|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
1-484 |
0e+00 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 954.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLRDVKALGIAGQMHGA 80
Cdd:PRK15027 1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 81 TLLDSQHRVLRPAILWNDGRCAEECAILEERVPASREITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLRFRM 160
Cdd:PRK15027 81 TLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 161 TGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPAVPVVAGGGDNAAGAVG 240
Cdd:PRK15027 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 241 VGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSVMLSAASCLDWAAKLTGMADVPALIAAAQQA 320
Cdd:PRK15027 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 321 DDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDCGLTPSSITLIGGGARSS 400
Cdd:PRK15027 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 401 YWRQMLSDISGLQLDYRTGGDVGPALGAARLAQIALNRDKPLPQLLPQLPLEQQHRPDAKNHARYAERRDVFRKIYQQLL 480
Cdd:PRK15027 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480
|
....
gi 550766384 481 PLMS 484
Cdd:PRK15027 481 PLMA 484
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
3-477 |
0e+00 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 639.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 3 IGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLR--DVKALGIAGQMHGA 80
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMgqDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 81 TLLDSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLRF 158
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERvlEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 159 RMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDNAAG 237
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAgVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 238 AVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSVMLSAASCLDWAAKLTGMADVPALIAAA 317
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGWLPMGVTLSATSSLEWFRELFGKEDVEALNELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 318 QQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVV-HDCGLTPSSITLIGGG 396
Cdd:TIGR01312 321 EQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILrEAGGIPIQSIRLIGGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 397 ARSSYWRQMLSDISGLQLDYRTgGDVGPALGAARLAQIALNRDKPLPQ-LLPQLPLEQQHRPDAKNHARYAERRDVFRKI 475
Cdd:TIGR01312 401 AKSPAWRQMLADIFGTPVDVPE-GEEGPALGAAILAAWALGEKDLAALcSEAVVKQTESVLPIAENVEAYEELYERYKKL 479
|
..
gi 550766384 476 YQ 477
Cdd:TIGR01312 480 YQ 481
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
1-476 |
0e+00 |
|
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: 606.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQH--SLRDVKALGIAGQMH 78
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAgiSPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQHRVLRPAILWNDGRCAEECAILEERVPA-SREITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLR 157
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDeILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 158 FRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDNAA 236
Cdd:cd07808 161 YRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEgTPVVAGAGDNAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 237 GAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSVMLSAASCLDWAAKLTGMADVP--ALI 314
Cdd:cd07808 241 AALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDRESfdELD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 315 AAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDCGLTPSSITLIG 394
Cdd:cd07808 321 AEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 395 GGARSSYWRQMLSDISGLQLDYRTGGDvGPALGAARLAQIALNR-DKPLPQLLPQLPLEQQHRPDAKNHARYAERRDVFR 473
Cdd:cd07808 401 GGAKSPLWRQILADVLGVPVVVPAEEE-GSAYGAALLAAVGAGVfDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYR 479
|
...
gi 550766384 474 KIY 476
Cdd:cd07808 480 ELY 482
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
1-483 |
0e+00 |
|
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: 586.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQH--SLRDVKALGIAGQMH 78
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAgvDPEEIAAIGVSGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYL 156
Cdd:COG1070 82 GLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEAlyEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 157 RFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDNA 235
Cdd:COG1070 162 RYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAgTPVVAGAGDNA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 236 AGAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSVMLSAASCLDWAAKLTG---MADVPA 312
Cdd:COG1070 242 AAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFAdgeLDDYEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 313 LIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDCGLTPSSITL 392
Cdd:COG1070 322 LNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIRA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 393 IGGGARSSYWRQMLSDISGLQLdYRTGGDVGPALGAARLAQIALNRDK-PLPQLLPQLPLEQQHRPDAKNHARYAERRDV 471
Cdd:COG1070 402 TGGGARSPLWRQILADVLGRPV-EVPEAEEGGALGAALLAAVGLGLYDdLEEAAAAMVRVGETIEPDPENVAAYDELYER 480
|
490
....*....|..
gi 550766384 472 FRKIYQQLLPLM 483
Cdd:COG1070 481 YRELYPALKPLF 492
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-473 |
8.48e-135 |
|
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: 398.05 E-value: 8.48e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 3 IGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQH--SLRDVKALGIAGQMHGA 80
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSgiDPSDIAAIAFSGQMQGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 81 TLLDSQHRVLRPAILWNDGRCAEECAILEERVPASRE---ITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLR 157
Cdd:cd07805 83 VPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGyrlGGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDYLN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 158 FRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDNAA 236
Cdd:cd07805 163 FRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAgTPVVGGGGDAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 237 GAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSVMLSAASCLDWAAKLTGM-----ADVP 311
Cdd:cd07805 243 AALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASADPGRYLLAAEQETAGGALEWARDNLGGdedlgADDY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 312 ALI-AAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDCGLTPSSI 390
Cdd:cd07805 323 ELLdELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTRKIDEL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 391 TLIGGGARSSYWRQMLSDISG---LQLDYRTggDVGpALGAARLAQIALNRDKPLPQLLPQLPLEQQHRPDAKNHARYAE 467
Cdd:cd07805 403 RLVGGGARSDLWCQILADVLGrpvEVPENPQ--EAG-ALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENRARYDR 479
|
....*.
