQE 321
Cdd:pfam00294 196 GAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEGDGEVHV-PAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEE 274
|
330
....*....|....*..
gi 1034613839 322 ALRFGCQVAGKKCGLQG 338
Cdd:pfam00294 275 ALRFANAAAALVVQKSG 291
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-338 |
2.27e-20 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 89.56 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 5 QILCVGLVVLDVislvdkYPKEDSEIRClSQRWQR--GGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVD 82
Cdd:cd01166 1 DVVTIGEVMVDL------SPPGGGRLEQ-ADSFRKffGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 83 LRYTVfqTTGSVPIATVII-NEASGSRTILYYdsflvadfrRRGVDVSQVawqskgdtpsscciinnsngnrtivlhdts 161
Cdd:cd01166 74 TSHVR--VDPGRPTGLYFLeIGAGGERRVLYY---------RAGSAASRL------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 162 lpdvSATDFEKVDLTQFKWIHIEG----RNASEQVKMLQRIdahntRQPPEQKIRVSVEV---------EKPREELFQLF 228
Cdd:cd01166 113 ----TPEDLDEAALAGADHLHLSGitlaLSESAREALLEAL-----EAAKARGVTVSFDLnyrpklwsaEEAREALEELL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 229 GYGDVVFVSK-DVAKHLGFQSAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGkLLHSDAFPPPrVVDTLGAGDTFNA 307
Cdd:cd01166 184 PYVDIVLPSEeEAEALLGDEDPTDAAERALALALGVKAVVVKLGAEGALVYTGGG-RVFVPAYPVE-VVDTTGAGDAFAA 261
|
330 340 350
....*....|....*....|....*....|.
gi 1034613839 308 SVIFSLSQGRSVQEALRFGCQVAGKKCGLQG 338
Cdd:cd01166 262 GFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-333 |
3.44e-19 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 85.83 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSmapghVADfvlDDLRRYSVDLry 85
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAA-----VGE---DFHGRLYLEE-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 86 tvfqttgsvpiatviineasgsrtilyydsflvadFRRRGVDVSQVawqSKGDTPSS--CCIINNSNGNRTIVLH----D 159
Cdd:cd01942 72 -----------------------------------LREEGVDTSHV---RVVDEDSTgvAFILTDGDDNQIAYFYpgamD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 160 TSLPDVSATDFEKVDLtqfkwIHIEGRnaseqvkmlqRIDAHNTRQPPEQKIRVS-----VEVEKPREELFQLFGYGDVV 234
Cdd:cd01942 114 ELEPNDEADPDGLADI-----VHLSSG----------PGLIELARELAAGGITVSfdpgqELPRLSGEELEEILERADIL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 235 FVSKDVAKHLgfqsAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLLHsDAFPPPRVVDTLGAGDTFNASVIFSLS 314
Cdd:cd01942 179 FVNDYEAELL----KERTGLSEAELASGVRVVVVTLGPKGAIVFEDGEEVEV-PAVPAVKVVDTTGAGDAFRAGFLYGLL 253
|
330
....*....|....*....
