|
Name |
Accession |
Description |
Interval |
E-value |
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
6-533 |
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: 961.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 6 TVIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDATCS 85
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLAESKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLPVSPEGDAKQNIIVWMDHRATEQAERINATHHPVLNYVGGKISPEMETPKILWLKENMPEIYERAGQFF 165
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPELFARCKFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 166 DLADFLTWRATGDLARSVCTVTCKWTWLAHE---NRWDPDYFRTIGLAELADEDFIRIGHHIVSPGTPCGNGLTAQAAAE 242
Cdd:TIGR01315 161 DLTDFLTWRATGKEIRSFCSVVCKWGFVPVDgsnKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 243 MGLLPGTPVAVGLIDAHAGGIGTVG---VEGGALN----NLAYVFGTSSCTMASTTSPSFVPGVWGPYYSAMVPGLWLVE 315
Cdd:TIGR01315 241 LGLPAGTAVGSGLIDAHAGWIGTVGakvAENGDVSqaftRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 316 GGQSAAGAAIDQLLDFHPAVEEAREMAQRVNQPLPVWLADRILEKTAQPSDA--VALAKGLHVVPEFLGNRAPFADPHAR 393
Cdd:TIGR01315 321 GGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHLKEMAAKTNAPsiSYLVRHFHVYPDLWGNRSPIADPNMR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 394 AVICGLGMERDLDNLLALYIAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPV 473
Cdd:TIGR01315 401 GVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1685051901 474 LLGSAILGAVAGNIAPSVGEAMQQFTHVDKYYYPQERYQ-SLHHRRYEAYKQLQHTAKLLR 533
Cdd:TIGR01315 481 LHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPRGDPAkKLHDRKYEIFLQLARTQQEYR 541
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
7-530 |
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: 801.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDATCSL 86
Cdd:cd07782 2 YIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATCSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 87 VVLDKNGDPLPVSPEGDAKQNIIVWMDHRATEQAERINATHHPVLNYVGGKISPEMETPKILWLKENMPEIYERAGQFFD 166
Cdd:cd07782 82 VVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPETWAKAGHFFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 167 LADFLTWRATGDLARSVCTVTCKWTWLAH---ENRWDPDYFRTIGLAELADEDFIRIGHHIVSPGTPCGNGLTAQAAAEM 243
Cdd:cd07782 162 LPDFLTWKATGSLTRSLCSLVCKWTYLAHegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 244 GLLPGTPVAVGLIDAHAGGIGTVGVEGGAL--------NNLAYVFGTSSCTMASTTSPSFVPGVWGPYYSAMVPGLWLVE 315
Cdd:cd07782 242 GLPEGTPVGVSLIDAHAGGLGTLGADVGGLpceadpltRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 316 GGQSAAGAAIDQLLDFHPAVEEAREMAQRVNQPLPVWLAdRILEKTAQPS--DAVALAKGLHVVPEFLGNRAPFADPHAR 393
Cdd:cd07782 322 GGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLN-ERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 394 AVICGLGMERDLDNLLALYIAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPV 473
Cdd:cd07782 401 GMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1685051901 474 LLGSAILGAVAGNIAPSVGEAMQQFTHVDKYYYPQERYQSLHHRRYEAYKQLQHTAK 530
Cdd:cd07782 481 LLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQR 537
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
4-529 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 663.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 4 TKTVIGVDVGSGSVRAGIFDL-NGSLLSHATEKITTTRR------SGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVA 76
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAaDGEELASAVHPYPRWVIglylppPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 77 GIGFDAT-CSLVVLDKNGDPLPVSPE--GDAKQNIIVWMDHRATEQAERIN----ATHHPVLNYVGGKISPEMETPKILW 149
Cdd:COG1069 81 GIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINelakARGEDYLRYVGGIISSEWFWPKILH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 150 LKENMPEIYERAGQFFDLADFLTWRATGDLARSVCTVTCKWTWLAHENRW-DPDYFRTIG--LAELADedfiRIGHHIVS 226
Cdd:COG1069 161 LLREDPEVYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAHEGGYpSEEFFAALDplLDGLAD----RLGTEIYP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 227 PGTPCGNgLTAQAAAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGalnNLAYVFGTSSCTMASTTSPSFVPGVWGPYYSA 306
Cdd:COG1069 237 LGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPG---TLVKVMGTSTCHMLVSPEERFVPGICGQVDGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 307 MVPGLWLVEGGQSAAGAAIDQLLDFHPAVEEAREMAQRVNQPLPVWLADRILektAQPsdavALAKGLHVVPEFLGNRAP 386
Cdd:COG1069 313 IVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLTEEAA---KLP----PGESGLHALDWFNGNRSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 387 FADPHARAVICGLGMERDLDnllALYIAGLCGIGYGLRQILDAQTAQGVVSKNIVISGG-AGQHPLVRQILADTCGIPVI 465
Cdd:COG1069 386 LADQRLKGVILGLTLGTDAE---DIYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIK 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1685051901 466 TTQCCEPVLLGSAILGAVAGNIAPSVGEAMQQFTHV-DKYYYPQERYQSLHHRRYEAYKQLQHTA 529
Cdd:COG1069 463 VAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYF 527
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
7-525 |
8.99e-146 |
|
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: 428.49 E-value: 8.99e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDL-NGSLLSHATEKITTTR---RSGsRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDA 82
Cdd:cd07781 2 VIGIDFGTQSVRAGLVDLaDGEELASAVVPYPTGYippRPG-WAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 83 TCS-LVVLDKNGDPL-PVspegdakqniIVWMDHRATEQAERINATHHPVLNY----VGGKISPEMETPKILWLKENMPE 156
Cdd:cd07781 81 TSStVVPVDEDGNPLaPA----------ILWMDHRAQEEAAEINETAHPALEYylayYGGVYSSEWMWPKALWLKRNAPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 157 IYERAGQFFDLADFLTWRATGDLARSVCTVTCKWTWLAHENRWDPDYFRTIGLAELADEDfiRIGHHIVSPGTPCGnGLT 236
Cdd:cd07781 151 VYDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGLLKLRE--KLPGEVVPVGEPAG-TLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 237 AQAAAEMGLLPGTPVAVGLIDAHAGGIGtVGVEGgaLNNLAYVFGTSSCTMASTTSPSFVPGVWGPYYSAMVPGLWLVEG 316
Cdd:cd07781 228 AEAAERLGLPAGIPVAQGGIDAHMGAIG-AGVVE--PGTLALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 317 GQSAAGAAIDQLLD--FHPAVEEAREMAQRVNQplpvwLADRIlektaQPSdavalAKGLHVVPEFLGNRAPFADPHARA 394
Cdd:cd07781 305 GQSAVGDIFAWFVRlfVPPAEERGDSIYALLSE-----EAAKL-----PPG-----ESGLVALDWFNGNRTPLVDPRLRG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 395 VICGLgmerdldNLL----ALYIAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQH-PLVRQILADTCGIPVITTQC 469
Cdd:cd07781 370 AIVGL-------TLGttpaHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAEKnPLWMQIYADVLGRPIKVPKS 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1685051901 470 CEPVLLGSAILGAVAGNIAPSVGEAMQQFTHVDKYYYPQERYQSLHHRRYEAYKQL 525
Cdd:cd07781 443 DQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
8-527 |
7.00e-138 |
|
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: 408.94 E-value: 7.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 8 IGVDVGSGSVRAGIFDL-NGSLLSHATEKITTTRRSGS-RVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDATCS 85
Cdd:cd07768 3 IGVDVGTSSARAGVYDLyAGLEMAQEPVPYYQDSSKKSwKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDATCS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLPVSPEGDAKQNIIVWMDHRATEQAERINATHHPVL-NYVGGKISPEMETPKILWLKENMPEIYERAGQF 164
Cdd:cd07768 83 LAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLlDYLGGKISPEMGVPKLKYFLDEYSHLRDKHFHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 165 FDLADFLTWRATGDLARSVCTVTCKWTWLAHENRWDPDYFRTIGLAELaDEDFIRIGHHIVSPGTPCGNGLTaQAAAEMG 244
Cdd:cd07768 163 FDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVALP-EMAEKMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 245 LLPGTPVAVGLIDAHAG--GIGTVGVEGgalnNLAYVFGTSSCTMASTTSPSFVPGVWGPYYSAMVPGLWLVEGGQSAAG 322
Cdd:cd07768 241 LHPGTAVVVSCIDAHASwfAVASPHLET----SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 323 AAIDQLLDFHP---AVEEAREMAQRVNQPLPvwladrilEKTAQPSDAVALAKGLHVVPEFLGNRAPFADPHARAVICGL 399
Cdd:cd07768 317 KLIEHLFESHPcarKFDEALKKGADIYQVLE--------QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 400 GMERDLDNLLALYIAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAI 479
Cdd:cd07768 389 SLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAV 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1685051901 480 LGAVAGNI---APSVGEAMQQFTHVDKYYYPQ-ERYQSLHHRRYEAYKQLQH 527
Cdd:cd07768 469 LAKVAAGKkqlADSITEADISNDRKSETFEPLaYRLGADYILLYKLLCVKYH 520
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-525 |
2.34e-107 |
|
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: 329.49 E-value: 2.34e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 5 KTVIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDAT- 83
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 84 CSLVVLDKNGDPLpvspeGDAkqniIVWMDHRATEQAERINATH--HPVLNYVGGKISPEMETPKILWLKENMPEIYERA 161
Cdd:COG1070 81 HGLVLLDADGEPL-----RPA----ILWNDTRAAAEAAELREELgeEALYEITGNPLHPGFTAPKLLWLKENEPEIFARI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 162 GQFFDLADFLTWRATGDLarsVCTVTCK-WTWL--AHENRWDPDYFRTIGLAE--LADedfirighhIVSPGTPCGnGLT 236
Cdd:COG1070 152 AKVLLPKDYLRYRLTGEF---VTDYSDAsGTGLldVRTRDWSDELLEALGIDRelLPE---------LVPPGEVAG-TLT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 237 AQAAAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGALNNlayVFGTSSCTMASTTSPSFVPGVWGPYYSAMVPGLWLVEG 316