gi 550766384 468 RRDVFR 473
Cdd:cd07805 480 LYEVFK 485
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
1-437 |
8.90e-123 |
|
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: 365.72 E-value: 8.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILL-SEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQH--SLRDVKALGIAGQM 77
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIdAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAgaELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 78 HGATLLDSQHRVLRPAILWNDGRCAEECAILEERVPASRE-ITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYL 156
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKClLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 157 RFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDH---MPALFEGSDITGALQPSVAERWNMPA-VPVVAGGG 232
Cdd:cd07809 161 NWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDLrdlLPEVLPAGEVAGRLTPEGAEELGLPAgIPVAPGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 233 DNAAGAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSVMLSAASCLDWAAKLTGMaDVPA 312
Cdd:cd07809 241 DNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDSTGGMLPLINTTNCLTAWTELFRELLGV-SYEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 313 LIAAAQQADDTAGAVWFLPYLSGERTPhNNPEAKGVFFGLTH-QHGPAELARAVLEGVGYALADGMDVVHDCGLTPSSIT 391
Cdd:cd07809 320 LDELAAQAPPGAGGLLLLPFLNGERTP-NLPHGRASLVGLTLsNFTRANLARAALEGATFGLRYGLDILRELGVEIDEIR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 550766384 392 LIGGGARSSYWRQMLSDISGLQLD-YRTGGDVgpALGAARLAQIALN 437
Cdd:cd07809 399 LIGGGSKSPVWRQILADVFGVPVVvPETGEGG--ALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
1-432 |
1.28e-122 |
|
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: 363.42 E-value: 1.28e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQH--SLRDVKALGIAGQMH 78
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAgiDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQHRVLRPAILWNDGRcaeecaileervpasreitgnlmmpgftapkllwvqrhepeifrqvAKVLLPKDYLRF 158
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRR----------------------------------------------AKFLQPNDYIVF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 159 RMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDNAAG 237
Cdd:cd00366 115 RLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAgTPVVAGGGDTAAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 238 AVGVGMVETGQAMLSLGTSGVYFAVSDGYRSnPESAVHSFCHALPGKWHLMSVMLSAASCLDWAAKLTG-----MADVPA 312
Cdd:cd00366 195 ALGAGVVEPGDAVDSTGTSSVLSVCTDEPVP-PDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFGeeedsDAEYEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 313 LIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDCGLTPSSITL 392
Cdd:cd00366 274 LDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKEIRV 353
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 550766384 393 IGGGARSSYWRQMLSDISGLQLdYRTGGDVGPALGAARLA 432
Cdd:cd00366 354 TGGGAKSRLWNQIKADVLGVPV-VVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
1-435 |
2.41e-117 |
|
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: 352.21 E-value: 2.41e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQ--HSLRDVKALGIAGqMH 78
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKagISPKEIAAIGVSG-LV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATL-LDSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDY 155
Cdd:cd07804 80 PALVpVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRifEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 156 LRFRMTGDFASDMSDAAGTMWL-DVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGD 233
Cdd:cd07804 160 IVYKLTGEYVIDYSSAGNEGGLfDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEgTPVVAGTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 234 NAAGAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSfcHALPGKWHLMSVMLSAASCLDW-----------AA 302
Cdd:cd07804 240 AAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDY--HDIPGTYVLNGGMATSGSLLRWfrdefageeveAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 303 KLTGMADVPALIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHD 382
Cdd:cd07804 318 KSGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIRE 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 550766384 383 CGLTPSSITLIGGGARSSYWRQMLSDISGLQLDYRtGGDVGPALGAARLAQIA 435
Cdd:cd07804 398 AGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYV-KDTVGASLGDAFLAGVG 449
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
1-437 |
3.07e-115 |
|
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: 346.50 E-value: 3.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLRDVKALGIAGQMHGA 80
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISVSSQGESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 81 TLLDSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLRF 158
Cdd:cd07773 81 VPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEElyRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 159 RMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVvagggdnaag 237
Cdd:cd07773 161 RLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAgTPV---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 238 avgV-------------GMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVH--SFCHALPGKWHLMSVMLSAASCLDWAA 302
Cdd:cd07773 231 ---VvgghdhlcaalgaGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGglSYGHHVPGGYYYLAGSLPGGALLEWFR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 303 KLTGMADVPALIAAAQQADDTAGA--VWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVV 380
Cdd:cd07773 308 DLFGGDESDLAAADELAEAAPPGPtgLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 550766384 381 HDCGLTPSSITLIGGGARSSYWRQMLSDISGLQLdYRTGGDVGPALGAARLAQIALN 437
Cdd:cd07773 388 EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPI-EVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
1-476 |
5.15e-110 |
|
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: 334.14 E-value: 5.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLRDVKALGIAGQMHGA 80
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 81 TLLDSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLRF 158
Cdd:cd07770 81 LGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSElyRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYLLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 159 RMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDNAAG 237
Cdd:cd07770 161 RLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAgTPVVLGASDGALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 238 AVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVhsFCHALPGKWHLMSVMLS-AASCLDWAAK--LTGMADVPALI 314
Cdd:cd07770 241 NLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRL--WCYRLDENRWLVGGAINnGGNVLDWLRDtlLLSGDDYEELD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 315 AAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDCGLTPSSITLIG 394
Cdd:cd07770 319 KLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAGPVKEIRASG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 395 GGARSSYWRQMLSDISGLQLDYRTGGDvGPALGAARLAQIALNRDKpLPQLLPQLPLEQQHRPDAKNHARYAERRDVFRK 474
Cdd:cd07770 399 GFLRSPLWLQILADVLGRPVLVPEEEE-ASALGAALLALEALGLIS-SLEADELVKIGKVVEPDPENHAIYAELYERFKK 476
|
..
gi 550766384 475 IY 476
Cdd:cd07770 477 LY 478
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
2-436 |
5.55e-104 |
|
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: 317.57 E-value: 5.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLR--DVKALGIAGQMHG 79
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDpsDIAGVGVTGHGNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 80 ATLLDSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLR 157
Cdd:cd07802 82 LYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKvyPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 158 FRMTGDFASDMSDaAGTMWLDVAKRDWSEAMLDACQLT--RDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDN 234
Cdd:cd07802 162 YRLTGEISTDYTD-AGSSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEgTPVAAGAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 235 AAGAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSfCHALPGKWHLMSVMLSAASCLDWA-------AKLTGM 307
Cdd:cd07802 241 VASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNS-LHADPGLYLIVEASPTSASNLDWFldtllgeEKEAGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 308 ADVPALIAAAQQADDTAGAVWFLPYLSGERTphnNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDCGlTP 387
Cdd:cd07802 320 SDYDELDELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR-KP 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 550766384 388 SSITLIGGGARSSYWRQMLSDISGLQLDYRTGGDVGpALGAARLAQIAL 436
Cdd:cd07802 396 ETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELG-ALGAAICAAVAA 443
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
1-227 |
4.86e-100 |
|
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: 300.41 E-value: 4.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQH--SLRDVKALGIAGQMH 78
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLgiSLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQHRVLRPAILWNDGRCAEECAILEE--RVPASREITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYL 156
