|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-474 |
1.23e-161 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 465.87 E-value: 1.23e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAETGELVRFGQAKHPNGT------SVDPSYWWSAFQEAAEQAGG-----LDDVSALAVGGQQ 74
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAETGRVVASGSAPHENILidpgwaEQDPEDWWDALQAAFAQLLKdagaeLRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 75 HG*VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAAPAQDgepedpiargkqrwvkaVGSSPVASYTLTKVAWVAENE 154
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLL-----------------VGLNIPARFTASKLLWLKENE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 155 PENVKKIAAICLPHDWLSWRIAGYgpvaegedahleaLFTDRSDASGTIYYDAASNEYRRDLIA*vleaaegaKAAQSHA 234
Cdd:cd07809 144 PEHYARIAKILLPHDYLNWKLTGE-------------KVTGLGDASGTFPIDPRTRDYDAELLA---------AIDPSRD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 235 EAIVLPTVLGPRDAAPVKADPAIAGKNVEGGCLLAPGGGDNA*ASLGLG*-AVGDVSISLGTSGVAAAISENPTYDLTGA 313
Cdd:cd07809 202 LRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGVvNPGTVAVSLGTSGTAYGVSDKPVSDPHGR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 314 VSGFADCTGHYLPLACTING-SRILDAGRAALGVDYDELAKLAFASKPGANGITLVPYFDGERTPNRPNATATFSG*TLA 392
Cdd:cd07809 282 VATFCDSTGGMLPLINTTNClTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLLPFLNGERTPNLPHGRASLVGLTLS 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 393 NTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAAWV 472
Cdd:cd07809 362 NFTRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWG 441
|
..
3I8B_A 473 LS 474
Cdd:cd07809 442 AG 443
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-505 |
7.75e-124 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 371.47 E-value: 7.75e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 5 TLVAGVDTSTQSCKVRVTDAEtGELVRFGQAKHP-----NGTS-VDPSYWWSAFQEA----AEQAGG-LDDVSALAVGGQ 73
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDAD-GEVVASASAEYPlssphPGWAeQDPEDWWEAVVEAirelLAKAGVdPEEIAAIGVSGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 74 QHG*VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAApaqdgepedpiargkqRWVKAVGSSPVASYTLTKVAWVAEN 153
Cdd:COG1070 80 MHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEE----------------ALYEITGNPLHPGFTAPKLLWLKEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 154 EPENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLia*vLEAAeGAKAAQsh 233
Cdd:COG1070 144 EPEIFARIAKVLLPKDYLRYRLTG-------------EFVTDYSDASGTGLLDVRTRDWSDEL----LEAL-GIDREL-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 234 aeaivLPTVLGPRDAA-PVKADPAiAGKNVEGGCLLAPGGGDNA*ASLGLG*-AVGDVSISLGTSGVAAAISENPTYDLT 311
Cdd:COG1070 204 -----LPELVPPGEVAgTLTAEAA-AETGLPAGTPVVAGAGDNAAAALGAGAvEPGDAAVSLGTSGVVFVVSDKPLPDPE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 312 GAVSGFADC-TGHYLPLACTINGSRILDAGRAALGV----DYDELAKLAFASKPGANGITLVPYFDGERTP-NRPNATAT 385
Cdd:COG1070 278 GRVHTFCHAvPGRWLPMGATNNGGSALRWFRDLFADgeldDYEELNALAAEVPPGADGLLFLPYLSGERTPhWDPNARGA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 386 FSG*TLaNTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGA 465
Cdd:COG1070 358 FFGLTL-SHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGA 436
|
490 500 510 520
....*....|....*....|....*....|....*....|.
3I8B_A 466 ARQAAWVLSGETEPPAWQLTIDGV-ETGEPTEAVYEAYAKA 505
Cdd:COG1070 437 ALLAAVGLGLYDDLEEAAAAMVRVgETIEPDPENVAAYDEL 477
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
9-506 |
1.52e-123 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 370.11 E-value: 1.52e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 9 GVDTSTQSCKVRVTDaETGELVRFGQAKHP-----NGTS-VDPSYWWSAFQEAAEQAG-----GLDDVSALAVGGQQHG* 77
Cdd:TIGR01312 2 GIDLGTSGVKALLVD-EQGEVIASGSAPHTvisphPGWSeQDPEDWWDATEEAIKELLeqaseMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 78 VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLgaapaqdgepedpiarGKQRWVKAVGSSPVASYTLTKVAWVAENEPEN 157
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAEL----------------GDERVLEITGNLALPGFTAPKLLWVRKHEPEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 158 VKKIAAICLPHDWLSWRIAGYGpvaegedahlealFTDRSDASGTIYYDAASNEYRRDLia*vLEAAEGAKAaqshaeai 237
Cdd:TIGR01312 145 FARIAKVMLPKDYLRYRLTGEY-------------VTEYSDASGTGWFDVAKRAWSKEL----LDALDLPES-------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 238 VLPTVLGPrDAAPVKADPAIAGK-NVEGGCLLAPGGGDNA*ASLGLG*-AVGDVSISLGTSGVAAAISENPTYDLTGAVS 315
Cdd:TIGR01312 200 QLPELIES-SEKAGTVRPEVAARlGLSAGVPVAAGGGDNAAGAIGTGTvDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVH 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 316 GFADCT-GHYLPLACTINGSRILDAGRAALG-VDYDELAKLAFASKPGANGITLVPYFDGERTPNR-PNATATFSG*TlA 392
Cdd:TIGR01312 279 GFCHALpGGWLPMGVTLSATSSLEWFRELFGkEDVEALNELAEQSPPGAEGVTFLPYLNGERTPHLdPQARGSFIGLT-H 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 393 NTTRENLARAFVEGLLCSQRDCLELIRSLGA-SITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAAW 471
Cdd:TIGR01312 358 NTTRADLTRAVLEGVTFALRDSLDILREAGGiPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAW 437
|
490 500 510
....*....|....*....|....*....|....*..
3I8B_A 472 VLsGETEPPAW--QLTIDGVETGEPTEAVYEAYAKAR 506
Cdd:TIGR01312 438 AL-GEKDLAALcsEAVVKQTESVLPIAENVEAYEELY 473
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
6-506 |
1.58e-91 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 287.90 E-value: 1.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDaETGELVRFGQAKHP-----NGTS-VDPSYWWSAFQEA-----AEQAGGLDDVSALAVGGQQ 74
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVD-EDGRVLASASAEYPtsspkPGWAeQDPEDWWQATKEAlrellAKAGISPSDIAAIGLTGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 75 HG*VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAapaqdgepedpiargkqRWVKAVGSSPVASYTLTKVAWVAENE 154
Cdd:cd07808 80 HGLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGD-----------------EILIITGNPPLPGFTLPKLLWLKENE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 155 PENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLIA*V-LEAAegakaaqsh 233
Cdd:cd07808 143 PEIFARIRKILLPKDYLRYRLTG-------------ELATDPSDASGTLLFDVEKREWSEELLEALgLDPS--------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 234 aeaiVLPTVLGPRDAA-PVKADPAIA-GKNVegGCLLAPGGGDNA*ASLGLG*AV-GDVSISLGTSGVAAAISENPTYDL 310
Cdd:cd07808 201 ----ILPPIVESTEIVgTLTPEAAEElGLPE--GTPVVAGAGDNAAAALGAGVVEpGDALISLGTSGVVFAPTDKPVPDP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 311 TGAVSGFADCT-GHYLPLACTINGSRILDAGRAALG---VDYDELAKLAFASKPGANGITLVPYFDGERTP-NRPNATAT 385
Cdd:cd07808 275 KGRLHTFPHAVpGKWYAMGVTLSAGLSLRWLRDLFGpdrESFDELDAEAAKVPPGSEGLLFLPYLSGERTPyWDPNARGS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 386 FSG*TLAnTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGA 465
Cdd:cd07808 355 FFGLSLS-HTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGA 433
|
490 500 510 520
....*....|....*....|....*....|....*....|..