Cdd:COG1070 219 AEAAAETGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAV---SLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 317 GQSAAGAAIDQLldfhpaveeAREMAQRVNQPLpvwlaDRILEKTAQpsdAVALAKGLHVVPEFLGNRAPFADPHARAVI 396
Cdd:COG1070 296 ATNNGGSALRWF---------RDLFADGELDDY-----EELNALAAE---VPPGADGLLFLPYLSGERTPHWDPNARGAF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 397 CGLGMERDLDNLLAlyiAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLG 476
Cdd:COG1070 359 FGLTLSHTRAHLAR---AVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALG 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1685051901 477 SAILGAVAGNIAPSVGEAMQQFTHVDKYYYPQERYQSLHHRRYEAYKQL 525
Cdd:COG1070 436 AALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYREL 484
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
7-523 |
9.53e-96 |
|
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: 299.44 E-value: 9.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDAT-CS 85
Cdd:cd07805 2 ILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQmQG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLPvspegdakqNIIVWMDHRATEQAERINATHHPVLNY---VGGKISPEMETPKILWLKENMPEIYERAG 162
Cdd:cd07805 82 VVPVDKDGNPLR---------NAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEIYAKTH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 163 QFFDLADFLTWRATGDLARSVCTVTCkwTWL--AHENRWDPDYFRTIGL-AELADEdfirighhIVSPGTPCGnGLTAQA 239
Cdd:cd07805 153 KFLDAKDYLNFRLTGRAATDPSTAST--TGLmdLRKRRWSEELLRAAGIdPDKLPE--------LVPSTEVVG-ELTPEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 240 AAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGAlnnlAYV-FGTSSCTMASTTSPSFVPGvwGPYYS--AMVPGLWLVEG 316
Cdd:cd07805 222 AAELGLPAGTPVVGGGGDAAAAALGAGAVEEGD----AHIyLGTSGWVAAHVPKPKTDPD--HGIFTlaSADPGRYLLAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 317 GQSAAGAAIDQLLD--FHPAVEEAREMAqrvnqplpvwladrILEKTAqpSDAVALAKGLHVVPEFLGNRAPFADPHARA 394
Cdd:cd07805 296 EQETAGGALEWARDnlGGDEDLGADDYE--------------LLDELA--AEAPPGSNGLLFLPWLNGERSPVEDPNARG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 395 VICGLGMERDLDNLLAlyiAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQccEPVL 474
Cdd:cd07805 360 AFIGLSLEHTRADLAR---AVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPE--NPQE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1685051901 475 ---LGSAILGAVAGNIAPSVGEAMqQFTHVDKYYYPQERYQSLHHRRYEAYK 523
Cdd:cd07805 435 agaLGAALLAAVGLGLLKSFDEAK-ALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
7-526 |
6.45e-81 |
|
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: 260.93 E-value: 6.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDA-TCS 85
Cdd:cd07808 2 LLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGqMHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLpvspegdakQNIIVWMDHRATEQAERINATH-HPVLNYVGGKISPEMETPKILWLKENMPEIYERAGQF 164
Cdd:cd07808 82 LVLLDKNGRPL---------RPAILWNDQRSAAECEELEARLgDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 165 FdLA-DFLTWRATGDLArsvcT-VTCKWTWL---AHENRWDPDYFRTIGLaelaDEDF---IRIGHHIVspGTpcgngLT 236
Cdd:cd07808 153 L-LPkDYLRYRLTGELA----TdPSDASGTLlfdVEKREWSEELLEALGL----DPSIlppIVESTEIV--GT-----LT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 237 AQAAAEMGLLPGTPVAVGLIDAHAGGIGTVGV-EGGALNNLayvfGTSSCTMASTTSPSFVP--GVWgpYYSAMVPGLWL 313
Cdd:cd07808 217 PEAAEELGLPEGTPVVAGAGDNAAAALGAGVVePGDALISL----GTSGVVFAPTDKPVPDPkgRLH--TFPHAVPGKWY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 314 VEGGQSAAGAAIDqlldfhpaveearemaqrvnqplpvWLADRILEKTAQPSDAVALAKGLHVVPE---FL----GNRAP 386
Cdd:cd07808 291 AMGVTLSAGLSLR-------------------------WLRDLFGPDRESFDELDAEAAKVPPGSEgllFLpylsGERTP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 387 FADPHARAVICGLGMERDLDNLLAlyiAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVIT 466
Cdd:cd07808 346 YWDPNARGSFFGLSLSHTRAHLAR---AVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 467 TQCCEPVLLGSAILGAVAGNIAPSVGEAMQQFTHVDKYYYPQERYQSLHHRRYEAYKQLQ 526
Cdd:cd07808 423 PAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYRELY 482
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
7-525 |
1.88e-79 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 259.01 E-value: 1.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDL-NGSLLSHATE------KITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIG 79
Cdd:PRK04123 5 VIGLDFGTDSVRALLVDCaTGEELATAVVeyphwvKGRYLDLPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAVVGIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 80 FDAT-CSLVVLDKNGDPLPVSPEGDAKQN--IIVWMDHRATEQAERINATHHP-----VLNYVGGKISPEMETPKILWLK 151
Cdd:PRK04123 85 VDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKILHVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 152 ENMPEIYERAGQFFDLADFLTWRATG-----DLARSVCTVTCKWTWlaHEnRWD----PDYFRTI--GLAELADEdfiRI 220
Cdd:PRK04123 165 REDPAVYEAAASWVEACDWVVALLTGttdpqDIVRSRCAAGHKALW--HE-SWGglpsADFFDALdpLLARGLRD---KL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 221 GHHIVSPGTPCGnGLTAQAAAEMGLLPGTPVAVGLIDAHAGGIGtVGVEGGALNNlayVFGTSSCTMASTTSPSFVPGVW 300
Cdd:PRK04123 239 FTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHMGAVG-AGAEPGTLVK---VMGTSTCDILLADKQRAVPGIC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 301 GPYYSAMVPGLWLVEGGQSAAG---AAIDQLLDFHPAVEEAREMAQRVNQPLpvwladrilekTAQPSDAVALAKGLHVV 377
Cdd:PRK04123 314 GQVDGSIVPGLIGYEAGQSAVGdifAWFARLLVPPEYKDEAEARGKQLLELL-----------TEAAAKQPPGEHGLVAL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 378 PEFLGNRAPFADPHARAVICGLGMERDLDNLLALYIAGLCgigYGLRQILDAQTAQGVVSKNIVISGGAGQH-PLVRQIL 456
Cdd:PRK04123 383 DWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATA---FGTRAIMECFEDQGVPVEEVIAAGGIARKnPVLMQIY 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1685051901 457 ADTCGIPVI---TTQCCEpvlLGSAILGAVAGNIAPSVGEAMQQFTH-VDKYYYPQERYQSLHHRRYEAYKQL 525
Cdd:PRK04123 460 ADVLNRPIQvvaSDQCPA---LGAAIFAAVAAGAYPDIPEAQQAMASpVEKTYQPDPENVARYEQLYQEYKQL 529
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
7-525 |
2.40e-75 |
|
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: 245.93 E-value: 2.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNAltLADVCAQSVAGIGFDATC-S 85
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEV--LAKLGGGEVDAIGFSSAMhS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLpvspegdakQNIIVWMDHRATEQAERINATH-------------HPvlnyvggkISPemeTPKILWLKE 152
Cdd:cd07770 80 LLGVDEDGEPL---------TPVITWADTRAAEEAERLRKEGdgselyrrtgcpiHP--------MYP---LAKLLWLKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 153 NMPEIYERAGQFFDLADFLTWRATGDLARSVCTVTckWTWL--AHENRWDPDyfrTIGLAELADEDFIRighhIVSPGTP 230
Cdd:cd07770 140 ERPELFAKAAKFVSIKEYLLYRLTGELVTDYSTAS--GTGLlnIHTLDWDEE---ALELLGIDEEQLPE----LVDPTEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 231 CGnGLTAQAAAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGG--ALNnlayvFGTSSctMASTTSPSFV----PGVWgPYY 304
Cdd:cd07770 211 LP-GLKPEFAERLGLLAGTPVVLGASDGALANLGSGALDPGraALT-----VGTSG--AIRVVSDRPVldppGRLW-CYR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 305 SAmvPGLWLVEGGQSAAGAAIDqlldfhpaveearemaqrvnqplpvWLADRILEKTAQPSDAVALAK-------GLHVV 377
Cdd:cd07770 282 LD--ENRWLVGGAINNGGNVLD-------------------------WLRDTLLLSGDDYEELDKLAEavppgshGLIFL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 378 PEFLGNRAPFADPHARAVICGLGMERDLDNLLAlyiAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILA 457
Cdd:cd07770 335 PYLAGERAPGWNPDARGAFFGLTLNHTRADILR---AVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILA 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685051901 458 DTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVGEAmqQFTHVDKYYYPQERYQSLHHRRYEAYKQL 525
Cdd:cd07770 412 DVLGRPVLVPEEEEASALGAALLALEALGLISSLEAD--ELVKIGKVVEPDPENHAIYAELYERFKKL 477
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
8-481 |
3.35e-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: 247.70 E-value: 3.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 8 IGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRS--GSRVEQSSQEIWQAVCSCIRNALTLADVcaQSVAGIGFDATCS 85
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLATSERPISYKQDPkdLWFVTQSSTEIWKAIKTALKELIEELSD--YIVSGIGVSATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGD-----PLPVSPEGDAK-QNIIVWMDHRATEQAERIN-ATHHPVLNYVGGKISPEMETPKILWLKENMPEIY 158
Cdd:cd07778 81 MVVMQRDSDtsylvPYNVIHEKSNPdQDIIFWMDHRASEETQWLNnILPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 159 ERAGQFFDLADFLTWRATGDLarsvctvtCKW--TWLAHENR-----------WDPDYFRTIGLAELADEDFIRIGHHIV 225
Cdd:cd07778 161 FKKLEVFDLHDWISYMLATNL--------GHSniVPVNAPPSigigidgslkgWSKDFYSKLKISTKVCNVGNTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 226 SPGTPCGNGLTAQAAAEMGLLPGTPVAV-GLIDAHAGGIGTVGVEGGALNNLAYVFGTSSCTMASTTSP--SFVPGVWGP 302
Cdd:cd07778 233 LPYAGIPIGKVNVILASYLGIDKSTVVGhGCIDCYAGWFSTFAAAKTLDTTLFMVAGTSTCFLYATSSSqvGPIPGIWGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 303 yYSAMVPGLWLVEGGQSAAGAAIDQLLDFHPAVEEAREMAQRVNQPLPVWLADrILEKTAQPSDAVALAKGLHvvPEFLG 382
Cdd:cd07778 313 -FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDANFFETVEEKIDK-YERLLGQSIHYLTRHMFFY--GDYLG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 383 NRAPFADPHARAVICGLGMERDLDNLLALYIAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGI 462
Cdd:cd07778 389 NRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSK 468
|
490 500
....*....|....*....|..
