|
Name |
Accession |
Description |
Interval |
E-value |
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
205-511 |
2.28e-112 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 335.30 E-value: 2.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 205 KILMVGDTIIDEYNYVEGMERSSKEQLVATLFKSREVFAGGIIATANHVADLVREVEVVTVLGEDDTWEDLVRASVKPNV 284
Cdd:cd01172 1 KVLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 285 KLTILYRPEAPTTRKTRFIEPTYvrKLFEVYHMDDRPYAADVVERLDSVLAERLPEADVVVVTDFGHGMLTPSTINLLQE 364
Cdd:cd01172 81 DTDGIVDEGRPTTTKTRVIARNQ--QLLRVDREDDSPLSAEEEQRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 365 RSKFLTVNTQTNAGNLGFnfaTKYRRADYLCIDHREARFTTAD--KYSDVAVLVGEKIPALIDCEKLIVTSGFHGCLSYE 442
Cdd:cd01172 159 AARELGIPVLVDPKGRDY---SKYRGATLLTPNEKEAREALGDeiNDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751364364 443 RGGSVQRVPAFTKQVVDTVGAGDALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIGHRSSVDKVALM 511
Cdd:cd01172 236 RDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELLL 304
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
32-175 |
8.18e-85 |
|
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .
Pssm-ID: 173923 [Multi-domain] Cd Length: 144 Bit Score: 258.50 E-value: 8.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 32 EAGEQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVNKGPGRPIFPEGLRAEMLAACQYVDWVAVNHAPTAE 111
Cdd:cd02172 1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVLFDNPTAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751364364 112 NVLDTVRPSVYVKGSDYENPEEDITGKIRAEKDAVEKHGGKLVFTKDITFSSSTLINRYLDVYD 175
Cdd:cd02172 81 EIIDALQPNIYVKGGDYENPENDVTGKIAPEAEAVKAYGGKIVFTGEIVFSSSALINRIFDELD 144
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
192-500 |
3.76e-47 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 166.52 E-value: 3.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 192 ASIAAYLDKIKDYKILMVGDTIIDEYNYVEgMERSSKEQLV-ATLFKSREVFAGGIIATANHVADLVREVEVVTVLGEDD 270
Cdd:COG2870 4 ERLKELLPRFSRARVLVVGDVMLDRYWYGD-VERISPEAPVpVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGDDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 271 TWEDLVRASVKPNVKLTILYRPEAP-TTRKTRFIEPTYvrKLFEVYHMDDRPYAADVVERLDSVLAERLPEADVVVVTDF 349
Cdd:COG2870 83 AGRELRRLLEEAGIDTDGLVVDPRRpTTTKTRVIAGGQ--QLLRLDFEDRFPLSAELEARLLAALEAALPEVDAVILSDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 350 GHGMLTPS----TINLLQERSKFLTVNTQtnagnlGFNFaTKYRRADYLCIDHREARFTT--ADKYSDVAVLVGEKIPAL 423
Cdd:COG2870 161 GKGVLTPEliqaLIALARAAGKPVLVDPK------GRDF-SRYRGATLLTPNLKEAEAAVgiPIADEEELVAAAAELLER 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751364364 424 IDCEKLIVTSGFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIG 500
Cdd:COG2870 234 LGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLG 310
|
|
| rfaE_dom_II |
TIGR02199 |
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ... |
26-167 |
1.05e-31 |
|
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. Domain I (TIGR02198) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131254 [Multi-domain] Cd Length: 144 Bit Score: 118.94 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 26 IVREAREAGEQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVN--KGPGRPIFPEGLRAEMLAACQYVDWVA 103
Cdd:TIGR02199 2 LVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKrlKGETRPINPEEDRAEVLAALSSVDYVV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751364364 104 VNHAPTAENVLDTVRPSVYVKGSDYENpeEDItgkirAEKDAVEKHGGKLVFTKDITFSSSTLI 167
Cdd:TIGR02199 82 IFDEDTPEELIGELKPDILVKGGDYKV--ETL-----VGAELVESYGGQVVLLPFVEGRSTTAI 138
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
17-169 |
3.39e-24 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 105.30 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 17 IVTLDAMGEIVREAREAGEQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVN--KGPGRPIFPEGLRAEMLA 94
Cdd:PRK11316 322 VMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKrlKGEGRPVNPLEQRMAVLA 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 751364364 95 ACQYVDWVAVNHAPTAENVLDTVRPSVYVKGSDYeNPeEDITGkiraeKDAVEKHGGK---LVFTKDItfSSSTLINR 169
