|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
2-462 |
0e+00 |
|
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: 646.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 2 TYLAIDFGGGSGRVVAGTIttEGGKkqLTMQLVHRFQNRQVRLGEHVYWDFPALFEDMKTGLRKASQLGLKVSGIAVDTW 81
Cdd:cd07771 1 NYLAVDLGASSGRVILGSL--DGGK--LELEEIHRFPNRPVEINGHLYWDIDRLFDEIKEGLKKAAEQGGDIDSIGIDTW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 82 GVDFGLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLFQLLSLKKANSPQLQIADKMLFTPD 161
Cdd:cd07771 77 GVDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 162 LFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGLGEVDVIAVGSHD 241
Cdd:cd07771 157 LLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLKGIPVIAVASHD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 242 TASAVAAVPAKDDESpvAFISSGTWSLLGVELNEPILTEEARRAEFTNEGGIGGKITFLQNITGLWFLQRLMAEWKEEGD 321
Cdd:cd07771 237 TASAVAAVPAEDEDA--AFISSGTWSLIGVELDEPVITEEAFEAGFTNEGGADGTIRLLKNITGLWLLQECRREWEEEGK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 322 EQQYDT-LLAAAAEAEIKTVIPVDAKEFQNPKSMQAAICDYCAEHALEVPQSKAATTRVVLQSLAAKYAEATAHLNSMLP 400
Cdd:cd07771 315 DYSYDElVALAEEAPPFGAFIDPDDPRFLNPGDMPEAIRAYCRETGQPVPESPGEIARCIYESLALKYAKTIEELEELTG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495178145 401 KPIQKLHIIGGGSQNKLLNRLTEEALGVPVEAGPVEATAIGNILCQALAKGEVKSVTEMRKI 462
Cdd:cd07771 395 KRIDRIHIVGGGSRNALLCQLTADATGLPVIAGPVEATAIGNLLVQLIALGEIKSLEEGREL 456
|
|
| rhamnulo_kin |
TIGR02627 |
rhamnulokinase; This model describes rhamnulokinase, an enzyme that catalyzes the second step ... |
4-462 |
1.55e-151 |
|
rhamnulokinase; This model describes rhamnulokinase, an enzyme that catalyzes the second step in rhamnose catabolism.
Pssm-ID: 274237 [Multi-domain] Cd Length: 454 Bit Score: 438.80 E-value: 1.55e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 4 LAIDFGGGSGRVVAGTITTEggKKQLTMQLVHRFQNRQVRLGEHVYWDFPALFEDMKTGLRKASQLGLKVSGIAVDTWGV 83
Cdd:TIGR02627 1 VAVDLGASSGRVMLASYENE--CQKLTLEEIHRFKNGLVSQNGHECWDIDALEQEIRLGLNKVDAEGIAPDSIGIDTWGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 84 DFGLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLFQLLSLKKANSPQLQIADKMLFTPDLF 163
Cdd:TIGR02627 79 DFVLLDQNGQRVGDPVSYRDSRTDGVMAQVQSELGKEAIYQRTGIQFLPFNTLYQLRALTEQQPDLLEKVAHFLLIPDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 164 SYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLrkdiaEETGLGEVDVIAVGSHDTA 243
Cdd:TIGR02627 159 NYRLTGKKVWEYTNATTTQLVNINTDDWDEDLLAYLGVPAAWFGRPTHPGNVIGLW-----ECPQGNQIPVVAVATHDTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 244 SAVAAVPAKDDESpvAFISSGTWSLLGVELNEPILTEEARRAEFTNEGGIGGKITFLQNITGLWFLQRLmaewKEEGDEQ 323
Cdd:TIGR02627 234 SAVVAAPLQGENA--AYLSSGTWSLMGFESQTPITNEQALAANITNEGGADGRYRVLKNIMGLWLLQRV----CRERDIN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 324 QY-DTLLAAAAEAEIKTVIPVDAKEFQNPKSMQAAICDYCAEHALEVPQSKAATTRVVLQSLAAKYAEATAHLNSMLPKP 402
Cdd:TIGR02627 308 DLpALIEQAQALPAFKSIINPNDDRFINPENMCEEIQAYCRETNQPIPESDAELARCIFDSLALLYRQVLLELAELRGKP 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 403 IQKLHIIGGGSQNKLLNRLTEEALGVPVEAGPVEATAIGNILCQALAKGEVKSVTEMRKI 462
Cdd:TIGR02627 388 ISQLHIVGGGSQNAFLNQLCADACGIRVIAGPVEASTLGNIGVQLMALDEINDMAAFRQI 447
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
23-462 |
1.28e-128 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 380.99 E-value: 1.28e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 23 EGGKKQLTMQLVHRFQNRQVRLGEHVYWDFPALFEDMKTGLRKASQLGLKVSGIAVDTWGVDFGLIDRNGDLIGNPVCYR 102
Cdd:PRK10640 6 ERECRSLTLREIHRFNNGLHSQDGFDTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDYVLLDKQGQRVGLPVSYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 103 DARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLFQLLSLKKANsPQL--QIADkMLFTPDLFSYFLTSEANTEYTIAST 180