gi 1685051901 463 PVITTQCCEP---VLLGSAILG 481
Cdd:cd07778 469 IHIIVPLSDSkyaVVKGAALLG 490
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
7-484 |
3.45e-75 |
|
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: 244.05 E-value: 3.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNAltLADVCAQSVAGIGFDATC-S 85
Cdd:cd07783 2 FLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLREL--PAELRPRRVVAIAVDGTSgT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLpvspegdakQNIIVWMDHRATEQAERINATHHPVLNYVGGKISPEMETPKILWLKENMPEIYERAGQFF 165
Cdd:cd07783 80 LVLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 166 DLADFLTWRATGDLARSVCTVTCKWTWLAHENRWDPDyfrtiglaeLADEDFIRIGH--HIVSPGTPCGNgLTAQAAAEM 243
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGRWPSW---------LLALLGIPPDLlpRVVAPGTVIGT-LTAEAAEEL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 244 GLLPGTPVAVGLIDAHAGGIGTVGVEGGALNNlayVFGTSSCTMASTTSPSFVPGvwGPYYSAMVP-GLWLVEGGQSAAG 322
Cdd:cd07783 221 GLPAGTPVVAGTTDSIAAFLASGAVRPGDAVT---SLGTTLVLKLLSDKRVPDPG--GGVYSHRHGdGYWLVGGASNTGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 323 AAIDQLLDfhpaVEEAREMAQRVNQPLPvwladrilektaqpsdavalaKGLHVVP-EFLGNRAPFADPHARAVICGLGM 401
Cdd:cd07783 296 AVLRWFFS----DDELAELSAQADPPGP---------------------SGLIYYPlPLRGERFPFWDPDARGFLLPRPH 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 402 ERDldnllALYIAGLCGIGYGLRQILDA-QTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPvLLGSAIL 480
Cdd:cd07783 351 DRA-----EFLRALLEGIAFIERLGYERlEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA-ALGAALL 424
|
....
gi 1685051901 481 GAVA 484
Cdd:cd07783 425 AAAG 428
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
7-484 |
3.14e-74 |
|
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: 242.43 E-value: 3.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLL-SHATEKITTTRRSGsRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDA-TC 84
Cdd:cd07804 2 LLGIDIGTTGTKGVLVDEDGKVLaSASIEHDLLTPKPG-WAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGlVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 85 SLVVLDKNGDPLpvspegdakQNIIVWMDHRATEQAERINAT--HHPVLNYVGGKISPEMETPKILWLKENMPEIYERAG 162
Cdd:cd07804 81 ALVPVDENGKPL---------RPAILYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 163 QFFDLADFLTWRATGdlarsvcTVTCKWTWLAHEN--------RWDPDYFRTIGLAELADEDfirighhIVSPGTPCGnG 234
Cdd:cd07804 152 KFLGAYDYIVYKLTG-------EYVIDYSSAGNEGglfdirkrTWDEELLEALGIDPDLLPE-------LVPSTEIVG-E 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 235 LTAQAAAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGalNNLAYvFGTSSCTMASTTSPSFVPGVWGPYYSamVPGLWLV 314
Cdd:cd07804 217 VTKEAAEETGLAEGTPVVAGTVDAAASALSAGVVEPG--DLLLM-LGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 315 EGGQSAAGAAI----DQLLDFHPAVEEAREMAqrvnqplpvwlADRILEKTAqpSDAVALAKGLHVVPEFLGNRAPFADP 390
Cdd:cd07804 292 NGGMATSGSLLrwfrDEFAGEEVEAEKSGGDS-----------AYDLLDEEA--EKIPPGSDGLIVLPYFMGERTPIWDP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 391 HARAVICGLgmerDLDNLLA-LYIAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQC 469
Cdd:cd07804 359 DARGVIFGL----TLSHTRAhLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKD 434
|
490
....*....|....*
gi 1685051901 470 CEPVLLGSAILGAVA 484
Cdd:cd07804 435 TVGASLGDAFLAGVG 449
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
6-484 |
7.77e-72 |
|
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: 235.94 E-value: 7.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 6 TVIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLA---DVCAQSVAGIGfda 82
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAgpdPIAAISVSSQG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 83 tCSLVVLDKNGDPLPvspegdakqNIIVWMDHRATEQAERINATHHP--VLNYVGGKISPEMETPKILWLKENMPEIYER 160
Cdd:cd07773 78 -ESGVPVDRDGEPLG---------PAIVWFDPRGKEEAEELAERIGAeeLYRITGLPPSPMYSLAKLLWLREHEPEIFAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 161 AGQFFDLADFLTWRATGDLARSvCTVTCKWTWL-AHENRWDPDYFRTIGLAE--LADedfirighhIVSPGTPCGNgLTA 237
Cdd:cd07773 148 AAKWLSVADYIAYRLTGEPVTD-YSLASRTMLFdIRKRTWSEELLEAAGIDAslLPE---------LVPSGTVIGT-VTP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 238 QAAAEMGLLPGTPVAVGLIDAHAGGIGT-VGVEGGALNNLayvfGTSSCTMASTTSPSFVPGVWGPYYS---AMVPGLWL 313
Cdd:cd07773 217 EAAEELGLPAGTPVVVGGHDHLCAALGAgVIEPGDVLDST----GTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 314 VEGGQSAaGAAIDQLLDFHPAVEEAREMAQRVNQPLPvwladrilektaqpsdavALAKGLHVVPEFLGNRAPFADPHAR 393
Cdd:cd07773 293 LAGSLPG-GALLEWFRDLFGGDESDLAAADELAEAAP------------------PGPTGLLFLPHLSGSGTPDFDPDAR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 394 AVICGLGMERDLDNLLAlyiAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPV 473
Cdd:cd07773 354 GAFLGLTLGTTRADLLR---AILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
490
....*....|.
