|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
9-534 |
0e+00 |
|
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: 777.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATCSLV 88
Cdd:cd07782 3 IGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATCSLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 89 VIGDNDAPLAVGPSDDADRNIIVWMDHRATGQAEKINATGHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARHFFDL 168
Cdd:cd07782 83 VLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPETWAKAGHFFDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 169 ADYLTWRSTGDEARSVCTVTCKWTYLAH---EQRWDAGYFRQIGLAELADEDFVRIGQRIVDPGTPCGEGLCATAAEEMG 245
Cdd:cd07782 163 PDFLTWKATGSLTRSLCSLVCKWTYLAHegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 246 LPIGTPVAVGMIDAHAGGIGTVGV--------LNGAVNNMAYVFGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWLSEG 317
Cdd:cd07782 243 LPEGTPVGVSLIDAHAGGLGTLGAdvgglpceADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 318 GQSAAGAAIDQLLSFHPAAAEAREQAKAAGVPLPVWLADRVLTQVASPSEAVT-LAAGLHVVPEFLGNRAPLADPHAKAL 396
Cdd:cd07782 323 GQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKGLPLAyLTRDLHVLPDFHGNRSPLADPTLRGM 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 397 IAGLGMERDLDNLTALYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLL 476
Cdd:cd07782 403 ISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLL 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 397405968 477 GSAILGAVAGRVAASLPEAMKQFTQVDATYHSETAFSPLHQRRYAAYKALQQAGRLIR 534
Cdd:cd07782 483 GAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREYR 540
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
8-534 |
0e+00 |
|
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.
Pssm-ID: 273552 [Multi-domain] Cd Length: 541 Bit Score: 750.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATCSL 87
Cdd:TIGR01315 2 YIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLAESKVDPNSVKGIGFDATCSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 88 VVIGDNDAPLAVGPSDDADRNIIVWMDHRATGQAEKINATGHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARHFFD 167
Cdd:TIGR01315 82 VVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPELFARCKFFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 168 LADYLTWRSTGDEARSVCTVTCKWTYLAHE---QRWDAGYFRQIGLAELADEDFVRIGQRIVDPGTPCGEGLCATAAEEM 244
Cdd:TIGR01315 162 LTDFLTWRATGKEIRSFCSVVCKWGFVPVDgsnKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 245 GLPIGTPVAVGMIDAHAGGIGTVGV-------LNGAVNNMAYVFGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWLSEG 317
Cdd:TIGR01315 242 GLPAGTAVGSGLIDAHAGWIGTVGAkvaengdVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 318 GQSAAGAAIDQLLSFHPAAAEAREQAKAAGVPLPVWLADRVLTQVASPSEA--VTLAAGLHVVPEFLGNRAPLADPHAKA 395
Cdd:TIGR01315 322 GQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHLKEMAAKTNAPsiSYLVRHFHVYPDLWGNRSPIADPNMRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 396 LIAGLGMERDLDNLTALYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVL 475
Cdd:TIGR01315 402 VIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVL 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 397405968 476 LGSAILGAVAGRVAASLPEAMKQFTQVDATYHS--ETAFSpLHQRRYAAYKALQQAGRLIR 534
Cdd:TIGR01315 482 HGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPrgDPAKK-LHDRKYEIFLQLARTQQEYR 541
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
9-529 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 657.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNLR-GELLAHATREITLFR------SAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGF 81
Cdd:COG1069 5 IGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWViglylpPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVVGIGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 82 DAT-CSLVVIGDNDAPLAVGP--SDDADRNIIVWMDHRATGQAEKIN----ATGHPVLRYVGGKISPEMQTPKILWLKEN 154
Cdd:COG1069 85 DATgCTPVPVDADGTPLALLPefAENPHAMVILWKDHTAQEEAERINelakARGEDYLRYVGGIISSEWFWPKILHLLRE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 155 RPHIYQQARHFFDLADYLTWRSTGDEARSVCTVTCKWTYLAHEQRW-DAGYFRQIG--LAELADedfvRIGQRIVDPGTP 231
Cdd:COG1069 165 DPEVYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAHEGGYpSEEFFAALDplLDGLAD----RLGTEIYPLGEP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 232 CGEgLCATAAEEMGLPIGTPVAVGMIDAHAGGIGTVGVLNGavnNMAYVFGTSSCTMTTTQEAVFVPGVWGPYYSAMVPG 311
Cdd:COG1069 241 AGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPG---TLVKVMGTSTCHMLVSPEERFVPGICGQVDGSIVPG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 312 YWLSEGGQSAAGAAIDQLLSFHPAAAEAREQAKAAGVPLPVWLADRVLTQVAspseavtLAAGLHVVPEFLGNRAPLADP 391
Cdd:COG1069 317 MWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLTEEAAKLPP-------GESGLHALDWFNGNRSPLADQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 392 HAKALIAGLGMERDLDnltALYVAGLCGIGYGLRQIIDAQRACGIESENIVISGG-AGQHPLVRQLLADACGVSVVSTAS 470
Cdd:COG1069 390 RLKGVILGLTLGTDAE---DIYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAAS 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 471 REPVLLGSAILGAVAGRVAASLPEAMKQFTQV-DATYHSETAFSPLHQRRYAAYKALQQA 529
Cdd:COG1069 467 EQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHDY 526
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
9-528 |
9.73e-137 |
|
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: 406.24 E-value: 9.73e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNL-RGELLAHATREITLFRSAGN-KVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATCS 86
Cdd:cd07768 3 IGVDVGTSSARAGVYDLyAGLEMAQEPVPYYQDSSKKSwKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDATCS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLAVGPSDDADRNIIVWMDHRATGQAEKINATGHPVLR-YVGGKISPEMQTPKILWLKENRPHIYQQARHF 165
Cdd:cd07768 83 LAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHLRDKHFHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 166 FDLADYLTWRSTGDEARSVCTVTCKWTYLAHEQRWDAGYFRQIGLAELaDEDFVRIGQRIVDPGTPCGEGLcATAAEEMG 245
Cdd:cd07768 163 FDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAEKMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 246 LPIGTPVAVGMIDAHAGGIGtVGVLNgAVNNMAYVFGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWLSEGGQSAAGAA 325
Cdd:cd07768 241 LHPGTAVVVSCIDAHASWFA-VASPH-LETSLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 326 IDQLLSFHPAAAeAREQAKAAGVPLpvwlaDRVLTQVASPSEAVT-LAAGLHVVPEFLGNRAPLADPHAKALIAGLGMER 404
Cdd:cd07768 319 IEHLFESHPCAR-KFDEALKKGADI-----YQVLEQTIRQIEKNNgLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 405 DLDNLTALYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAV 484
Cdd:cd07768 393 SMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKV 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 397405968 485 AGRV---AASLPEAMKQFTQVDATyhsetaFSPLHQRRYAAYKALQQ 528
Cdd:cd07768 473 AAGKkqlADSITEADISNDRKSET------FEPLAYRLGADYILLYK 513
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
9-526 |
1.94e-135 |
|
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: 402.30 E-value: 1.94e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNLR-GELLAHATREITLFRSAGNK--VEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATC 85
Cdd:cd07781 3 IGIDFGTQSVRAGLVDLAdGEELASAVVPYPTGYIPPRPgwAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDTTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 86 S-LVVIGDNDAPLAvgpsddadrNIIVWMDHRATGQAEKINATGHPVLRY----VGGKISPEMQTPKILWLKENRPHIYQ 160
Cdd:cd07781 83 StVVPVDEDGNPLA---------PAILWMDHRAQEEAAEINETAHPALEYylayYGGVYSSEWMWPKALWLKRNAPEVYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 161 QARHFFDLADYLTWRSTGDEARSVCTVTCKWTYLAHEQRWDAGYFRQIGLAELADEDfvRIGQRIVDPGTPCGeGLCATA 240
Cdd:cd07781 154 AAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGLLKLRE--KLPGEVVPVGEPAG-TLTAEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 241 AEEMGLPIGTPVAVGMIDAHAGGIGtVGVLngAVNNMAYVFGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWLSEGGQS 320
Cdd:cd07781 231 AERLGLPAGIPVAQGGIDAHMGAIG-AGVV--EPGTLALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 321 AAGAAIDQLLS-FHPAAAEARE------QAKAAGVPlpvwladrvltqvaspseavTLAAGLHVVPEFLGNRAPLADPHA 393
Cdd:cd07781 308 AVGDIFAWFVRlFVPPAEERGDsiyallSEEAAKLP--------------------PGESGLVALDWFNGNRTPLVDPRL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 394 KALIAGLgmerDLDNLTA-LYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQH-PLVRQLLADACGVSVVSTASR 471
Cdd:cd07781 368 RGAIVGL----TLGTTPAhIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAEKnPLWMQIYADVLGRPIKVPKSD 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 397405968 472 EPVLLGSAILGAVAGRVAASLPEAMKQFTQVDATYHSETAFSPLHQRRYAAYKAL 526
Cdd:cd07781 444 QAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
8-535 |
6.06e-101 |
|
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: 313.31 E-value: 6.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDAT-CS 86
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQmHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINAT--GHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARH 164
Cdd:COG1070 83 LVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 165 FFDLADYLTWRSTGdeaRSVCTVTCK-WTYL--AHEQRWDAGYFRQIGLaelaDEDFVrigQRIVDPGTPCGEgLCATAA 241