3I8B_A 466 ARQAAWVLSG-ETEPPAWQLTIDGVETGEPTEAVYEAYAKAR 506
Cdd:cd07808 434 ALLAAVGAGVfDDLEEAAAACIKIEKTIEPDPERHEAYDELY 475
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-469 |
6.83e-72 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 234.00 E-value: 6.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAEtGELVRFGQAKH------PNGTSVDPSYWWSAFQEA-----AEQAGGLDDVSALAVGGQQ 74
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDED-GNLVASASREYpliypqPGWAEQDPEDWWQAVVEAirevlAKAGIDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 75 HG*VILDNQGNVIRDA*LWNDTSsapqaaalieklgaapaqdgepedpiargkqrwvkavgsspvasytltkvawvaene 154
Cdd:cd00366 80 PGVVLVDADGNPLRPAIIWLDRR--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 155 penvkkiAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLIA*VLEAAEgakaaqsha 234
Cdd:cd00366 103 -------AKFLQPNDYIVFRLTG-------------EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPRE--------- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 235 eaiVLPTVLGPRDAAPVKADPAIAGKNVEGGCLLAPGGGDNA*ASLGLG-*AVGDVSISLGTSGVAAAISENPTYDLTGA 313
Cdd:cd00366 154 ---KLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGvVEPGDAVDSTGTSSVLSVCTDEPVPPDPRL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 314 VSGFADCTGHYLPLACTINGSRILDAGRAALG------VDYDELAKLAFASKPGANGITLVPYFDGERTPN-RPNATATF 386
Cdd:cd00366 231 LNRCHVVPGLWLLEGAINTGGASLRWFRDEFGeeedsdAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPIwDPAARGVF 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 387 SG*TLaNTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAA 466
Cdd:cd00366 311 FGLTL-SHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAA 389
|
...
3I8B_A 467 RQA 469
Cdd:cd00366 390 ILA 392
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
6-504 |
3.05e-58 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 200.44 E-value: 3.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAEtGELVRFGQA----KHPNGTSV--DPSYWWSAFQEA-----AEQAGGLDDVSALAVGGQQ 74
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLD-GELVASAFApyptYYPKPGWAeqDPEDWWDAVCRAtrallEKSGIDPSDIAAIAFSGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 75 HG*VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGaapaqdgepedpiarGKQRWVKAVGSSPVASYTLTKVAWVAENE 154
Cdd:cd07805 80 QGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLG---------------GIEGYRLGGGNPPSGKDPLAKILWLKENE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 155 PENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLIA*V-LEAAegakaaqsh 233
Cdd:cd07805 145 PEIYAKTHKFLDAKDYLNFRLTG-------------RAATDPSTASTTGLMDLRKRRWSEELLRAAgIDPD--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 234 aeaiVLPTVLGPRD-AAPVKADPAIA-GknVEGGCLLAPGGGDNA*ASLGLG*-AVGDVSISLGTSGVAAAISENPTYDL 310
Cdd:cd07805 203 ----KLPELVPSTEvVGELTPEAAAElG--LPAGTPVVGGGGDAAAAALGAGAvEEGDAHIYLGTSGWVAAHVPKPKTDP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 311 TGAVSGFADCT-GHYLPLACTINGSRILDAGRAALG-------VDYDELAKLAFASKPGANGITLVPYFDGERTP-NRPN 381
Cdd:cd07805 277 DHGIFTLASADpGRYLLAAEQETAGGALEWARDNLGgdedlgaDDYELLDELAAEAPPGSNGLLFLPWLNGERSPvEDPN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 382 ATATFSG*TLaNTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIR-TLApSILG*DVTRPATDEY 460
Cdd:cd07805 357 ARGAFIGLSL-EHTRADLARAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCqILA-DVLGRPVEVPENPQE 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
3I8B_A 461 V-AIGAARQAA----WvLSGETEPPAWqltIDGVETGEPTEAVYEAYAK 504
Cdd:cd07805 435 AgALGAALLAAvglgL-LKSFDEAKAL---VKVEKVFEPDPENRARYDR 479
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
6-506 |
2.69e-55 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 192.39 E-value: 2.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAEtGELVRFGQAKHPNGTSV------DPSYWWSAFQEAAEQA---GGLDDVSALAVGGQQHG 76
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEpgwaeqDPEEILEAVLEALKEVlakLGGGEVDAIGFSSAMHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 77 *VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAapaqdgepedpiargkQRWVKAVGSSPVASYTLTKVAWVAENEPE 156
Cdd:cd07770 80 LLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDG----------------SELYRRTGCPIHPMYPLAKLLWLKEERPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 157 ---NVKKIAAIClphDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLia*vLEAAeGAKAAQsh 233
Cdd:cd07770 144 lfaKAAKFVSIK---EYLLYRLTG-------------ELVTDYSTASGTGLLNIHTLDWDEEA----LELL-GIDEEQ-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 234 aeaivLPTVLGPRDAAPVKADPAIAGKNVEGGCLLAPGGGDNA*ASLGLG*-AVGDVSISLGTSGVAAAISENPTYDLTG 312
Cdd:cd07770 201 -----LPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALANLGSGAlDPGRAALTVGTSGAIRVVSDRPVLDPPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 313 AVSGFADCTGHYLPLACTINGSRILDAGR---AALGVDYDELAKLAFASKPGANGITLVPYFDGERTPN-RPNATATFSG 388
Cdd:cd07770 276 RLWCYRLDENRWLVGGAINNGGNVLDWLRdtlLLSGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGwNPDARGAFFG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 389 *TLaNTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAARq 468
Cdd:cd07770 356 LTL-NHTRADILRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAAL- 433
|
490 500 510
....*....|....*....|....*....|....*...
3I8B_A 469 AAWVLSGETEPPAWQLTIDGVETGEPTEAVYEAYAKAR 506
Cdd:cd07770 434 LALEALGLISSLEADELVKIGKVVEPDPENHAIYAELY 471
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
6-471 |
1.88e-51 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 181.25 E-value: 1.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDaETGELVrfGQAKHPNGTSVDPSYW--------WSAFQEAAEQA---GGLDDVSALAVGGQQ 74
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFD-EDGRIL--ASASRETPLIHPGPGWaeldpeelWEAVKEAIREAaaqAGPDPIAAISVSSQG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 75 HG*VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAapaqdgepedpiargkQRWVKAVGSSPVASYTLTKVAWVAENE 154
Cdd:cd07773 78 ESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGA----------------EELYRITGLPPSPMYSLAKLLWLREHE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 155 PENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLIA*VLEAAEgakaaqsha 234
Cdd:cd07773 142 PEIFAKAAKWLSVADYIAYRLTG-------------EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDAS--------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 235 eaiVLPTVLGP-RDAAPVKADPAIAGKNVEGgCLLAPGGGDNA*ASLGLG*AV-GDVSISLGTSGVAAAISENPTYDLTG 312
Cdd:cd07773 200 ---LLPELVPSgTVIGTVTPEAAEELGLPAG-TPVVVGGHDHLCAALGAGVIEpGDVLDSTGTAEALLAVVDEPPLDEML 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 313 AVSGFadCTGHYLP-----LACTINGSRILDAGRAALGVDYDELA---KLAFASKPGANGITLVPYFDGERTPNR-PNAT 383
Cdd:cd07773 276 AEGGL--SYGHHVPggyyyLAGSLPGGALLEWFRDLFGGDESDLAaadELAEAAPPGPTGLLFLPHLSGSGTPDFdPDAR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 384 ATFSG*TLAnTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAI 463
Cdd:cd07773 354 GAFLGLTLG-TTRADLLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATAL 432
|
....*...