gi 1685051901 474 LLGSAILGAVA 484
Cdd:cd07773 431 ALGAALLAGVG 441
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
7-519 |
2.47e-70 |
|
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: 231.64 E-value: 2.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDAT-CS 85
Cdd:cd07779 2 ILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQrST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLpvspegdakQNIIVWMDHRateqaerinaTHHpvlnyvggkispemetpkilwlkenmpeiyeragqFF 165
Cdd:cd07779 82 FVPVDEDGRPL---------RPAISWQDKR----------TAK-----------------------------------FL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 166 DLADFLTWRATGDLARSVCTVTCKWTWLAHENRWDPDYFRTIGLAE--LADedfirighhIVSPGTPCGNgLTAQAAAEM 243
Cdd:cd07779 108 TVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRdkLPE---------LVPPGTVIGT-LTKEAAEET 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 244 GLLPGTPVAVGLIDAHAGGIGTvGV--EGGALNNLayvfGTSSCTMASTTSPSFVPGVWGPYYSAMVPGLWLVEGGQSAA 321
Cdd:cd07779 178 GLPEGTPVVAGGGDQQCAALGA-GVlePGTASLSL----GTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 322 GAAI----DQLLDFHPAVEEAREMAqrvnqplpvwlaDRILEKTAqpSDAVALAKGLHVVPEFLGNRAPFADPHARAVIC 397
Cdd:cd07779 253 GSAVrwfrDEFGQDEVAEKELGVSP------------YELLNEEA--AKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFI 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 398 GLGmerdldnlLA-----LYIAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEP 472
Cdd:cd07779 319 GLT--------LShtrahLARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEA 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1685051901 473 VLLGSAILGAVAGNIAPSVGEAMQQFTHVDKYYYPQERyqslHHRRY 519
Cdd:cd07779 391 TALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPE----NVAIY 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
7-481 |
7.25e-68 |
|
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: 223.98 E-value: 7.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDAT-CS 85
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQmPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLPvspegdakqNIIVWMDHRAteqaerinathhpvlnyvggkispemetpkilwlkenmpeiyeragQFF 165
Cdd:cd00366 82 VVLVDADGNPLR---------PAIIWLDRRA----------------------------------------------KFL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 166 DLADFLTWRATGDLARSVCTVTCKWTWLAHENRWDPDYFRTIGLAE--LADedfirighhIVSPGTPCGnGLTAQAAAEM 243
Cdd:cd00366 107 QPNDYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPRekLPP---------IVESGEVVG-RVTPEAAEET 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 244 GLLPGTPVAVGLIDAHAGGIGTVGVEGGALnnlAYVFGTSSCTMASTTSPSFVPGVWGPYYSAmVPGLWLVEGGQSAAGA 323
Cdd:cd00366 177 GLPAGTPVVAGGGDTAAAALGAGVVEPGDA---VDSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLWLLEGAINTGGA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 324 AIDQLLD-FHPAVEEAREMAQrvnqplpvwlADRILEKTAQPSDavalakGLHVVPEFLGNRAPFADPHARAVICGLGME 402
Cdd:cd00366 253 SLRWFRDeFGEEEDSDAEYEG----------LDELAAEVPPGSD------GLIFLPYLSGERSPIWDPAARGVFFGLTLS 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1685051901 403 RDLDNLLAlyiAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILG 481
Cdd:cd00366 317 HTRAHLIR---AVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
7-484 |
5.51e-66 |
|
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: 220.50 E-value: 5.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDAT-CS 85
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHgNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLpvspegdakQNIIVWMDHRATEQAERINA--THHPVLNYVGGKISPEMETPKILWLKENMPEIYERAGQ 163
Cdd:cd07802 82 LYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 164 FFDLADFLTWRATGDLArsvctvtCKWT------WLAHENRWDPDYFRTIGLAELAD---EdfirighhIVSPGTPCGnG 234
Cdd:cd07802 153 VLFCKDWIRYRLTGEIS-------TDYTdagsslLDLDTGEYDDELLDLLGIEELKDklpP--------LVPSTEIAG-R 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 235 LTAQAAAEMGLLPGTPVAVGLIDAHAGGIGTvgvegGALN--NLAYVFGTSSCTMASTTSPSFVPGVWGpYYSAMVPGLW 312
Cdd:cd07802 217 VTAEAAALTGLPEGTPVAAGAFDVVASALGA-----GAVDegQLCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 313 LVEGGQSAAGAAIDQLLD-FHPAVEEAREMAQRVnqplpvwlADRILEKT-AQPSDAValakglhvvpeFLgnraPF--- 387
Cdd:cd07802 291 LIVEASPTSASNLDWFLDtLLGEEKEAGGSDYDE--------LDELIAAVpPGSSGVI-----------FL----PYlyg 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 388 --ADPHARAVICGLGMERDLDNLL-ALYIaglcGIGYGLRQILDAQTAQGVVSKnIVISGGAGQHPLVRQILADTCGIPV 464
Cdd:cd07802 348 sgANPNARGGFFGLTAWHTRAHLLrAVYE----GIAFSHRDHLERLLVARKPET-IRLTGGGARSPVWAQIFADVLGLPV 422
|
490 500
....*....|....*....|
gi 1685051901 465 ITTQCCEPVLLGSAILGAVA 484
Cdd:cd07802 423 EVPDGEELGALGAAICAAVA 442
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
276-484 |
1.31e-58 |
|
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: 192.92 E-value: 1.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 276 LAYVFGTSSCTMASTTSP-SFVPGVWGPYYSAMVPGLWLVEGGQSAAGAAIDQLLDFHPAVEEAREMAqrvnqplpvwLA 354
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAG----------NV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 355 DRILEKTAqpSDAVALAKGLHVVPEFLGNRAPFADPHARAVICGLGMERDLdnlLALYIAGLCGIGYGLRQILDAQTAQ- 433
Cdd:pfam02782 71 ESLAELAA--LAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKQe 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1685051901 434 GVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVA 484
Cdd:pfam02782 146 GHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
7-484 |
3.18e-52 |
|
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: 183.98 E-value: 3.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDAT--- 83
Cdd:cd24121 2 LIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQgdg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 84 CSLVvlDKNGDPLpvspeGDAkqniIVWMDHRATEQAERINA--THHPVLNYVGGKISPEMETPKILWLKENMPEIYERA 161
Cdd:cd24121 82 TWLV--DEDGRPV-----RDA----ILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 162 GQFFDLADFLTWRATGDLARSVCTVTckWTWLAHENR-WDPDYFRTIGLAELAD---EdfIRIGHHIVSPgtpcgngLTA 237
Cdd:cd24121 151 RTALHCKDWLFYKLTGEIATDPSDAS--LTFLDFRTRqYDDEVLDLLGLEELRHllpP--IRPGTEVIGP-------LTP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 238 QAAAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGAlnnlAY-VFGTSSCTMASTTSPSFvpgvwGPYYSAM-----VPGL 311
Cdd:cd24121 220 EAAAATGLPAGTPVVLGPFDVVATALGSGAIEPGD----ACsILGTTGVHEVVVDEPDL-----EPEGVGYticlgVPGR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 312 WLVEGGQSAAGAAIDQLLD--FHPAVEEAREMAQRVNQPLPVWLADrilektAQPSdavalAKGLHVVPeFL---GNRAP 386
Cdd:cd24121 291 WLRAMANMAGTPNLDWFLRelGEVLKEGAEPAGSDLFQDLEELAAS------SPPG-----AEGVLYHP-YLspaGERAP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 387 FADPHARAVICGLGMERDLDNLL-ALYIaglcGIGYGLRqilDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVI 465
Cdd:cd24121 359 FVNPNARAQFTGLSLEHTRADLLrAVYE----GVALAMR---DCYEHMGEDPGELRLSGGGARSDTWCQILADALGVPVR 431
|
490
....*....|....*....
gi 1685051901 466 TTQCCEPVLLGSAILGAVA 484
Cdd:cd24121 432 VPAGEEFGARGAAMNAAVA 450
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-484 |
9.49e-45 |
|
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: 163.49 E-value: 9.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 6 TVIGVDVGSGSVRAGIFDL-NGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDATC 84
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAeTGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 85 -SLVVLDKNGDPLPvspegdakqNIIVWMDHRATEQAERI-NATHHPVLNYVGGKISPEMETPKILWLKENMPEIYERAG 162
Cdd:cd07809 81 hGLVALDADGKVLR---------PAKLWCDTRTAPEAEELtEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 163 QFFDLADFLTWRATGDLARSVCTVTCKWTWLAHENRWDPDYFRTIGlAELADEDFI-RIghhiVSPGTPCGnGLTAQAAA 241
Cdd:cd07809 152 KILLPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAID-PSRDLRDLLpEV----LPAGEVAG-RLTPEGAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 242 EMGLLPGTPVAVGLIDAHAGGIGTvgvegGALNN--LAYVFGTSSCTMASTTSPSFVP--GVWGPyysAMVPGLWL-VEG 316
Cdd:cd07809 226 ELGLPAGIPVAPGEGDNMTGALGT-----GVVNPgtVAVSLGTSGTAYGVSDKPVSDPhgRVATF---CDSTGGMLpLIN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 317 GQSAAGAAIDQLL-DFHPAVEEAREMAQRvnqplpvwladrilektaqpsdAVALAKGLHVVPEFLGNRAPfADPHARAV 395
Cdd:cd07809 298 TTNCLTAWTELFReLLGVSYEELDELAAQ----------------------APPGAGGLLLLPFLNGERTP-NLPHGRAS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 396 ICGLGMER-DLDNLL--ALYiAGLCGIGYGLRQILDaqtaQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEP 472
Cdd:cd07809 355 LVGLTLSNfTRANLAraALE-GATFGLRYGLDILRE----LGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEG 429
|
490
....*....|..