Cdd:COG1070 154 VLLPKDYLRYRLTG---EFVTDYSDAsGTGLldVRTRDWSDELLEALGI----DRELL---PELVPPGEVAGT-LTAEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 242 EEMGLPIGTPVAVGMIDAHAGGIGTvGVLN-GAVNNMAyvfGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWLSEGGQS 320
Cdd:COG1070 223 AETGLPAGTPVVAGAGDNAAAALGA-GAVEpGDAAVSL---GTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 321 AAGAAIDqllsfhpaaaeareqakaagvplpvWLADRVLTQVASPSEAVTLAA--------GLHVVPEFLGNRAPLADPH 392
Cdd:COG1070 299 NGGSALR-------------------------WFRDLFADGELDDYEELNALAaevppgadGLLFLPYLSGERTPHWDPN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 393 AKALIAGLGMERDLDNLTAlyvAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASRE 472
Cdd:COG1070 354 ARGAFFGLTLSHTRAHLAR---AVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEE 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 397405968 473 PVLLGSAILGAVAGRVAASLPEAMKQFTQVDATYHSETAFSPLHQRRYAAYKALQQAGRLIRE 535
Cdd:COG1070 431 GGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKPLFE 493
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
8-524 |
6.71e-86 |
|
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: 274.01 E-value: 6.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDAT-CS 86
Cdd:cd07805 2 ILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQmQG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINATGHPVLRY---VGGKISPEMQTPKILWLKENRPHIYQQAR 163
Cdd:cd07805 82 VVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEIYAKTH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 164 HFFDLADYLTWRSTGDEARSVCTVTCKWTYLAHEQRWDAGYFRQIGL-AELADEdfvrigqrIVDPGTPCGEgLCATAAE 242
Cdd:cd07805 153 KFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIdPDKLPE--------LVPSTEVVGE-LTPEAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 243 EMGLPIGTPVAVGMIDAHAGGIGTvgvlnGAVN-NMAYV-FGTSSCTMTTTQEAVFVPGvwGPYYS--AMVPGYWLSEGG 318
Cdd:cd07805 224 ELGLPAGTPVVGGGGDAAAAALGA-----GAVEeGDAHIyLGTSGWVAAHVPKPKTDPD--HGIFTlaSADPGRYLLAAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 319 QSAAGAAIDQLLSFHPAAAEAREQAKAAgvplpvwladrvLTQVASPSEAVtlAAGLHVVPEFLGNRAPLADPHAKALIA 398
Cdd:cd07805 297 QETAGGALEWARDNLGGDEDLGADDYEL------------LDELAAEAPPG--SNGLLFLPWLNGERSPVEDPNARGAFI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 399 GLGME---RDldnltaLYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPV- 474
Cdd:cd07805 363 GLSLEhtrAD------LARAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQEAg 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 397405968 475 LLGSAILGAVAGRVAASLPEAmKQFTQVDATYHSETAFSPLHQRRYAAYK 524
Cdd:cd07805 437 ALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-527 |
3.80e-75 |
|
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: 245.53 E-value: 3.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDA-TCS 86
Cdd:cd07808 2 LLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGqMHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINAT-GHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARHF 165
Cdd:cd07808 82 LVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 166 FdLA-DYLTWRSTGDearsVCT-VTCKWTYL---AHEQRWDAGYFRQIGLaelaDEDFVrigQRIVDPGTPCGEgLCATA 240
Cdd:cd07808 153 L-LPkDYLRYRLTGE----LATdPSDASGTLlfdVEKREWSEELLEALGL----DPSIL---PPIVESTEIVGT-LTPEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 241 AEEMGLPIGTPVAVGMIDAHAGGIGTVGVLNGAVnnmAYVFGTSSCTMTTTQEAVFVP--GVWgpYYSAMVPGYWLSEGG 318
Cdd:cd07808 220 AEELGLPEGTPVVAGAGDNAAAALGAGVVEPGDA---LISLGTSGVVFAPTDKPVPDPkgRLH--TFPHAVPGKWYAMGV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 319 QSAAGAAID---QLLSFHPAAAEAREqAKAAGVPLPvwlADRVLtqvaspseavtlaaglhvvpeFL----GNRAPLADP 391
Cdd:cd07808 295 TLSAGLSLRwlrDLFGPDRESFDELD-AEAAKVPPG---SEGLL---------------------FLpylsGERTPYWDP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 392 HAKALIAGLGMERDLDNLTAlyvAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASR 471
Cdd:cd07808 350 NARGSFFGLSLSHTRAHLAR---AVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEE 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 397405968 472 EPVLLGSAILGAVAGRVAASLPEAMKQFTQVDATYHSETAFSPLHQRRYAAYKALQ 527
Cdd:cd07808 427 EGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
9-482 |
9.14e-75 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. 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: 466797 [Multi-domain] Cd Length: 544 Bit Score: 246.55 E-value: 9.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGN--KVEQSSREIWQAVCYCIKTAVANAGVSpsSIAGIGFDATCS 86
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLATSERPISYKQDPKDlwFVTQSSTEIWKAIKTALKELIEELSDY--IVSGIGVSATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVI-----GDNDAPLAVGP-SDDADRNIIVWMDHRATGQAEKIN-ATGHPVLRYVGGKISPEMQTPKILWLKENRPHIY 159
Cdd:cd07778 81 MVVMqrdsdTSYLVPYNVIHeKSNPDQDIIFWMDHRASEETQWLNnILPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 160 QQARHFFDLADYLTWRstgdearsVCTVTCKW--TYLAHE-----------QRWDAGYFRQIGLAELADED--FVRIGQR 224
Cdd:cd07778 161 FKKLEVFDLHDWISYM--------LATNLGHSniVPVNAPpsigigidgslKGWSKDFYSKLKISTKVCNVgnTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 225 IVDPGTPCGEgLCATAAEEMGLPIGTPVAVGMIDAHAGGIGTVGVLNGAVNNMAYVFGTSSCTMTTTQ--EAVFVPGVWG 302
Cdd:cd07778 233 LPYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFSTFAAAKTLDTTLFMVAGTSTCFLYATSssQVGPIPGIWG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 303 PyYSAMVPGYWLSEGGQSAAGAAIDQLLSFHPAAAEAREqakaaGVPLPVWLADRVL---TQVASPSEAVtLAAGLHVVP 379
Cdd:cd07778 312 P-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLK-----SDANFFETVEEKIdkyERLLGQSIHY-LTRHMFFYG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 380 EFLGNRAPLADPHAKALIAGLGMERDLDNLTALYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLA- 458
Cdd:cd07778 385 DYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSt 464
|
490 500
....*....|....*....|....*.
gi 397405968 459 --DACGVSVVSTASREPVLLGSAILG 482
Cdd:cd07778 465 vlSKIHIIVPLSDSKYAVVKGAALLG 490
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
9-526 |
4.89e-74 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 244.76 E-value: 4.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNLR-GELLAHATREITLfrsagnkveqssreiWQAVCYC---------------------IKTAV 66
Cdd:PRK04123 6 IGLDFGTDSVRALLVDCAtGEELATAVVEYPH---------------WVKGRYLdlppnqalqhpldyiesleaaIPAVL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 67 ANAGVSPSSIAGIGFDAT-CSLVVIGDNDAPLAVGPsDDADRN---IIVWMDHRATGQAEKINATGHP-----VLRYVGG 137
Cdd:PRK04123 71 KEAGVDPAAVVGIGVDFTgSTPAPVDADGTPLALLP-EFAENPhamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 138 KISPEMQTPKILWLKENRPHIYQQARHFFDLADYLTWRSTGDEA-----RSVCTVTCKWTYlaHEqRWD----AGYFRQI 208
Cdd:PRK04123 150 IYSSEWFWAKILHVLREDPAVYEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALW--HE-SWGglpsADFFDAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 209 --GLAELADEdfvRIGQRIVDPGTPCGeGLCATAAEEMGLPIGTPVAVGMIDAHAGGIGtVGVLNGAvnnMAYVFGTSSC 286
Cdd:PRK04123 227 dpLLARGLRD---KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHMGAVG-AGAEPGT---LVKVMGTSTC 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 287 TMTTTQEAVFVPGVWGPYYSAMVPGYWLSEGGQSAAG---AAIDQLLSfhpaAAEAREQAKAAGVPLPVWLADRVLTQVA 363
Cdd:PRK04123 299 DILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGdifAWFARLLV----PPEYKDEAEARGKQLLELLTEAAAKQPP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 364 spseavtLAAGLHVVPEFLGNRAPLADPHAKALIAGLGMERDLDnltALYVAGLCGIGYGLRQIIDAQRACGIESENIVI 443
Cdd:PRK04123 375 -------GEHGLVALDWFNGRRTPLADQRLKGVITGLTLGTDAP---DIYRALIEATAFGTRAIMECFEDQGVPVEEVIA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 444 SGGAGQH-PLVRQLLADACGVSVVSTASREPVLLGSAILGAVAGRVAASLPEAMKQFTQ-VDATYHSETAFSPLHQRRYA 521
Cdd:PRK04123 445 AGGIARKnPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASpVEKTYQPDPENVARYEQLYQ 524
|
....*
gi 397405968 522 AYKAL 526
Cdd:PRK04123 525 EYKQL 529
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
8-485 |
8.42e-74 |
|
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: 240.59 E-value: 8.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGvsPSSIAGIGFDATC-S 86
Cdd:cd07783 2 FLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELR--PRRVVAIAVDGTSgT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINATGHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARHFF 166
Cdd:cd07783 80 LVLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 167 DLADYLTWRSTGDEARSVCTVTCKWTYLAHEQRWDAGYFRQIGLaelaDEDFVrigQRIVDPGTPCGEgLCATAAEEMGL 246
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGRWPSWLLALLGI----PPDLL---PRVVAPGTVIGT-LTAEAAEELGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 247 PIGTPVAVGMIDAHAGGIGTVGVLNGAVNNMAyvfGTSSCTMTTTQEAVFVPGVwGPYYSAMVPGYWLSEGGQSAAGAAI 326
Cdd:cd07783 223 PAGTPVVAGTTDSIAAFLASGAVRPGDAVTSL---GTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 327 DQLLSfhpaAAEAREQAKAAGVPLPvwladrvltqvaspseavtlaAGLHVVP-EFLGNRAPLADPHAKALIAGLGMERD 405
Cdd:cd07783 299 RWFFS----DDELAELSAQADPPGP---------------------SGLIYYPlPLRGERFPFWDPDARGFLLPRPHDRA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 406 ldnltALYVAGLCGIGYGLRQIIDA-QRACGIESENIVISGGAGQHPLVRQLLADACGVSVVsTASREPVLLGSAILGAV 484
Cdd:cd07783 354 -----EFLRALLEGIAFIERLGYERlEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVV-IAEEEEAALGAALLAAA 427
|
.