3I8B_A 464 GAARQAAW 471
Cdd:cd07773 433 GAALLAGV 440
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
6-471 |
1.37e-49 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 175.87 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDaETGELVRFGQA------KHPNGTSVDPSYWWSAFQEAAEQ---AGGLDDVSALAVGGQQHG 76
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVD-EDGTVLASASEpyptsrPGPGWVEQDPEDWWEALRSLLRElpaELRPRRVVAIAVDGTSGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 77 *VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAAPAQDGEPEDPiargkqrwvkavgsspvaSYTLTKVAWVAENEPE 156
Cdd:cd07783 80 LVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSP------------------SSSLAKLLWLKRHEPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 157 NVKKIAAICLPHDWLSWRIAGYGPVaegedahlealfTDRSDASgTIYYDAASNEYRRDLIA*VLEAAEgakaaqshaea 236
Cdd:cd07783 142 VLAKTAKFLHQADWLAGRLTGDRGV------------TDYNNAL-KLGYDPETGRWPSWLLALLGIPPD----------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 237 iVLPTVLGPRDA-APVKADPAiAGKNVEGGCLLAPGGGDNA*ASLGLG-*AVGDVSISLGTSGVAAAISENPTYDLTGAV 314
Cdd:cd07783 198 -LLPRVVAPGTViGTLTAEAA-EELGLPAGTPVVAGTTDSIAAFLASGaVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 315 SGFADCTGHYLPLACTINGSRILDagRAALGVDYDELAKLafASKPGANGITLVPY-FDGERTP-NRPNATATFSG*Tla 392
Cdd:cd07783 276 YSHRHGDGYWLVGGASNTGGAVLR--WFFSDDELAELSAQ--ADPPGPSGLIYYPLpLRGERFPfWDPDARGFLLPRP-- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 393 nTTRENLARAFVEGLLCSQRDCLELIRSLGAS-ITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEyVAIGAARQAAW 471
Cdd:cd07783 350 -HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE-AALGAALLAAA 427
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
9-469 |
2.13e-47 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 171.30 E-value: 2.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 9 GVDTSTQSCKVRVTDaETGELVRFGQAK------HPNGTSVDPSYWWSAFQEAAEQAG---GLDDVSALAVGGQQHG*VI 79
Cdd:PRK15027 4 GIDLGTSGVKVILLN-EQGEVVASQTEKltvsrpHPLWSEQDPEQWWQATDRAMKALGdqhSLQDVKALGIAGQMHGATL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 80 LDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAAPAQDGEPEDPiargkqrwvkavgsspvaSYTLTKVAWVAENEPENVK 159
Cdd:PRK15027 83 LDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMP------------------GFTAPKLLWVQRHEPEIFR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 160 KIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYR----------RDLIA*VLEAAEGAKA 229
Cdd:PRK15027 145 QIDKVLLPKDYLRLRMTG-------------EFASDMSDAAGTMWLDVAKRDWSdvmlqachlsRDQMPALYEGSEITGA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 230 AQSH-AEAIVLPTVlgprdaaPVKAdpaiagknveggcllapGGGDNA*ASLGLG*A-VGDVSISLGTSGVAAAISENPT 307
Cdd:PRK15027 212 LLPEvAKAWGMATV-------PVVA-----------------GGGDNAAGAVGVGMVdANQAMLSLGTSGVYFAVSEGFL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 308 YDLTGAVSGFAdctgHYLP-----LACTINGSRILDAGRAALGV-DYDELAKLAFASKPGANGITLVPYFDGERTP-NRP 380
Cdd:PRK15027 268 SKPESAVHSFC----HALPqrwhlMSVMLSAASCLDWAAKLTGLsNVPALIAAAQQADESAEPVWFLPYLSGERTPhNNP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 381 NATATFSG*TLANTTREnLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*DVT-RPATDE 459
Cdd:PRK15027 344 QAKGVFFGLTHQHGPNE-LARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRTGGDV 422
|
490
....*....|
3I8B_A 460 YVAIGAARQA 469
Cdd:PRK15027 423 GPALGAARLA 432
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-471 |
1.54e-45 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 165.39 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAEtGELVRFGQAKH------PNGTSVDPSYWWSAF----QEAAEQAG-GLDDVSALAVGGQQ 74
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDED-GKVLASASIEHdlltpkPGWAEHDPEVWWGAVceiiRELLAKAGiSPKEIAAIGVSGLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 75 HG*VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGaapaqdgepEDpiargkqrWVKAVGSSPVASY-TLTKVAWVAEN 153
Cdd:cd07804 80 PALVPVDENGKPLRPAILYGDRRATEEIEWLNENIG---------ED--------RIFEITGNPLDSQsVGPKLLWIKRN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 154 EPENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGT-IYYDAASNEYRRDLIa*vleaaegakaaqs 232
Cdd:cd07804 143 EPEVFKKTRKFLGAYDYIVYKLTG-------------EYVIDYSSAGNEgGLFDIRKRTWDEELL--------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 233 haEAIVLPTVLGPRdaaPVKADpAIAG---KNVEGGCLLAP------GGGDNA*ASLGLG-*AVGDVSISLGTSGVAAAI 302
Cdd:cd07804 195 --EALGIDPDLLPE---LVPST-EIVGevtKEAAEETGLAEgtpvvaGTVDAAASALSAGvVEPGDLLLMLGTAGDIGVV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 303 SENPTYDLTGAVSGFADcTGHYLPLACTINGSRIL------------DAGRAALGVDYDELAKLAFASKPGANGITLVPY 370
Cdd:cd07804 269 TDKLPTDPRLWLDYHDI-PGTYVLNGGMATSGSLLrwfrdefageevEAEKSGGDSAYDLLDEEAEKIPPGSDGLIVLPY 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 371 FDGERTP-NRPNATATFSG*TLaNTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG 449
Cdd:cd07804 348 FMGERTPiWDPDARGVIFGLTL-SHTRAHLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTG 426
|
490 500
....*....|....*....|..
3I8B_A 450 *DVTRPATDEYVAIGAARQAAW 471
Cdd:cd07804 427 VPQEYVKDTVGASLGDAFLAGV 448
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
6-470 |
7.88e-44 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 160.38 E-value: 7.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAEtGELVRFGQAKH------PNGTSVDPSYWW----SAFQEAAEQAGGL-DDVSALAVGGQQ 74
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLD-GNIVASGYREYppyypePGWVEQDPDDWWdalcEALKEAVAKAGVDpEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 75 HG*VILDNQGNVIRDA*LWNDtssapqaaalieklgaapaqdgepedpiargkqrwvkavgsspvasytltkvawvaene 154
Cdd:cd07779 80 STFVPVDEDGRPLRPAISWQD----------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 155 penvKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLIA*VleaaeGAKAAQsha 234
Cdd:cd07779 101 ----KRTAKFLTVQDYLLYRLTG-------------EFVTDTTSASRTGLPDIRTRDWSDDLLDAF-----GIDRDK--- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 235 eaivLP------TVLGP--RDAApvkadpAIAGknVEGGCLLAPGGGDNA*ASLGLG*AV--GDVSISLGTSGVAAAISE 304
Cdd:cd07779 156 ----LPelvppgTVIGTltKEAA------EETG--LPEGTPVVAGGGDQQCAALGAG-VLepGTASLSLGTAAVVIAVSD 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 305 NPTYDLTGAVSGFADC-TGHYLPLACTINGSRILD----------AGRAALGVD-YDELAKLAFASKPGANGITLVPYFD 372
Cdd:cd07779 223 KPVEDPERRIPCNPSAvPGKWVLEGSINTGGSAVRwfrdefgqdeVAEKELGVSpYELLNEEAAKSPPGSDGLLFLPYLA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 373 GERTPN-RPNATATFSG*TLAnTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*D 451
Cdd:cd07779 303 GAGTPYwNPEARGAFIGLTLS-HTRAHLARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRP 381
|
490
....*....|....*....