Cdd:PRK11316 402 ALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDY-KP-EEIAG-----SKEVWANGGEvkvLNFEDGC--STTNIIKK 470
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
37-171 |
3.53e-20 |
|
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440380 [Multi-domain] Cd Length: 131 Bit Score: 86.31 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 37 VVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFV-NKGPgRPIFPEGLRAEMLAACQYVDWVAVNHAPTAENVLD 115
Cdd:COG0615 2 RVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVaSKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFEDIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751364364 116 TVRPSVYVKGSDYENPEEDItgkiraeKDAVEKH--GGKLVF---TKDItfsSSTLINRYL 171
Cdd:COG0615 81 EIKPDVIVLGDDWKGDFDFL-------KEELEKRgiGCEVVYlprTEGI---SSTKIKKRI 131
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
205-497 |
9.03e-17 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 80.85 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 205 KILMVGDTIIDEYNYVEGMERSSKEQlvatlfKSREVFAGGiiATANH---VADLVREVEVVTVLGeDDTWEDLVRASVK 281
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRV------STVEKGPGG--KGANVavaLARLGGDVAFIGAVG-DDNFGEFLLQELK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 282 P-NVKLTILYR-PEAPTTRKTRFIEPTYVRKLfevyhMDDRPYAADVVERLDSVLAERLPEADVVVVTDFGHGMLTPSTI 359
Cdd:pfam00294 72 KeGVDTDYVVIdEDTRTGTALIEVDGDGERTI-----VFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 360 NLLQERSKFLTVNTQTNAGNLGfNFATKYRR----ADYLCIDHREARFTTADKYSDVAVLVgEKIPALIDC--EKLIVTS 433
Cdd:pfam00294 147 EELIEAAKNGGTFDPNLLDPLG-AAREALLEllplADLLKPNEEELEALTGAKLDDIEEAL-AALHKLLAKgiKTVIVTL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751364364 434 GFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLA-VTAPLvAAGCPMHQVGFVGNAAGAIKVG 497
Cdd:pfam00294 225 GADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGgFLAGL-LAGKSLEEALRFANAAAALVVQ 288
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
42-167 |
1.04e-11 |
|
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.
Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 62.34 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 42 GVFDLLHMGHVRHLEAARREG-TKLCVTLTGDRFVNKgPGRPIFPEGLRAEMLAACQYVD-WVAVNHAPTAENVLDTVRP 119
Cdd:pfam01467 4 GTFDPIHLGHLRLLEQAKELFdEDLIVGVPSDEPPHK-LKRPLFSAEERLEMLELAKWVDeVIVVAPWELTRELLKELNP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 751364364 120 SVYVKGSD-YENPEEDITGKIRAEKDAVEKHGGKLVFTKDITFSSSTLI 167
Cdd:pfam01467 83 DVLVIGADsLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDI 131
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
205-500 |
1.96e-09 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 59.84 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 205 KILMVGDTIIDEYNYvEGMERSSKEQLVATL-FKSREVFAGGIIATANHVADLVREVEVVTVLGEDDTWEDLVRASVKPN 283
Cdd:PRK11316 12 GVLVVGDVMLDRYWY-GPTSRISPEAPVPVVkVNQIEERPGGAANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 284 VKLTILYRPEAPTTRKTRFI--EPTYVRKLFE-VYHMDDrpyAADVVERLDSVLaerlPEADVVVVTDFGHGMLT--PST 358
Cdd:PRK11316 91 VKCDFVSVPTHPTITKLRVLsrNQQLIRLDFEeGFEGVD---PQPLLERIEQAL----PSIGALVLSDYAKGALAsvQAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 359 INLLQERSKFLTVNTQtnagnlGFNFAtKYRRADYLCIDHREarF-TTADKYSDVAVLV--GEKIPALIDCEKLIVTSGF 435
Cdd:PRK11316 164 IQLARKAGVPVLIDPK------GTDFE-RYRGATLLTPNLSE--FeAVVGKCKDEAELVekGMKLIADYDLSALLVTRSE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751364364 436 HGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIG 500
Cdd:PRK11316 235 QGMTLLQPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLG 299
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
391-504 |
1.08e-05 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 47.21 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 391 ADYLCIDHREARFTTADKYSDV--AVLVGEKIPALiDCEKLIVTSGFHGCLSYERGGSVQrVPAFTKQVVDTVGAGDALL 468
Cdd:TIGR02152 172 VDIITPNETEAEILTGIEVTDEedAEKAAEKLLEK-GVKNVIITLGSKGALLVSKDESKL-IPAFKVKAVDTTAAGDTFN 249
|
90 100 110
....*....|....*....|....*....|....*.