gi 397405968 485 A 485
Cdd:cd07783 428 G 428
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
8-485 |
2.57e-71 |
|
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: 234.73 E-value: 2.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDA-TCS 86
Cdd:cd07804 2 LLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGlVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINATGHP--VLRYVGGKISPEMQTPKILWLKENRPHIYQQARH 164
Cdd:cd07804 82 LVPVDENGKPL---------RPAILYGDRRATEEIEWLNENIGEdrIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 165 FFDLADYLTWRSTG----DEARSVCTVTCkwtYLAHEQRWDAGYFRQIGLaelaDEDFVrigQRIVDPGTPCGEgLCATA 240
Cdd:cd07804 153 FLGAYDYIVYKLTGeyviDYSSAGNEGGL---FDIRKRTWDEELLEALGI----DPDLL---PELVPSTEIVGE-VTKEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 241 AEEMGLPIGTPVAVGMIDAHAGGIGtVGVLN-GavNNMAYvFGTSSCTMTTTQEAVFVPGVWGPYYSamVPGYWLSEGGQ 319
Cdd:cd07804 222 AEETGLAEGTPVVAGTVDAAASALS-AGVVEpG--DLLLM-LGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVLNGGM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 320 SAAGAAI----DQLlsfhpaAAEAREQAKAAGVPlpvwlADRVLTQVASPSEAvtLAAGLHVVPEFLGNRAPLADPHAKA 395
Cdd:cd07804 296 ATSGSLLrwfrDEF------AGEEVEAEKSGGDS-----AYDLLDEEAEKIPP--GSDGLIVLPYFMGERTPIWDPDARG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 396 LIAGLGMERDLDNLtalYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVL 475
Cdd:cd07804 363 VIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGAS 439
|
490
....*....|
gi 397405968 476 LGSAILGAVA 485
Cdd:cd07804 440 LGDAFLAGVG 449
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
8-485 |
1.26e-68 |
|
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: 227.47 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGvsPSSIAGIGFdAT--C 85
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISV-SSqgE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 86 SLVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINA----------TGHPVlryvggkiSPEMQTPKILWLKENR 155
Cdd:cd07773 79 SGVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAErigaeelyriTGLPP--------SPMYSLAKLLWLREHE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 156 PHIYQQARHFFDLADYLTWRSTGdEARSVCTVTCKWTYL-AHEQRWDAgyfrqiGLAELADEDfVRIGQRIVDPGTPCGE 234
Cdd:cd07773 142 PEIFAKAAKWLSVADYIAYRLTG-EPVTDYSLASRTMLFdIRKRTWSE------ELLEAAGID-ASLLPELVPSGTVIGT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 235 gLCATAAEEMGLPIGTPVAVGMIDAHAGGIGtVGVLNGavNNMAYVFGTSSCTMTTTQEAVFVPGVWGPYYS---AMVPG 311
Cdd:cd07773 214 -VTPEAAEELGLPAGTPVVVGGHDHLCAALG-AGVIEP--GDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 312 YWLSEGGQSaAGAAIDQLLS--FHPAAAEAREQAKAAGVPlpvwladrvltqvaspseavTLAAGLHVVPEFLGNRAPLA 389
Cdd:cd07773 290 YYYLAGSLP-GGALLEWFRDlfGGDESDLAAADELAEAAP--------------------PGPTGLLFLPHLSGSGTPDF 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 390 DPHAKALIAGLGMERDLDnltALYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTA 469
Cdd:cd07773 349 DPDARGAFLGLTLGTTRA---DLLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPE 425
|
490
....*....|....*.
gi 397405968 470 SREPVLLGSAILGAVA 485
Cdd:cd07773 426 VPEATALGAALLAGVG 441
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
8-507 |
7.56e-68 |
|
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: 225.09 E-value: 7.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDAT-CS 86
Cdd:cd07779 2 ILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQrST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRAtgqaekinatghpvlryvggkispemqtpkilwlkenrphiyqqaRHFF 166
Cdd:cd07779 82 FVPVDEDGRPL---------RPAISWQDKRT---------------------------------------------AKFL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 167 DLADYLTWRSTGDEARSVCTVTCKWTYLAHEQRWDAGYFRQIGLAE--LADedfvrigqrIVDPGTPCGEgLCATAAEEM 244
Cdd:cd07779 108 TVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRdkLPE---------LVPPGTVIGT-LTKEAAEET 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 245 GLPIGTPVAVGMIDAHAGGIGTvGVLNgavNNMAYV-FGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWLSEGGQSAAG 323
Cdd:cd07779 178 GLPEGTPVVAGGGDQQCAALGA-GVLE---PGTASLsLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 324 AAI----DQLlsfhpaaAEAREQAKAAGVPlpvwlADRVLTQVASPSEAVtlAAGLHVVPEFLGNRAPLADPHAKALIAG 399
Cdd:cd07779 254 SAVrwfrDEF-------GQDEVAEKELGVS-----PYELLNEEAAKSPPG--SDGLLFLPYLAGAGTPYWNPEARGAFIG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 400 LGMERDLDNLtalYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSA 479
Cdd:cd07779 320 LTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAA 396
|
490 500
....*....|....*....|....*...
gi 397405968 480 ILGAVAGRVAASLPEAMKQFTQVDATYH 507
Cdd:cd07779 397 ILAAVGAGIYPDFEEAVKAMVRVTDTFE 424
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
8-526 |
5.80e-66 |
|
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: 221.28 E-value: 5.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGvsPSSIAGIGFDATC-S 86
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG--GGEVDAIGFSSAMhS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLAvgpsddadrNIIVWMDHRATGQAEKI--NATGHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARH 164
Cdd:cd07770 80 LLGVDEDGEPLT---------PVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 165 FFDLADYLTWRSTGDEARSVCTVTckWTYL--AHEQRWDAGYFRQIGLAE--LAdedfvrigqRIVDPGTPCgEGLCATA 240
Cdd:cd07770 151 FVSIKEYLLYRLTGELVTDYSTAS--GTGLlnIHTLDWDEEALELLGIDEeqLP---------ELVDPTEVL-PGLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 241 AEEMGLPIGTPVAVGMIDahaGGIGTVGVLNGAVNNMAYVFGTSSCTMTTTQEAVFVP--GVWgPYYSAmvPGYWLSEGG 318
Cdd:cd07770 219 AERLGLLAGTPVVLGASD---GALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPpgRLW-CYRLD--ENRWLVGGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 319 QSAAGAAIDqllsfhpaaaeareqakaagvplpvWLADRVLTQVASPSEAVTLAA-------GLHVVPEFLGNRAPLADP 391
Cdd:cd07770 293 INNGGNVLD-------------------------WLRDTLLLSGDDYEELDKLAEavppgshGLIFLPYLAGERAPGWNP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 392 HAKALIAGLGMERDLDnltALYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASR 471
Cdd:cd07770 348 DARGAFFGLTLNHTRA---DILRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEE 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 397405968 472 EPVLLGSAILGAVAGRVAASLpeAMKQFTQVDATYHSETAFSPLHQRRYAAYKAL 526
Cdd:cd07770 425 EASALGAALLALEALGLISSL--EADELVKIGKVVEPDPENHAIYAELYERFKKL 477
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
8-482 |
9.41e-65 |
|
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: 215.89 E-value: 9.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDAT-CS 86
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQmPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRAtgqaekinatghpvlryvggkispemqtpkilwlkenrphiyqqarHFF 166
Cdd:cd00366 82 VVLVDADGNPL---------RPAIIWLDRRA----------------------------------------------KFL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 167 DLADYLTWRSTGDEARSVCTVTckWTYL--AHEQRWDAgyfrqiglaELADEDFVRIGQ--RIVDPGTPCGEgLCATAAE 242
Cdd:cd00366 107 QPNDYIVFRLTGEFAIDYSNAS--GTGLydIKTGDWSE---------ELLDALGIPREKlpPIVESGEVVGR-VTPEAAE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 243 EMGLPIGTPVAVGMIDAHAGGIGtVGVLN-GAVNNMAyvfGTSSCTMTTTQEAVFVPGVWGPYYSAmVPGYWLSEGGQSA 321
Cdd:cd00366 175 ETGLPAGTPVVAGGGDTAAAALG-AGVVEpGDAVDST---GTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLWLLEGAINT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 322 AGAAI----DQLLSFHPAAAEAREQAKAAgvplpvwladrvltqvaspSEAVTLAAGLHVVPEFLGNRAPLADPHAKALI 397
Cdd:cd00366 250 GGASLrwfrDEFGEEEDSDAEYEGLDELA-------------------AEVPPGSDGLIFLPYLSGERSPIWDPAARGVF 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 398 AGLGMERDLDNLTAlyvAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLLG 477
Cdd:cd00366 311 FGLTLSHTRAHLIR---AVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALG 387
|
....*
gi 397405968 478 SAILG 482
Cdd:cd00366 388 AAILA 392
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
8-485 |
2.79e-62 |
|
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: 210.87 E-value: 2.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDAT-CS 86
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHgNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINATGHP--VLRYVGGKISPEMQTPKILWLKENRPHIYQQARH 164
Cdd:cd07802 82 LYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEDGTLekVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 165 FFDLADYLTWRSTGDearsvctVTCKWT------YLAHEQRWDAGYFRQIGLAELADedfvRIGqRIVDPGTPCGEgLCA 238
Cdd:cd07802 153 VLFCKDWIRYRLTGE-------ISTDYTdagsslLDLDTGEYDDELLDLLGIEELKD----KLP-PLVPSTEIAGR-VTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 239 TAAEEMGLPIGTPVAVGMIDAHAGGIGTvgvlnGAVN--NMAYVFGTSSCTMTTTQEAVFVPGVWGpYYSAMVPGYWLSE 316
Cdd:cd07802 220 EAAALTGLPEGTPVAAGAFDVVASALGA-----GAVDegQLCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLYLIV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 317 GGQSAAGAAIDQLLSFHpaaaeAREQAKAAGVPLPVWLAdrvltqvaspsEAVTLAAGLHVV---PEFLGNRaplADPHA 393
Cdd:cd07802 294 EASPTSASNLDWFLDTL-----LGEEKEAGGSDYDELDE-----------LIAAVPPGSSGViflPYLYGSG---ANPNA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 394 KALIAGLGMERDLDN-LTALYVaglcGIGYGLRQIIDAQRACGiESENIVISGGAGQHPLVRQLLADACGVSVVSTASRE 472
Cdd:cd07802 355 RGGFFGLTAWHTRAHlLRAVYE----GIAFSHRDHLERLLVAR-KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEE 429
|
490
....*....|...