3I8B_A 452 VTRPATDEYVAIGAARQAA 470
Cdd:cd07779 382 VERPETSEATALGAAILAA 400
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
50-471 |
1.25e-42 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 157.33 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 50 SAFQEAAEQAGGL-DDVSALAVGGQQHG*VILDNQGNVIRDA*LWNDTssapQAAALIEKLgaapAQDGEPEdpiargkq 128
Cdd:cd07802 54 EAIRELLEKSGVDpSDIAGVGVTGHGNGLYLVDKDGKPVRNAILSNDS----RAADIVDRW----EEDGTLE-------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 129 RWVKAVGSSPVASYTLTKVAWVAENEPENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDAsGTIYYDAA 208
Cdd:cd07802 118 KVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWIRYRLTG-------------EISTDYTDA-GSSLLDLD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 209 SNEYRRDLIA*V-LEAAEGAkaaqshaeaivLPTVLGPRD-AAPVKADPAIA-GKNVegGCLLAPGGGDNA*ASLGLG-* 284
Cdd:cd07802 184 TGEYDDELLDLLgIEELKDK-----------LPPLVPSTEiAGRVTAEAAALtGLPE--GTPVAAGAFDVVASALGAGaV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 285 AVGDVSISLGTSGVAAAISENPTYDLTGAVSG-FADcTGHYLPLACTINGS--------RILDAGRAALGVDYDELAKLA 355
Cdd:cd07802 251 DEGQLCVILGTWSINEVVTDEPVVPDSVGSNSlHAD-PGLYLIVEASPTSAsnldwfldTLLGEEKEAGGSDYDELDELI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 356 FASKPGANGITLVPYFDGERTpnRPNATATFSG*TlANTTRENLARAFVEGLLCSQRDCLELIRSLGAsITRILLIGGGA 435
Cdd:cd07802 330 AAVPPGSSGVIFLPYLYGSGA--NPNARGGFFGLT-AWHTRAHLLRAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGA 405
|
410 420 430
....*....|....*....|....*....|....*.
3I8B_A 436 KSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAAW 471
Cdd:cd07802 406 RSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAV 441
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
53-470 |
9.77e-34 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 132.75 E-value: 9.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 53 QEAAEQAGGL-DDVSALAVGGQQHG*VILDNQGNVIRDA*LWNDTssapQAAALIEKLgaapaqdgePEDPIARgkqRWV 131
Cdd:cd24121 57 REVVAKLDVLpDRVAAIGVTGQGDGTWLVDEDGRPVRDAILWLDG----RAADIVERW---------QADGIAE---AVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 132 KAVGSSPVASYTLTKVAWVAENEPENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTiYYDAASNE 211
Cdd:cd24121 121 EITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWLFYKLTG-------------EIATDPSDASLT-FLDFRTRQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 212 YRRDLIA*V-LEAAEGakaaqshaeaiVLPTVLGPRD-AAPVKADPAIAgKNVEGGCLLAPGGGDNA*ASLGLG*-AVGD 288
Cdd:cd24121 187 YDDEVLDLLgLEELRH-----------LLPPIRPGTEvIGPLTPEAAAA-TGLPAGTPVVLGPFDVVATALGSGAiEPGD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 289 VSISLGTSGVAAAISENPtyDLTGAVSGFADCT---GHYL----PLACTIN--------GSRILDAGRAALGVDYDELAK 353
Cdd:cd24121 255 ACSILGTTGVHEVVVDEP--DLEPEGVGYTICLgvpGRWLramaNMAGTPNldwflrelGEVLKEGAEPAGSDLFQDLEE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 354 LAFASKPGANGITLVPYFD--GERTPN-RPNATATFSG*TLaNTTRENLARAFVEGLLCSQRDCLElirSLGASITRILL 430
Cdd:cd24121 333 LAASSPPGAEGVLYHPYLSpaGERAPFvNPNARAQFTGLSL-EHTRADLLRAVYEGVALAMRDCYE---HMGEDPGELRL 408
|
410 420 430 440
....*....|....*....|....*....|....*....|
3I8B_A 431 IGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAA 470
Cdd:cd24121 409 SGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAA 448
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
6-504 |
2.26e-32 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 129.99 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDaETGELV----------------RFGQAKHPNGTSVD-PSYWWSA-----FQEAAEQAGGLD 63
Cdd:cd07776 1 LYLGLDLSTQSLKAVVID-SDLKVVaeesvnfdsdlpeygtKGGVHRDGDGGEVTsPVLMWVEaldllLEKLKAAGFDFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 64 DVSALAVGGQQHG*VILDNQGNVIR--------------------DA*LWNDTSSAPQAAALIEKLGaapaqdgepedpi 123
Cdd:cd07776 80 RVKAISGSGQQHGSVYWSKGAESALanldpskslaeqlegafsvpDSPIWMDSSTTKQCRELEKAVG------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 124 arGKQRWVKAVGSSPVASYTLTKVAWVAENEPENVKKIAAICLPHDWLSWRIAG-YGPVaegedahlealftDRSDASGT 202
Cdd:cd07776 147 --GPEALAKLTGSRAYERFTGPQIAKIAQTDPEAYENTERISLVSSFLASLLLGrYAPI-------------DESDGSGM 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 203 IYYDAASNEYRRDLIA*vleaaegakaaqsHAEAIVLPTVLGPRDAAPVKADPaIAGKNVE--GG---CLLAPGGGDNA* 277
Cdd:cd07776 212 NLMDIRSRKWSPELLD--------------AATAPDLKEKLGELVPSSTVAGG-ISSYFVEryGFspdCLVVAFTGDNPA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 278 ASLGLG*AVGDVSISLGTSGVAAAISENPTYDLTGAVSGFADCTGHYLPLACTINGS----RILDagRAALGvDYDELAK 353
Cdd:cd07776 277 SLAGLGLEPGDVAVSLGTSDTVFLVLDEPKPGPEGHVFANPVDPGSYMAMLCYKNGSlareRVRD--RYAGG-SWEKFNE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 354 LAFASKPGANGITLVPYFDGERTPN--RPNATATFSG*TLANTTRENLARAFVEGLLCSQRdclELIRSLGASI--TRIL 429
Cdd:cd07776 354 LLESTPPGNNGNLGLYFDEPEITPPvpGGGRRFFGDDGVDAFFDPAVEVRAVVESQFLSMR---LHAERLGSDIppTRIL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 430 LIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAAWVLSGETEPPAWQLTIDGVETG-----EPTEAVYEAYAK 504
Cdd:cd07776 431 ATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAEEpklvaEPDPEAAEVYDK 510
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
9-469 |
2.71e-31 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 125.41 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 9 GVDTSTQSCKVRVTDAETGELVRFGQAKHP---NGTS-----VDPSYWWSAFQEAAEQ--AGGLDDVSALAVGGQQHG*V 78
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILESVSRPTPapiSSDDpgrseQDPEKILEAVRNLIDElpREYLSDVTGIGITGQMHGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 79 ILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAAPAQDGepedpiargkqrwvkavGSSPVASYTLTKVAWVAENEPENv 158
Cdd:cd07777 84 LWDEDGNPVSPLITWQDQRCSEEFLGGLSTYGEELLPKS-----------------GMRLKPGYGLATLFWLLRNGPLP- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 159 KKIAAICLPHDWLSWRIAGygpvaegedahLEALFTDRSDASGTIYYDAASNEYRRDLIa*vleaaegakaaqshaEAIV 238
Cdd:cd07777 146 SKADRAGTIGDYIVARLTG-----------LPKPVMHPTNAASWGLFDLETGTWNKDLL-----------------EALG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 239 LPTVLGPRdaapVKADPAIAGKNVE---GGCLLAPGGGDNA*ASLGLG*A-VGDVSISLGTSGVAAAISenPTYDLTGAV 314
Cdd:cd07777 198 LPVILLPE----IVPSGEIVGTLSSalpKGIPVYVALGDNQASVLGSGLNeENDAVLNIGTGAQLSFLT--PKFELSGSV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 315 SGFADCTGHYLPLACTINGSRILD---------AGRAALGVDYDEL-AKLAF-ASKPGANGITLVPYFDGERTpnRPNAT 383
Cdd:cd07777 272 EIRPFFDGRYLLVAASLPGGRALAvlvdflrewLRELGGSLSDDEIwEKLDElAESEESSDLSVDPTFFGERH--DPEGR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 384 ATFSG*TLANTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGA-KSEAIRTLAPSILG*DVTRPATDEYVA 462
Cdd:cd07777 350 GSITNIGESNFTLGNLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAA 429
|
....*..