gi 1685051901 473 VLLGSAILGAVA 484
Cdd:cd07809 430 GALGAALQAAWG 441
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
7-484 |
1.39e-43 |
|
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: 160.47 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGS--RVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIgfdATC 84
Cdd:cd07798 2 YLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYpdAKEFDPEELWEKICEAIREALKKAGISPEDISAV---SST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 85 S----LVVLDKNGDPLPVSPegdakqNIivwmDHRATEQAERINATHHPVLNYVGGKISPEMETP-KILWLKENMPEIYE 159
Cdd:cd07798 79 SqregIVFLDKDGRELYAGP------NI----DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEIFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 160 RAGQFFDLADFLTWRATGDLA--RSVCTVTCkwtwL--AHENRWDPDyfrtigLAELADedfirIGHHI----VSPGTPC 231
Cdd:cd07798 149 RIATVLSISDWIGYRLTGELVsePSQASETQ----LfdIKKREWSQE------LLEALG-----LPPEIlpeiVPSGTVL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 232 GNgLTAQAAAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGAlnnLAYVFGTSSCTMASTTSPSFVP--GVW-GPYysaMV 308
Cdd:cd07798 214 GT-VSEEAARELGLPEGTPVVVGGADTQCALLGSGAIEPGD---IGIVAGTTTPVQMVTDEPIIDPerRLWtGCH---LV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 309 PGLWLVEGGQSAAGAAIDQLLD-FHPAVEEAREmaqrvnqplpvwLADRILEKTAQPSDAVaLAkglhvvpeFLGNRapF 387
Cdd:cd07798 287 PGKWVLESNAGVTGLNYQWLKElLYGDPEDSYE------------VLEEEASEIPPGANGV-LA--------FLGPQ--I 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 388 ADPHARAVICGLGMERDLDNLLALYIAG-----LCGIGYGLR---QILDAQTaqGVVSKNIVISGGAGQHPLVRQILADT 459
Cdd:cd07798 344 FDARLSGLKNGGFLFPTPLSASELTRGDfaraiLENIAFAIRanlEQLEEVS--GREIPYIILCGGGSRSALLCQILADV 421
|
490 500
....*....|....*....|....*
gi 1685051901 460 CGIPVITTQCCEPVLLGSAILGAVA 484
Cdd:cd07798 422 LGKPVLVPEGREASALGAAICAAVG 446
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
7-517 |
4.15e-39 |
|
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: 149.02 E-value: 4.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKitTTRRSGSRVEQS----SQEIWQAVCSCIRNALTLADVCAQSVAGIgfdA 82
Cdd:cd07775 2 LLALDAGTGSGRAVIFDLEGNQIAVAQRE--WRHKEVPDVPGSmdfdTEKNWKLICECIREALKKAGIAPKSIAAI---S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 83 TCS----LVVLDKNGDPLPVSPEGDAkqniivwmdhRATEQAERINATHhPVLNYVGGKISPEMET----PKILWLKENM 154
Cdd:cd07775 77 TTSmregIVLYDNEGEEIWACANVDA----------RAAEEVSELKELY-NTLEEEVYRISGQTFAlgaiPRLLWLKNNR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 155 PEIYERAGQFFDLADFLTWRATGDLAR--SVCTVTCKWTwlAHENRWDPDYFRTIGLAELADEDfirighhIVSPGTPCG 232
Cdd:cd07775 146 PEIYRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD--LKTRDWDPEILEMAGLKADILPP-------VVESGTVIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 233 NgLTAQAAAEMGLLPGTPVAVGLIDAHAGGIGtVGVEGGalNNLAYVFGTSSCTMASTTSP------------SFVPGVW 300
Cdd:cd07775 217 K-VTKEAAEETGLKEGTPVVVGGGDVQLGCLG-LGVVRP--GQTAVLGGSFWQQEVNTAAPvtdpamnirvncHVIPDMW 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 301 GPYYSAMVPGL---WLV-----EGGQSAAGAAIDqlldfhpAVEEAREMAQRVnqP------LPVWladrilektaqpSD 366
Cdd:cd07775 293 QAEGISFFPGLvmrWFRdafcaEEKEIAERLGID-------AYDLLEEMAKDV--PpgsygiMPIF------------SD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 367 AVALAKGLHVVPEFLG--------NRAPFadphARAVicglgMERdldnllalyiAGLcgIGYGLRQILDAQTaqGVVSK 438
Cdd:cd07775 352 VMNYKNWRHAAPSFLNldidpekcNKATF----FRAI-----MEN----------AAI--VSAGNLERIAEFS--GIFPD 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 439 NIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVGEAMQQFTHVDKYYYP----QERYQSL 514
Cdd:cd07775 409 SLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPnpenHEVYQDL 488
|
...
gi 1685051901 515 HHR 517
Cdd:cd07775 489 YEK 491
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
7-264 |
7.84e-36 |
|
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: 134.00 E-value: 7.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFDATC-S 85
Cdd:pfam00370 2 YLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGhG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 86 LVVLDKNGDPLpvspegdakQNIIVWMDHRATEQAERINATHHPVLNYV--GGKISPEMETPKILWLKENMPEIYERAGQ 163
Cdd:pfam00370 82 TVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEEGNNQKLYEitGLPIWPGFTLSKLRWIKENEPEVFEKIHK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 164 FFDLADFLTWRATGDLarsVCTVTCKWT--WL-AHENRWDPDYFRTIGLAEladedfiRIGHHIVSPGTPCGNgLTAQAA 240
Cdd:pfam00370 153 FLTIHDYLRWRLTGVF---VTDHTNASRsmMFnIHKLDWDPELLAALGIPR-------DHLPPLVESSEIYGE-LNPELA 221
|
250 260
....*....|....*....|....
gi 1685051901 241 AEMGLLPGTPVAVGLIDAHAGGIG 264
Cdd:pfam00370 222 AMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
4-526 |
1.54e-35 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 139.37 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 4 TKTVIGVDVGSGSVRAGIFDLNGSLLSHATEKitTTRRSGSRVEQSS----QEIWQAVCSCIRNALTLADVCAQSVAGIg 79
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAVGQAE--WRHLAVPDVPGSMefdlEKNWQLACQCIRQALQKAGIPASDIAAV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 80 fdATCSL----VVLDKNGDPLpvspegdakqniivW----MDHRATEQAERINATHhPVLNYVGGKISPEM----ETPKI 147
Cdd:PRK10939 79 --SATSMregiVLYDRNGTEI--------------WacanVDARASREVSELKELH-NNFEEEVYRCSGQTlalgALPRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 148 LWLKENMPEIYERAGQFFDLADFLTWRATGDLA---RSVCTVTCkwtwLAHENR-WDPDYFRTIGLAelADedfirIGHH 223
Cdd:PRK10939 142 LWLAHHRPDIYRQAHTITMISDWIAYMLSGELAvdpSNAGTTGL----LDLVTRdWDPALLEMAGLR--AD-----ILPP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 224 IVSPGTPCGNgLTAQAAAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGAlnnlAYVFG-------------TSSCTMAST 290
Cdd:PRK10939 211 VKETGTVLGH-VTAKAAAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQ----TAVLGgtfwqqvvnlpapVTDPNMNIR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 291 TSPSFVPGVWGPYYSAMVPGL---WLV-----EGGQSAAGAAIDqlldfhpAVEEAREMAQRVnqplPVWLADRIlekta 362
Cdd:PRK10939 286 INPHVIPGMVQAESISFFTGLtmrWFRdafcaEEKLLAERLGID-------AYSLLEEMASRV----PVGSHGII----- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 363 qP--SDAVALAKGLHVVPEFLgNRApfADPHaravICGLG-MERDLDNLLAlyIAGLCgigyGLRQIldaQTAQGVVSKN 439
Cdd:PRK10939 350 -PifSDVMRFKSWYHAAPSFI-NLS--IDPE----KCNKAtLFRALEENAA--IVSAC----NLQQI---AAFSGVFPSS 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 440 IVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVGEAMQQFTHVDKYYYP----QERYQSLH 515
Cdd:PRK10939 413 LVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPnpenHELYQEAK 492
|
570
....*....|..
gi 1685051901 516 HRRYEAY-KQLQ 526
Cdd:PRK10939 493 EKWQAVYaDQLG 504
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
7-480 |
1.07e-30 |
|
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: 124.26 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGS---RVEQSSQEIWQAVCSCIRNaltLADVCAQSVAGIGFdaT 83
Cdd:cd07777 2 VLGIDIGTTSIKAALLDLESGRILESVSRPTPAPISSDdpgRSEQDPEKILEAVRNLIDE---LPREYLSDVTGIGI--T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 84 C---SLVVLDKNGDPlpVSpegdakqNIIVWMDHRATEQ-AERINATHHPVLNYVGGKISPEMETPKILWLKENMPeIYE 159
Cdd:cd07777 77 GqmhGIVLWDEDGNP--VS-------PLITWQDQRCSEEfLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGP-LPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 160 RAGQFFDLADFLTWRATGdLARSVCTVTCkwtwlAH--------ENRWDPDYFRTIGLaeladeDFIRIGHhIVSPGTPC 231
Cdd:cd07777 147 KADRAGTIGDYIVARLTG-LPKPVMHPTN-----AAswglfdleTGTWNKDLLEALGL------PVILLPE-IVPSGEIV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 232 GNgltaqaaAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGA--LNnlayvFGTSScTMASTTSPSFVPGVW------GPY 303
Cdd:cd07777 214 GT-------LSSALPKGIPVYVALGDNQASVLGSGLNEENDavLN-----IGTGA-QLSFLTPKFELSGSVeirpffDGR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 304 YSAMVPGLwlveggqsAAGAAIDQLLDFHpaveeaREMAQRVNQPLP---VWlaDRILEKTAQPSDAvalakGLHVVPEF 380
Cdd:cd07777 281 YLLVAASL--------PGGRALAVLVDFL------REWLRELGGSLSddeIW--EKLDELAESEESS-----DLSVDPTF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 381 LGNRApfaDPHARAVICGLGMerdlDNL-LALYIAGLC-GIGYGLRQILDAQTAQGVVSKNIVISGGAGQH-PLVRQILA 457
Cdd:cd07777 340 FGERH---DPEGRGSITNIGE----SNFtLGNLFRALCrGIAENLHEMLPRLDLDLSGIERIVGSGGALRKnPVLRRIIE 412
|
490 500
....*....|....*....|...