gi 397405968 473 PVLLGSAILGAVA 485
Cdd:cd07802 430 LGALGAAICAAVA 442
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
8-526 |
4.31e-59 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 204.77 E-value: 4.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLR-GELLAHATREI-----------TLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSS 75
Cdd:TIGR01234 3 AIGVDFGTLSGRALAVDVAtGEEIATAVEWYrhwvkgqflpkTGAKLPNDQALQHPADYIEVLEAAIPTVLAELGVDPAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 76 IAGIGFDAT-CSLVVIGDNDAPLAVGP--SDDADRNIIVWMDHRATGQAEKIN----ATGHPVLRYVGGKISPEMQTPKI 148
Cdd:TIGR01234 83 VVGIGVDFTaCTPAPIDSDGNPLCLLPefAENPHAYFKLWKHHAAQEEADRINrlahAPGEVDLSRYGGIISSEWFWAKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 149 LWLKENRPHIYQQARHFFDLADYLTWRSTGDEARSVCTVTCKwtYLAHEQrwdAGYFRQIGLAELaDEDFVR-----IGQ 223
Cdd:TIGR01234 163 LQITEEDPAIYQAADRWIELADWIVAQLSGDIRRGRCTAGYK--ALWHES---WGYPSASFFDEL-NPILNRhlpdkLFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 224 RIVDPGTPCGEgLCATAAEEMGLPIGTPVAVGMIDAHaggIGTVGVLNGAVNNMAYVFGTSSCTMTTTQEAVFVPGVWGP 303
Cdd:TIGR01234 237 DIWTAGEPAGT-LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGIAQPGALVKIMGTSTCHVLIGDKQRAVPGMCGV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 304 YYSAMVPGYWLSEGGQSAAGAAIDQLLS--FHPaaaEAREQAKAAGVPLpvwlaDRVLTQVASPSEavTLAAGLHVVPEF 381
Cdd:TIGR01234 313 VDGGIVPGFIGYEAGQSAVGDIFAWFGKvcVPP---ELKTEANASQKQL-----HEALSEAAAKQP--SGEHGLVALDWF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 382 LGNRAPLADPHAKALIAGLGMERDLDNltaLYVAGLCGIGYGLRQIIDAQRACGIESENIVISGG-AGQHPLVRQLLADA 460
Cdd:TIGR01234 383 NGNRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGiARKNPVIMQIYADV 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 397405968 461 CGVSVVSTASREPVLLGSAILGAVAGRVAASLPEAMKQF-TQVDATYHSETAFSPLHQRRYAAYKAL 526
Cdd:TIGR01234 460 TNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMgSAVEKTLTPCSENAQRYEQLYARYQEL 526
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
277-485 |
3.74e-56 |
|
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: 186.76 E-value: 3.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 277 MAYVFGTSSCTMTTTQEAV-FVPGVWGPYYSAMVPGYWLSEGGQSAAGAAIDQLLSFHPAAAEAREQAKAAgvPLPVWLA 355
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAGNVE--SLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 356 drvltqvaspSEAVTLAAGLHVVPEFLGNRAPLADPHAKALIAGLGMERDLdnlTALYVAGLCGIGYGLRQIIDAQRAC- 434
Cdd:pfam02782 79 ----------LAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKQe 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 397405968 435 GIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAVA 485
Cdd:pfam02782 146 GHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
9-526 |
4.25e-46 |
|
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: 168.26 E-value: 4.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATC-SL 87
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMhGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 88 VVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINAT--GHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARHF 165
Cdd:TIGR01312 81 VLLDANGEVL---------RPAILWNDTRTAQECEELEAElgDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 166 FDLADYLTWRSTGDEA--RSVCTVTckwTYLAHEQR-WDAGYFRQIGLaelaDEDFVrigQRIVDPGTPCGEgLCATAAE 242
Cdd:TIGR01312 152 MLPKDYLRYRLTGEYVteYSDASGT---GWFDVAKRaWSKELLDALDL----PESQL---PELIESSEKAGT-VRPEVAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 243 EMGLPIGTPVAVGMIDAHAGGIGTvGVLNGAVNNMAyvFGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWLSEGGQSAA 322
Cdd:TIGR01312 221 RLGLSAGVPVAAGGGDNAAGAIGT-GTVDPGDAMMS--LGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGWLPMGVTLSA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 323 GAAIDQLlsfhpaaaeaREQAKAAGVPLPVWLADrvltQVASPSEAVTLaaglhvVPEFLGNRAPLADPHAKALIAGLGM 402
Cdd:TIGR01312 298 TSSLEWF----------RELFGKEDVEALNELAE----QSPPGAEGVTF------LPYLNGERTPHLDPQARGSFIGLTH 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 403 ERDLDNLTAlyvAGLCGIGYGLRQIIDAQR-ACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAIL 481
Cdd:TIGR01312 358 NTTRADLTR---AVLEGVTFALRDSLDILReAGGIPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAIL 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 397405968 482 GAVAGRVAASLPEAMKQFTQVDATYHSETAFSPLHQRRYAAYKAL 526
Cdd:TIGR01312 435 AAWALGEKDLAALCSEAVVKQTESVLPIAENVEAYEELYERYKKL 479
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
8-485 |
2.79e-44 |
|
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: 162.41 E-value: 2.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDAT-CS 86
Cdd:cd24121 2 LIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQgDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINATG--HPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARH 164
Cdd:cd24121 82 TWLVDEDGRPV---------RDAILWLDGRAADIVERWQADGiaEAVFEITGTGLFPGSQAAQLAWLKENEPERLERART 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 165 FFDLADYLTWRSTG----DEARSVctvtckWTYLAHEQR-WDAGYFRQIGLAELADEdfvrigQRIVDPGTPCGEGLCAT 239
Cdd:cd24121 153 ALHCKDWLFYKLTGeiatDPSDAS------LTFLDFRTRqYDDEVLDLLGLEELRHL------LPPIRPGTEVIGPLTPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 240 AAEEMGLPIGTPVAVGMIDAHAGGIGtVGVLNGAVnnmAY-VFGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWLSEGG 318
Cdd:cd24121 221 AAAATGLPAGTPVVLGPFDVVATALG-SGAIEPGD---ACsILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWLRAMA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 319 QSAAGAAIDQLLsfHPAAAEAREQAKAAGVPLPVwLADRVLTQVASPSEAVT----LAAGlhvvpeflGNRAPLADPHAK 394
Cdd:cd24121 297 NMAGTPNLDWFL--RELGEVLKEGAEPAGSDLFQ-DLEELAASSPPGAEGVLyhpyLSPA--------GERAPFVNPNAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 395 ALIAGLGMERDLDNLT-ALYVaglcGIGYGLRqiiDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREP 473
Cdd:cd24121 366 AQFTGLSLEHTRADLLrAVYE----GVALAMR---DCYEHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEF 438
|
490
....*....|..