3I8B_A 463 IGAARQA 469
Cdd:cd07777 430 VGAALLA 436
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
6-470 |
1.70e-29 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 121.49 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAETGELVRFGQAKHPNGTSV--------DPSYWWSAF----QEAAEQAGGL-DDVSALAVGG 72
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLADGEELASAVVPYPTGYIPprpgwaeqNPADYWEALeeavRGALAEAGVDpEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 73 QQHG*VILDNQGNVIRDA*LWNDTSSAPQAAALIEklgaapaqdgepedpIARGKQRWVKAVGSSPVAS-YTLTKVAWVA 151
Cdd:cd07781 81 TSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINE---------------TAHPALEYYLAYYGGVYSSeWMWPKALWLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 152 ENEPENVKKIAAICLPHDWLSWRIAGygpvaegedahleaLFTdRSDASGTI--YYDAASNEYRRDLIA*V--LEAAEGA 227
Cdd:cd07781 146 RNAPEVYDAAYTIVEACDWINARLTG--------------RWV-RSRCAAGHkwMYNEWGGGPPREFLAALdpGLLKLRE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 228 KaaqshaeaivLPTVLGPRDAAPVKADPAIAGK-NVEGGCLLAPGGGDNA*ASLGLG-*AVGDVSISLGTSGVAAAISEN 305
Cdd:cd07781 211 K----------LPGEVVPVGEPAGTLTAEAAERlGLPAGIPVAQGGIDAHMGAIGAGvVEPGTLALIMGTSTCHLMVSPK 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 306 PTyDLTGAVSGFADC--TGHYLplactingsriLDAGRAALG-------------------VDYDELAKLAFASKPGANG 364
Cdd:cd07781 281 PV-DIPGICGPVPDAvvPGLYG-----------LEAGQSAVGdifawfvrlfvppaeergdSIYALLSEEAAKLPPGESG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 365 ITLVPYFDGERTPNR-PNATATFSG*TLAnTTRENLARAFVEGLLCSQRDCLELIRSLGASITRILLIGGGA-KSEAI-R 441
Cdd:cd07781 349 LVALDWFNGNRTPLVdPRLRGAIVGLTLG-TTPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWmQ 427
|
490 500
....*....|....*....|....*....
3I8B_A 442 TLApSILG*DVTRPATDEYVAIGAARQAA 470
Cdd:cd07781 428 IYA-DVLGRPIKVPKSDQAPALGAAILAA 455
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-470 |
5.85e-29 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 119.25 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAEtGELVRFGQAK--------HPNGTSVDPSYWW----SAFQEAAEQAGGLD-DVSALAVGG 72
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSE-GKIVAIAYREweyytdddYPDAKEFDPEELWekicEAIREALKKAGISPeDISAVSSTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 73 QQHG*VILDNQGNVIRda*lwndtssapqaaalieklgAAPAQDgepedpiARGKQrWVKAVGSS-PVASYTLT------ 145
Cdd:cd07798 80 QREGIVFLDKDGRELY----------------------AGPNID-------ARGVE-EAAEIDDEfGEEIYTTTghwpte 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 146 -----KVAWVAENEPENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLIa*V 220
Cdd:cd07798 130 lfpaaRLLWFKENRPEIFERIATVLSISDWIGYRLTG-------------ELVSEPSQASETQLFDIKKREWSQELL-EA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 221 LEaaegakaaqshAEAIVLP------TVLGprdaaPVKADPAiAGKNVEGGCLLAPGGGDNA*ASLGLG*AV-GDVSISL 293
Cdd:cd07798 196 LG-----------LPPEILPeivpsgTVLG-----TVSEEAA-RELGLPEGTPVVVGGADTQCALLGSGAIEpGDIGIVA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 294 GTSGVAAAISENPTYDLTGAVsgFADC---TGHYL----PLACTINGSRILDAGRAALGVDYDELAKLAFASKPGANGI- 365
Cdd:cd07798 259 GTTTPVQMVTDEPIIDPERRL--WTGChlvPGKWVlesnAGVTGLNYQWLKELLYGDPEDSYEVLEEEASEIPPGANGVl 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 366 -TLVPY-FDGERTPNRPnatATFSG*TLANT---TRENLARAFVEGLLCSQRDCLELIRSL-GASITRILLIGGGAKSEA 439
Cdd:cd07798 337 aFLGPQiFDARLSGLKN---GGFLFPTPLSAselTRGDFARAILENIAFAIRANLEQLEEVsGREIPYIILCGGGSRSAL 413
|
490 500 510
....*....|....*....|....*....|.
3I8B_A 440 IRTLAPSILG*DVTRPATDEYVAIGAARQAA 470
Cdd:cd07798 414 LCQILADVLGKPVLVPEGREASALGAAICAA 444
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
9-281 |
5.60e-25 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 103.57 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 9 GVDTSTQSCKVRVTDaETGELVRFGQAKHP-----NGTSV-DPSYWWSAFQEAAEQAG-----GLDDVSALAVGGQQHG* 77
Cdd:pfam00370 4 GIDCGTTSTKAILFN-EQGKIIAVAQLENPqitphPGWAEqDPDEIWQAVAQCIAKTLsqlgiSLKQIKGIGISNQGHGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 78 VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGAAPAQD--GEPEDPiargkqrwvkavgsspvaSYTLTKVAWVAENEP 155
Cdd:pfam00370 83 VLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEitGLPIWP------------------GFTLSKLRWIKENEP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 156 ENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLia*vLEAAEGAKaaqshae 235
Cdd:pfam00370 145 EVFEKIHKFLTIHDYLRWRLTG-------------VFVTDHTNASRSMMFNIHKLDWDPEL----LAALGIPR------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
3I8B_A 236 aIVLPTVLGPRDAAPVKADPAIAGKNVEGGCLLAPGGGDNA*ASLG 281
Cdd:pfam00370 201 -DHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
289-471 |
1.73e-20 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 89.31 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 289 VSISLGTSGVAAAISENPTYDLTGAVSGFAD--CTGHYLPLACTINGSRILD-----------AGRAALGVDYDELAKLA 355
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNemLPGYWGLEGGQSAAGSLLAwllqfhglreeLRDAGNVESLAELAALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 356 FASKPGanGITLVPYFDGERTPN-RPNATATFSG*TLaNTTRENLARAFVEGLLCSQRDCLE-LIRSLGASITRILLIGG 433
Cdd:pfam02782 81 AVAPAG--GLLFYPDFSGNRAPGaDPGARGSITGLSS-PTTLAHLYRAILESLALQLRQILEaLTKQEGHPIDTIHVSGG 157
|
170 180 190
....*....|....*....|....*....|....*...
3I8B_A 434 GAKSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAAW 471
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAV 195
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
7-466 |
2.36e-14 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 75.20 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 7 VAGVDTSTQSCKVRVTDaETGELVRFGQAKH------PNGTSVDPSYWW----SAFQEAAEQAG-GLDDVSALAVGGQQH 75
Cdd:cd07769 2 ILAIDQGTTSTRAILFD-EDGNIVASAQKEHeqiypqPGWVEHDPEEIWentlEVIREALAKAGiSASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 76 G*VILDNQ-GNVIRDA*LWNDTssapQAAALIEKLgaapaqdgepedpIARGKQRWVKAVGSSPVASY-TLTKVAWVAEN 153
Cdd:cd07769 81 TTVVWDKKtGKPLYNAIVWQDR----RTADICEEL-------------KAKGLEERIREKTGLPLDPYfSATKIKWILDN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 154 EPENVKKIAA-------IclphD-WLSWRIAGYGpvaegedAHLealfTDRSDASGTIYYDAASNEYRRDLia*vLEAAE 225
Cdd:cd07769 144 VPGARERAERgellfgtI----DtWLIWKLTGGK-------VHV----TDVTNASRTMLFNIHTLEWDDEL----LELFG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 226 GAKAaqshaeaiVLPTVlgpRDAAPV--KADPAIAGKNVE-GGCLlapggGDNA*ASLGLG*-AVGDVSISLGT------ 295
Cdd:cd07769 205 IPRS--------MLPEV---RPSSEVfgYTDPEGLGAGIPiAGIL-----GDQQAALFGQGCfEPGMAKNTYGTgcfllm 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 296 --------------SGVAAAISENPTYDLTGAVSgfadCTGhylplaCTIN----GSRILDagraalgvDYDELAKLAfA 357
Cdd:cd07769 269 ntgekpvpskngllTTIAWQIGGKVTYALEGSIF----IAG------AAIQwlrdNLGLIE--------DAAETEELA-R 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 358 SKPGANGITLVPYFDGERTP-NRPNATATFSG*TlANTTRENLARAFVEGLlCSQ-RDCLELIRS-LGASITRILLIGGG 434
Cdd:cd07769 330 SVEDNGGVYFVPAFSGLGAPyWDPDARGAIVGLT-RGTTKAHIVRAALESI-AYQtRDVLEAMEKdSGIKLKELRVDGGA 407
|
490 500 510
....*....|....*....|....*....|..