Cdd:PRK10640 86 DSRTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQ-PELiaQVAH-ALLIPDYFSYRLTGKMNWEYTNATT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 181 SEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEetglgEVDVIAVGSHDTASAVAAVPAKDDESpvAF 260
Cdd:PRK10640 164 TQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQGN-----EIPVVAVASHDTASAVIASPLNDSDA--AY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 261 ISSGTWSLLGVELNEPILTEEARRAEFTNEGGIGGKITFLQNITGLWFLQRLMaewkeegDEQQYDT----LLAAAAEAE 336
Cdd:PRK10640 237 LSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVL-------QERQITDlpalIAATAALPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 337 IKTVIPVDAKEFQNPKSMQAAICDYCAEHALEVPQSKAATTRVVLQSLAAKYAEATAHLNSMLPKPIQKLHIIGGGSQNK 416
Cdd:PRK10640 310 CRFLINPNDDRFINPPSMCSEIQAACRETAQPVPESDAELARCIFDSLALLYADVLHELAQLRGEPFSQLHIVGGGCQNA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 495178145 417 LLNRLTEEALGVPVEAGPVEATAIGNILCQALAKGEVKSVTEMRKI 462
Cdd:PRK10640 390 LLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQV 435
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
2-441 |
8.46e-43 |
|
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: 156.59 E-value: 8.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 2 TYLAIDFG---------GGSGRVVAgtitteggkkqltmqlVHRFQNRQVRLGEH-VYWDFPALFEDMKTGLRKA-SQLG 70
Cdd:cd07773 1 YLLGIDIGttnvkavlfDEDGRILA----------------SASRETPLIHPGPGwAELDPEELWEAVKEAIREAaAQAG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 71 LK-VSGIAVDTWGVDFGLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLFQLLSLKKANSPQ 149
Cdd:cd07773 65 PDpIAAISVSSQGESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 150 LQIADKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGL 229
Cdd:cd07773 145 FAKAAKWLSVADYIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 230 GEVDVIAVGSHDtaSAVAAVPAKDDESPVAFISSGTWSLLGVELNEPILTEEARRAEFTNEGGI-GGKITFLQNITG--- 305
Cdd:cd07773 225 PAGTPVVVGGHD--HLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSYGHHVpGGYYYLAGSLPGgal 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 306 -LWFLQRLMAEWKEEGDEQQYDTLLAAAAEAEIktVIPvdakefqNPKSMQAAICDYCAEHA---LEVPQSKAATTRVVL 381
Cdd:cd07773 303 lEWFRDLFGGDESDLAAADELAEAAPPGPTGLL--FLP-------HLSGSGTPDFDPDARGAflgLTLGTTRADLLRAIL 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495178145 382 QSLAAKYAEATAHLNSmLPKPIQKLHIIGGGSQNKLLNRLTEEALGVPVEAGPV-EATAIG 441
Cdd:cd07773 374 EGLAFELRLNLEALEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVpEATALG 433
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
47-441 |
2.82e-37 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 142.09 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 47 HVyWDFPALFEDMKTGLRKA-SQLGLK-VSGIAVDTWGVDFGLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYS 124
Cdd:PRK10331 45 HQ-WSLDAILQRFADCCRQInSELTEChIRGITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 125 VNGTQVMEINTLFQLLSLKKaNSPQL-QIADKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPR 203
Cdd:PRK10331 124 ISGVGAFSFNTLYKLVWLKE-NHPQLlEQAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 204 HLFCPIVMPGTVRGKLRKDIAEETGLG-EVDVIAVGsHDTASAVAAVPAKDDEspvAFISSGTWSLLGVELNEPILTEEA 282
Cdd:PRK10331 203 RLFPRLVEAGEQIGTLQPSAAALLGLPvGIPVISAG-HDTQFALFGSGAGQNQ---PVLSSGTWEILMVRSAQVDTSLLS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 283 RRAEFTNE-----GGIGGKITFLQNITGLWFLQRLmaeWKEegdEQQYDTLLAAAaeaeiKTVIP-VDAKEFQNP--KSM 354
Cdd:PRK10331 279 QYAGSTCEldsqsGLYNPGMQWLASGVLEWVRKLF---WTA---ETPYQTMIEEA-----RAIPPgADGVKMQCDllACQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 355 QAAICdycaehALEVPQSKAATTRVVLQSLAAK------YAEATAHLNSmlpkpiQKLHIIGGGSQNKLLNRLTEEALGV 428
Cdd:PRK10331 348 NAGWQ------GVTLNTTRGHFYRAALEGLTAQlkrnlqVLEKIGHFKA------SELLLVGGGSRNALWNQIKANMLDI 415
|
410
....*....|....