gi 397405968 474 VLLGSAILGAVA 485
Cdd:cd24121 439 GARGAAMNAAVA 450
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
9-485 |
3.25e-44 |
|
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: 161.95 E-value: 3.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNL-RGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATC-S 86
Cdd:cd07809 3 LGIDLGTQSIKAVLIDAeTGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQMhG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKI-NATGHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQARHF 165
Cdd:cd07809 83 LVALDADGKVL---------RPAKLWCDTRTAPEAEELtEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 166 FDLADYLTWRSTGD------EARSVCtvtckWTYLAHEQrWDAGyFRQIGLAELADEDFVrigQRIVDPGTPCGEgLCAT 239
Cdd:cd07809 154 LLPHDYLNWKLTGEkvtglgDASGTF-----PIDPRTRD-YDAE-LLAAIDPSRDLRDLL---PEVLPAGEVAGR-LTPE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 240 AAEEMGLPIGTPVAVGMIDAHAGGIGTVGVLNGAVnNMAyvFGTSSCTMTTTQEAVF-VPGVWGPYYSAMVpGYWLSEGG 318
Cdd:cd07809 223 GAEELGLPAGIPVAPGEGDNMTGALGTGVVNPGTV-AVS--LGTSGTAYGVSDKPVSdPHGRVATFCDSTG-GMLPLINT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 319 QSAAGAAIDQLLsfhpaaaeareqaKAAGVPLPVwlADRVLTQVASPSEavtlaaGLHVVPEFLGNRAPlADPHAKALIA 398
Cdd:cd07809 299 TNCLTAWTELFR-------------ELLGVSYEE--LDELAAQAPPGAG------GLLLLPFLNGERTP-NLPHGRASLV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 399 GLgmerDLDNLTA--LYVAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLL 476
Cdd:cd07809 357 GL----TLSNFTRanLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGAL 432
|
....*....
gi 397405968 477 GSAILGAVA 485
Cdd:cd07809 433 GAALQAAWG 441
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
9-485 |
2.14e-36 |
|
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: 140.44 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNLRGELLAHATREITLFR--SAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIgfdATCS 86
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTddDYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAV---SSTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 ----LVVIGDNDAPLAVGPsddadrNIivwmDHRATGQAEKIN-ATGHPVLRYVGGKISPEMQTPKILWLKENRPHIYQQ 161
Cdd:cd07798 80 qregIVFLDKDGRELYAGP------NI----DARGVEEAAEIDdEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 162 ARHFFDLADYLTWRSTGDEA--RSVCTVTCkwTYLAHEQRWDagyfrqiglAELADE-DF-VRIGQRIVDPGTPCGEgLC 237
Cdd:cd07798 150 IATVLSISDWIGYRLTGELVsePSQASETQ--LFDIKKREWS---------QELLEAlGLpPEILPEIVPSGTVLGT-VS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 238 ATAAEEMGLPIGTPVAVGMIDAHAGGIGTVGVLNGAVnnmAYVFGTSSCTMTTTQEAVFVP--GVW-GPYysaMVPGYWL 314
Cdd:cd07798 218 EEAARELGLPEGTPVVVGGADTQCALLGSGAIEPGDI---GIVAGTTTPVQMVTDEPIIDPerRLWtGCH---LVPGKWV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 315 SEGGQSAAGAAID---QLLSFHPAAAEAREQAKAAGVPLPvwlADRVL----TQVASPSEAVTLAAGLHVVPEFLGNRap 387
Cdd:cd07798 292 LESNAGVTGLNYQwlkELLYGDPEDSYEVLEEEASEIPPG---ANGVLaflgPQIFDARLSGLKNGGFLFPTPLSASE-- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 388 ladPHAKALIAGLgmerdldnltalyvagLCGIGYGLRQIID-AQRACGIESENIVISGGAGQHPLVRQLLADACGVSVV 466
Cdd:cd07798 367 ---LTRGDFARAI----------------LENIAFAIRANLEqLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVL 427
|
490
....*....|....*....
gi 397405968 467 STASREPVLLGSAILGAVA 485
Cdd:cd07798 428 VPEGREASALGAAICAAVG 446
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
7-523 |
3.83e-31 |
|
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: 126.29 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 7 NIIGVDVGSGSVRAGIFNLRGELLAHATREITlfRSAGNKVEQSSR----EIWQAVCYCIKTAVANAGVSPSSIAGIgfd 82
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWR--HKEVPDVPGSMDfdteKNWKLICECIREALKKAGIAPKSIAAI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 83 ATCS----LVVIGDNDAPLAVGPSDDAdrniivwmdhRATGQAEKINATgHPVLRYVGGKISPemQT------PKILWLK 152
Cdd:cd07775 76 STTSmregIVLYDNEGEEIWACANVDA----------RAAEEVSELKEL-YNTLEEEVYRISG--QTfalgaiPRLLWLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 153 ENRPHIYQQARHFFDLADYLTWRSTGD---EARSVCTvTCkwTYLAHEQRWDAGYFRQIGLAEladedfvRIGQRIVDPG 229
Cdd:cd07775 143 NNRPEIYRKAAKITMLSDWIAYKLSGElavEPSNGST-TG--LFDLKTRDWDPEILEMAGLKA-------DILPPVVESG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 230 TPCGEgLCATAAEEMGLPIGTPVAVGMIDAHAGGIGtVGVLNGAvnnmayvfGTSSCTMTTTQEAVFVPgvwGPYYS--- 306
Cdd:cd07775 213 TVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLG-LGVVRPG--------QTAVLGGSFWQQEVNTA---APVTDpam 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 307 ------AMVPGYWLSEGgqsaagaaidqlLSFHPA----------AAEAREQAKAAGVPlpvwlADRVLTQVAS--P--- 365
Cdd:cd07775 280 nirvncHVIPDMWQAEG------------ISFFPGlvmrwfrdafCAEEKEIAERLGID-----AYDLLEEMAKdvPpgs 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 366 -------SEAVTLAAGLHVVPEFLgNRAPLADPHAKALIAGLGMErdldnlTALYVAglcgigYGLRQIIDAqrACGIES 438
Cdd:cd07775 343 ygimpifSDVMNYKNWRHAAPSFL-NLDIDPEKCNKATFFRAIME------NAAIVS------AGNLERIAE--FSGIFP 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 439 ENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAVAGRVAASLPEAMKQFTQVDATYHSETAFSPLHQR 518
Cdd:cd07775 408 DSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQD 487
|
....*
gi 397405968 519 RYAAY 523
Cdd:cd07775 488 LYEKW 492
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
8-265 |
5.44e-31 |
|
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: 120.52 E-value: 5.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATC-S 86
Cdd:pfam00370 2 YLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGhG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKINATGHPVLRYV--GGKISPEMQTPKILWLKENRPHIYQQARH 164
Cdd:pfam00370 82 TVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEEGNNQKLYEitGLPIWPGFTLSKLRWIKENEPEVFEKIHK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 165 FFDLADYLTWRSTGDEARSVCTVTCKWTYLAHEQRWDAGYFRQIGLAEladedfvRIGQRIVDPGTPCGEgLCATAAEEM 244
Cdd:pfam00370 153 FLTIHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPR-------DHLPPLVESSEIYGE-LNPELAAMW 224
|
250 260
....*....|....*....|.
gi 397405968 245 GLPIGTPVAVGMIDAHAGGIG 265
Cdd:pfam00370 225 GLDEGVPVVGGGGDQQAAAFG 245
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
11-529 |
8.94e-26 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 110.87 E-value: 8.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 11 VDVGSGSVRAGIFNLRGELLAHATREITLFRSAG--NKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIgfdATCSL- 87
Cdd:PRK10939 8 LDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvpGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAV---SATSMr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 88 --VVIGDNDA-PL-AVGpsddadrNIivwmDHRATGQAEKINATgHPVLRYVGGKISPemQT------PKILWLKENRPH 157
Cdd:PRK10939 85 egIVLYDRNGtEIwACA-------NV----DARASREVSELKEL-HNNFEEEVYRCSG--QTlalgalPRLLWLAHHRPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 158 IYQQARHFFDLADYLTWRSTGD---EARSVCTVTckwTYLAHEQRWDAGYFRQIGLAelADedfvrIGQRIVDPGTPCGE 234
Cdd:PRK10939 151 IYRQAHTITMISDWIAYMLSGElavDPSNAGTTG---LLDLVTRDWDPALLEMAGLR--AD-----ILPPVKETGTVLGH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 235 gLCATAAEEMGLPIGTPVAVGMIDAHAGGIGTvgvlnGAVN-NMAYVFGTssctmTTTQEAVFVP-GVWGPYYS-----A 307
Cdd:PRK10939 221 -VTAKAAAETGLRAGTPVVMGGGDVQLGCLGL-----GVVRpGQTAVLGG-----TFWQQVVNLPaPVTDPNMNirinpH 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 308 MVPGYWLSEG--------------------GQSAAGAAIDqllsfhpaAAEAREQaKAAGVP------LPVWladrvltq 361
Cdd:PRK10939 290 VIPGMVQAESisfftgltmrwfrdafcaeeKLLAERLGID--------AYSLLEE-MASRVPvgshgiIPIF-------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 362 vaspSEAVTLAAGLHVVPEFLgNRAPLADPHAKAliaglGMERDLDNLTALYVAGlcgigyGLRQIidaQRACGIESENI 441
Cdd:PRK10939 353 ----SDVMRFKSWYHAAPSFI-NLSIDPEKCNKA-----TLFRALEENAAIVSAC------NLQQI---AAFSGVFPSSL 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 442 VISGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAVAGRVAASLPEAMKQFTQVDATYHSETAFSPLHQRRYA 521
Cdd:PRK10939 414 VFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEAKE 493
|
....*...