3I8B_A 435 AKSEAIRTLAPSILG*DVTRPATDEYVAIGAA 466
Cdd:cd07769 408 TANNFLMQFQADILGVPVVRPKVAETTALGAA 439
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
6-470 |
1.89e-13 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 72.50 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 6 LVAGVDTSTQSCKVRVTDAE----TGELVRF-----------GQAKHP--NGTSVDPSYWW-SAF----QEAAEQAGGLD 63
Cdd:PLN02669 9 LFLGFDSSTQSLKATVLDSNlrivASEIVHFdsdlphygtkdGVYRDPkvNGRIVSPTLMWvEALdlllQKLAKEKFPFH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 64 DVSALAVGGQQHG*VI-----------LDNQGNV---------IRDA*LWNDTSSAPQAAALIEKLGaapaqdgepedpi 123
Cdd:PLN02669 89 KVVAISGSGQQHGSVYwrkgasavlksLDPSKSLvaqlqdafsTKDSPIWMDSSTTKQCREIEEAVG------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 124 arGKQRWVKAVGSSPVASYTLTKVAWVAENEPENVKKIAAICLPHDWL-SWRIAGYGPVaegedahlealftDRSDASGT 202
Cdd:PLN02669 156 --GAAELSKLTGSRAYERFTGPQIRKIYETQPEVYHDTERISLVSSFMaSLLVGDYASI-------------DETDGAGM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 203 IYYDAASNEYRRDlia*VLEAAegakaaqshaeAIVLPTVLGPRDAAPvkadpAIAGK---------NVEGGCLLAPGGG 273
Cdd:PLN02669 221 NLMDIEKRCWSKA----ALEAT-----------APGLEEKLGKLAPAH-----AVAGKihpyfvqrfGFSSNCLVVQWSG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 274 DNA*ASLGLG*AV-GDVSISLGTSGVAAAISENPTYDLTGAVSGFADCTGHYLPLACTINGS------RILDAGRAalgv 346
Cdd:PLN02669 281 DNPNSLAGLTLSTpGDLAISLGTSDTVFGITREPQPSLEGHVFPNPVDPESYMVMLCYKNGSltrediRNRCADGS---- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 347 dYDELAKLAFASKPGANGITLVPYFDGERTPNRPnatATFSG*TLANTTRENL----------------ARAFVEGLLCS 410
Cdd:PLN02669 357 -WDVFNKLLEQTPPLNGGKLGFYYKEHEILPPLP---VGFHRYILENFSGEALdglveeevgefdppseVRAIIEGQFLS 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 411 QRDCLELIrSLGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAA 470
Cdd:PLN02669 433 MRAHAERF-GMPVPPKRIIATGGASANQSILKLIASIFGCDVYTVQRPDSASLGAALRAA 491
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
286-466 |
3.63e-13 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 71.44 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 286 VGDVSISLGT----------------SG----VAAAISENPTYDLTGAVSGfadcTGHYLPLACTINGSRildagraalg 345
Cdd:cd07793 269 KGDVKITMGTgtfidintgskphasvKGlyplVGWKIGGEITYLAEGNASD----TGTVIDWAKSIGLFD---------- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 346 vDYDELAKLAFaSKPGANGITLVPYFDGERTP-NRPNATATFSG*TLaNTTRENLARAFVEGLLCSQRDCLELIRS-LGA 423
Cdd:cd07793 335 -DPSETEDIAE-SVEDTNGVYFVPAFSGLQAPyNDPTACAGFIGLTP-STTKAHLVRAILESIAFRVKQLLETMEKeTSI 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....
3I8B_A 424 SITRILLIGGGAKSEAI-RTLApSILG*DVTRPATDEYVAIGAA 466
Cdd:cd07793 412 KISSIRVDGGVSNNDFIlQLIA-DLLGKPVERPKNTEMSALGAA 454
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
347-466 |
3.96e-09 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 58.83 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 347 DYDELAKLAfASKPGANGITLVPYFDGERTPN-RPNATATFSG*TLaNTTRENLARAFVEGLLCSQRDCLE-LIRSLGAS 424
Cdd:PTZ00294 329 HPSEIEKLA-RSVKDTGGVVFVPAFSGLFAPYwRPDARGTIVGMTL-KTTRAHIVRAALEAIALQTNDVIEsMEKDAGIE 406
|
90 100 110 120
....*....|....*....|....*....|....*....|..
3I8B_A 425 ITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAA 466
Cdd:PTZ00294 407 LNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAA 448
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
50-470 |
1.23e-08 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 57.40 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 50 SAFQEAAEQAGGLDD-VSALAVGGQQHG*VILDNQ-GNVIRDA*LWNDTSSAPQAAALIEKLGAapaqdgepedpiarGK 127
Cdd:PLN02295 58 KALEKAAAKGHNVDSgLKAIGITNQRETTVAWSKStGRPLYNAIVWMDSRTSSICRRLEKELSG--------------GR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 128 QRWVKAVGSsPVASY-TLTKVAWVAENEPE----NVKKIAAICLPHDWLSWRIAGYgpvAEGeDAHLealfTDRSDASGT 202
Cdd:PLN02295 124 KHFVETCGL-PISTYfSATKLLWLLENVDAvkeaVKSGDALFGTIDSWLIWNLTGG---ASG-GVHV----TDVTNASRT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 203 IYYDAASNEYRRDLIA*VLEAAEGAKAAQSHAEAIVLPTVLGPRDAAPVkadpaiagknveGGCLlapggGDNA*ASLGL 282
Cdd:PLN02295 195 MLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLAGVPI------------AGCL-----GDQHAAMLGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 283 G*AVGDVSISLGTSG-VAAAISENPTYDLTGAVSGFADCTGHYLPLACTINGSrILDAG------RAALGV--DYDELAK 353
Cdd:PLN02295 258 RCRPGEAKSTYGTGCfILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGS-VAIAGaavqwlRDNLGIikSASEIEA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 354 LAfASKPGANGITLVPYFDGERTPN-RPNATATFSG*TlANTTRENLARAFVEGLLCSQRDCLELIR---SLGASITRIL 429
Cdd:PLN02295 337 LA-ATVDDTGGVYFVPAFSGLFAPRwRDDARGVCVGIT-RFTNKAHIARAVLESMCFQVKDVLDAMRkdaGEEKSHKGLF 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....