gi 751364364 469 AVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIGHRSS 504
Cdd:TIGR02152 250 GAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSS 285
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
205-511 |
2.28e-112 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 335.30 E-value: 2.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 205 KILMVGDTIIDEYNYVEGMERSSKEQLVATLFKSREVFAGGIIATANHVADLVREVEVVTVLGEDDTWEDLVRASVKPNV 284
Cdd:cd01172 1 KVLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 285 KLTILYRPEAPTTRKTRFIEPTYvrKLFEVYHMDDRPYAADVVERLDSVLAERLPEADVVVVTDFGHGMLTPSTINLLQE 364
Cdd:cd01172 81 DTDGIVDEGRPTTTKTRVIARNQ--QLLRVDREDDSPLSAEEEQRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 365 RSKFLTVNTQTNAGNLGFnfaTKYRRADYLCIDHREARFTTAD--KYSDVAVLVGEKIPALIDCEKLIVTSGFHGCLSYE 442
Cdd:cd01172 159 AARELGIPVLVDPKGRDY---SKYRGATLLTPNEKEAREALGDeiNDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751364364 443 RGGSVQRVPAFTKQVVDTVGAGDALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIGHRSSVDKVALM 511
Cdd:cd01172 236 RDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELLL 304
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
32-175 |
8.18e-85 |
|
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .
Pssm-ID: 173923 [Multi-domain] Cd Length: 144 Bit Score: 258.50 E-value: 8.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 32 EAGEQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVNKGPGRPIFPEGLRAEMLAACQYVDWVAVNHAPTAE 111
Cdd:cd02172 1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVLFDNPTAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751364364 112 NVLDTVRPSVYVKGSDYENPEEDITGKIRAEKDAVEKHGGKLVFTKDITFSSSTLINRYLDVYD 175
Cdd:cd02172 81 EIIDALQPNIYVKGGDYENPENDVTGKIAPEAEAVKAYGGKIVFTGEIVFSSSALINRIFDELD 144
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
192-500 |
3.76e-47 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 166.52 E-value: 3.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 192 ASIAAYLDKIKDYKILMVGDTIIDEYNYVEgMERSSKEQLV-ATLFKSREVFAGGIIATANHVADLVREVEVVTVLGEDD 270
Cdd:COG2870 4 ERLKELLPRFSRARVLVVGDVMLDRYWYGD-VERISPEAPVpVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGDDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 271 TWEDLVRASVKPNVKLTILYRPEAP-TTRKTRFIEPTYvrKLFEVYHMDDRPYAADVVERLDSVLAERLPEADVVVVTDF 349
Cdd:COG2870 83 AGRELRRLLEEAGIDTDGLVVDPRRpTTTKTRVIAGGQ--QLLRLDFEDRFPLSAELEARLLAALEAALPEVDAVILSDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 350 GHGMLTPS----TINLLQERSKFLTVNTQtnagnlGFNFaTKYRRADYLCIDHREARFTT--ADKYSDVAVLVGEKIPAL 423
Cdd:COG2870 161 GKGVLTPEliqaLIALARAAGKPVLVDPK------GRDF-SRYRGATLLTPNLKEAEAAVgiPIADEEELVAAAAELLER 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751364364 424 IDCEKLIVTSGFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIG 500
Cdd:COG2870 234 LGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLG 310
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
35-173 |
1.77e-44 |
|
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.