gi 397405968 522 AYKALQQA 529
Cdd:PRK10939 494 KWQAVYAD 501
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
8-509 |
2.41e-24 |
|
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: 106.01 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREIT-LFRSAGnKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATCS 86
Cdd:cd07769 2 ILAIDQGTTSTRAILFDEDGNIVASAQKEHEqIYPQPG-WVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDND--APLAvgpsddadrNIIVWMDHRATGQAEKINATGHP--VLRYVGGKISPEMQTPKILWLKENRPHIYQQA 162
Cdd:cd07769 81 TTVVWDKKtgKPLY---------NAIVWQDRRTADICEELKAKGLEerIREKTGLPLDPYFSATKIKWILDNVPGARERA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 163 RH----FFDLADYLTWRSTGDEA---------RsvctvtckwTYL--AHEQRWDagyfrqiglAELADEdfVRIGQRIVD 227
Cdd:cd07769 152 ERgellFGTIDTWLIWKLTGGKVhvtdvtnasR---------TMLfnIHTLEWD---------DELLEL--FGIPRSMLP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 228 PGTPCGEGLCATAAEemGLPIGTPVAvGMI-DAHAGGIGTVGVLNGAVNNmayVFGT-SSCTMTTTQEAVFV-PGV---- 300
Cdd:cd07769 212 EVRPSSEVFGYTDPE--GLGAGIPIA-GILgDQQAALFGQGCFEPGMAKN---TYGTgCFLLMNTGEKPVPSkNGLltti 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 301 -WG----PYYSAmvpgywlsEGGQSAAGAAIDqllsfhpaaaeareqakaagvplpvWLADrVLTQVASPSEAVTLAA-- 373
Cdd:cd07769 286 aWQiggkVTYAL--------EGSIFIAGAAIQ-------------------------WLRD-NLGLIEDAAETEELARsv 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 374 ----GLHVVPEFLGNRAPLADPHAKALIAGL--GMERDldnltALYVAGLCGIGYGLRQIIDA-QRACGIESENIVISGG 446
Cdd:cd07769 332 edngGVYFVPAFSGLGAPYWDPDARGAIVGLtrGTTKA-----HIVRAALESIAYQTRDVLEAmEKDSGIKLKELRVDGG 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 397405968 447 AGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAVAGRVAASLpEAMKQFTQVDATYHSE 509
Cdd:cd07769 407 ATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDL-DELASLWQVDKRFEPS 468
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
9-528 |
3.07e-23 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 102.74 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 9 IGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVAN---AGVSPSSIAGIGFDATC 85
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQhslQDVKALGIAGQMHGATL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 86 slvvigdndaplaVGPSDDADRNIIVWMDHRATGQAEKINATGhPVLRYVGGKIS-PEMQTPKILWLKENRPHIYQQARH 164
Cdd:PRK15027 83 -------------LDAQQRVLRPAILWNDGRCAQECALLEARV-PQSRVITGNLMmPGFTAPKLLWVQRHEPEIFRQIDK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 165 FFDLADYLTWRSTGDEARSVCTVT-CKWTYLAhEQRWDAgyfrqiglAELADEDFVRIGQRIVDPGTPCGEGLCATAAEE 243
Cdd:PRK15027 149 VLLPKDYLRLRMTGEFASDMSDAAgTMWLDVA-KRDWSD--------VMLQACHLSRDQMPALYEGSEITGALLPEVAKA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 244 MGLPiGTPVAVGMIDAHAGGIGtVGVLNGavNNMAYVFGTSSCTMTTTQEAVFVPGVWGPYYSAMVPGYWlseggqsaag 323
Cdd:PRK15027 220 WGMA-TVPVVAGGGDNAAGAVG-VGMVDA--NQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW---------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 324 aaidQLLSFHPAAAEARE-QAKAAGVplpvwlaDRVLTQVASPSEAVTLAAGLHVVPEFLGNRAPLADPHAKALIAGLGM 402
Cdd:PRK15027 286 ----HLMSVMLSAASCLDwAAKLTGL-------SNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 403 ERDLDNLTAlyvAGLCGIGYGLRQIIDAQRACGIESENIVISGGAGQHPLVRQLLADACGVSV-VSTASREPVLLGSAIL 481
Cdd:PRK15027 355 QHGPNELAR---AVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARL 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 397405968 482 GAVAGRVAASLPEAMKQFTQVDATYHSETAFSPLHQRRYAAYKALQQ 528
Cdd:PRK15027 432 AQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQ 478
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
8-506 |
5.37e-22 |
|
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: 99.10 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATCSL 87
Cdd:cd07786 2 ILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 88 VVIGDND--APLAvgpsddadrNIIVWMDHRATGQAEKINATGHpvLRYVGGK----ISPEMQTPKILWLKENRPHIYQQ 161
Cdd:cd07786 82 TVVWDREtgKPVY---------NAIVWQDRRTADICEELKAEGH--EEMIREKtglvLDPYFSATKIRWILDNVPGARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 162 A---RHFFDLAD-YLTWRSTGDE---------ARsvctvtckwTYL--AHEQRWDAGYFRQIGL-AELADEdfVRigqri 225
Cdd:cd07786 151 AergELAFGTIDsWLIWKLTGGKvhatdvtnaSR---------TMLfnIHTLEWDDELLELFGIpASMLPE--VK----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 226 vdpgtPCGEGLCATAAEEMGLPIgtPVAvGMI-DAHAGGIGTVGVLNGAVNNmayVFGTSS-CTMTTTQEAVF------- 296
Cdd:cd07786 215 -----PSSEVFGYTDPDLLGAEI--PIA-GIAgDQQAALFGQACFEPGMAKN---TYGTGCfMLMNTGEKPVRskngllt 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 297 -----VPGvwgpyysamVPGYWLsEGGQSAAGAAIDqllsfhpaaaeareqakaagvplpvWLADRV-LTQVASPSEAvt 370
Cdd:cd07786 284 tiawqLGG---------KVTYAL-EGSIFIAGAAVQ-------------------------WLRDGLgLIESAAETEA-- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 371 LAA------GLHVVPEFLGNRAPLADPHAKALIagLGMERDlDNLTALYVAGLCGIGYGLRQIIDA-QRACGIESENIVI 443
Cdd:cd07786 327 LARsvpdngGVYFVPAFTGLGAPYWDPDARGAI--FGLTRG-TTRAHIARAALESIAYQTRDLLEAmEADSGIPLKELRV 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 397405968 444 SGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAVAGRVAASLPEAMKQFtQVDATY 506
Cdd:cd07786 404 DGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLW-QVDRRF 465
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
7-481 |
9.64e-22 |
|
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: 97.68 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 7 NIIGVDVGSGSVRAGIFNL-RGELLAHATREITLFRSAGNKV--EQSSREIWQAVCYCIKTAVANAGvspSSIAGIGFda 83
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLeSGRILESVSRPTPAPISSDDPGrsEQDPEKILEAVRNLIDELPREYL---SDVTGIGI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 84 TC---SLVVIGDNDAPLavgpsddadRNIIVWMDHRATGQ-AEKINATGHPVLRYVGGKISPEMQTPKILWLKENRPhIY 159
Cdd:cd07777 76 TGqmhGIVLWDEDGNPV---------SPLITWQDQRCSEEfLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGP-LP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 160 QQARHFFDLADYLTWRSTGDEaRSVCTVTCkwtylAH--------EQRWDAGYFRQIGLaeladedFVRIGQRIVDPGTP 231
Cdd:cd07777 146 SKADRAGTIGDYIVARLTGLP-KPVMHPTN-----AAswglfdleTGTWNKDLLEALGL-------PVILLPEIVPSGEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 232 CGEGLCAtaaeemgLPIGTPVAVGMIDAHAGGIGTV-GVLNGAVNNMayvfGTSSctmtttQEAVFVP-GVWGPYYsAMV 309
Cdd:cd07777 213 VGTLSSA-------LPKGIPVYVALGDNQASVLGSGlNEENDAVLNI----GTGA------QLSFLTPkFELSGSV-EIR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 310 P---GYWLSEGGQSAAGAAIDQLLSFHpaaaeaREQAKAAGVPLP---VWlaDRVLTQVASPSEavtlaAGLHVVPEFLG 383
Cdd:cd07777 275 PffdGRYLLVAASLPGGRALAVLVDFL------REWLRELGGSLSddeIW--EKLDELAESEES-----SDLSVDPTFFG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 384 NRaplADPHAKALIAGLGMerdlDNLT-ALYVAGLCgigyglRQIID-----AQRACGIES--ENIVISGGAGQH-PLVR 454
Cdd:cd07777 342 ER---HDPEGRGSITNIGE----SNFTlGNLFRALC------RGIAEnlhemLPRLDLDLSgiERIVGSGGALRKnPVLR 408
|
490 500
....*....|....*....|....*..