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550766384 157 RFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPV 227
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEgVPV 232
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
1-436 |
7.51e-99 |
|
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: 303.76 E-value: 7.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLRDVKALGIAGQMHGA 80
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 81 TLLDSQHRVLRPAILWNDGRCAEECAILEERVPASREITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLRFRM 160
Cdd:cd07783 81 VLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 161 TGDF-ASDMSDAAgTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDNAAGA 238
Cdd:cd07783 161 TGDRgVTDYNNAL-KLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAgTPVVAGTTDSIAAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 239 VGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALpGKWhlmsvMLSAAS-----CLDWAAKLTGMADVPAL 313
Cdd:cd07783 240 LASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGD-GYW-----LVGGASntggaVLRWFFSDDELAELSAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 314 IaaaqqADDTAGAVWFLPY-LSGERTPHNNPEAKGVFfgLTHQHGPAELARAVLEGVGYALADGMDVVHDCGLTP-SSIT 391
Cdd:cd07783 314 A-----DPPGPSGLIYYPLpLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLEELGAPPvEEVR 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 550766384 392 LIGGGARSSYWRQMLSDISGLQLdyRTGGDVGPALGAARLAQIAL 436
Cdd:cd07783 387 TAGGGARNDLWNQIRADVLGVPV--VIAEEEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
1-436 |
1.24e-93 |
|
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: 290.57 E-value: 1.24e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLR--DVKALGIAGQmh 78
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDpeDIAAIGLTSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GAT--LLDSQHRVLRPAILWNDGRcaeecaileervpasreitgnlmmpgftapkllwvqrhepeifrqVAKVLLPKDYL 156
Cdd:cd07779 79 RSTfvPVDEDGRPLRPAISWQDKR---------------------------------------------TAKFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 157 RFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVvagggdna 235
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEgTPV-------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 236 agavgV-------------GMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSVMLSAASCLDW-- 300
Cdd:cd07779 186 -----VagggdqqcaalgaGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWfr 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 301 --------AAKLTGM----------ADVPAliaaaqqaddtaGA--VWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAE 360
Cdd:cd07779 261 defgqdevAEKELGVspyellneeaAKSPP------------GSdgLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAH 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 361 LARAVLEGVGYALADGMDVVHDCGLTPSSITLIGGGARSSYWRQMLSDISGLQL----DYRTGgdvgpALGAARLAQIAL 436
Cdd:cd07779 329 LARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVerpeTSEAT-----ALGAAILAAVGA 403
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
1-436 |
6.99e-93 |
|
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: 289.14 E-value: 6.99e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLR--DVKALGIAGQMH 78
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLpdRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYL 156
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAvfEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 157 RFRMTGDFASDMSDAAGTmWLDVAKRDWSEAMLDACQLT--RDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGD 233
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAgTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 234 NAAGAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKW-HLMSVMlSAASCLDWAAKL-------- 304
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWlRAMANM-AGTPNLDWFLRElgevlkeg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 305 ---TGMADVPALIAAAQQADDTAGAVWFLPYLS--GERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALAdgmdv 379
Cdd:cd24121 319 aepAGSDLFQDLEELAASSPPGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMR----- 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550766384 380 vhDC----GLTPSSITLIGGGARSSYWRQMLSDISGLQLDYRTGGDVGpALGAARLAQIAL 436
Cdd:cd24121 394 --DCyehmGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFG-ARGAAMNAAVAL 451
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
2-479 |
1.20e-53 |
|
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: 187.74 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIGIDLGTSGVKAILL-SEQGDVLATQTE--KLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQH--SLRDVKALGIAGQ 76
Cdd:cd07781 2 VIGIDFGTQSVRAGLVdLADGEELASAVVpyPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAgvDPEDVVGIGVDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 77 mhGATLL--DSQHRVLRPAILWNDGRCAEECAILEERvpASREITGNLMMPGFT------APKLLWVQRHEPEIFRQVAK 148
Cdd:cd07781 82 --SSTVVpvDEDGNPLAPAILWMDHRAQEEAAEINET--AHPALEYYLAYYGGVyssewmWPKALWLKRNAPEVYDAAYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 149 VLLPKDYLRFRMTGDFASDMSdAAGTMWL-DVAKRDWSEAMLDACQL----TRDHMPALFEGSD-ITGALQPSVAERWNM 222
Cdd:cd07781 158 IVEACDWINARLTGRWVRSRC-AAGHKWMyNEWGGGPPREFLAALDPgllkLREKLPGEVVPVGePAGTLTAEAAERLGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 223 PA-VPVVAGGGDNAAGAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNP------ESAVHsfchalPGKWHLMSVMLSAA 295
Cdd:cd07781 237 PAgIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDIPgicgpvPDAVV------PGLYGLEAGQSAVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 296 SCLDWAAKL-------TGMADVPALIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEG 368
Cdd:cd07781 311 DIFAWFVRLfvppaeeRGDSIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 369 VGYALADGMDVVHDCGLTPSSITLIGGGA-RSSYWRQMLSDISGLQLdYRTGGDVGPALGAARLAQIALNR-DKPLPQLL 446
Cdd:cd07781 391 TAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPI-KVPKSDQAPALGAAILAAVAAGVyADIEEAAD 469
|
490 500 510
....*....|....*....|....*....|...
gi 550766384 447 PQLPLEQQHRPDAKNHARYAERRDVFRKIYQQL 479
Cdd:cd07781 470 AMVRVDRVYEPDPENHAVYEELYALYKELYDAL 502
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
2-437 |
7.63e-53 |
|
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: 184.35 E-value: 7.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRP--QPLWSEQDPEQWWQATDRAMK-ALGE-QHSLRDVKALGIAGQM 77
Cdd:cd07798 2 YLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIReALKKaGISPEDISAVSSTSQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 78 HGATLLDSQHRVLR--PAIlwnDGRCAEECAIL-EERVPASREITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKD 154
Cdd:cd07798 82 EGIVFLDKDGRELYagPNI---DARGVEEAAEIdDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIATVLSISD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 155 YLRFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGD 233
Cdd:cd07798 159 WIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEgTPVVVGGAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 234 NAAGAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSVMLSAASCLDWAAKL--TGMADVP 311
Cdd:cd07798 239 TQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVLESNAGVTGLNYQWLKELlyGDPEDSY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 312 ALI--AAAQQADDTAGAVWFLpylsGERTPH--NNPEAKGVFFG---LTHQH-GPAELARAVLEGVGYALADGMD-VVHD 382
Cdd:cd07798 319 EVLeeEASEIPPGANGVLAFL----GPQIFDarLSGLKNGGFLFptpLSASElTRGDFARAILENIAFAIRANLEqLEEV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 550766384 383 CGLTPSSITLIGGGARSSYWRQMLSDISGLQLdYRTGGDVGPALGAARLAQIALN 437
Cdd:cd07798 395 SGREIPYIILCGGGSRSALLCQILADVLGKPV-LVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
2-436 |
3.12e-44 |
|
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: 162.35 E-value: 3.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YI-GIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMK-AL-GEQHSLRDVKALGIAGQMH 78
Cdd:cd07793 1 YIlAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKeALkNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQ-HRVLRPAILWNDGRCAEECAILEE-------RVPA---------SREITGNLM--MPGFTAPKLLWVQRHE 139
Cdd:cd07793 81 TFLTWDKKtGKPLHNFITWQDLRAAELCESWNRslllkalRGGSkflhfltrnKRFLAASVLkfSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 140 PEifrqvAKVLLPKDYLRF---------RMTGD--FASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDI 208
Cdd:cd07793 161 PE-----LKEAAEKGELLFgtidtwllwKLTGGkvHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 209 TGALQPSV--AErwnmpaVPVVAGGGDNAAGAVGVGMVETGQAMLSLGTsGVYFAVsdgyrsNPESAVHSFCHAL-P--G 283
Cdd:cd07793 236 FGSTDPSIfgAE------IPITAVVADQQAALFGECCFDKGDVKITMGT-GTFIDI------NTGSKPHASVKGLyPlvG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 284 kWHLMS--------VMLSAASCLDWAaKLTGMADVPALIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQ 355
Cdd:cd07793 303 -WKIGGeitylaegNASDTGTVIDWA-KSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 356 HGPAELARAVLEGVGYALADGMDVVH-DCGLTPSSITLIGGGARSSYWRQMLSDISGLQLDYRTGGDVGpALGAARLAQI 434
Cdd:cd07793 381 TTKAHLVRAILESIAFRVKQLLETMEkETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMS-ALGAAFLAGL 459
|
..