gi 1685051901 458 DTCGIPVITTQCCEPVLLGSAIL 480
Cdd:cd07777 413 KRFGLPVVLSEGSEEAAVGAALL 435
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
7-508 |
3.65e-29 |
|
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: 120.26 E-value: 3.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFdaTC-- 84
Cdd:cd07769 2 ILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGI--TNqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 85 -SLVVLDKN-GDPLpvspegdakQNIIVWMDHRATEQAERINATHHP--VLNYVGGKISPEMETPKILWLKENMPEIYER 160
Cdd:cd07769 80 eTTVVWDKKtGKPL---------YNAIVWQDRRTADICEELKAKGLEerIREKTGLPLDPYFSATKIKWILDNVPGARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 161 AGQ----FFDLADFLTWRATGDlARSVCTVTCkwtwlA--------HENRWDPDYFRTIG-----LAELAD--EDFiriG 221
Cdd:cd07769 151 AERgellFGTIDTWLIWKLTGG-KVHVTDVTN-----AsrtmlfniHTLEWDDELLELFGiprsmLPEVRPssEVF---G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 222 HhiVSPGtpcgngltaqaaaemGLLPGTPVAvGLI-DAHAGGIGTVGVEGGALNNlayVFGTsSCTMASTTSPSFVP--- 297
Cdd:cd07769 222 Y--TDPE---------------GLGAGIPIA-GILgDQQAALFGQGCFEPGMAKN---TYGT-GCFLLMNTGEKPVPskn 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 298 GV-----WG----PYYsamvpglwLVEGGQSAAGAAI----DQLLDFHPAvEEAREMAqrvnqplpvwladrileKTAQP 364
Cdd:cd07769 280 GLlttiaWQiggkVTY--------ALEGSIFIAGAAIqwlrDNLGLIEDA-AETEELA-----------------RSVED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 365 SDavalakGLHVVPEFLGNRAPFADPHARAVICGL--GMERDldnllalYI--AGLCGIGYGLRQILDA-QTAQGVVSKN 439
Cdd:cd07769 334 NG------GVYFVPAFSGLGAPYWDPDARGAIVGLtrGTTKA-------HIvrAALESIAYQTRDVLEAmEKDSGIKLKE 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1685051901 440 IVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVGEAMQQFThVDKYYYPQ 508
Cdd:cd07769 401 LRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQ-VDKRFEPS 468
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
7-508 |
6.07e-26 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 110.92 E-value: 6.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITT-TRRSGsRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFD---A 82
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRDGNIVAVAQREFTQiYPQPG-WVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITnqrE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 83 TCslVVLDKN-GDPLpvspegdakQNIIVWMDHRATEQAERINATHHP--VLNYVGGKISPEMETPKILWLKENMPEIYE 159
Cdd:COG0554 84 TT--VVWDRKtGKPL---------YNAIVWQDRRTADICEELKADGLEdlIREKTGLVLDPYFSATKIKWILDNVPGARE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 160 RA--GqffDLA----D-FLTWRATGDlARSVCTVTckwtwLA--------HENRWDPDYFRTIG-----LAELAD--EDF 217
Cdd:COG0554 153 RAeaG---ELLfgtiDsWLIWKLTGG-KVHVTDVT-----NAsrtmlfniHTLDWDDELLELFGiprsmLPEVRPssEVF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 218 irighhivspgtpcgnGLTAQAaaemGLLPGTPVAvGLI-DAHAGGIGTVGVEGGALNNlayVFGTSSCTMASTTSPSFV 296
Cdd:COG0554 224 ----------------GETDPD----LFGAEIPIA-GIAgDQQAALFGQACFEPGMAKN---TYGTGCFLLMNTGDEPVR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 297 PG-------VWG----PYYSamvpglwlVEGGQSAAGAAIDqlldfhpaveearemaqrvnqplpvWLAD--RILEKtaq 363
Cdd:COG0554 280 SKngllttiAWGlggkVTYA--------LEGSIFVAGAAVQ-------------------------WLRDglGLIDS--- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 364 PSDAVALAK------GLHVVPEFLGNRAPFADPHARAVICGL--GMERdldNLLALyiAGLCGIGYGLRQILDA-QTAQG 434
Cdd:COG0554 324 AAESEALARsvedngGVYFVPAFTGLGAPYWDPDARGAIFGLtrGTTR---AHIAR--AALESIAYQTRDVLDAmEADSG 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1685051901 435 VVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVgEAMQQFTHVDKYYYPQ 508
Cdd:COG0554 399 IPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSL-EELAALWKVDRRFEPQ 471
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-525 |
1.58e-24 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 106.59 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 8 IGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRnAL----TLADVCAQSVAGIGFDAT 83
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMK-ALgdqhSLQDVKALGIAGQMHGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 84 cslvVLDKNGDPLpvspegdakQNIIVWMDHRATEQAERINATHHPVLNYVGGKISPEMETPKILWLKENMPEIYERAGQ 163
Cdd:PRK15027 82 ----LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 164 FFDLADFLTWRATGDLARSVCTVTCKwTWLAHENR-WDPdyfrtiglAELADEDFIRIGHHIVSPGTPCGNGLTAQAAAE 242
Cdd:PRK15027 149 VLLPKDYLRLRMTGEFASDMSDAAGT-MWLDVAKRdWSD--------VMLQACHLSRDQMPALYEGSEITGALLPEVAKA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 243 MGlLPGTPVAVGLIDAHAGGIGTVGVEGG----ALNNLAYVFGTSSCTMASTTSP--SF---VPGVWGpYYSAMVPGLWL 313
Cdd:PRK15027 220 WG-MATVPVVAGGGDNAAGAVGVGMVDANqamlSLGTSGVYFAVSEGFLSKPESAvhSFchaLPQRWH-LMSVMLSAASC 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 314 VEGGQSAAG-AAIDQLLDfhpAVEEAREMAQrvnqplPVWLadrilektaqpsdavalakglhvVPEFLGNRAPFADPHA 392
Cdd:PRK15027 298 LDWAAKLTGlSNVPALIA---AAQQADESAE------PVWF-----------------------LPYLSGERTPHNNPQA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 393 RAVICGLGMERDLDNLLAlyiAGLCGIGYGLRQILDAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPV--ITTQCC 470
Cdd:PRK15027 346 KGVFFGLTHQHGPNELAR---AVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyRTGGDV 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1685051901 471 EPVlLGSAILGAVAGNIAPSVGEAMQQFThVDKYYYPQERYQSLHHRRYEAYKQL 525
Cdd:PRK15027 423 GPA-LGAARLAQIAANPEKSLIELLPQLP-LEQSHLPDAQRYAAYQPRRETFRRL 475
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
7-514 |
9.06e-23 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 101.26 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLL-SHATEKITTTRRSGSRVEQ-SSQEIWQAVCSCIR---NALTLADVCAQSVAGIGFD 81
Cdd:PRK10331 4 ILVLDCGATNVRAIAVDRQGKIVaRASTPNASDIAAENSDWHQwSLDAILQRFADCCRqinSELTECHIRGITVTTFGVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 82 ATcslvVLDKNGDPL-PvspegdakqnIIVWMDHRATeqaerinathhPVLNYVGGKISPE------------METP-KI 147
Cdd:PRK10331 84 GA----LVDKQGNLLyP----------IISWKCPRTA-----------AVMENIERYISAQqlqqisgvgafsFNTLyKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 148 LWLKENMPEIYERAGQFFDLADFLTWRATGDLARSVCTV-TCKWTWLAHENrWDPDYFRTIGLAEladEDFIRighhIVS 226
Cdd:PRK10331 139 VWLKENHPQLLEQAHAWLFISSLINHRLTGEFTTDITMAgTSQMLDIQQRD-FSPEILQATGLSR---RLFPR----LVE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 227 PGTPCGNgLTAQAAAEMGLLPGTPVavglIDA-HAGGIGTVGvEGGALNNLAYVFGTSSCTMASTTSpsfVPGVWGPYYS 305
Cdd:PRK10331 211 AGEQIGT-LQPSAAALLGLPVGIPV----ISAgHDTQFALFG-SGAGQNQPVLSSGTWEILMVRSAQ---VDTSLLSQYA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 306 AMVPGLwlveggQSAAGAaidqlldFHPAVEearemaqrvnqplpvWLADRILE-------KTAQP-----SDAVAL--- 370
Cdd:PRK10331 282 GSTCEL------DSQSGL-------YNPGMQ---------------WLASGVLEwvrklfwTAETPyqtmiEEARAIppg 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 371 AKGLHVVPEFLGNRapfadphaRAVICGLGMERdldNLLALYIAGLCGIGYGLRQILDA-QTAQGVVSKNIVISGGAGQH 449
Cdd:PRK10331 334 ADGVKMQCDLLACQ--------NAGWQGVTLNT---TRGHFYRAALEGLTAQLKRNLQVlEKIGHFKASELLLVGGGSRN 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685051901 450 PLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVGEAMQQFTHVDKYYYPQER---YQSL 514
Cdd:PRK10331 403 ALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYPQTEpefIEEV 470
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
7-508 |
5.06e-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: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFD---AT 83