gi 397405968 455 QLLADACGVSVVSTASREPVLLGSAIL 481
Cdd:cd07777 409 RIIEKRFGLPVVLSEGSEEAAVGAALL 435
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
8-486 |
1.56e-19 |
|
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: 91.47 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATCSL 87
Cdd:cd07793 2 ILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 88 VVIGDNDA--PLavgpsddadRNIIVWMDHRATGQAEKINA-----------------TGHPvlRYVGG---KISPEMQT 145
Cdd:cd07793 82 FLTWDKKTgkPL---------HNFITWQDLRAAELCESWNRslllkalrggskflhflTRNK--RFLAAsvlKFSTAHVS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 146 PKILWLKENRPHIYQQARH---FFDLAD-YLTWRSTGDEAR----SVCTVTCKW-TYlahEQRWDAGYFRQIGlaelade 216
Cdd:cd07793 151 IRLLWILQNNPELKEAAEKgelLFGTIDtWLLWKLTGGKVHatdySNASATGLFdPF---TLEWSPILLSLFG------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 217 dfvrIGQRIVDPGTPCGEGLCATAAEEMG--LPIGTPVAvgmiDAHAGGIGTVGVLNGAVNnmayvfgtssCTMTTtqeA 294
Cdd:cd07793 221 ----IPSSILPEVKDTSGDFGSTDPSIFGaeIPITAVVA----DQQAALFGECCFDKGDVK----------ITMGT---G 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 295 VFVPGVWG--PYYSA-----MVpGY-------WLSEGGQSAAGAAIDqllsfhpaaaeareqakaagvplpvWLADRVLt 360
Cdd:cd07793 280 TFIDINTGskPHASVkglypLV-GWkiggeitYLAEGNASDTGTVID-------------------------WAKSIGL- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 361 qVASPSEAVTLAA------GLHVVPEFLGNRAPLADPHAKALIAGLG-------MERdldnltalyvAGLCGIGYGLRQI 427
Cdd:cd07793 333 -FDDPSETEDIAEsvedtnGVYFVPAFSGLQAPYNDPTACAGFIGLTpsttkahLVR----------AILESIAFRVKQL 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 397405968 428 IDA-QRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAIL-GAVAG 486
Cdd:cd07793 402 LETmEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLaGLASG 462
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
8-529 |
1.00e-16 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 82.95 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREIT-LFRSAGnKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGFDATCS 86
Cdd:PRK00047 7 ILALDQGTTSSRAIIFDHDGNIVSVAQKEFTqIFPQPG-WVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDAPLAVgpsddadRNIIVWMDHRATGQAEKINATGHP--VLRYVGGKISPEMQTPKILWLKENRPHIYQQARH 164
Cdd:PRK00047 86 TTVVWDKETGRPI-------YNAIVWQDRRTADICEELKRDGYEdyIREKTGLVIDPYFSGTKIKWILDNVEGARERAEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 165 ---FFDLAD-YLTWRSTGDEARsVCTVT-CKWTYL--AHEQRWDagyfrqiglaelaDE--DFVRIGQRIVDPGTPCGEG 235
Cdd:PRK00047 159 gelLFGTIDtWLVWKLTGGKVH-VTDYTnASRTMLfnIHTLDWD-------------DEllELLDIPRSMLPEVRPSSEV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 236 LCATAAEEmglPIGTPVAV-GMI-DAHAGGIGTVGVLNGAVNNmayVFGTSSCT-MTTTQEAVFVP---------GVWGP 303
Cdd:PRK00047 225 YGKTNPYG---FFGGEVPIaGIAgDQQAALFGQLCFEPGMAKN---TYGTGCFMlMNTGEKAVKSEngllttiawGIDGK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 304 yysamvPGYWLsEGGQSAAGAAIDqllsfhpaaaeareqakaagvplpvWLADRV-LTQVASPSEA----VTLAAGLHVV 378
Cdd:PRK00047 299 ------VVYAL-EGSIFVAGSAIQ-------------------------WLRDGLkIISDASDSEAlarkVEDNDGVYVV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 379 PEFLGNRAPLADPHAKALIAGL--GMERDldnltALYVAGLCGIGYGLRQIIDA-QRACGIESENIVISGGAGQHPLVRQ 455
Cdd:PRK00047 347 PAFTGLGAPYWDSDARGAIFGLtrGTTKE-----HIIRATLESIAYQTRDVLDAmQADSGIRLKELRVDGGAVANNFLMQ 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 397405968 456 LLADACGVSVVSTASREPVLLGSAILGAVAGRVAASLPEaMKQFTQVDATYHSETAfsplHQRRYAAYKALQQA 529
Cdd:PRK00047 422 FQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDE-LKEQWKIDRRFEPQMD----EEEREKLYAGWKKA 490
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
8-533 |
1.55e-14 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 76.17 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 8 IIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAG--VSPSSIAGIGFDATC 85
Cdd:PTZ00294 4 IGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLRekGPSFKIKAIGITNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 86 SLVVIGDNDA--PLAvgpsddadrNIIVWMDHRATGQAEKINAT--GHPVLRYVGG-KISPEMQTPKILWLKENRPHIYQ 160
Cdd:PTZ00294 84 ETVVAWDKVTgkPLY---------NAIVWLDTRTYDIVNELTKKygGSNFFQKITGlPISTYFSAFKIRWMLENVPAVKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 161 QARH----FFDLADYLTWRSTGDEARsVCTVT-CKWTYLA--HEQRWDAGYFRQIGLAELA-------DEDFvrigqriv 226
Cdd:PTZ00294 155 AVKEgtllFGTIDTWLIWNLTGGKSH-VTDVTnASRTFLMniKTLKWDEELLNKFGIPKETlpeikssSENF-------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 227 dpgtpcGEGLCATAAEEMGLPIGtpvavGMI-DAHAGGIGTVGVLNGAVNNmayVFGTSsC--TMTTTQEAVFVP----- 298
Cdd:PTZ00294 226 ------GTISGEAVPLLEGVPIT-----GCIgDQQAALIGHGCFEKGDAKN---TYGTG-CflLMNTGTEIVFSKhgllt 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 299 ------GVWGPYYSAMvpgywlsEGGQSAAGAAIDqllsfhpaaaeareqakaagvplpvWLADRvLTQVASPSEAVTLA 372
Cdd:PTZ00294 291 tvcyqlGPNGPTVYAL-------EGSIAVAGAGVE-------------------------WLRDN-MGLISHPSEIEKLA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 373 ------AGLHVVPEFLGNRAPLADPHAKALIAGL--GMERDldnltALYVAGLCGIGYGLRQIIDA-QRACGIESENIVI 443
Cdd:PTZ00294 338 rsvkdtGGVVFVPAFSGLFAPYWRPDARGTIVGMtlKTTRA-----HIVRAALEAIALQTNDVIESmEKDAGIELNSLRV 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 444 SGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAVAGRVAASLPEaMKQFTQVDATYHSETAFSPLHQRRYAAY 523
Cdd:PTZ00294 413 DGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEE-VKKLIRRSNSTFSPQMSAEERKAIYKEW 491
|
570
....*....|.
gi 397405968 524 -KALQQAGRLI 533
Cdd:PTZ00294 492 nKAVERSLKWA 502
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
11-485 |
4.39e-14 |
|
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: 74.48 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 11 VDVGSGSVRAGIFNLRGELLAHATREIT-LFRSAGnKVEQSSREIWQAVCYCIKTAVANA---GVSPSSIAGIGFDATCS 86
Cdd:cd07792 6 IDQGTTSTRFIVFDSTGELVASHQVEHKqIYPKPG-WVEHDPMEILESVYECIEEAVEKLkalGISPSDIKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDA--PLAvgpsddadrNIIVWMDHRATGQAEKINAtghpvlRYVGGK----------ISPEMQTPKILWLKEN 154
Cdd:cd07792 85 TTVVWDKSTgkPLY---------NAIVWLDTRTSDTVEELSA------KTPGGKdhfrkktglpISTYFSAVKLRWLLDN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 155 RPHIyQQARHFFDLA----D-YLTWRSTGDEARSV-CT-VT-CKWTYLA--HEQRWDAgyfrqiglaELADedFVRIGQ- 223
Cdd:cd07792 150 VPEV-KKAVDDGRLLfgtvDsWLIWNLTGGKNGGVhVTdVTnASRTMLMnlRTLQWDP---------ELCE--FFGIPMs 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 224 ---RIVdpgtpcgeglcaTAAEEMGL----PI-GTPVAvGMI-DAHAGGIGtvgvlngavnNMAYVFGTSSCT------- 287
Cdd:cd07792 218 ilpEIR------------SSSEVYGKiasgPLaGVPIS-GCLgDQQAALVG----------QGCFKPGEAKNTygtgcfl 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 288 -MTTTQEAVFvpgvwgpyySA----MVPGYWLS---------EGGQSAAGAAIDqllsfhpaaaeareqakaagvplpvW 353
Cdd:cd07792 275 lYNTGEEPVF---------SKhgllTTVAYKLGpdappvyalEGSIAIAGAAVQ-------------------------W 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 354 LADRvLTQVASPSEAVTLAA------GLHVVPEFLGNRAPLADPHAKALIAGLGMerdldNLTALYV--AGLCGIGYGLR 425
Cdd:cd07792 321 LRDN-LGIISSASEVETLAAsvpdtgGVYFVPAFSGLFAPYWRPDARGTIVGLTQ-----FTTKAHIarAALEAVCFQTR 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 397405968 426 QIIDA-QRACGIESENIVISGGAGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAVA 485
Cdd:cd07792 395 EILDAmNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLA 455
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