gi 550766384 435 AL 436
Cdd:cd07793 460 AS 461
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
2-436 |
4.69e-43 |
|
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: 158.78 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIG-IDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSL--RDVKALGIAGQMH 78
Cdd:cd07769 1 YILaIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGIsaSDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQ-HRVLRPAILWNDGRCAEECAILEERVPAS--REITGNLMMPGFTAPKLLWVQRHEPEifrqvAKVLLPKDY 155
Cdd:cd07769 81 TTVVWDKKtGKPLYNAIVWQDRRTADICEELKAKGLEEriREKTGLPLDPYFSATKIKWILDNVPG-----ARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 156 LRF---------RMTGD--FASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERwnmpA 224
Cdd:cd07769 156 LLFgtidtwliwKLTGGkvHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLGA----G 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 225 VPVvagggdnaagavgVGMV-------------ETGQAMLSLGTsGVYFAVSDGyrsnpESAVHS--------------- 276
Cdd:cd07769 232 IPI-------------AGILgdqqaalfgqgcfEPGMAKNTYGT-GCFLLMNTG-----EKPVPSkngllttiawqiggk 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 277 FCHALPGkwhlmSVMlSAASCLDWAAKLTGMADVPALIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQH 356
Cdd:cd07769 293 VTYALEG-----SIF-IAGAAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 357 GPAELARAVLEGVGYALADGMDVVH-DCGLTPSSITLIGGGARSSYWRQMLSDISGLQLdyrtggdVGP------ALGAA 429
Cdd:cd07769 367 TKAHIVRAALESIAYQTRDVLEAMEkDSGIKLKELRVDGGATANNFLMQFQADILGVPV-------VRPkvaettALGAA 439
|
....*..
gi 550766384 430 RLAQIAL 436
Cdd:cd07769 440 YLAGLAV 446
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
2-437 |
2.03e-38 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 146.27 E-value: 2.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIG-IDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAM----KALGEQHSLRDVKALGIAGQ 76
Cdd:PTZ00294 3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMneaiKKLREKGPSFKIKAIGITNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 77 MHGATLLDSQH-RVLRPAILWNDGRCAEECAILEERVPAS---REITGNLMMPGFTAPKLLWVQRHEPEI----FRQVAK 148
Cdd:PTZ00294 83 RETVVAWDKVTgKPLYNAIVWLDTRTYDIVNELTKKYGGSnffQKITGLPISTYFSAFKIRWMLENVPAVkdavKEGTLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 149 VLLPKDYLRFRMTGD--FASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQpSVAERWNMPaVP 226
Cdd:PTZ00294 163 FGTIDTWLIWNLTGGksHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTIS-GEAVPLLEG-VP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 227 VVAGGGDNAAGAVGVGMVETGQAMLSLGTsGVYFAVSDG---------------YRSNPESavhSFCHALPGkwhlmSVM 291
Cdd:PTZ00294 241 ITGCIGDQQAALIGHGCFEKGDAKNTYGT-GCFLLMNTGteivfskhgllttvcYQLGPNG---PTVYALEG-----SIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 292 lSAASCLDWAAKLTGMADVPALIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGY 371
Cdd:PTZ00294 312 -VAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIAL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 372 ALAdgmDVVH----DCGLTPSSITLIGGGARSSYWRQMLSDISGLQLdYRTGGDVGPALGAARLAQIALN 437
Cdd:PTZ00294 391 QTN---DVIEsmekDAGIELNSLRVDGGLTKNKLLMQFQADILGKDI-VVPEMAETTALGAALLAGLAVG 456
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
1-432 |
7.80e-37 |
|
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: 140.82 E-value: 7.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILL-SEQGDVLATQTEKLQVSRPQ--PLWSEQDPEQWWQATDRAMKALGEqHSLRDVKALGIAGQM 77
Cdd:cd07777 1 NVLGIDIGTTSIKAALLdLESGRILESVSRPTPAPISSddPGRSEQDPEKILEAVRNLIDELPR-EYLSDVTGIGITGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 78 HGATLLDSQHRVLRPAILWNDGRCAEECAI-LEERVPASREITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPkDYL 156
Cdd:cd07777 80 HGIVLWDEDGNPVSPLITWQDQRCSEEFLGgLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGPLPSKADRAGTIG-DYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 157 RFRMTGDF--ASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAErwnmpAVPVvagggdn 234
Cdd:cd07777 159 VARLTGLPkpVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPK-----GIPV------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 235 aagavGVGM------------VETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHalpGKWhlmsvmLSAASCL---- 298
Cdd:cd07777 227 -----YVALgdnqasvlgsglNEENDAVLNIGTGAQLSFLTPKFELSGSVEIRPFFD---GRY------LLVAASLpggr 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 299 ----------DWAAKLTGMADVPAL--IAAAQQADDTAGAVWFLPYLSGERTphnNPEAKGVFFGLTHQH-GPAELARAV 365
Cdd:cd07777 293 alavlvdflrEWLRELGGSLSDDEIweKLDELAESEESSDLSVDPTFFGERH---DPEGRGSITNIGESNfTLGNLFRAL 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550766384 366 LEGVGYALADGMDVVHDCGLTPSSITLIGGGARSSYW-RQMLSDISGLQLDYRTGGDvGPALGAARLA 432
Cdd:cd07777 370 CRGIAENLHEMLPRLDLDLSGIERIVGSGGALRKNPVlRRIIEKRFGLPVVLSEGSE-EAAVGAALLA 436
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
2-435 |
1.11e-33 |
|
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: 132.61 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YI-GIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLR--DVKALGIAGQMH 78
Cdd:cd07786 1 YIlAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRasDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQH-RVLRPAILWNDGRCAEECAIL-----EERVpasREITGNLMMPGFTAPKLLWVQRHEPEIFRQVAK---- 148
Cdd:cd07786 81 TTVVWDRETgKPVYNAIVWQDRRTADICEELkaeghEEMI---REKTGLVLDPYFSATKIRWILDNVPGARERAERgela 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 149 ---VllpkD-YLRFRMTGD--FASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERwnm 222
Cdd:cd07786 158 fgtI----DsWLIWKLTGGkvHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLGA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 223 pAVPVVagggdnaagavgvGMV-------------ETGQAMLSLGTS-------GVYFAVSD-------GYRSNPESavh 275
Cdd:cd07786 231 -EIPIA-------------GIAgdqqaalfgqacfEPGMAKNTYGTGcfmlmntGEKPVRSKngllttiAWQLGGKV--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 276 sfCHALPGkwhlmSVMlSAASCLDW----------AAKLTGMAD-VPaliaaaqqaddTAGAVWFLPYLSGERTPHNNPE 344
Cdd:cd07786 294 --TYALEG-----SIF-IAGAAVQWlrdglgliesAAETEALARsVP-----------DNGGVYFVPAFTGLGAPYWDPD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 345 AKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVH-DCGLTPSSITLIGGGARSSYWRQMLSDISGLQLdyrtggdVG 423
Cdd:cd07786 355 ARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEaDSGIPLKELRVDGGASANDFLMQFQADILGVPV-------ER 427
|
490
....*....|....*...