gi 495178145 429 PVEAGPV-EATAIG 441
Cdd:PRK10331 416 PIKVLDDaETTVAG 429
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-444 |
2.02e-33 |
|
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: 129.99 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 3 YLAIDFGGGSGRVVagtITTEGGKkqltmqlVHRFQNRQVRLG-------EH---VYWDfpALFEDMKTGLRKASQLGLK 72
Cdd:cd00366 2 LLGIDIGTTSVKAA---LFDEDGN-------LVASASREYPLIypqpgwaEQdpeDWWQ--AVVEAIREVLAKAGIDPSD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 73 VSGIAVDTWGVDFGLIDRNGDLIGNPVCYRDARtqgmtdeffadtdrtahysvngtqvmeintlfqllslkkanspqlqi 152
Cdd:cd00366 70 IAAIGISGQMPGVVLVDADGNPLRPAIIWLDRR----------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 153 aDKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGLGEV 232
Cdd:cd00366 103 -AKFLQPNDYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 233 DVIAVGSHDTASAVAAVPAKDDEspVAFISSGTWSLLGVELNEPIlteEARRAEFTNEGGIGGKITFLQNI--TGL---W 307
Cdd:cd00366 182 TPVVAGGGDTAAAALGAGVVEPG--DAVDSTGTSSVLSVCTDEPV---PPDPRLLNRCHVVPGLWLLEGAIntGGAslrW 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 308 FLQRLMAEWKEEGDEQQYDTllaaaaeaeiktvipvDAKEfQNPKS--------MQAAICDYCAEHA------LEVPQSK 373
Cdd:cd00366 257 FRDEFGEEEDSDAEYEGLDE----------------LAAE-VPPGSdgliflpyLSGERSPIWDPAArgvffgLTLSHTR 319
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495178145 374 AATTRVVLQSLAAKYAEATAHLNSMLPKpIQKLHIIGGGSQNKLLNRLTEEALGVPVEAGPV-EATAIGNIL 444
Cdd:cd00366 320 AHLIRAVLEGVAYALRDNLEILEELGVK-IKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVaEGAALGAAI 390
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-451 |
4.09e-32 |
|
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: 127.34 E-value: 4.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 3 YLAIDFGGGSGRVV----AGTITTEGGKKqltmqlvhrfqNRQVRLGEH---VYWD----FPALFEDMKTGLRKASQLGL 71
Cdd:cd07798 2 YLVIDIGTGGGRCAlvdsEGKIVAIAYRE-----------WEYYTDDDYpdaKEFDpeelWEKICEAIREALKKAGISPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 72 KVSGIAVDTWGVDFGLIDRNG-DLIGNPvcYRDARTQGMTDEFFADTdRTAHYSVNGTQVMEINTLFQLLSLKKaNSPQL 150
Cdd:cd07798 71 DISAVSSTSQREGIVFLDKDGrELYAGP--NIDARGVEEAAEIDDEF-GEEIYTTTGHWPTELFPAARLLWFKE-NRPEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 151 -QIADKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGL 229
Cdd:cd07798 147 fERIATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 230 GEVDVIAVGSHDTASAVAAVPAKDDESpvAFISSGTWSLLGVELNEPILTEEARRaeFTNEGGIGGKITFLQN--ITGL- 306
Cdd:cd07798 227 PEGTPVVVGGADTQCALLGSGAIEPGD--IGIVAGTTTPVQMVTDEPIIDPERRL--WTGCHLVPGKWVLESNagVTGLn 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 307 --WFLQRLMaewkeEGDEQQYDTLLAAAAEaeiktvIPVDAKE---FQNPKSMQAAICDYC-AEHALEVPQS-----KAA 375
Cdd:cd07798 303 yqWLKELLY-----GDPEDSYEVLEEEASE------IPPGANGvlaFLGPQIFDARLSGLKnGGFLFPTPLSaseltRGD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 376 TTRVVLQSLA----AKYAEatahLNSMLPKPIQKLHIIGGGSQNKLLNR----LTEEALGVPVEAgpvEATAIGNILCQA 447
Cdd:cd07798 372 FARAILENIAfairANLEQ----LEEVSGREIPYIILCGGGSRSALLCQiladVLGKPVLVPEGR---EASALGAAICAA 444
|
....