Cdd:cd07786 2 ILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITnqrET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 84 CslVVLDKN-GDPLpvspegdakQNIIVWMDHRATEQAERINATHHpvLNYVGGK----ISPEMETPKILWLKENMPEIY 158
Cdd:cd07786 82 T--VVWDREtGKPV---------YNAIVWQDRRTADICEELKAEGH--EEMIREKtglvLDPYFSATKIRWILDNVPGAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 159 ERAGQ---FFDLAD-FLTWRATGDL---------ARsvctvtckwTWL--AHENRWDPDYFRTIG-----LAELAD--ED 216
Cdd:cd07786 149 ERAERgelAFGTIDsWLIWKLTGGKvhatdvtnaSR---------TMLfnIHTLEWDDELLELFGipasmLPEVKPssEV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 217 FirighhivspGTPCGNGLTAqaaaemgllpGTPVAvGLI-DAHAGGIGTVGVEGGALNNlayVFGTsSCTMASTTSPSF 295
Cdd:cd07786 220 F----------GYTDPDLLGA----------EIPIA-GIAgDQQAALFGQACFEPGMAKN---TYGT-GCFMLMNTGEKP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 296 VPG--------VWG----PYYSamvpglwlVEGGQSAAGAAIDqlldfhpaveearemaqrvnqplpvWLADRI-LEKTA 362
Cdd:cd07786 275 VRSkngllttiAWQlggkVTYA--------LEGSIFIAGAAVQ-------------------------WLRDGLgLIESA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 363 qpSDAVALAK------GLHVVPEFLGNRAPFADPHARAVICGLgmERDLDnllALYI--AGLCGIGYGLRQILDAQTAQG 434
Cdd:cd07786 322 --AETEALARsvpdngGVYFVPAFTGLGAPYWDPDARGAIFGL--TRGTT---RAHIarAALESIAYQTRDLLEAMEADS 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1685051901 435 VVS-KNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVGEAMQQFtHVDKYYYPQ 508
Cdd:cd07786 395 GIPlKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLW-QVDRRFEPS 468
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
7-512 |
9.36e-21 |
|
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: 95.32 E-value: 9.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 7 VIGVDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGFdAT--C 84
Cdd:cd07793 2 ILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGI-STqrN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 85 SLVVLDK-NGDPLpvspegdakQNIIVWMDHRATEQAERINA-THHPVLNYVGG-----------------KISPEMETP 145
Cdd:cd07793 81 TFLTWDKkTGKPL---------HNFITWQDLRAAELCESWNRsLLLKALRGGSKflhfltrnkrflaasvlKFSTAHVSI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 146 KILWLKENMPEIYERA--GQ-FFDLAD-FLTWRATG------DLarSVCTVTckwtwlaheNRWDP------DYFRTIgl 209
Cdd:cd07793 152 RLLWILQNNPELKEAAekGElLFGTIDtWLLWKLTGgkvhatDY--SNASAT---------GLFDPftlewsPILLSL-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 210 aeladedfIRIGHHIVSPGTPCgNGLTAQAAAEMGllpGTPVAV-GLI-DAHAGGIGTVGVEGGALNnlayvfgtssCTM 287
Cdd:cd07793 219 --------FGIPSSILPEVKDT-SGDFGSTDPSIF---GAEIPItAVVaDQQAALFGECCFDKGDVK----------ITM 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 288 ASTTspsFVPGVWGPYYSAMVPGL-----W--------LVEGGQSAAGAAID--QLLDFHPAVEEAREMAQRVNqplpvw 352
Cdd:cd07793 277 GTGT---FIDINTGSKPHASVKGLyplvgWkiggeityLAEGNASDTGTVIDwaKSIGLFDDPSETEDIAESVE------ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 353 ladrilektaqPSDavalakGLHVVPEFLGNRAPFADPHARAVICGLG-------MERdldnllalyiAGLCGIGYGLRQ 425
Cdd:cd07793 348 -----------DTN------GVYFVPAFSGLQAPYNDPTACAGFIGLTpsttkahLVR----------AILESIAFRVKQ 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 426 ILDA-QTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVgEAMQQFTHVDKY 504
Cdd:cd07793 401 LLETmEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKI 479
|
....*...
gi 1685051901 505 YYPQERYQ 512
Cdd:cd07793 480 FEPKMDNE 487
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
6-508 |
4.73e-16 |
|
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: 80.65 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 6 TVIG-VDVGSGSVRAGIFDLNGSLL-SHATEKITTTRRSGsRVEQSSQEIWQAVCSCIRNA---LTLADVCAQSVAGIGF 80
Cdd:cd07792 1 PLVGaIDQGTTSTRFIVFDSTGELVaSHQVEHKQIYPKPG-WVEHDPMEILESVYECIEEAvekLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 81 daTC---SLVVLDKN-GDPLpvspegdakQNIIVWMDHRATEQAERINATHHPVLNYVGGK----ISPEMETPKILWLKE 152
Cdd:cd07792 80 --TNqreTTVVWDKStGKPL---------YNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKtglpISTYFSAVKLRWLLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 153 NMPEIyeRAGQFFDLADF------LTWRATGDLARSV-CT-VT------------CKwtwlahenrWDPDYFRTIGlael 212
Cdd:cd07792 149 NVPEV--KKAVDDGRLLFgtvdswLIWNLTGGKNGGVhVTdVTnasrtmlmnlrtLQ---------WDPELCEFFG---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 213 adedfIRIGH--HIVSpgtpcgngltaqAAAEMGL-----LPGTPVAVGLIDAHAGGIGTVGVEGGALNNlayVFGTsSC 285
Cdd:cd07792 214 -----IPMSIlpEIRS------------SSEVYGKiasgpLAGVPISGCLGDQQAALVGQGCFKPGEAKN---TYGT-GC 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 286 TMASTTSPSFVPGVWG--------------PYYsAMvpglwlvEGGQSAAGAAIDqlldfhpaveearemaqrvnqplpv 351
Cdd:cd07792 273 FLLYNTGEEPVFSKHGllttvayklgpdapPVY-AL-------EGSIAIAGAAVQ------------------------- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 352 WLAD--RILEKtaqPSDAVALAK------GLHVVPEFLGNRAPFADPHARAVICGLGME-------RdldnllalyiAGL 416
Cdd:cd07792 320 WLRDnlGIISS---ASEVETLAAsvpdtgGVYFVPAFSGLFAPYWRPDARGTIVGLTQFttkahiaR----------AAL 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 417 CGIGYGLRQILDAQTA-QGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVGEAM 495
Cdd:cd07792 387 EAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELK 466
|
570
....*....|...
gi 1685051901 496 QQFTHVDKYYYPQ 508
Cdd:cd07792 467 SLNEGGRTVFEPQ 479
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
10-487 |
1.75e-15 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 78.97 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 10 VDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEQSSQEIWQAVCSCIRNALTLADVCAQSVA------GIGFDAT 83
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDsglkaiGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 84 CSLVVLDKNGDPLpvspegdakQNIIVWMDHRATEQAERINATHHPVLNYV----GGKISPEMETPKILWLKENMPEIYE 159
Cdd:PLN02295 85 TTVAWSKSTGRPL---------YNAIVWMDSRTSSICRRLEKELSGGRKHFvetcGLPISTYFSATKLLWLLENVDAVKE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 160 --RAGQ--FFDLADFLTWRATGDLARSV----CTVTCKWTWLAHENR-WDPDYFRTIG-----LAELAD--EDFIRIghh 223
Cdd:PLN02295 156 avKSGDalFGTIDSWLIWNLTGGASGGVhvtdVTNASRTMLMNLKTLdWDKPTLEALGipaeiLPKIVSnsEVIGTI--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 224 ivSPGTPCGngltaqaaaemgllpGTPVAVGLIDAHAGGIGTVGVEGGALNnlayVFGTsSCTMASTTSPSFVPGVWGpY 303
Cdd:PLN02295 233 --AKGWPLA---------------GVPIAGCLGDQHAAMLGQRCRPGEAKS----TYGT-GCFILLNTGEEVVPSKHG-L 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 304 YSAMV-------PGLWLVEGGQSAAGAAIDqlldfhpaveearemaqrvnqplpvWLADRI-LEKTAqpSDAVALAK--- 372
Cdd:PLN02295 290 LTTVAyklgpdaPTNYALEGSVAIAGAAVQ-------------------------WLRDNLgIIKSA--SEIEALAAtvd 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 373 ---GLHVVPEFLGNRAPFADPHARAVIcgLGMERdLDNLLALYIAGLCGIGYGLRQILDAQTAQGVVSKNIV------IS 443
Cdd:PLN02295 343 dtgGVYFVPAFSGLFAPRWRDDARGVC--VGITR-FTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKSHKglfllrVD 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1685051901 444 GGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNI 487
Cdd:PLN02295 420 GGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
5-500 |
2.75e-15 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 78.48 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 5 KTVIGVDVGSGSVRAGIFDLNGSLLshATEKIT---TTRRSGSrVEQSSQEIWQAVCSCIRNALTLA--DVCAQSVAGIG 79
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEKGNVV--SSHQIPheqITPHPGW-LEHDPEEILRNVYKCMNEAIKKLreKGPSFKIKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 80 FdaTC---SLVVLDKN-GDPLpvspegdakQNIIVWMDHRATEQAERINAtHHPVLNYV----GGKISPEMETPKILWLK 151