gi 550766384 424 P------ALGAARLAQIA 435
Cdd:cd07786 428 PkvtettALGAAYLAGLA 445
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
2-436 |
1.22e-32 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 129.80 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIG-IDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMK-ALGEQH-SLRDVKALGIAGQMH 78
Cdd:COG0554 4 YILaIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIReALAKAGiSAEDIAAIGITNQRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 79 GATLLDSQH-RVLRPAILWNDGRCAEECA-----ILEERVpasREITGNLMMPGFTAPKLLWVQRHEPEIfRQVAKvllp 152
Cdd:COG0554 84 TTVVWDRKTgKPLYNAIVWQDRRTADICEelkadGLEDLI---REKTGLVLDPYFSATKIKWILDNVPGA-RERAE---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 153 KDYLRF---------RMTGD--FASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERwn 221
Cdd:COG0554 156 AGELLFgtidswliwKLTGGkvHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGA-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 222 mpAVPVVagggdnaagavgvGMV-------------ETGQA----------MLSLGTSGVyfaVSD-------GYRSNPE 271
Cdd:COG0554 234 --EIPIA-------------GIAgdqqaalfgqacfEPGMAkntygtgcflLMNTGDEPV---RSKngllttiAWGLGGK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 272 SavhsfCHALPGkwhlmsVMLSAASCLDWAAKLTGMADVPALIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFG 351
Cdd:COG0554 296 V-----TYALEG------SIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 352 LTHQHGPAELARAVLEGVGYALADGMDVVH-DCGLTPSSITLIGGGARSSYWRQMLSDISGLQLDyRtggdvgP------ 424
Cdd:COG0554 365 LTRGTTRAHIARAALESIAYQTRDVLDAMEaDSGIPLKELRVDGGASANDLLMQFQADILGVPVE-R------Pkvtett 437
|
490
....*....|..
gi 550766384 425 ALGAARLAQIAL 436
Cdd:COG0554 438 ALGAAYLAGLAV 449
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
2-437 |
5.30e-32 |
|
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: 128.03 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIG-IDLGTSGVKAILLSEQGDVLAT-QTEKLQVSrPQPLWSEQDPEQWWQAT----DRAMKALGEQ-HSLRDVKALGIA 74
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVAShQVEHKQIY-PKPGWVEHDPMEILESVyeciEEAVEKLKALgISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 75 GQMHGATLLDSQHRV-LRPAILWNDGRCAEECAILEERVPAS----REITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKv 149
Cdd:cd07792 81 NQRETTVVWDKSTGKpLYNAIVWLDTRTSDTVEELSAKTPGGkdhfRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 150 llpkDYLRF---------RMTG-----DFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGalqpS 215
Cdd:cd07792 160 ----GRLLFgtvdswliwNLTGgknggVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYG----K 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 216 VAERWnMPAVPVVagggdnaagavgvGMV-------------ETGQAMLSLGTsGVYF--------AVSD-------GYR 267
Cdd:cd07792 232 IASGP-LAGVPIS-------------GCLgdqqaalvgqgcfKPGEAKNTYGT-GCFLlyntgeepVFSKhgllttvAYK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 268 SNPESAVHsfcHALPGkwhlmSVMLsAASCLDWAAKLTGMADVPALIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKG 347
Cdd:cd07792 297 LGPDAPPV---YALEG-----SIAI-AGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 348 VFFGLTHQHGPAELARAVLEGVGYALADGMDVVH-DCGLTPSSITLIGGGARSSYWRQMLSDISGLQLdyrtggdVGP-- 424
Cdd:cd07792 368 TIVGLTQFTTKAHIARAALEAVCFQTREILDAMNkDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPV-------ERPsm 440
|
490
....*....|....*..
gi 550766384 425 ----ALGAARLAQIALN 437
Cdd:cd07792 441 vettALGAAIAAGLAVG 457
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
2-467 |
1.32e-30 |
|
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: 123.98 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIGIDLGTSGVKAILLSEQGDVLA-TQTEKLQVSRPQ-PLWSEQDPEQWWQATDRAMKALGEQHSL--RDVKALGIAGQM 77
Cdd:cd07775 2 LLALDAGTGSGRAVIFDLEGNQIAvAQREWRHKEVPDvPGSMDFDTEKNWKLICECIREALKKAGIapKSIAAISTTSMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 78 HGATLLDSQHRVLrpailWN----DGRCAEECAILEERVPASRE----ITGNLMMPGfTAPKLLWVQRHEPEIFRQVAKV 149
Cdd:cd07775 82 EGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTLEEevyrISGQTFALG-AIPRLLWLKNNRPEIYRKAAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 150 LLPKDYLRFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNM-PAVPVV 228
Cdd:cd07775 156 TMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLkEGTPVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 229 AGGGDNAAGAVGVGMVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSFCHALPGKWHLMSV------------------ 290
Cdd:cd07775 236 VGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIPDMWQAEGIsffpglvmrwfrdafcae 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 291 --MLSAASCLDWAAKLTGMA-DVPAliaaaqqaddtaGAVWFLPYLSGERTPHNNPEAKGVFFGLT---HQHGPAELARA 364
Cdd:cd07775 316 ekEIAERLGIDAYDLLEEMAkDVPP------------GSYGIMPIFSDVMNYKNWRHAAPSFLNLDidpEKCNKATFFRA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 365 VLEGVGYALADGMDVVHDC-GLTPSSITLIGGGARSSYWRQMLSDISGLQLdyrTGGDV--GPALGAARLAQIALNRDKP 441
Cdd:cd07775 384 IMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPV---KVPVVkeATALGAAIAAGVGAGIYSS 460
|
490 500
....*....|....*....|....*..
gi 550766384 442 LPQLLPQLPL-EQQHRPDAKNHARYAE 467
Cdd:cd07775 461 LEEAVESLVKwEREYLPNPENHEVYQD 487
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
6-415 |
1.68e-30 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 123.60 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 6 DLGTSGVKAILLSEQGDVLATQTEK--LQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLRDVKALGIAGQMHGATLL 83
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnaSDIAAENSDWHQWSLDAILQRFADCCRQINSELTECHIRGITVTTFGVDGALV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 84 DSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLRFRMT 161
Cdd:PRK10331 88 DKQGNLLYPIISWKCPRTAAVMENIERYISAQQlqQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLFISSLINHRLT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 162 GDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGGGDNAAGAVG 240
Cdd:PRK10331 168 GEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVgIPVISAGHDTQFALFG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 241 VGmVETGQAMLSLGTSGVYFAVSdgyrSNPESAVHSFCHAL------------PG-KWhlmsvmlSAASCLDWAAKL--T 305
Cdd:PRK10331 248 SG-AGQNQPVLSSGTWEILMVRS----AQVDTSLLSQYAGStceldsqsglynPGmQW-------LASGVLEWVRKLfwT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 306 GMADVPALIAAAQQADDTAGAVWFLPYLSGERTphnnpeakGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHD-CG 384
Cdd:PRK10331 316 AETPYQTMIEEARAIPPGADGVKMQCDLLACQN--------AGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKiGH 387
|
410 420 430
....*....|....*....|....*....|.