3I8B_A 430 LI---GGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAA 470
Cdd:PLN02295 415 LLrvdGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAG 458
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
5-466 |
5.71e-08 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 55.22 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 5 TLVAGVDTSTQSCKVRVTDaETGELVRFGQAKH------PNGTSVDPSYWWS----AFQEAAEQAGGL----DDVSALAV 70
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFD-STGELVASHQVEHkqiypkPGWVEHDPMEILEsvyeCIEEAVEKLKALgispSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 71 GGQQHG*VILDNQ-GNVIRDA*LWNDTSSAPQAAALIEKLGaapaqdgepedpiaRGKQRWVKAVGSsPVASY-TLTKVA 148
Cdd:cd07792 80 TNQRETTVVWDKStGKPLYNAIVWLDTRTSDTVEELSAKTP--------------GGKDHFRKKTGL-PISTYfSAVKLR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 149 WVAENEPEnVKKiaAI----CL---PHDWLSWRIAGyGPvaeGEDAHLealfTDRSDASGTIYYDAASNEYRRDLIA*vl 221
Cdd:cd07792 145 WLLDNVPE-VKK--AVddgrLLfgtVDSWLIWNLTG-GK---NGGVHV----TDVTNASRTMLMNLRTLQWDPELCE--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 222 eaaegakaaqshaeaivlptVLG-PRDAAP-VKADPAIAGKNVEG--------GCLlapggGDNA*ASLG-LG*AVGDVS 290
Cdd:cd07792 211 --------------------FFGiPMSILPeIRSSSEVYGKIASGplagvpisGCL-----GDQQAALVGqGCFKPGEAK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 291 ISLGT-------SGVAAAISEN---------------PTYDLTGAVSgfadctghylplactINGSRI--LdagRAALGV 346
Cdd:cd07792 266 NTYGTgcfllynTGEEPVFSKHgllttvayklgpdapPVYALEGSIA---------------IAGAAVqwL---RDNLGI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 347 --DYDELAKLAfASKPGANGITLVPYFDGERTPN-RPNATATFSG*TlANTTRENLARAFVEGLlCSQ-RDCLE-LIRSL 421
Cdd:cd07792 328 isSASEVETLA-ASVPDTGGVYFVPAFSGLFAPYwRPDARGTIVGLT-QFTTKAHIARAALEAV-CFQtREILDaMNKDS 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
3I8B_A 422 GASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAA 466
Cdd:cd07792 405 GIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAA 449
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
10-470 |
4.81e-07 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 52.33 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 10 VDTSTQSCKVRVTDaETGELVRFGQA--------KHPNGTSVDPSYWW----SAFQEAAEQAGGL-DDVSALAVGGQQHG 76
Cdd:cd07775 5 LDAGTGSGRAVIFD-LEGNQIAVAQRewrhkevpDVPGSMDFDTEKNWklicECIREALKKAGIApKSIAAISTTSMREG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 77 *VILDNQGNVIrda*lWN----DTSSAPQAAALIEklgaapaQDGEPEDPIARGKQRWVkAVGSSPvasytltKVAWVAE 152
Cdd:cd07775 84 IVLYDNEGEEI-----WAcanvDARAAEEVSELKE-------LYNTLEEEVYRISGQTF-ALGAIP-------RLLWLKN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 153 NEPENVKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLIA*VleaaeGAKAAQS 232
Cdd:cd07775 144 NRPEIYRKAAKITMLSDWIAYKLSG-------------ELAVEPSNGSTTGLFDLKTRDWDPEILEMA-----GLKADIL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 233 haeAIVLP--TVLGprdaapvKADPAIAGK-NVEGGCLLAPGGGDNA*ASLGLG*-AVGDVSISLGTSGVAAAISENPTY 308
Cdd:cd07775 206 ---PPVVEsgTVIG-------KVTKEAAEEtGLKEGTPVVVGGGDVQLGCLGLGVvRPGQTAVLGGSFWQQEVNTAAPVT 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 309 DLTG-------AVSG--FADCTGHYLPLACtingSRILDA-------GRAALGVD-YDELAKLAFASKPGANGItlVPYF 371
Cdd:cd07775 276 DPAMnirvnchVIPDmwQAEGISFFPGLVM----RWFRDAfcaeekeIAERLGIDaYDLLEEMAKDVPPGSYGI--MPIF 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 372 -DGERTPNRPNATATFSG*TL--ANTTRENLARAFVEGLLCSQRDCLELIRSL-GASITRILLIGGGAKSEAIRTLAPSI 447
Cdd:cd07775 350 sDVMNYKNWRHAAPSFLNLDIdpEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADV 429
|
490 500
....*....|....*....|...
3I8B_A 448 LG*DVTRPATDEYVAIGAARQAA 470
Cdd:cd07775 430 LGLPVKVPVVKEATALGAAIAAG 452
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
349-466 |
8.12e-07 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 51.77 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 349 DELAKLAFASKPGANGIT----LVPYFDGERTP-NRPNATATFSG*TLANTTrENLAR---AFVEGLLCSQRDCLELIRS 420
Cdd:cd07782 361 ERLEQLAEEKGLPLAYLTrdlhVLPDFHGNRSPlADPTLRGMISGLTLDTSL-DDLALlylATLQALAYGTRHIIEAMNA 439
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
3I8B_A 421 LGASITRILLIGGGAKSEA-IRTLApSILG*DVTRPATDEYVAIGAA 466
Cdd:cd07782 440 AGHKIDTIFMCGGLSKNPLfVQLHA-DVTGCPVVLPKEPEAVLLGAA 485
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
78-438 |
1.86e-06 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 50.22 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 78 VILDNQGNVIRDA*LWNDTSSAPQAAALIEKLGaapaqdgepedpiargKQRWVKAVGSSPVASYTLTKVAWVAENEPEN 157
Cdd:cd07771 81 GLLDKNGELLGNPVHYRDPRTEGMMEELFEKIS----------------KEELYERTGIQFQPINTLYQLYALKKEGPEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 158 VKKIAAICLPHDWLSWRIAGygpvaegedahleALFTDRSDASGTIYYDAASNEYRRDLia*vLEAAEgakaAQSHAEA- 236
Cdd:cd07771 145 LERADKLLMLPDLLNYLLTG-------------EKVAEYTIASTTQLLDPRTKDWSEEL----LEKLG----LPRDLFPp 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 237 IVLP-TVLGPRdAAPVKADPAIAGKNVeggclLAPGGGDNA*ASLGLG*AVGD-VSISLGTSGVAAAISENPtyDLTGAV 314
Cdd:cd07771 204 IVPPgTVLGTL-KPEVAEELGLKGIPV-----IAVASHDTASAVAAVPAEDEDaAFISSGTWSLIGVELDEP--VITEEA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 315 -------SGFADCTghYLPLAcTINGSRILDAGRAALG-----VDYDELAKLAFASKPgangitLVPYFDgertPNRP-- 380
Cdd:cd07771 276 feagftnEGGADGT--IRLLK-NITGLWLLQECRREWEeegkdYSYDELVALAEEAPP------FGAFID----PDDPrf 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3I8B_A 381 -------NATATFSG*TLAN--TTRENLARAFVEGLLCSQRDCLELIRSL-GASITRILLIGGGAKSE 438
Cdd:cd07771 343 lnpgdmpEAIRAYCRETGQPvpESPGEIARCIYESLALKYAKTIEELEELtGKRIDRIHIVGGGSRNA 410
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
50-466 |
2.46e-06 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 49.80 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 50 SAFQEAAEQAG-GLDDVSALAVGGQQHG*VILD-NQGNVIRDA*LWNDTSSAPQAAALIEKlgaapaqdgepedpiarGK 127
Cdd:cd07786 54 AVAREALAKAGiRASDIAAIGITNQRETTVVWDrETGKPVYNAIVWQDRRTADICEELKAE-----------------GH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 128 QRWVKAVGSSPVASY-TLTKVAWVAENEPENVKKIAA-------IclphD-WLSWRIAGygpvaeGEdAHLealfTDRSD 198
Cdd:cd07786 117 EEMIREKTGLVLDPYfSATKIRWILDNVPGARERAERgelafgtI----DsWLIWKLTG------GK-VHA----TDVTN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 199 ASGTIYYDAASNEYRRDLia*vLEAAEGAKAaqshaeaiVLPTVlgpRDAAPV--KADPAIAGKNVEGGCLLapggGDNA 276
Cdd:cd07786 182 ASRTMLFNIHTLEWDDEL----LELFGIPAS--------MLPEV---KPSSEVfgYTDPDLLGAEIPIAGIA----GDQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 277 *ASLG-LG*AVGDVSISLGTSG--------------------VAAAISENPTYDLTGAVsgFadctghylplactINGSR 335
Cdd:cd07786 243 AALFGqACFEPGMAKNTYGTGCfmlmntgekpvrskngllttIAWQLGGKVTYALEGSI--F-------------IAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 336 I--LdagRAALGV--DYDELAKLAfASKPGANGITLVPYFDGERTPN-RPNATATFSG*TlANTTRENLARAFVEGLLCS 410