gi 495178145 448 LAKG 451
Cdd:cd07798 445 VGAG 448
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-458 |
4.49e-28 |
|
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: 116.47 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 2 TYLAIDFGGGSGRVVA----GTITTEGGKKqltmqlvHRFQNRQVRLGEH---VYWDfpALFEDMKTGLRKASQLGLKVS 74
Cdd:COG1070 2 YVLGIDIGTTSVKAVLfdadGEVVASASAE-------YPLSSPHPGWAEQdpeDWWE--AVVEAIRELLAKAGVDPEEIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 75 GIAVDTWGVDFGLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLFQLLSLKKaNSPQL--QI 152
Cdd:COG1070 73 AIGVSGQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKE-NEPEIfaRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 153 AdKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGLGEV 232
Cdd:COG1070 152 A-KVLLPKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 233 DVIAVGSHDT-ASAVAAVPAKDDEspvAFISSGTWSLLGVELNEPILTEEARRAEFTneGGIGGKITFL--QNITGL--- 306
Cdd:COG1070 231 TPVVAGAGDNaAAALGAGAVEPGD---AAVSLGTSGVVFVVSDKPLPDPEGRVHTFC--HAVPGRWLPMgaTNNGGSalr 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 307 WFLQRLMAEwkEEGDEQQYDTLLAAaaeaeiktvIPVDAK----------E---FQNPKsMQAAICDYCAEHalevpqSK 373
Cdd:COG1070 306 WFRDLFADG--ELDDYEELNALAAE---------VPPGADgllflpylsgErtpHWDPN-ARGAFFGLTLSH------TR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 374 AATTRVVLQSLAAKYAEATAHLNSMLPKpIQKLHIIGGGSQNKLLNRLTEEALGVPVEAGPV-EATAIGNILCQALAKGE 452
Cdd:COG1070 368 AHLARAVLEGVAFALRDGLEALEEAGVK-IDRIRATGGGARSPLWRQILADVLGRPVEVPEAeEGGALGAALLAAVGLGL 446
|
....*.
gi 495178145 453 VKSVTE 458
Cdd:COG1070 447 YDDLEE 452
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
259-449 |
1.65e-27 |
|
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: 108.57 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 259 AFISSGTWSLLGVELNEPILTEEARRAEFTNE-----GGIGGKITFLQNITGlWFLQ--RLMAEWKEEGDEQQYDTLLAA 331
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEmlpgyWGLEGGQSAAGSLLA-WLLQfhGLREELRDAGNVESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 332 AAEAEIK--TVIPVDAKEFqNPKSMQAAICDYcaeHALEVPQSKAATTRVVLQSLAAKYAEATAHLNSMLPKPIQKLHII 409
Cdd:pfam02782 80 AAVAPAGglLFYPDFSGNR-APGADPGARGSI---TGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495178145 410 GGGSQNKLLNRLTEEALGVPVE-AGPVEATAIGNILCQALA 449
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVvPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
47-463 |
2.83e-26 |
|
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: 110.30 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 47 HVYWDfpALFEDMKTGLRKASQLGLKVSGIAVDTWGVDFGLIDRNGDLIGNPVCYRDARTqgmtdeffadtdrtahysvn 126
Cdd:cd07779 46 DDWWD--ALCEALKEAVAKAGVDPEDIAAIGLTSQRSTFVPVDEDGRPLRPAISWQDKRT-------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 127 gtqvmeintlfqllslkkanspqlqiaDKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLF 206
Cdd:cd07779 104 ---------------------------AKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 207 CPIVMPGTVRGKLRKDIAEETGLGE-VDVIAvGSHDTASAVAAVPAKDDEspVAFISSGTWSLLGVELNEPIltEEARRA 285
Cdd:cd07779 157 PELVPPGTVIGTLTKEAAEETGLPEgTPVVA-GGGDQQCAALGAGVLEPG--TASLSLGTAAVVIAVSDKPV--EDPERR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 286 EFTNEGGIGGK--ITFLQNITGL---WFLQRLMAEWKEEGDEQQYDTLLAAAAEAEIK------TVIPvdakefqnpkSM 354