gi 550766384 385 LTPSSITLIGGGARSSYWRQMLSDISGLQLD 415
Cdd:PRK10331 388 FKASELLLVGGGSRNALWNQIKANMLDIPIK 418
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
249-436 |
1.35e-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: 108.95 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 249 AMLSLGTSGVYFAVSdgyrSNPESAVHSFCH-----ALPGKWHLMSVMLSAASCLDWAAKLTGMADV--------PALIA 315
Cdd:pfam02782 1 LAISAGTSSFVLVET----PEPVLSVHGVWGpytneMLPGYWGLEGGQSAAGSLLAWLLQFHGLREElrdagnveSLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 316 AAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDC-GLTPSSITLIG 394
Cdd:pfam02782 77 AALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQeGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 550766384 395 GGARSSYWRQMLSDISGLQLdYRTGGDVGPALGAARLAQIAL 436
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPV-VVPGPDEATALGAALLAAVAA 197
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
2-437 |
1.70e-27 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 115.18 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIG-IDLGTSGVKAILLSEQGDVLAT-QTEKLQVSrPQPLWSEQDPEQWWQATDRAMKALGEQHSLR------DVKALGI 73
Cdd:PLN02295 1 FVGaIDQGTTSTRFIIYDRDARPVAShQVEFTQIY-PQAGWVEHDPMEILESVLTCIAKALEKAAAKghnvdsGLKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 74 AGQMHgATLL--DSQHRVLRPAILWNDGRCAEECAILEERVPAS----REITGNLMMPGFTAPKLLWVQRHEPeifrQVA 147
Cdd:PLN02295 80 TNQRE-TTVAwsKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGrkhfVETCGLPISTYFSATKLLWLLENVD----AVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 148 KVLLPKD--------YLRFRMTGD-----FASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGalqp 214
Cdd:PLN02295 155 EAVKSGDalfgtidsWLIWNLTGGasggvHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 215 SVAERWNMPAVPVVAGGGDNAAGAvgVGM-VETGQAMLSLGTsGVYFAVSDG---------------YRSNPESAVhsfC 278
Cdd:PLN02295 231 TIAKGWPLAGVPIAGCLGDQHAAM--LGQrCRPGEAKSTYGT-GCFILLNTGeevvpskhgllttvaYKLGPDAPT---N 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 279 HALPGkwhlmSVMLSAAScLDWAAKLTGMADVPALIAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLTHQHGP 358
Cdd:PLN02295 305 YALEG-----SVAIAGAA-VQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 359 AELARAVLEGVGYALADGMDVVH-DCGLTPSSITLI-----GGGARSSYWRQMLSDISGLQL----DYRTggdvgPALGA 428
Cdd:PLN02295 379 AHIARAVLESMCFQVKDVLDAMRkDAGEEKSHKGLFllrvdGGATANNLLMQIQADLLGSPVvrpaDIET-----TALGA 453
|
....*....
gi 550766384 429 ARLAQIALN 437
Cdd:PLN02295 454 AYAAGLAVG 462
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
5-482 |
3.37e-25 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 108.55 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 5 IDLGTSGVKAILLSEQGDVLAT-QTEKLQVSRPQ-PLWSEQDPEQWWQATDRAMK-ALGE-QHSLRDVKALGIAGQMHGA 80
Cdd:PRK10939 8 LDAGTGSIRAVIFDLNGNQIAVgQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIRqALQKaGIPASDIAAVSATSMREGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 81 TLLDSQHRVLrpailWN----DGRCAEECAILEERVPASRE----ITGNLMMPGfTAPKLLWVQRHEPEIFRQVAKVLLP 152
Cdd:PRK10939 88 VLYDRNGTEI-----WAcanvDARASREVSELKELHNNFEEevyrCSGQTLALG-ALPRLLWLAHHRPDIYRQAHTITMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 153 KDYLRFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPA-VPVVAGG 231
Cdd:PRK10939 162 SDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLRAgTPVVMGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 232 GDNAAGAVGVGMVETGQAMLSLGT-----SGVYFAVSDgyrsnPESAVHSFCHALPGKWHLMS-------VM-------- 291
Cdd:PRK10939 242 GDVQLGCLGLGVVRPGQTAVLGGTfwqqvVNLPAPVTD-----PNMNIRINPHVIPGMVQAESisfftglTMrwfrdafc 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 292 -----LSAASCLDWAAKLTGMA-DVPAliaaaqqaddtaGAVWFLPYLSGERTPHNNPEAKGVFFGLT---HQHGPAELA 362
Cdd:PRK10939 317 aeeklLAERLGIDAYSLLEEMAsRVPV------------GSHGIIPIFSDVMRFKSWYHAAPSFINLSidpEKCNKATLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 363 RAVLEGVGYALADGMDVVHD-CGLTPSSITLIGGGARSSYWRQMLSDISGLQLDYRT-------GGDVGPALGAARLAQI 434
Cdd:PRK10939 385 RALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVvkeatalGCAIAAGVGAGIYSSL 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 550766384 435 ALNRDKplpqllpQLPLEQQHRPDAKNHARYAERRDVFRKIYQQLLPL 482
Cdd:PRK10939 465 AETGER-------LVRWERTFEPNPENHELYQEAKEKWQAVYADQLGL 505
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
2-413 |
1.34e-22 |
|
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: 100.30 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIGIDLGTSGVKAILLSEQGDVLATQTeklqVSR-PQPLWSEQDPEQW-----WQATDRAMKALGEQHslRDVKALGIA- 74
Cdd:cd07771 2 YLAVDLGASSGRVILGSLDGGKLELEE----IHRfPNRPVEINGHLYWdidrlFDEIKEGLKKAAEQG--GDIDSIGIDt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 75 -GQMHGatLLDSQHRVLRPAILWNDGRCAEECAILEERVPASR--EITGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLL 151
Cdd:cd07771 76 wGVDFG--LLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEElyERTGIQFQPINTLYQLYALKKEGPELLERADKLLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 152 PKDYLRFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSVAERWNMPAVPVvagg 231
Cdd:cd07771 154 LPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLKGIPV---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 232 gdnaagaVGVG------------MVETGQAMLSLGTSGVYFAVSDGYRSNPESAVHSF---CHA---------LPGKW-- 285
Cdd:cd07771 230 -------IAVAshdtasavaavpAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGFtneGGAdgtirllknITGLWll 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 286 -HLMSVMLSAASCLDWaAKLTGMA----DVPALIaaaqqaddtagavwflpYLSGER--TPHNNPEAKGVFFGLTHQ--- 355
Cdd:cd07771 303 qECRREWEEEGKDYSY-DELVALAeeapPFGAFI-----------------DPDDPRflNPGDMPEAIRAYCRETGQpvp 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 550766384 356 HGPAELARAVLEGVGYALADGMDVVHDC-GLTPSSITLIGGGARSSYWRQMLSDISGLQ 413
Cdd:cd07771 365 ESPGEIARCIYESLALKYAKTIEELEELtGKRIDRIHIVGGGSRNALLCQLTADATGLP 423
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
1-467 |
4.03e-22 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 99.17 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQ------------PLWSEQDPEQWWQATDRA---MKALGEQhsL 65
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEygtkggvhrdgdGGEVTSPVLMWVEALDLLlekLKAAGFD--F 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 66 RDVKALGIAGQMHG------------ATLLDSQ--HRVLRPA-------IlWNDGRCAEECAILEERVP---ASREITGN 121