Pssm-ID: 173921 [Multi-domain] Cd Length: 136 Bit Score: 153.22 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 35 EQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVNKGPGRPIFPEGLRAEMLAACQYVDWVAVNHAPTAENVL 114
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751364364 115 DTVRPSVYVKGSDYENPEeditgKIRAEKDAVEKHGGKLVFT--KDITFSSSTLINRYLDV 173
Cdd:cd02170 81 EELKPDVIVLGDDQKNGV-----DEEEVYEELKKRGKVIEVPrkKTEGISSSDIIKRILEL 136
|
|
| rfaE_dom_II |
TIGR02199 |
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ... |
26-167 |
1.05e-31 |
|
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. Domain I (TIGR02198) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131254 [Multi-domain] Cd Length: 144 Bit Score: 118.94 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 26 IVREAREAGEQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVN--KGPGRPIFPEGLRAEMLAACQYVDWVA 103
Cdd:TIGR02199 2 LVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKrlKGETRPINPEEDRAEVLAALSSVDYVV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751364364 104 VNHAPTAENVLDTVRPSVYVKGSDYENpeEDItgkirAEKDAVEKHGGKLVFTKDITFSSSTLI 167
Cdd:TIGR02199 82 IFDEDTPEELIGELKPDILVKGGDYKV--ETL-----VGAELVESYGGQVVLLPFVEGRSTTAI 138
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
17-169 |
3.39e-24 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 105.30 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 17 IVTLDAMGEIVREAREAGEQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVN--KGPGRPIFPEGLRAEMLA 94
Cdd:PRK11316 322 VMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKrlKGEGRPVNPLEQRMAVLA 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 751364364 95 ACQYVDWVAVNHAPTAENVLDTVRPSVYVKGSDYeNPeEDITGkiraeKDAVEKHGGK---LVFTKDItfSSSTLINR 169
Cdd:PRK11316 402 ALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDY-KP-EEIAG-----SKEVWANGGEvkvLNFEDGC--STTNIIKK 470
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
37-171 |
3.53e-20 |
|
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440380 [Multi-domain] Cd Length: 131 Bit Score: 86.31 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 37 VVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFV-NKGPgRPIFPEGLRAEMLAACQYVDWVAVNHAPTAENVLD 115
Cdd:COG0615 2 RVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVaSKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFEDIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751364364 116 TVRPSVYVKGSDYENPEEDItgkiraeKDAVEKH--GGKLVF---TKDItfsSSTLINRYL 171
Cdd:COG0615 81 EIKPDVIVLGDDWKGDFDFL-------KEELEKRgiGCEVVYlprTEGI---SSTKIKKRI 131
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
205-497 |
9.03e-17 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 80.85 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 205 KILMVGDTIIDEYNYVEGMERSSKEQlvatlfKSREVFAGGiiATANH---VADLVREVEVVTVLGeDDTWEDLVRASVK 281
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRV------STVEKGPGG--KGANVavaLARLGGDVAFIGAVG-DDNFGEFLLQELK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 282 P-NVKLTILYR-PEAPTTRKTRFIEPTYVRKLfevyhMDDRPYAADVVERLDSVLAERLPEADVVVVTDFGHGMLTPSTI 359
Cdd:pfam00294 72 KeGVDTDYVVIdEDTRTGTALIEVDGDGERTI-----VFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 360 NLLQERSKFLTVNTQTNAGNLGfNFATKYRR----ADYLCIDHREARFTTADKYSDVAVLVgEKIPALIDC--EKLIVTS 433
Cdd:pfam00294 147 EELIEAAKNGGTFDPNLLDPLG-AAREALLEllplADLLKPNEEELEALTGAKLDDIEEAL-AALHKLLAKgiKTVIVTL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751364364 434 GFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLA-VTAPLvAAGCPMHQVGFVGNAAGAIKVG 497
Cdd:pfam00294 225 GADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGgFLAGL-LAGKSLEEALRFANAAAALVVQ 288
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
205-505 |
6.55e-14 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 72.22 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 205 KILMVGDTIIDEYNYVEGMERSSKEQLVATLfksrEVFAGGIIA-TANHVADLVREVEVVTVLGEDDTWEDLVRASVKPN 283
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSF----RRSPGGAAAnVAVALARLGARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 284 VKLT-ILYRPEAPTTRKTRFIEPTYVRKlFEVYHMDDRPYAADVVErldsvlAERLPEADVVVVTdfGHGMLTPST---- 358
Cdd:COG0524 77 VDTSgVRRDPGAPTGLAFILVDPDGERT-IVFYRGANAELTPEDLD------EALLAGADILHLG--GITLASEPPreal 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 359 ---INLLQERSKFLTVNTqtnagNLGFNFATKYR--------RADYLCIDHREARFTT-ADKYSDVAVLVGEKIPALIdc 426
Cdd:COG0524 148 laaLEAARAAGVPVSLDP-----NYRPALWEPARellrellaLVDILFPNEEEAELLTgETDPEEAAAALLARGVKLV-- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751364364 427 eklIVTSGFHGCLSYERGGSVqRVPAFTKQVVDTVGAGDALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIGHRSSV 505
Cdd:COG0524 221 ---VVTLGAEGALLYTGGEVV-HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPAL 295
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
34-131 |
1.90e-12 |
|
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.