Cdd:cd07779 232 IPCNPSAVPGKwvLEGSINTGGSavrWFRDEFGQDEVAEKELGVSPYELLNEEAAKSPpgsdglLFLP----------YL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 355 QAAICDYCAEHA------LEVPQSKAATTRVVLQSLA---AKYAEATAHLNsmlpKPIQKLHIIGGGSQNKLLNRLTEEA 425
Cdd:cd07779 302 AGAGTPYWNPEArgafigLTLSHTRAHLARAILEGIAfelRDNLEAMEKAG----VPIEEIRVSGGGSKSDLWNQIIADV 377
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 495178145 426 LGVPVEAGPV-EATAIGNILCQALAKGEVKSVTE----MRKIE 463
Cdd:cd07779 378 FGRPVERPETsEATALGAAILAAVGAGIYPDFEEavkaMVRVT 420
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-246 |
1.09e-23 |
|
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: 99.33 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 3 YLAIDFGGGSGRVVAGTitteggkKQLTMQLVHRFQNRQVRLGE-HVYWD----FPALFEDMKTGLRKASQLGLKVSGIA 77
Cdd:pfam00370 2 YLGIDCGTTSTKAILFN-------EQGKIIAVAQLENPQITPHPgWAEQDpdeiWQAVAQCIAKTLSQLGISLKQIKGIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 78 VDTWGVDFGLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLFQLLSLKKaNSPQL-QIADKM 156
Cdd:pfam00370 75 ISNQGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKE-NEPEVfEKIHKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 157 LFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGLGEVDVIA 236
Cdd:pfam00370 154 LTIHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVV 233
|
250
....*....|
gi 495178145 237 VGSHDTASAV 246
Cdd:pfam00370 234 GGGGDQQAAA 243
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
87-322 |
2.14e-22 |
|
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: 99.16 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 87 LIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLFQLLSLKKaNSPQ-LQIADKMLFTPDLFSY 165
Cdd:cd07802 84 LVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKE-NEPErYDRIRTVLFCKDWIRY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 166 FLTSEANTEYTIASTSeMLNATTRDWDWELIDRLQLP--RHLFCPIVMPGTVRGKLRKDIAEETGLGEVDVIAVGSHDTA 243
Cdd:cd07802 163 RLTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 244 SAVAAVPAKDDesPVAFISSGTWSLLGVELNEPILTEEARRAEFTNEGGiggkiTFLQNITGL-------WFLQRLMAEW 316
Cdd:cd07802 242 ASALGAGAVDE--GQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPG-----LYLIVEASPtsasnldWFLDTLLGEE 314
|
....*.
gi 495178145 317 KEEGDE 322
Cdd:cd07802 315 KEAGGS 320
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-441 |
8.36e-22 |
|
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: 97.29 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 3 YLAIDFGGGSGRVVAgtITTEG---GKKQLTMQLVHRFQNRQVRLGEhVYWdfpalfEDMKTGLRK-ASQLGL-KVSGIA 77
Cdd:cd07783 2 FLGIDLGTSGVRAVV--VDEDGtvlASASEPYPTSRPGPGWVEQDPE-DWW------EALRSLLRElPAELRPrRVVAIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 78 VD-TWGVDFgLIDRNGDLIGNPVCYRDARTQGMTDEF---FADTDRTAHYSVNGTqvmeiNTLFQLLSLKKaNSPQLQIA 153
Cdd:cd07783 73 VDgTSGTLV-LVDREGEPLRPAIMYNDARAVAEAEELaeaAGAVAPRTGLAVSPS-----SSLAKLLWLKR-HEPEVLAK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 154 DKMLFTP-DLFSYFLTSEAN-TEYTIASTSeMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGLGE 231