Cdd:cd07776 79 SRVKAISGSGQQHGsvywskgaesalANLDPSKslAEQLEGAfsvpdspI-WMDSSTTKQCRELEKAVGgpeALAKLTGS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 122 LMMPGFTAPKLLWVQRHEPEIFRQVAKV---------LLpkdylrfrmTGDFAS-DMSDAAGTMWLDVAKRDWSEAMLDA 191
Cdd:cd07776 158 RAYERFTGPQIAKIAQTDPEAYENTERIslvssflasLL---------LGRYAPiDESDGSGMNLMDIRSRKWSPELLDA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 192 C---QLtRDHMPALFEGSDITGALQPSVAERW--------------NmPAvpvvagggdnaagaVGVGM-VETGQAMLSL 253
Cdd:cd07776 229 AtapDL-KEKLGELVPSSTVAGGISSYFVERYgfspdclvvaftgdN-PA--------------SLAGLgLEPGDVAVSL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 254 GTSGVYFAVSDGYRSNPESavHSFCH-ALPGkwHLMSvML-------------SAASCLDWA--AKLtgMADVPAliaaa 317
Cdd:cd07776 293 GTSDTVFLVLDEPKPGPEG--HVFANpVDPG--SYMA-MLcykngslarervrDRYAGGSWEkfNEL--LESTPP----- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 318 qqaddTAGAVWFLPYLSGERTPHnnpeAKGVFFGLTHQHG------PAELARAVLEgvGYALAdgMdVVHDCGLT----P 387
Cdd:cd07776 361 -----GNNGNLGLYFDEPEITPP----VPGGGRRFFGDDGvdaffdPAVEVRAVVE--SQFLS--M-RLHAERLGsdipP 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 388 SSITLIGGGARSSYWRQMLSDIsgLQLD-YRTGGDVGPALGAARLAQIALNRDKPLPQLLPQLPLEQQH-----RPDAKN 461
Cdd:cd07776 427 TRILATGGASANKAILQVLADV--FGAPvYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAEEpklvaEPDPEA 504
|
....*.
gi 550766384 462 HARYAE 467
Cdd:cd07776 505 AEVYDK 510
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-435 |
6.36e-19 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 89.11 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIG-IDLGTSGVKAILLSEQGDVLAT-QTEKLQVSrPQPLWSEQDPEQWWQATDRAMK-ALGEQH-SLRDVKALGIAGQM 77
Cdd:PRK00047 6 YILaLDQGTTSSRAIIFDHDGNIVSVaQKEFTQIF-PQPGWVEHDPNEIWASQLSVIAeALAKAGiSPDQIAAIGITNQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 78 HGATLLDSQHRvlRP---AILWNDGRCAEECAILEE--RVPASREITGNLMMPGFTAPKLLWVQRHEPEIfRQVAKvllp 152
Cdd:PRK00047 85 ETTVVWDKETG--RPiynAIVWQDRRTADICEELKRdgYEDYIREKTGLVIDPYFSGTKIKWILDNVEGA-RERAE---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 153 KDYLRF---------RMTGD--FASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDITGALQPSvaeRWN 221
Cdd:PRK00047 158 KGELLFgtidtwlvwKLTGGkvHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPY---GFF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 222 MPAVPVVagggdnaagavgvGM-------------VETGQAMLSLGTsGVYFAVSDGyrsnpESAVHS------------ 276
Cdd:PRK00047 235 GGEVPIA-------------GIagdqqaalfgqlcFEPGMAKNTYGT-GCFMLMNTG-----EKAVKSengllttiawgi 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 277 ---FCHALPG---------KWhL---MSVMLSAASCLDWAAKLTgmadvpaliaaaqqaddTAGAVWFLPYLSGERTPHN 341
Cdd:PRK00047 296 dgkVVYALEGsifvagsaiQW-LrdgLKIISDASDSEALARKVE-----------------DNDGVYVVPAFTGLGAPYW 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 342 NPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMD-VVHDCGLTPSSITLIGGGARSSYWRQMLSDISGLQLdyrtgg 420
Cdd:PRK00047 358 DSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDaMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPV------ 431
|
490 500
....*....|....*....|.
gi 550766384 421 dVGP------ALGAARLAQIA 435
Cdd:PRK00047 432 -ERPvvaettALGAAYLAGLA 451
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
2-435 |
3.72e-18 |
|
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: 86.91 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIGIDLGTSGVKAILLS-EQGDVLATQ-TEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQHSLR--DVKALGIA--- 74
Cdd:cd07768 2 GIGVDVGTSSARAGVYDlYAGLEMAQEpVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDayEVKGCGVDatc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 75 --------GQMHGATLLDSQHRVLrpaILWNDGRCAEEC-AILEERVPASREITGNLMMPGFTAPKLLWVQRHEPEIFRQ 145
Cdd:cd07768 82 slaifdreGTPLMALIPYPNEDNV---IFWMDHSAVNEAqWINMQCPQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 146 VAKVLLPKDYLRFRMTGDFASDMSDAAGTMWLDVAKRDWSEAMLDACQLTRDHMPALFEGSDI------TGALQPSVAER 219
Cdd:cd07768 159 HFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLEHLTTTKNLPSNvpigttSGVALPEMAEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 220 WNM-PAVPVVAGGGDNAAGAVGVGMVET-GQAMLSLGTSGVYFAVSDGYRSNP------ESAVhsfchaLPGKW------ 285
Cdd:cd07768 239 MGLhPGTAVVVSCIDAHASWFAVASPHLeTSLFMIAGTSSCHMYGTTISDRIPgvwgpfDTII------DPDYSvyeagq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 286 --------HLMSVMLSAASCLDwaAKLTGmADVPAL----IAAAQQADDTAGAVWFLPYLSGERTPHNNPEAKGVFFGLT 353
Cdd:cd07768 313 satgklieHLFESHPCARKFDE--ALKKG-ADIYQVleqtIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGES 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 354 HQHGPAELA---RAVLEGVGYALADGMDVVHDCGLTPSSITLIGGGARSSYWRQMLSDISGLQLdYRTGGDVGPALGAAR 430
Cdd:cd07768 390 LDTSMLNLTykyIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAI-IKPKENMMGILGAAV 468
|
....*
gi 550766384 431 LAQIA 435
Cdd:cd07768 469 LAKVA 473
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
2-412 |
1.43e-14 |
|
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: 76.03 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSEQDPEQWWQATDRAMKALGEQ--HSLRDVKALGIAgqmhg 79
Cdd:cd07782 2 YIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGagVDPEQVKGIGFD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 80 AT----LLDSQHRVL---------RPAILWNDGRCAEECaileERVPASRE----ITGNLMMPGFTAPKLLWVQRHEPEI 142
Cdd:cd07782 77 ATcslvVLDAEGKPVsvspsgddeRNVILWMDHRAVEEA----ERINATGHevlkYVGGKISPEMEPPKLLWLKENLPET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 143 FRQVAKVL-LPkDYLRFRMTGDFASDMSdaagTM---WLDVAKRD----WSEAML------DACQLTRDHMP--ALFEGS 206
Cdd:cd07782 153 WAKAGHFFdLP-DFLTWKATGSLTRSLC----SLvckWTYLAHEGseggWDDDFFkeigleDLVEDNFAKIGsvVLPPGE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 207 DITGALQPSVAErwNM---PAVPVVAG----------GGDNAAGAVGVGMVETGQAM-LSLGTSGVYFAVSdgyrSNP-- 270
Cdd:cd07782 228 PVGGGLTAEAAK--ELglpEGTPVGVSlidahagglgTLGADVGGLPCEADPLTRRLaLICGTSSCHMAVS----PEPvf 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 271 --------ESAVhsfchaLPGKW----------HLMSVML---SAASCLDWAAKLTGMADVPALIAAAQQADDTAGA--- 326
Cdd:cd07782 302 vpgvwgpyYSAM------LPGLWlneggqsatgALLDHIIethPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKGLpla 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 327 -----VWFLPYLSGERTPHNNPEAKGVFFGLTHQHGPAELAR---AVLEGVGYALADGMDVVHDCGLTPSSITLIGGGAR 398
Cdd:cd07782 376 yltrdLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSK 455
|
490
....*....|....