Cdd:cd07786 308 VqwL---RDGLGLieSAAETEALA-RSVPDNGGVYFVPAFTGLGAPYwDPDARGAIFGLT-RGTTRAHIARAALESIAYQ 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
3I8B_A 411 QRDCLELIRS-LGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAA 466
Cdd:cd07786 383 TRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAA 439
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
348-480 |
3.31e-06 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 49.64 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 348 YDELAKLAFASKPGANGITLVPYFDGertpnrpNATATFSG*TLaNTTRENLARAFVEGLLCSQRDCLELIRSLGA-SIT 426
Cdd:PRK10331 320 YQTMIEEARAIPPGADGVKMQCDLLA-------CQNAGWQGVTL-NTTRGHFYRAALEGLTAQLKRNLQVLEKIGHfKAS 391
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
3I8B_A 427 RILLIGGGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAArQAAWVLSGETEPP 480
Cdd:PRK10331 392 ELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAA-MFGWYGVGEFSSP 444
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
7-466 |
4.24e-06 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 49.05 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 7 VAGVDTSTQSCKVRVTDAEtGELVRFGQAKH----PNGTSV--DPSYWW----SAFQEAAEQAG-GLDDVSALAVGGQQH 75
Cdd:PRK00047 7 ILALDQGTTSSRAIIFDHD-GNIVSVAQKEFtqifPQPGWVehDPNEIWasqlSVIAEALAKAGiSPDQIAAIGITNQRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 76 G*VILD-NQGNVIRDA*LWNDTSSAPQAAALIEKlgaapaqdgepedpiarGKQRWVKAVGSSPVASY-TLTKVAWVAEN 153
Cdd:PRK00047 86 TTVVWDkETGRPIYNAIVWQDRRTADICEELKRD-----------------GYEDYIREKTGLVIDPYfSGTKIKWILDN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 154 EPENVKKIAAICL----PHDWLSWRIAGygpvaegEDAHLealfTDRSDASGTIYYDAASNEYRRDLIA*---------- 219
Cdd:PRK00047 149 VEGARERAEKGELlfgtIDTWLVWKLTG-------GKVHV----TDYTNASRTMLFNIHTLDWDDELLELldiprsmlpe 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 220 VLEAAEG---AKAAQSHAEAIVLPTVLGPRDAA---PVKADPAIAgKNVEG-GCLLAPGGGDNA*ASL-GLg*avgdvsi 291
Cdd:PRK00047 218 VRPSSEVygkTNPYGFFGGEVPIAGIAGDQQAAlfgQLCFEPGMA-KNTYGtGCFMLMNTGEKAVKSEnGL--------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 292 sLGTsgVAAAISENPTYDLTGAVSgfadctghylplactINGSRI--LdagRAALGVDYDELAKLAFASK-PGANGITLV 368
Cdd:PRK00047 288 -LTT--IAWGIDGKVVYALEGSIF---------------VAGSAIqwL---RDGLKIISDASDSEALARKvEDNDGVYVV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 369 PYFDGERTPN-RPNATATFSG*TlANTTRENLARAFVEGLlCSQ-RDCLELIRS-LGASITRILLIGGGAKSEAIRTLAP 445
Cdd:PRK00047 347 PAFTGLGAPYwDSDARGAIFGLT-RGTTKEHIIRATLESI-AYQtRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQA 424
|
490 500
....*....|....*....|.
3I8B_A 446 SILG*DVTRPATDEYVAIGAA 466
Cdd:PRK00047 425 DILGVPVERPVVAETTALGAA 445
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
423-476 |
1.65e-04 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 44.34 E-value: 1.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
3I8B_A 423 ASITRILLIGGGAKSEAIRTLAPSILG*DVTRPAT-DEYVAIGAARQAAwVLSGE 476
Cdd:CHL00094 327 SDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNpDEVVAIGAAVQAG-VLAGE 380
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
9-466 |
8.53e-04 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 41.84 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 9 GVDTSTQSCKVRVTDAETGELVrfGQAKHPNGTSVDPSYWW-------------SAFQEAAEQAG---------GLDDVS 66
Cdd:cd07768 4 GVDVGTSSARAGVYDLYAGLEM--AQEPVPYYQDSSKKSWKfwqksteiikalqKCVQKLNIREGvdayevkgcGVDATC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 67 ALAV---GGQQHG*VILD-NQGNVIrda*LWNDTSSAPQAaaliEKLGAAPAQDGEPEdpiargkqrwvkaVGSSPVASY 142
Cdd:cd07768 82 SLAIfdrEGTPLMALIPYpNEDNVI----FWMDHSAVNEA----QWINMQCPQQLLDY-------------LGGKISPEM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 143 TLTKVAWVAENEPENVKKIAAICLPHDWLSWRIAGYgPVAEGEDAHLEALFTDRSDASGTIYYDAasneyrrdlia*VLE 222
Cdd:cd07768 141 GVPKLKYFLDEYSHLRDKHFHIFDLHDYIAYELTRL-YEWNICGLLGKENLDGEESGWSSSFFKN------------IDP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 223 AAEGAKAAQSHAEAIVLPTVLG---PRDAAPVKADPAIAgknVEGGCLlapgggDNA*ASLGLG*AVGDVSISL--GTSG 297
Cdd:cd07768 208 RLEHLTTTKNLPSNVPIGTTSGvalPEMAEKMGLHPGTA---VVVSCI------DAHASWFAVASPHLETSLFMiaGTSS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 298 VAAAISE---------NPTYD-LTGAVSGFA---DCTG----HYLPL-ACTINGSRILDAG---RAALGVDYDELAKLAF 356
Cdd:cd07768 279 CHMYGTTisdripgvwGPFDTiIDPDYSVYEagqSATGklieHLFEShPCARKFDEALKKGadiYQVLEQTIRQIEKNNG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 357 askpGANGITLVPYFDGERTP-NRPNATATFSG*TLaNTTRENLA---RAFVEGLLCSQRDCLELIRSLGASITRILLIG 432
Cdd:cd07768 359 ----LSIHILTLDMFFGNRSEfADPRLKGSFIGESL-DTSMLNLTykyIAILEALAFGTRLIIDTFQNEGIHIKELRASG 433
|
490 500 510
....*....|....*....|....*....|....
3I8B_A 433 GGAKSEAIRTLAPSILG*DVTRPATDEYVAIGAA 466
Cdd:cd07768 434 GQAKNERLLQLIALVTNVAIIKPKENMMGILGAA 467
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
348-470 |
1.79e-03 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 40.98 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 348 YDELAKLAFASKPGANGITLVPYFDGERTPN-RPNATATFSG*TLAnTTRENLARAFVEGLLCSQRDCLELIRSLGASIT 426
Cdd:PRK04123 362 LELLTEAAAKQPPGEHGLVALDWFNGRRTPLaDQRLKGVITGLTLG-TDAPDIYRALIEATAFGTRAIMECFEDQGVPVE 440
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
3I8B_A 427 RILLIGGGA-KSEAIRTLAPSILG*DVTRPATDEYVAIGAARQAA 470
Cdd:PRK04123 441 EVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAA 485
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
398-470 |
3.00e-03 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; HSPA14, also called HSP70-like protein 1 (Hsp70L1), or heat shock protein HSP60, is a component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, HSPA14 binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466836 [Multi-domain] Cd Length: 377 Bit Score: 39.92 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3I8B_A 398 NLARAFVEGLlCSQ--RDCLELIRSL-------GASITRILLIGGGAK----SEAIRTLAPSIlg*DVTRPATDEYVAIG 464
Cdd:cd10238 293 NVSRARFESL-CSSlfQQCLEPIQEVlnsagltKEDIDKVILCGGSSRipklQQLIKDLFPSA--EVLSSIPPDEVIAIG 369
|
....*.
3I8B_A 465 AARQAA 470
Cdd:cd10238 370 AAKQAG 375
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
423-478 |
5.12e-03 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 39.42 E-value: 5.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
3I8B_A 423 ASITRILLIGGGAKSEAIRTLAPSILG*D-VTRPATDEYVAIGAARQAAwVLSGETE 478
Cdd:COG0443 299 SDIDAVLLVGGSTRMPAVRERVKELFGKEpLKGVDPDEAVALGAAIQAG-VLAGDVK 354
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
412-471 |
9.44e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466879 [Multi-domain] Cd Length: 351 Bit Score: 38.33 E-value: 9.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
3I8B_A 412 RDCLELIRSLGASITRILLIGGGAKSEAIRTLAPSILG*DVTRPA-TDEYVAIGAARQAAW 471
Cdd:cd24029 289 EKALKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVdPDEAVAKGAAIYAAS 349
|
|
| |