gi 1034613839 315 QGRSVQEALRFGCQVAGKK 333
Cdd:cd01942 254 RGYDLEESLRLGNLAASLK 272
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
3-338 |
7.80e-19 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 85.36 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 3 EKQILCVGLVVLDVISLVDKYP------KEDSEIRCLSQRWQR-----------GGNASNSCTVLSLLGAPCAFMGSMAP 65
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFleklglKKGDMILADMEEQEEllaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 66 GHVADFVLDDLRRYSVDLRYtvfqttgsvpiatviineasgsrtilyydsflvadfrrrgvdvsqvawQSKGDTPSSCCI 145
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTRY------------------------------------------------QVQPDGPTGTCA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 146 IN-NSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEG--RNASEQVKMLQRIDAHntrqppEQKIRVSV------E 216
Cdd:cd01168 113 VLvTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGylLTVPPEAILLAAEHAK------ENGVKIALnlsapfI 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 217 VEKPREELFQLFGYGDVVFVSKDVAKHLGFQ----SAEEALRGLYGRVRKGAVLVCAwaeEGAdALGPDGKLLHSDAFPP 292
Cdd:cd01168 187 VQRFKEALLELLPYVDILFGNEEEAEALAEAettdDLEAALKLLALRCRIVVITQGA---KGA-VVVEGGEVYPVPAIPV 262
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034613839 293 PRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQG 338
Cdd:cd01168 263 EKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
19-338 |
4.57e-13 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 68.15 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 19 LVDKYPKEDseirclsqRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFVLDDLRRYSVDLRYtVFQTTGSVPIAT 98
Cdd:cd01940 9 VVDKYLHLG--------KMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISH-CRVKEGENAVAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 99 VIINEasGSRTILYYDSFLVADFRRrgvdvsqvawqskgdtpsscciinnsngnrtivlhdtslpdvSATDFEKvdLTQF 178
Cdd:cd01940 80 VELVD--GDRIFGLSNKGGVAREHP------------------------------------------FEADLEY--LSQF 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 179 KWIHIegrNASEQVKMLQRidahNTRQPPEQKIRVSVEVEKPR--EELFQLFGYGDVVFVSkdvAKHLGFQSAEEALRGL 256
Cdd:cd01940 114 DLVHT---GIYSHEGHLEK----ALQALVGAGALISFDFSDRWddDYLQLVCPYVDFAFFS---ASDLSDEEVKAKLKEA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 257 YGRvrkGAVLVCAwaeegadALGPDGKLLHSDAF---PPPR---VVDTLGAGDTFNASVIFSLSQGR-SVQEALRFGCQV 329
Cdd:cd01940 184 VSR---GAKLVIV-------TRGEDGAIAYDGAVfysVAPRpveVVDTLGAGDSFIAGFLLSLLAGGtAIAEAMRQGAQF 253
|
....*....
gi 1034613839 330 AGKKCGLQG 338
Cdd:cd01940 254 AAKTCGHEG 262
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
5-338 |
3.30e-12 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 66.12 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 5 QILCVGLVVLDVISlvDKYPKEDSEIRCLsqrwqrGGNASNSCTVLSLLGAPCAFMGSmapghVADfvlDDLRRysvdlr 84
Cdd:cd01167 1 KVVCFGEALIDFIP--EGSGAPETFTKAP------GGAPANVAVALARLGGKAAFIGK-----VGD---DEFGD------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 85 ytvfqttgsvpiatviineasgsrtilyydsFLVADFRRRGVDVSQVawQSKGDTPSSCCIIN-NSNGNRTIVLHDTSLP 163
Cdd:cd01167 59 -------------------------------FLLETLKEAGVDTRGI--QFDPAAPTTLAFVTlDADGERSFEFYRGPAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 164 DVSA-TDFEKVDLTQFKWIH------IEGRNASEQVKMLQRIDAH--------NTRQPPEQKIrvsvevEKPREELFQLF 228
Cdd:cd01167 106 DLLLdTELNPDLLSEADILHfgsialASEPSRSALLELLEAAKKAgvlisfdpNLRPPLWRDE------EEARERIAELL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 229 GYGDVVFVSKDVAKHLGFQSAEEALRGLYGRVRKGAVLVcawaeegadALGPDGKLLHSDAF------PPPRVVDTLGAG 302
Cdd:cd01167 180 ELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLV---------TRGADGALLYTKGGvgevpgIPVEVVDTTGAG 250
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1034613839 303 DTFNASVIFSLSQG-------RSVQEALRFGCQVAGKKCGLQG 338
Cdd:cd01167 251 DAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAG 293
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
246-330 |
1.70e-10 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 61.08 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 246 FQSAEEALRGLYGRVRKGAVLvcawaeegadALGPDGKLLHSDA----FPPPRV--VDTLGAGDTFNASVIFSLSQGRSV 319
Cdd:TIGR02152 193 EEDAEKAAEKLLEKGVKNVII----------TLGSKGALLVSKDesklIPAFKVkaVDTTAAGDTFNGAFAVALAEGKSL 262
|
90
....*....|.