gi 550766384 399 SSYWRQMLSDISGL 412
Cdd:cd07782 456 NPLFVQLHADVTGC 469
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
5-227 |
5.20e-11 |
|
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: 64.59 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 5 IDLGTSGVKAILLSEQGDVLATQTEKLQVSrPQPLWSEQDPEQWWQAtdrAMKALGEQHSLRDVKALGIAGqmHGAT--L 82
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEI-EEDGYPCEDVEAIWEW---LLDSLAELAKRHRIDAINFTT--HGATfaL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 83 LDSQHRVLRPAI-LWNDGRCAEECAILEERVPasREITGNLMMPGFT--APKLLWVQRHEPEIFRQVAKVL-LPkDYLRF 158
Cdd:cd07772 79 LDENGELALPVYdYEKPIPDEINEAYYAERGP--FEETGSPPLPGGLnlGKQLYWLKREKPELFARAKTILpLP-QYWAW 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550766384 159 RMTGDFASDMSdAAGT---MWlDVAKRDWSeAMLDACQLTRdHMPALFEGSDITGALQPSVAERWNMP-AVPV 227
Cdd:cd07772 156 RLTGKAASEIT-SLGChtdLW-DFEKNEYS-SLVKKEGWDK-LFPPLRKAWEVLGPLRPDLARRTGLPkDIPV 224
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
1-191 |
7.48e-09 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 57.86 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVSRPQPLWSE---QDPEQ----------WWQATDRAMKALG-EQHSLR 66
Cdd:PLN02669 9 LFLGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHYGTKDgvyRDPKVngrivsptlmWVEALDLLLQKLAkEKFPFH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 67 DVKALGIAGQMHGA-----------TLLDSQHRV---LRPAI------LWNDGRCAEECAILEERVPASRE---ITGNLM 123
Cdd:PLN02669 89 KVVAISGSGQQHGSvywrkgasavlKSLDPSKSLvaqLQDAFstkdspIWMDSSTTKQCREIEEAVGGAAElskLTGSRA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550766384 124 MPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLRFRMTGDFAS-DMSDAAGTMWLDVAKRDWSEAMLDA 191
Cdd:PLN02669 169 YERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYASiDETDGAGMNLMDIEKRCWSKAALEA 237
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
2-164 |
2.75e-08 |
|
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: 56.26 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 2 YIGIDLGTSGVKAILLSEQGDVLATQTEKL-QVSRPQPLWS-EQDPEQWWQATDRAMKALGEQHSLRDVKALGIAgqmhg 79
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsYKQDPKDLWFvTQSSTEIWKAIKTALKELIEELSDYIVSGIGVS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 80 ATL------LDSQHRVLRP-------------AILWNDGRCAEECAILEERVPASREI-TGNLMMPGFTAPKLLWVQRHE 139
Cdd:cd07778 77 ATCsmvvmqRDSDTSYLVPynviheksnpdqdIIFWMDHRASEETQWLNNILPDDILDyLGGGFIPEMAIPKLKYLIDLI 156
|
170 180
....*....|....*....|....*
gi 550766384 140 PEIFRQVAKVLLPKDYLRFRMTGDF 164
Cdd:cd07778 157 KEDTFKKLEVFDLHDWISYMLATNL 181
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
330-479 |
1.59e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 50.61 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 330 LPYLSGERTPHNNPEAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHDCGLTPSSITLIGGGAR-SSYWRQMLSD 408
Cdd:PRK04123 382 LDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIARkNPVLMQIYAD 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550766384 409 ISGLQLDYRTgGDVGPALGAARLAQIA--LNRDKPLPQLLPQLPLEQQHRPDAKNHARYAERrdvFRKiYQQL 479
Cdd:PRK04123 462 VLNRPIQVVA-SDQCPALGAAIFAAVAagAYPDIPEAQQAMASPVEKTYQPDPENVARYEQL---YQE-YKQL 529
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
82-190 |
1.72e-06 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 50.49 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 82 LLDSQHRVLRPAILWNDGRCAEECAILEERVpASREI---TGNLMMPGFTAPKLLWVQRHEPEIFRQVAKVLLPKDYLRF 158
Cdd:PRK10640 70 LLDKQGQRVGLPVSYRDSRTDGVMAQAQQQL-GKRDIyrrSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSY 148
|
90 100 110
....*....|....*....|....*....|..
gi 550766384 159 RMTGDFASDMSDAAGTMWLDVAKRDWSEAMLD 190
Cdd:PRK10640 149 RLTGKMNWEYTNATTTQLVNINSDDWDESLLA 180
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-98 |
9.88e-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: 44.12 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766384 1 MYIGIDLGTSGVKAILLSEQGDVLATQTEKLQVsrpqplwsEQDPEQWWQATDRAMKALGEQH--SLRDVKALGIAgqMH 78
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTPA--------GAGPEAVLEAIAELIEELLAEAgiSRGRILGIGIG--VP 75
|
90 100
....*....|....*....|...
gi 550766384 79 GatLLDSQH-RVLRPAIL--WND 98
Cdd:COG1940 76 G--PVDPETgVVLNAPNLpgWRG 96
|
|
| |