Pssm-ID: 173924 Cd Length: 152 Bit Score: 64.97 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 34 GEQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVN--KGPGRPIFPEGLRAEMLAACQYVDWVaVNHAP--- 108
Cdd:cd02173 1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNeyKGSNYPIMNLHERVLSVLACRYVDEV-VIGAPyvi 79
|
90 100
....*....|....*....|...
gi 751364364 109 TAEnVLDTVRPSVYVKGSDYENP 131
Cdd:cd02173 80 TKE-LIEHFKIDVVVHGKTEETP 101
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
37-102 |
5.70e-12 |
|
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 60.78 E-value: 5.70e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751364364 37 VVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVNKGPGRPIFPEGLRAEMLAACQYVDWV 102
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
38-184 |
7.99e-12 |
|
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.
Pssm-ID: 173925 Cd Length: 150 Bit Score: 62.97 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 38 VLCHGVFDLLHMGHVRHLEAARREG--TKLCVTLTGDRFVNKGPGRPIFPEGLRAEMLAACQYVDWVAVNhAP--TAENV 113
Cdd:cd02174 5 VYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEG-APyvTTPEF 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751364364 114 LDTVRPSVYVKGSD--YENPEEDITGKIRAEkdavekhgGKLVFTKDiT--FSSSTLINRYLDVYDPPLRDFLDE 184
Cdd:cd02174 84 LDKYKCDYVAHGDDiyLDADGEDCYQEVKDA--------GRFKEVKR-TegVSTTDLIGRILLDYRDYHRRNLQR 149
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
42-167 |
1.04e-11 |
|
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.
Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 62.34 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 42 GVFDLLHMGHVRHLEAARREG-TKLCVTLTGDRFVNKgPGRPIFPEGLRAEMLAACQYVD-WVAVNHAPTAENVLDTVRP 119
Cdd:pfam01467 4 GTFDPIHLGHLRLLEQAKELFdEDLIVGVPSDEPPHK-LKRPLFSAEERLEMLELAKWVDeVIVVAPWELTRELLKELNP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 751364364 120 SVYVKGSD-YENPEEDITGKIRAEKDAVEKHGGKLVFTKDITFSSSTLI 167
Cdd:pfam01467 83 DVLVIGADsLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDI 131
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
35-102 |
2.28e-10 |
|
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.