gi 1034613839 320 QEALRFGCQVA 330
Cdd:TIGR02152 263 EDAIRFANAAA 273
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
278-331 |
5.86e-10 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 59.49 E-value: 5.86e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 278 LGPDGKLLHSD----AFPPPRV--VDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAG 331
Cdd:cd01174 219 LGAKGALLASGgeveHVPAFKVkaVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
219-326 |
1.67e-08 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 54.85 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 219 KP-REELFQLFGygdvvfvskdvAKHLGFQSAEEALRGLygrVRKGA--VLVcawaeegadALGPDGKLL-HSDAF---- 290
Cdd:cd01164 182 KPnREELEELFG-----------RPLGDEEDVIAAARKL---IERGAenVLV---------SLGADGALLvTKDGVyras 238
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034613839 291 -PPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 326
Cdd:cd01164 239 pPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
3-330 |
2.26e-08 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 54.74 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 3 EKQILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGsmapghvadFVLDDlrrysvd 82
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVG---------MVGTD------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 83 lrytvfqttgsvpiatviineASGSRTIlyydsflvADFRRRGVDVSQVAWQSKGDTPSSCCIINNSNGNRTIVLHDTS- 161
Cdd:PTZ00292 79 ---------------------GFGSDTI--------KNFKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGAn 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 162 ------LPDVSATDFE---KVDLTQFKwIHIEG-----RNASEQ--VKMLQRIDAHNTRQPPEQK-IRVSVEVEKPRE-E 223
Cdd:PTZ00292 130 naltpqMVDAQTDNIQnicKYLICQNE-IPLETtldalKEAKERgcYTVFNPAPAPKLAEVEIIKpFLKYVSLFCVNEvE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 224 LFQLFGyGDVV--FVSKDVAKHLGFQSAEEALRGLYGrvrKGavlvCAWAEEGADALGPDGKLLhsdafpppRVVDTLGA 301
Cdd:PTZ00292 209 AALITG-MEVTdtESAFKASKELQQLGVENVIITLGA---NG----CLIVEKENEPVHVPGKRV--------KAVDTTGA 272
|
330 340
....*....|....*....|....*....
gi 1034613839 302 GDTFNASVIFSLSQGRSVQEALRFGCQVA 330
Cdd:PTZ00292 273 GDCFVGSMAYFMSRGKDLKESCKRANRIA 301
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
211-326 |
4.20e-08 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 53.99 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 211 IRVSVEVEKP-REELFQLFGygdvvfvsKDVAkhlGFQSAEEALRGLygrVRKGAVLVCAwaeegadALGPDG------- 282
Cdd:COG1105 174 LEAGPDLIKPnLEELEELLG--------RPLE---TLEDIIAAAREL---LERGAENVVV-------SLGADGallvted 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034613839 283 KLLHSDAfPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 326
Cdd:COG1105 233 GVYRAKP-PKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
113-338 |
2.65e-07 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 51.28 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 113 YDSFLVADFRRRGVDVSQVawqSKGDTPSSCCIINNSNGNRtiVLHDTS---LPDVSATDFEKVDLTQFKWIH--IEGrN 187
Cdd:PRK09813 51 YGTKLKQDLARMGVDISHV---HTKHGVTAQTQVELHDNDR--VFGDYTegvMADFALSEEDYAWLAQYDIVHaaIWG-H 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 188 ASEQvkmLQRIDAHNTRqppeqkirVSVE-VEKPREELFQ-LFGYGDVVFVSKDvakhlgfQSAEEALRGLYGRVRKGA- 264
Cdd:PRK09813 125 AEDA---FPQLHAAGKL--------TAFDfSDKWDSPLWQtLVPHLDYAFASAP-------QEDEFLRLKMKAIVARGAg 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613839 265 VLVCAWAEEGAdaLGPDGKLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQG 338
Cdd:PRK09813 187 VVIVTLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
115-333 |