6-500 |
7.43e-12 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 67.36 E-value: 7.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 6 QNIIGV-DVGSGSVRAGIFNLRGELLAHAtreitlfrSAGNKVEQ----------SSREIWQAVCYCIKtaVANAGVSPS 74
Cdd:PRK10331 1 QDVILVlDCGATNVRAIAVDRQGKIVARA--------STPNASDIaaensdwhqwSLDAILQRFADCCR--QINSELTEC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 75 SIAGIgfdatcSLVVIGDNDAPLavgpsDDADRN---IIVWMDHRATgqaekinatghPVLRYVGGKISPE-MQTP---- 146
Cdd:PRK10331 71 HIRGI------TVTTFGVDGALV-----DKQGNLlypIISWKCPRTA-----------AVMENIERYISAQqLQQIsgvg 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 147 --------KILWLKENRPHIYQQARHFFDLADYLTWRSTGDEARSVCTV-TCKWTYLAHEQrWDAGYFRQIGLAEladed 217
Cdd:PRK10331 129 afsfntlyKLVWLKENHPQLLEQAHAWLFISSLINHRLTGEFTTDITMAgTSQMLDIQQRD-FSPEILQATGLSR----- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 218 fvRIGQRIVDPGTPCGEgLCATAAEEMGLPIGTPVavgmIDA-HAGGIGTVGvlNGAVNNMAYV-FGTSSCTMTTTQEav 295
Cdd:PRK10331 203 --RLFPRLVEAGEQIGT-LQPSAAALLGLPVGIPV----ISAgHDTQFALFG--SGAGQNQPVLsSGTWEILMVRSAQ-- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 296 fVPGVWGPYYSAM------VPGYwLSEGGQSAAGAAIDQL--LSFHPAAAEAREQAKAAGVPlpvwladrvltqvasPSe 367
Cdd:PRK10331 272 -VDTSLLSQYAGStceldsQSGL-YNPGMQWLASGVLEWVrkLFWTAETPYQTMIEEARAIP---------------PG- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 368 avtlAAGLHVVPEFLGNRapladphaKALIAGLGMERdldNLTALYVAGLCGIGYGLRQIIDA-QRACGIESENIVISGG 446
Cdd:PRK10331 334 ----ADGVKMQCDLLACQ--------NAGWQGVTLNT---TRGHFYRAALEGLTAQLKRNLQVlEKIGHFKASELLLVGG 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 397405968 447 AGQHPLVRQLLADACGVSVVSTASREPVLLGSAILGAVAGRVAASLPEAMKQFT 500
Cdd:PRK10331 399 GSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMK 452
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
11-535 |
8.24e-12 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 67.42 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 11 VDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSREIWQAVCYCIKTAVANAGVS----PSSIAGIGFDATCS 86
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKghnvDSGLKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 87 LVVIGDNDA--PLAvgpsddadrNIIVWMDHRATGQAEKIN---ATGHPVLRYVGG-KISPEMQTPKILWLKENRPHIYQ 160
Cdd:PLN02295 85 TTVAWSKSTgrPLY---------NAIVWMDSRTSSICRRLEkelSGGRKHFVETCGlPISTYFSATKLLWLLENVDAVKE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 161 QARH----FFDLADYLTWRSTGDEARSV----CTVTCKWTYL-AHEQRWDAGYFRQIGLAeladedfVRIGQRIVdpgtP 231
Cdd:PLN02295 156 AVKSgdalFGTIDSWLIWNLTGGASGGVhvtdVTNASRTMLMnLKTLDWDKPTLEALGIP-------AEILPKIV----S 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 232 CGEGLCATAAeemGLPI-GTPVAVGMIDAHAGGIGTVGVLNGAVNNmayvFGTSSCTMTTTQEAVfVPGVWGpYYSAMV- 309
Cdd:PLN02295 225 NSEVIGTIAK---GWPLaGVPIAGCLGDQHAAMLGQRCRPGEAKST----YGTGCFILLNTGEEV-VPSKHG-LLTTVAy 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 310 ------PGYWLSEGGQSAAGAAIDqllsfhpaaaeareqakaagvplpvWLADRvLTQVASPSEAVTLAA------GLHV 377
Cdd:PLN02295 296 klgpdaPTNYALEGSVAIAGAAVQ-------------------------WLRDN-LGIIKSASEIEALAAtvddtgGVYF 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 378 VPEFLGNRAPLADPHAKALIagLGMERdLDNLTALYVAGLCGIGYGLRQIIDAQRACGIESENIV------ISGGAGQHP 451
Cdd:PLN02295 350 VPAFSGLFAPRWRDDARGVC--VGITR-FTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKSHKglfllrVDGGATANN 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 452 LVRQLLADACGVSVVSTASREPVLLGSailgAVAGRVAASLPEAMKQFTQVDATyhSETAFSP-----LHQRRYAA-YKA 525
Cdd:PLN02295 427 LLMQIQADLLGSPVVRPADIETTALGA----AYAAGLAVGLWTEEEIFASEKWK--NTTTFRPkldeeERAKRYASwCKA 500
|
570
....*....|
gi 397405968 526 LQQAGRLIRE 535
Cdd:PLN02295 501 VERSFDLADL 510
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
7-495 |
1.95e-07 |
|
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: 53.69 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 7 NIIGVDVGSGSVRAGIFNLRGELLAhaTREITLFRSAGNKVEQSSR----EIWQAvcycIKTAVANAGVSPSSIAGIGFD 82
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKLE--LEEIHRFPNRPVEINGHLYwdidRLFDE----IKEGLKKAAEQGGDIDSIGID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 83 AT-CSLVVIGDNDAPLavgpsddadRNIIVWMDHRATGQAEKI----------NATGHPVLRyvggkISPEMQtpkILWL 151
Cdd:cd07771 75 TWgVDFGLLDKNGELL---------GNPVHYRDPRTEGMMEELfekiskeelyERTGIQFQP-----INTLYQ---LYAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 152 KENRPHIYQQARHFFDLADYLTWRSTGDEA--RSVCTVtckwTYL--AHEQRWDAGYFRQIGLAEladedfvRIGQRIVD 227
Cdd:cd07771 138 KKEGPELLERADKLLMLPDLLNYLLTGEKVaeYTIAST----TQLldPRTKDWSEELLEKLGLPR-------DLFPPIVP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 228 PGTPCGEgLCATAAEEMGLPiGTPV-AVGmidAH--AGGIGTVGVLNgavNNMAYVF-GTSSCTMTTTQ-----EAVFVP 298
Cdd:cd07771 207 PGTVLGT-LKPEVAEELGLK-GIPViAVA---SHdtASAVAAVPAED---EDAAFISsGTWSLIGVELDepvitEEAFEA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 299 GV---WGPYYSAM----VPGYWLseggqsaagaaIDQLlsfhpaaaeaREQAKAAGVPLPVwladrvltqvaspSEAVTL 371
Cdd:cd07771 279 GFtneGGADGTIRllknITGLWL-----------LQEC----------RREWEEEGKDYSY-------------DELVAL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 372 AAGLHVVPEFLgnraplaDPHAKALIAGLGMERDLDN-LTALYVAGLCGIG---------------YGLRQIidaQRACG 435
Cdd:cd07771 325 AEEAPPFGAFI-------DPDDPRFLNPGDMPEAIRAyCRETGQPVPESPGeiarciyeslalkyaKTIEEL---EELTG 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 397405968 436 IESENIVISGGAGQHPLVRQLLADACGVSVVS-----TAsrepvlLGSAILGAVAGRVAASLPEA 495
Cdd:cd07771 395 KRIDRIHIVGGGSRNALLCQLTADATGLPVIAgpveaTA------IGNLLVQLIALGEIKSLEEG 453
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
3-81 |
9.40e-06 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 47.58 E-value: 9.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 397405968 3 NDTQNIIGVDVGSGSVRAGIFNLRGELLAHATREItlfrsagnKVEQSSREIWQAVCYCIKTAVANAGVSPSSIAGIGF 81
Cdd:COG1940 2 PDAGYVIGIDIGGTKIKAALVDLDGEVLARERIPT--------PAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-258 |
1.59e-04 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. 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: 466792 [Multi-domain] Cd Length: 424 Bit Score: 44.17 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 7 NIIGVDVGSGSVRAGIFNLRGELLAHATREITLFRSAGNKVEQSSReIWQAVCYCIKTAVANAgvspsSIAGIGFdaTC- 85
Cdd:cd07772 1 VIAVFDIGKTNKKLLLFDENGEVLAERSTPNPEIEEDGYPCEDVEA-IWEWLLDSLAELAKRH-----RIDAINF--TTh 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 86 --SLVVIGDNDAPlaVGPSDDADRNIIVWMDHRATGQAEKINATGHPVLryvGGKISPEMQtpkILWLKENRPHIYQQAR 163
Cdd:cd07772 73 gaTFALLDENGEL--ALPVYDYEKPIPDEINEAYYAERGPFEETGSPPL---PGGLNLGKQ---LYWLKREKPELFARAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397405968 164 HFFDLADYLTWRSTGDEARSVCTVTCKwTYLaheqrWDagyFRQIGLAELADEdfvRIGQRIVDPGTPCGEGL---CATA 240
Cdd:cd07772 145 TILPLPQYWAWRLTGKAASEITSLGCH-TDL-----WD---FEKNEYSSLVKK---EGWDKLFPPLRKAWEVLgplRPDL 212
|
250
....*....|....*...
gi 397405968 241 AEEMGLPIGTPVAVGMID 258
Cdd:cd07772 213 ARRTGLPKDIPVGCGIHD 230
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
9-80 |
4.16e-04 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 42.07 E-value: 4.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 397405968 9 IGVDVGSGSVRAGIFNLRGELLAHATREITlfrsagnkVEQSSREIWQAVCYCIKTAVANAGVsPSSIAGIG 80
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTP--------AEEGPEAVLDRIAELIEELLAEAGV-RERILGIG 63
|
|
| |