Cdd:cd07783 146 TAKFLHQaDWLAGRLTGDRGvTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 232 VDVIAVGSHD-TASAVAAVPAkddESPVAFISSGTWSLLGvelnepILTEEARRAeftNEGGI------------GGKIt 298
Cdd:cd07783 225 GTPVVAGTTDsIAAFLASGAV---RPGDAVTSLGTTLVLK------LLSDKRVPD---PGGGVyshrhgdgywlvGGAS- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 299 flqNITGLWFLQRL----MAEWKEEGDEQQYDTLlaaaaeaeikTVIPVDAK----EFQNPKsMQAAIcdycaehaLEVP 370
Cdd:cd07783 292 ---NTGGAVLRWFFsddeLAELSAQADPPGPSGL----------IYYPLPLRgerfPFWDPD-ARGFL--------LPRP 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495178145 371 QSKAATTRVVLQSLAakYAEATA--HLNSMLPKPIQKLHIIGGGSQNKLLNRLTEEALGVPVEAGPVEATAIG 441
Cdd:cd07783 350 HDRAEFLRALLEGIA--FIERLGyeRLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAALG 420
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-265 |
2.77e-19 |
|
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: 90.29 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 3 YLAIDFGGGSGRVVA----GTITTEGGKkqltmqlvhRFQNRQVRLGEH-----VYWDfpALFEDMKTGLRKASQLGLKV 73
Cdd:cd07808 2 LLGIDLGTSSVKAVLvdedGRVLASASA---------EYPTSSPKPGWAeqdpeDWWQ--ATKEALRELLAKAGISPSDI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 74 SGIAVDtwgvdfG------LIDRNGDLIGNPVCYRDARTQGMTDEFfADTDRTAHYSVNGTQVMEINTLFQLLSLKKaNS 147
Cdd:cd07808 71 AAIGLT------GqmhglvLLDKNGRPLRPAILWNDQRSAAECEEL-EARLGDEILIITGNPPLPGFTLPKLLWLKE-NE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 148 PQL--QIAdKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAE 225
Cdd:cd07808 143 PEIfaRIR-KILLPKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 495178145 226 ETGLGEVDVIAVGSHDTASAVAAVPAKDDEspVAFISSGT 265
Cdd:cd07808 222 ELGLPEGTPVVAGAGDNAAAALGAGVVEPG--DALISLGT 259
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-463 |
4.65e-19 |
|
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: 89.31 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 3 YLAIDFGGGSGRVVagtITTEGGKkQLTMQlvhrfQNRQVRLGEHVY-----WDFPA----LFEDMKTGLRKASQLGLKV 73
Cdd:cd07775 2 LLALDAGTGSGRAV---IFDLEGN-QIAVA-----QREWRHKEVPDVpgsmdFDTEKnwklICECIREALKKAGIAPKSI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 74 SGIAVDTWGVDFGLIDRNGDLIGnpVCYR-DARTQGMTD---EFFADTDRTAhYSVNGtQVMEINTLFQLLSLKKaNSPQ 149
Cdd:cd07775 73 AAISTTSMREGIVLYDNEGEEIW--ACANvDARAAEEVSelkELYNTLEEEV-YRISG-QTFALGAIPRLLWLKN-NRPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 150 L--QIAdKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEET 227
Cdd:cd07775 148 IyrKAA-KITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 228 GLGEVDVIAVGSHDTASAVAAVPAKdDESPVAFISSGTWSLLgVELNEPILTEEAR--------RAEFTNEGgiggkITF 299
Cdd:cd07775 227 GLKEGTPVVVGGGDVQLGCLGLGVV-RPGQTAVLGGSFWQQE-VNTAAPVTDPAMNirvnchviPDMWQAEG-----ISF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 300 LQNITGLWFLQRLMAEWKEEGDEQQYDTLLAAAAEAEiktVIPVDAKEFQNPKS--MQAAICDYCAEHALEVP-----QS 372
Cdd:cd07775 300 FPGLVMRWFRDAFCAEEKEIAERLGIDAYDLLEEMAK---DVPPGSYGIMPIFSdvMNYKNWRHAAPSFLNLDidpekCN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 373 KAATTRVVLQSLA-------AKYAEATAHlnsmlpkPIQKLHIIGGGSQNKLLNRLTEEALGVPVEAgPV--EATAIGNI 443
Cdd:cd07775 377 KATFFRAIMENAAivsagnlERIAEFSGI-------FPDSLVFAGGASKGKLWCQILADVLGLPVKV-PVvkEATALGAA 448
|
490 500
....*....|....*....|....