8.29e-07 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 50.00 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 115 SFLVADFRRRGVDVSQVawQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDVSATDFE---KVDLTQFKWIHIEGrNASEQ 191
Cdd:cd01941 65 ESILEESEKAGLNVRGI--VFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLrkiREALKEAKPIVVDA-NLPEE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 192 VkmLQRIdahnTRQPPEQKIRVSVEVEK-PR-EELFQLFGYGDVVFVSKDVAKHLgfqsAEEALRGLYGRVRKGAVLVCA 269
Cdd:cd01941 142 A--LEYL----LALAAKHGVPVAFEPTSaPKlKKLFYLLHAIDLLTPNRAELEAL----AGALIENNEDENKAAKILLLP 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613839 270 WAEEGADALGPDGKLLHSDA-------FPPP---RVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGcQVAGKK 333
Cdd:cd01941 212 GIKNVIVTLGAKGVLLSSREggvetklFPAPqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA-QAAAAL 284
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
272-332 |
6.90e-06 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 47.03 E-value: 6.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034613839 272 EEGAdALGPDGKLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGK 332
Cdd:cd01947 199 ELGA-ILYPGGRYNHVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAI 257
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
172-313 |
7.80e-06 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 45.93 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 172 KVDLTQFKWIHIEGRNASEQVkMLQRIDAHNTRQPPeqkirVSVE-----VEKPREELFQLFGYGDVVFVSKDVAKHLGF 246
Cdd:cd00287 52 SVTLVGADAVVISGLSPAPEA-VLDALEEARRRGVP-----VVLDpgpraVRLDGEELEKLLPGVDILTPNEEEAEALTG 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 247 Q---SAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLLHSDAFPPPRVVDTLGAGDTFNASVIFSL 313
Cdd:cd00287 126 RrdlEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
118-327 |
1.35e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 46.32 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 118 VADFRRRGVDVSQVAwQSKGDTPSSCCIINNSnGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIegRNASEQVKMLQR 197
Cdd:PLN02379 120 VSNMGFSGVDLSRLR-AKKGPTAQCVCLVDAL-GNRTMRPCLSSAVKLQADELTKEDFKGSKWLVL--RYGFYNLEVIEA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 198 IdAHNTRQppeQKIRVSVE------VEKPREELFQLFGYGDV--VFVSKDVAKHL--GFQSA--EEALRGLYGRvrkgav 265
Cdd:PLN02379 196 A-IRLAKQ---EGLSVSLDlasfemVRNFRSPLLQLLESGKIdlCFANEDEARELlrGEQESdpEAALEFLAKY------ 265
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613839 266 lvCAWAeegADALGPDG-------KLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGC 327
Cdd:PLN02379 266 --CNWA---VVTLGSKGciarhgkEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGA 329
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
247-331 |
1.37e-05 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 46.34 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 247 QSAEEALRGLYGRVRKGAVLVCAwAEEGADALGPDGKLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 326
Cdd:COG2870 221 EELVAAAAELLERLGLEALLVTR-GEEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEAAELA 298
|
....*
gi 1034613839 327 CQVAG 331
Cdd:COG2870 299 NLAAG 303
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
248-331 |
1.96e-05 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 45.49 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 248 SAEEALRGLYGRVRkgAVLVCAWAEEGADALGPDGKLLHSDAFPPpRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGC 327
Cdd:cd01944 202 AAEASALRIYAKTA--APVVVRLGSNGAWIRLPDGNTHIIPGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLAN 278
|
....