Cdd:PTZ00294 79 I--TNqreTVVAWDKVtGKPL---------YNAIVWLDTRTYDIVNELTK-KYGGSNFFqkitGLPISTYFSAFKIRWML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 152 ENMPEIYERAGQ----FFDLADFLTWRATGdlARSVCT-VT-CKWTWLA--HENRWDPDYFRTIGLAELA-------DED 216
Cdd:PTZ00294 147 ENVPAVKDAVKEgtllFGTIDTWLIWNLTG--GKSHVTdVTnASRTFLMniKTLKWDEELLNKFGIPKETlpeikssSEN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 217 FirigHHIVSPGTPcgngltaqaaaemgLLPGTPVAVGLIDAHAGGIGTVGVEGGALNNlayVFGTSSCTMAST------ 290
Cdd:PTZ00294 225 F----GTISGEAVP--------------LLEGVPITGCIGDQQAALIGHGCFEKGDAKN---TYGTGCFLLMNTgteivf 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 291 ------TSPSFVPGVWGPYYSAMvpglwlvEGGQSAAGAAIDqlldfhpaveearemaqrvnqplpvWLADR--ILEkta 362
Cdd:PTZ00294 284 skhgllTTVCYQLGPNGPTVYAL-------EGSIAVAGAGVE-------------------------WLRDNmgLIS--- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 363 QPSDAVALAK------GLHVVPEFLGNRAPFADPHARAVICGLGMERDLDNLLAlyiAGLCGIGYGLRQILDA-QTAQGV 435
Cdd:PTZ00294 329 HPSEIEKLARsvkdtgGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVR---AALEAIALQTNDVIESmEKDAGI 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1685051901 436 VSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAGNIAPSVGEaMQQFTH 500
Cdd:PTZ00294 406 ELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEE-VKKLIR 469
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-508 |
5.78e-15 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 77.17 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 1 MTITKTVIGVDVGSGSVRAGIFDLNGSLLSHATEKITTT-RRSGsRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIG 79
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIfPQPG-WVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 80 F----DATcslVVLDKN-GDPLpvspegdakQNIIVWMDHRATEQAERINATHHPvlNYVGGK----ISPEMETPKILWL 150
Cdd:PRK00047 80 ItnqrETT---VVWDKEtGRPI---------YNAIVWQDRRTADICEELKRDGYE--DYIREKtglvIDPYFSGTKIKWI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 151 KENMPEIYERAGQ---FFDLAD-FLTWRATGDLARsVCTVT-CKWTWL--AHENRWDPDYFRTIG-----LAELAD--ED 216
Cdd:PRK00047 146 LDNVEGARERAEKgelLFGTIDtWLVWKLTGGKVH-VTDYTnASRTMLfnIHTLDWDDELLELLDiprsmLPEVRPssEV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 217 FirighhivspgtpcgngltAQAAAEMGLLPGTPVAVGLIDAHAGGIGTVGVEGGALNNlayVFGTsSCTMASTTSPSFV 296
Cdd:PRK00047 225 Y-------------------GKTNPYGFFGGEVPIAGIAGDQQAALFGQLCFEPGMAKN---TYGT-GCFMLMNTGEKAV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 297 PG--------VWG----PYYSamvpglwlVEGGQSAAGAAIdQlldfhpaveearemaqrvnqplpvWLAD--RILEKTA 362
Cdd:PRK00047 282 KSengllttiAWGidgkVVYA--------LEGSIFVAGSAI-Q------------------------WLRDglKIISDAS 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 363 QpSDAVALA----KGLHVVPEFLGNRAPFADPHARAVICGL--GMERDldnllALYIAGLCGIGYGLRQILDA-QTAQGV 435
Cdd:PRK00047 329 D-SEALARKvednDGVYVVPAFTGLGAPYWDSDARGAIFGLtrGTTKE-----HIIRATLESIAYQTRDVLDAmQADSGI 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685051901 436 VSKNIVISGGAGQHPLVRQILADTCGIPVITTQCCEPVLLGSAILGAVAgniapsVG-----EAMQQFTHVDKYYYPQ 508
Cdd:PRK00047 403 RLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLA------VGfwkdlDELKEQWKIDRRFEPQ 474
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
6-494 |
1.17e-09 |
|
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: 60.62 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 6 TVIGVDVGSGSVRA--GIFDlngsllshaTEKITTT---RRSGSRVEQSSQEIW--QAVCSCIRNALTLADVCAQSVAGI 78
Cdd:cd07771 1 NYLAVDLGASSGRVilGSLD---------GGKLELEeihRFPNRPVEINGHLYWdiDRLFDEIKEGLKKAAEQGGDIDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 79 GFDAT-CSLVVLDKNGDPLpvspegdakQNIIVWMDHRateqaerinatHHPVLNYVGGKISPE---MET---------- 144
Cdd:cd07771 72 GIDTWgVDFGLLDKNGELL---------GNPVHYRDPR-----------TEGMMEELFEKISKEelyERTgiqfqpintl 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 145 PKILWLKENMPEIYERAGQFFDLADFLTWRATGDlarsvctVTCKWTWL-------AHENRWDPDYFRTIGL-AELADEd 216
Cdd:cd07771 132 YQLYALKKEGPELLERADKLLMLPDLLNYLLTGE-------KVAEYTIAsttqlldPRTKDWSEELLEKLGLpRDLFPP- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 217 firighhIVSPGTPCGNgLTAQAAAEmGLLPGTPV-AVGlidAH--AGGIGTVGVEGgalNNLAYVF-GTSSCTMASTTS 292
Cdd:cd07771 204 -------IVPPGTVLGT-LKPEVAEE-LGLKGIPViAVA---SHdtASAVAAVPAED---EDAAFISsGTWSLIGVELDE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 293 P-----SFVPGV---WGPYYSAM----VPGLWLVEG-----GQSAAGAAIDQLLDfhpAVEEAREMAQR--VNQPL---P 350
Cdd:cd07771 269 PviteeAFEAGFtneGGADGTIRllknITGLWLLQEcrrewEEEGKDYSYDELVA---LAEEAPPFGAFidPDDPRflnP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 351 VWLADRI---LEKTAQPsdavalakglhvVPEflgNRAPFadphARAVicglgmerdLDNlLALYIAglcgigyglRQIL 427
Cdd:cd07771 346 GDMPEAIrayCRETGQP------------VPE---SPGEI----ARCI---------YES-LALKYA---------KTIE 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 428 DAQTAQGVVSKNIVISGGAGQHPLVRQILADTCGIPVITTqccePV---LLGSAILGAVAGNIAPSVGEA 494
Cdd:cd07771 388 ELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG----PVeatAIGNLLVQLIALGEIKSLEEG 453
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
10-480 |
2.24e-08 |
|
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: 56.50 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 10 VDVGSGSVRAGIFDLNGSLLSHATEKITTTRRSGSRVEqSSQEIWQAVCSCIRNALTLADVCAQSVAGIGfdatCSLVVL 89
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEIEEDGYPCE-DVEAIWEWLLDSLAELAKRHRIDAINFTTHG----ATFALL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 90 DKNGDP-LPVSpegDAKQNIIVWMDHRATEQAERINATHHPV----LNYvgGKispemetpKILWLKENMPEIYERAGQF 164
Cdd:cd07772 80 DENGELaLPVY---DYEKPIPDEINEAYYAERGPFEETGSPPlpggLNL--GK--------QLYWLKREKPELFARAKTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 165 FDLADFLTWRATGDLARSVCTVTCkwtwlaHENRWDPDYFRTIGLAElaDEDFIRIGHHIVSPGTPCGNgLTAQAAAEMG 244
Cdd:cd07772 147 LPLPQYWAWRLTGKAASEITSLGC------HTDLWDFEKNEYSSLVK--KEGWDKLFPPLRKAWEVLGP-LRPDLARRTG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 245 LLPGTPVAVGLIDAHAggigtvgveggALnnLAY-VFGTSSCTMASTtspsfvpGVWgpyYSAMVPGLWLVEGGQSAAGA 323
Cdd:cd07772 218 LPKDIPVGCGIHDSNA-----------AL--LPYlAAGKEPFTLLST-------GTW---CIAMNPGNDLPLTELDLARD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 324 AIDQLLDFHPAVEEAREMA----QRVNQPLPVWLADRILEKTAqpsdAVALAKGLHVVPEFLGNRAPFADPHARAVICGL 399
Cdd:cd07772 275 CLYNLDVFGRPVKTARFMGgreyERLVERIAKSFPQLPSLADL----AKLLARGTFALPSFAPGGGPFPGSGGRGVLSAF 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685051901 400 GMERDLDNLLALYIAglCGIGYGLRQILDAQtaqgvvsKNIVISGGAGQHPLVRQILADTC-GIPVITTQCCEPVLLGSA 478
Cdd:cd07772 351 PSAEEAYALAILYLA--LMTDYALDLLGSGV-------GRIIVEGGFAKNPVFLRLLAALRpDQPVYLSDDSEGTALGAA 421
|
..
gi 1685051901 479 IL 480
Cdd:cd07772 422 LL 423
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
4-80 |
2.35e-05 |
|
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: 46.43 E-value: 2.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1685051901 4 TKTVIGVDVGSGSVRAGIFDLNGSLLshATEKITTtrrsgsRVEQSSQEIWQAVCSCIRNALTLADVCAQSVAGIGF 80
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVDLDGEVL--ARERIPT------PAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
8-79 |
5.21e-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: 41.68 E-value: 5.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1685051901 8 IGVDVGSGSVRAGIFDLNGSLLSHATEKItttrrsgsRVEQSSQEIWQAVCSCIRNALTLADVCAQsVAGIG 79
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPT--------PAEEGPEAVLDRIAELIEELLAEAGVRER-ILGIG 63
|
|
| |