Pssm-ID: 173922 [Multi-domain] Cd Length: 129 Bit Score: 58.26 E-value: 2.28e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751364364 35 EQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFvNKGPGRPIF-PEGLRAEMLAACQYVDWV 102
Cdd:cd02171 1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEF-NAGKGKKAViPYEQRAEILESIRYVDLV 68
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
34-132 |
1.23e-09 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 59.80 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 34 GEQVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVN--KGPGRPIFPEGLRAEMLAACQYVDWVaVNHAPTA- 110
Cdd:PTZ00308 191 GDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNeqKGSNYPIMNLNERVLGVLSCRYVDEV-VIGAPFDv 269
|
90 100
....*....|....*....|....*
gi 751364364 111 -ENVLDTVRPSVYVKG--SDYENPE 132
Cdd:PTZ00308 270 tKEVIDSLHINVVVGGkfSDLVNEE 294
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
205-500 |
1.96e-09 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 59.84 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 205 KILMVGDTIIDEYNYvEGMERSSKEQLVATL-FKSREVFAGGIIATANHVADLVREVEVVTVLGEDDTWEDLVRASVKPN 283
Cdd:PRK11316 12 GVLVVGDVMLDRYWY-GPTSRISPEAPVPVVkVNQIEERPGGAANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 284 VKLTILYRPEAPTTRKTRFI--EPTYVRKLFE-VYHMDDrpyAADVVERLDSVLaerlPEADVVVVTDFGHGMLT--PST 358
Cdd:PRK11316 91 VKCDFVSVPTHPTITKLRVLsrNQQLIRLDFEeGFEGVD---PQPLLERIEQAL----PSIGALVLSDYAKGALAsvQAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 359 INLLQERSKFLTVNTQtnagnlGFNFAtKYRRADYLCIDHREarF-TTADKYSDVAVLV--GEKIPALIDCEKLIVTSGF 435
Cdd:PRK11316 164 IQLARKAGVPVLIDPK------GTDFE-RYRGATLLTPNLSE--FeAVVGKCKDEAELVekGMKLIADYDLSALLVTRSE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751364364 436 HGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIG 500
Cdd:PRK11316 235 QGMTLLQPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLG 299
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
240-500 |
1.63e-08 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 56.05 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 240 EVFAGGiiATAN---HVADLVREVEVVTVLGEDDTWEDLVRASVKPNVKLT-ILYRPEAPTtrKTRFIEPTYVRKlFEVY 315
Cdd:cd01166 27 RKFFGG--AEANvavGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTShVRVDPGRPT--GLYFLEIGAGGE-RRVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 316 HmdDRPYAAD---VVERLDsvlAERLPEADVVVVTdfGHGM-LTPSTINLLQErskFLTVntqtnAGNLG------FNFA 385
Cdd:cd01166 102 Y--YRAGSAAsrlTPEDLD---EAALAGADHLHLS--GITLaLSESAREALLE---ALEA-----AKARGvtvsfdLNYR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 386 TKYRRADylcidHREARFTTADKYSDVAV--------LVGEKIPA---------LIDCEKLIVTSGFHGCLSYERGGSVq 448
Cdd:cd01166 167 PKLWSAE-----EAREALEELLPYVDIVLpseeeaeaLLGDEDPTdaaeralalALGVKAVVVKLGAEGALVYTGGGRV- 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 751364364 449 RVPAFTKQVVDTVGAGDALlavTAPLVAA---GCPMHQVGFVGNAAGAIKVGIIG 500
Cdd:cd01166 241 FVPAYPVEVVDTTGAGDAF---AAGFLAGlleGWDLEEALRFANAAAALVVTRPG 292
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
429-497 |
2.36e-08 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 55.51 E-value: 2.36e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751364364 429 LIVTSGFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVG 497
Cdd:cd01944 218 VVVRLGSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVT 286
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
388-504 |
4.10e-08 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 54.86 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 388 YRRADYLCIDHREARFTTADKYSDV--AVLVGEKIPALIdCEKLIVTSGFHGCLSYERGGsVQRVPAFTKQVVDTVGAGD 465
Cdd:cd01174 173 LALVDILVPNETEAALLTGIEVTDEedAEKAARLLLAKG-VKNVIVTLGAKGALLASGGE-VEHVPAFKVKAVDTTGAGD 250
|
90 100 110
....*....|....*....|....*....|....*....
gi 751364364 466 ALLAVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIGHRSS 504
Cdd:cd01174 251 TFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPS 289
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
36-172 |
1.15e-07 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 53.92 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 36 QVVLCHGVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFV--NKGPGRPIFPEGLRAEMLAACQYVDWVAVNhAP--TAE 111
Cdd:PLN02406 252 RIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVsaHRGAHRPIMNLHERSLSVLACRYVDEVIIG-APweVSK 330
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751364364 112 NVLDTVRPSVYVKGSDYENPEediTGKIRAEKDAVEKHGGK---LVFTKDITfsSSTLINRYLD 172
Cdd:PLN02406 331 DMITTFNISLVVHGTVAENND---FLKGEDDPYAVPKSMGIfqvLESPLDIT--TSTIIRRIVA 389
|
|
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
38-193 |
3.05e-07 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 52.26 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 38 VLCHGVFDLLHMGHVRHLEAARR--EGTKLCVTLTGDRFVNKGPGRPIFPEGLRAEMLAACQYVDWVaVNHAP--TAENV 113
Cdd:PLN02413 30 VYADGIYDLFHFGHARSLEQAKKlfPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEV-IPDAPwvITQEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 114 LDTVRPSvYVKGSDYenPEEDITGkirAEKDAVE--KHGGKLVFTKDIT-FSSSTLINRYLDVYDP-PLRDFLDELRQED 189
Cdd:PLN02413 109 LDKHRID-YVAHDAL--PYADASG---AGKDVYEfvKKIGKFKETKRTDgISTSDIIMRIVKDYNQyVMRNLARGYSRKD 182
|
....