gi 1034613839 328 QVAG 331
Cdd:cd01944 279 AAAA 282
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
278-326 |
2.07e-05 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 45.63 E-value: 2.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034613839 278 LGPDGKLLHSDAF----PPPRV--VDTLGAGDTFNASVIFSLSQGRSVQEALRFG 326
Cdd:PRK11142 222 LGSRGVWLSENGEgqrvPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
6-61 |
2.81e-05 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 44.39 E-value: 2.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613839 6 ILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMG 61
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG 57
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
216-333 |
5.92e-04 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 40.85 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 216 EVEKPREELFQLFGYGDVVFVSKDVAKHLgfQSAEEALRGLygRVRKGAVLVCAWAEEGADALgpDGKLLHSDAFPPPRV 295
Cdd:cd01937 141 RANQEKLIKCVILKLHDVLKLSRVEAEVI--STPTELARLI--KETGVKEIIVTDGEEGGYIF--DGNGKYTIPASKKDV 214
|
90 100 110
....*....|....*....|....*....|....*...
gi 1034613839 296 VDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKK 333
Cdd:cd01937 215 VDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKF 252
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
247-335 |
1.03e-03 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 40.24 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 247 QSAEEALRGLYGRVRKGAVLVcAWAEEGADALGPDGKLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSQGRSVQEALRFG 326
Cdd:cd01172 204 DELEAAGEKLLELLNLEALLV-TLGEEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLA 281
|
....*....
gi 1034613839 327 CQVAGKKCG 335
Cdd:cd01172 282 NAAAGVVVG 290
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
217-322 |
3.28e-03 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 38.60 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 217 VEKPREELFQLFGYGDVVFVSKDVAKHLgfqsaeealRGLYGRVrKGAVLVCAWaeeGADAL----GPDGKLLHSD---- 288
Cdd:cd01946 150 ISIKPEKLKKVLAKVDVVIINDGEARQL---------TGAANLV-KAARLILAM---GPKALiikrGEYGALLFTDdgyf 216
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034613839 289 ---AFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEA 322
Cdd:cd01946 217 aapAYPLESVFDPTGAGDTFAGGFIGYLASQKDTSEA 253
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
272-330 |
3.83e-03 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 38.52 E-value: 3.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 272 EEGADALGPDGKLLhsdAFPPP-RVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVA 330
Cdd:PRK09513 226 AEGALWVNASGEWI---AKPPAcDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVS 282
|
|
| RRM3_NGR1_NAM8_like |
cd12346 |
RNA recognition motif 3 (RRM3) found in yeast negative growth regulatory protein NGR1 (RBP1), ... |
222-270 |
3.93e-03 |
|
RNA recognition motif 3 (RRM3) found in yeast negative growth regulatory protein NGR1 (RBP1), yeast protein NAM8 and similar proteins; This subfamily corresponds to the RRM3 of NGR1 and NAM8. NGR1, also termed RNA-binding protein RBP1, is a putative glucose-repressible protein that binds both RNA and single-stranded DNA (ssDNA) in yeast. It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the carboxyl terminus which also harbors a methionine-rich region. The family also includes protein NAM8, which is a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. Like NGR1, NAM8 contains two RRMs.
Pssm-ID: 409782 [Multi-domain] Cd Length: 72 Bit Score: 35.76 E-value: 3.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613839 222 EELFQLFG-YGDVVFVSKDVAKHLGF------QSAEEALRGLYGRVRKGAVLVCAW 270
Cdd:cd12346 16 EDLRVLFGpFGEIVYVKIPPGKGCGFvqfvnrASAEAAIQKLQGTPIGGSRIRLSW 71
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
221-316 |
7.76e-03 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 37.61 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613839 221 REELFQLFGYGDVvfvskdvakhlgfQSAEEALRGLYGR----VRKGAVLVCAWAEegadalgpdGKLLHsdaFPPPRV- 295
Cdd:PRK09434 188 EEELCFLSGTSQL-------------EDAIYALADRYPIalllVTLGAEGVLVHTR---------GQVQH---FPAPSVd 242
|
90 100
....*....|....*....|..
gi 1034613839 296 -VDTLGAGDTFNASVIFSLSQG 316
Cdd:PRK09434 243 pVDTTGAGDAFVAGLLAGLSQA 264
|
|
| |