gi 495178145 444 LCQALAKGEVKSVTE----MRKIE 463
Cdd:cd07775 449 IAAGVGAGIYSSLEEavesLVKWE 472
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
63-265 |
3.42e-18 |
|
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: 86.80 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 63 LRKASQLGLKVSGIAVDTWGVDFGLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVN-GTQVMEINTLFQLLS 141
Cdd:cd07805 60 LEKSGIDPSDIAAIAFSGQMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGgGNPPSGKDPLAKILW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 142 LKKaNSPQL-QIADKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLR 220
Cdd:cd07805 140 LKE-NEPEIyAKTHKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELT 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495178145 221 KDIAEETGLGE-VDVIAvGSHDT-ASAVAAVPAKDDEspvAFISSGT 265
Cdd:cd07805 219 PEAAAELGLPAgTPVVG-GGGDAaAAALGAGAVEEGD---AHIYLGT 261
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-283 |
1.10e-15 |
|
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: 79.14 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 3 YLAIDFGGGSGRVVAgtITTEGgkkqltmQLVHRFQNRQVRLGEHVYW---DFPALFEDMKTGLRKASQL--GLKVSGIA 77
Cdd:cd07770 2 ILGIDIGTTSTKAVL--FDEDG-------RVVASSSAEYPLIRPEPGWaeqDPEEILEAVLEALKEVLAKlgGGEVDAIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 78 VDT-WgvdFGLI--DRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLFQLLSLKKANSPQLQIAD 154
Cdd:cd07770 73 FSSaM---HSLLgvDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 155 KMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGL-GEVD 233
Cdd:cd07770 150 KFVSIKEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLlAGTP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495178145 234 VIAVGSHDTASAVAAvpAKDDESPVAfISSGTWSLLGVELNEPILTEEAR 283
Cdd:cd07770 230 VVLGASDGALANLGS--GALDPGRAA-LTVGTSGAIRVVSDRPVLDPPGR 276
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
63-319 |
1.47e-15 |
|
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: 78.44 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 63 LRKASQLGLKVSGIAV----D-TWgvdfgLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAHYSVNGTQVMEINTLF 137
Cdd:cd24121 60 VAKLDVLPDRVAAIGVtgqgDgTW-----LVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 138 QLLSLKKANSPQLQIADKMLFTPDLFSYFLTSEANTEYTIASTSeMLNATTRDWDWELIDRLQLP--RHLFCPIVMPGTV 215
Cdd:cd24121 135 QLAWLKENEPERLERARTALHCKDWLFYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 216 RGKLRKDIAEETGL--------GEVDVIAvgshdTASAVAAVPAKDdespvAFISSGTWSLLGVELNEPILteEARRAEF 287
Cdd:cd24121 214 IGPLTPEAAAATGLpagtpvvlGPFDVVA-----TALGSGAIEPGD-----ACSILGTTGVHEVVVDEPDL--EPEGVGY 281
|
250 260 270
....*....|....*....|....*....|....*..
gi 495178145 288 TNEGGIGGKIT-FLQNITGL----WFLQRLMAEWKEE 319
Cdd:cd24121 282 TICLGVPGRWLrAMANMAGTpnldWFLRELGEVLKEG 318
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|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
51-267 |
1.89e-13 |
|
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: 71.91 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 51 DFPALFEDMKTGLRKASQLGlKVSGIAVDTWGVDFGLIDRNGDLIGNPVCYRDArtqgMTDEFFADTDRTA-HYSVNGTQ 129
Cdd:cd07772 43 DVEAIWEWLLDSLAELAKRH-RIDAINFTTHGATFALLDENGELALPVYDYEKP----IPDEINEAYYAERgPFEETGSP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 130 VME--INTLFQLLSLKKANSPQLQIADKMLFTPDLFSYFLTSEANTEYTIAST-SEMLNATTRDW-DW---ELIDRLqlp 202
Cdd:cd07772 118 PLPggLNLGKQLYWLKREKPELFARAKTILPLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEYsSLvkkEGWDKL--- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495178145 203 rhlFCPIVMPGTVRGKLRKDIAEETGLGEVDVIAVGSHDTASAVAAVPAKDDESPVAfISSGTWS 267
Cdd:cd07772 195 ---FPPLRKAWEVLGPLRPDLARRTGLPKDIPVGCGIHDSNAALLPYLAAGKEPFTL-LSTGTWC 255
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|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
46-248 |
3.98e-12 |
|
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: 67.94 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 46 EH---VYWDfpALFEDMKTGLRKASQLGLKVSGIAVDTWGVDFGLIDRNGDLIGNPVCYRDARTQGMTDEFFADTDRTAH 122
Cdd:cd07804 42 EHdpeVWWG--AVCEIIRELLAKAGISPKEIAAIGVSGLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 123 YSVNGtqvmeiNTLFQ------LLSLKKaNSPQL-QIADKMLFTPDLFSYFLTSEANTEYTIAS-TSEMLNATTRDWDWE 194
Cdd:cd07804 120 FEITG------NPLDSqsvgpkLLWIKR-NEPEVfKKTRKFLGAYDYIVYKLTGEYVIDYSSAGnEGGLFDIRKRTWDEE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495178145 195 LIDRLQLPRHLFCPIVMPGTVRGKLRKDIAEETGLGE-VDVIAvGSHDT-ASAVAA 248
Cdd:cd07804 193 LLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEgTPVVA-GTVDAaASALSA 247
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|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-461 |
1.23e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 56.94 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 1 MTYL-AIDFGGGSGRVVagtITTEGGkkqltmqlvhrfqnRQVRLGEHVYW-----DFPALFE-DMKTG----------- 62
Cdd:PRK10939 2 MSYLmALDAGTGSIRAV---IFDLNG--------------NQIAVGQAEWRhlavpDVPGSMEfDLEKNwqlacqcirqa 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 63 LRKASQLGLKVSGIAVDTWGVDFGLIDRNGDLI---GNpVCYRDARTQGMTDEFFADTDRtAHYSVNGtQVMEINTLFQL 139
Cdd:PRK10939 65 LQKAGIPASDIAAVSATSMREGIVLYDRNGTEIwacAN-VDARASREVSELKELHNNFEE-EVYRCSG-QTLALGALPRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 140 LSLKKaNSPQL-QIADKMLFTPDLFSYFLTSEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGK 218
Cdd:PRK10939 142 LWLAH-HRPDIyRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGH 220
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 219 LRKDIAEETGLGEVDVIAVGSHDT---ASAVAAVPAKDdespvAFISSGTWSLLGVELNEPILTEEAR-RaefTNEGGIG 294
Cdd:PRK10939 221 VTAKAAAETGLRAGTPVVMGGGDVqlgCLGLGVVRPGQ-----TAVLGGTFWQQVVNLPAPVTDPNMNiR---INPHVIP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 295 G-----KITFLQNITGLWFLQRLMAEWKEEGDEQQYDTLLAAAAEAE-----IKTVIPV--DAKEFQN-----PK----S 353
Cdd:PRK10939 293 GmvqaeSISFFTGLTMRWFRDAFCAEEKLLAERLGIDAYSLLEEMASrvpvgSHGIIPIfsDVMRFKSwyhaaPSfinlS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 354 MQAAICDycaehalevpqsKAATTRvVLQSLAAKYA----EATAHLNSMLPkpiQKLHIIGGGSQNKLLNRLTEEALGVP 429
Cdd:PRK10939 373 IDPEKCN------------KATLFR-ALEENAAIVSacnlQQIAAFSGVFP---SSLVFAGGGSKGKLWSQILADVTGLP 436
|
490 500 510
....*....|....*....|....*....|....
gi 495178145 430 VEAgPV--EATAIGNILCQALAKGEVKSVTEMRK 461
Cdd:PRK10939 437 VKV-PVvkEATALGCAIAAGVGAGIYSSLAETGE 469
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|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
144-245 |
7.80e-08 |
|
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: 54.48 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 144 KANSPQL--QIAdKMLfTP-DLFSYFLTSEANTEYTIASTSEMLNATTRDWDWEL---IDRLQLPRHLFCPIVMPGTVRG 217
Cdd:cd07809 140 KENEPEHyaRIA-KIL-LPhDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELlaaIDPSRDLRDLLPEVLPAGEVAG 217
|
90 100
....*....|....*....|....*...
gi 495178145 218 KLRKDIAEETGLGEVDVIAVGSHDTASA 245
Cdd:cd07809 218 RLTPEGAEELGLPAGIPVAPGEGDNMTG 245
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-281 |
2.93e-05 |
|
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: 46.06 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 3 YLAIDFGGGSgrvVAGTITTEGGKKQLTMQ-LVHRFQNRQVRLGEHVyWDFPALFEDMKTGLRK-ASQLGLKVSGIAVDT 80
Cdd:cd07777 2 VLGIDIGTTS---IKAALLDLESGRILESVsRPTPAPISSDDPGRSE-QDPEKILEAVRNLIDElPREYLSDVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 81 W--GvdFGLIDRNGDLIGNPVCYRDARTqgmtDEFFADTDRTAHYSVNGTQVMEIN------TLFQLLSLKKANSPqlqi 152
Cdd:cd07777 78 QmhG--IVLWDEDGNPVSPLITWQDQRC----SEEFLGGLSTYGEELLPKSGMRLKpgyglaTLFWLLRNGPLPSK---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 153 ADKMLFTPDLFSYFLT--SEANTEYTIASTSEMLNATTRDWDWELIDRLQLPRHLFCPIVMPGTVRGKLRKDIAeetglG 230
Cdd:cd07777 148 ADRAGTIGDYIVARLTglPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALP-----K 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 495178145 231 EVDV-IAVGSHDtASAVAAVPAKDDEspvAFISSGTWSLLGVELNEPILTEE 281
Cdd:cd07777 223 GIPVyVALGDNQ-ASVLGSGLNEEND---AVLNIGTGAQLSFLTPKFELSGS 270
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
372-463 |
3.75e-03 |
|
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: 39.47 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495178145 372 SKAATTRVVLQSLAAKYAEATAHLNSMLPKPIQKLHIIGGGSQNKLLNRLTEEALGVPVEAGP-VEATAIGNILCQALAK 450
Cdd:cd07793 382 TKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKnTEMSALGAAFLAGLAS 461
|
90
....*....|....*.
gi 495178145 451 GEVKSVTE---MRKIE 463
Cdd:cd07793 462 GIWKSKEElkkLRKIE 477
|
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