gi 751364364 190 AGAS 193
Cdd:PLN02413 183 LGVS 186
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
389-469 |
3.12e-07 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 50.94 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 389 RRADYLCIDHREARFTT-ADKYSDVAVLVGEKIPALIDCEKLIVTSGFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDAL 467
Cdd:cd00287 108 PGVDILTPNEEEAEALTgRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAF 187
|
..
gi 751364364 468 LA 469
Cdd:cd00287 188 LA 189
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
42-136 |
3.36e-07 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 52.48 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 42 GVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFVNKGPGRPIFPEGLRAEMLAACQYVDWVAVNhAPTAENVLDTVRPSV 121
Cdd:PTZ00308 18 GCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEG-YPYTTRLEDLERLEC 96
|
90
....*....|....*
gi 751364364 122 yvkgsDYENPEEDIT 136
Cdd:PTZ00308 97 -----DFVVHGDDIS 106
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
424-519 |
3.57e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 52.12 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 424 IDCEK------LIVTSGFHGCLSYERGGSVqRVPAFTKQVVDTVGAGDALLA-VTAPLVaAGCPMHQVGFVGNAAGAIKV 496
Cdd:PLN02630 195 IDVEEvrqkccVIVTNGKKGCRIYWKDGEM-RVPPFPAIQVDPTGAGDSFLGgFVAGLV-QGLAVPDAALLGNYFGSLAV 272
|
90 100
....*....|....*....|...
gi 751364364 497 GIIGhrssvdkvaLMKFITTLLK 519
Cdd:PLN02630 273 EQVG---------IPKFDLRQLQ 286
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
242-500 |
6.02e-07 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 51.10 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 242 FAGGiiATAN---HVADLVREVEVVTVLGEDDTWEDLVRASVKPNVKLT-ILYRPEAPTTRKTRFIEPTYVRKlFEVYhm 317
Cdd:cd01167 26 APGG--APANvavALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRgIQFDPAAPTTLAFVTLDADGERS-FEFY-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 318 ddRPYAADVVERLDsVLAERLPEADVVVvtdFG-HGMLTP---STINLLQERSK------FLTVN-------TQTNAGNL 380
Cdd:cd01167 101 --RGPAADLLLDTE-LNPDLLSEADILH---FGsIALASEpsrSALLELLEAAKkagvliSFDPNlrpplwrDEEEARER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 381 GFNFATkyrRADYLCIDHREARFTTADKYSDVAVlvgeKIPALIDCEKLIVTSGFHGCLSYeRGGSVQRVPAFTKQVVDT 460
Cdd:cd01167 175 IAELLE---LADIVKLSDEELELLFGEEDPEEIA----ALLLLFGLKLVLVTRGADGALLY-TKGGVGEVPGIPVEVVDT 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 751364364 461 VGAGDALLA-VTAPLVAAGCPMH-------QVGFvGNAAGAIKVGIIG 500
Cdd:cd01167 247 TGAGDAFVAgLLAQLLSRGLLALdedelaeALRF-ANAVGALTCTKAG 293
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
422-466 |
1.78e-06 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 49.60 E-value: 1.78e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 751364364 422 ALIDCEKLIVTSGFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDA 466
Cdd:cd01945 199 ASLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVEVVDTTGAGDV 243
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
391-504 |
1.08e-05 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 47.21 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 391 ADYLCIDHREARFTTADKYSDV--AVLVGEKIPALiDCEKLIVTSGFHGCLSYERGGSVQrVPAFTKQVVDTVGAGDALL 468
Cdd:TIGR02152 172 VDIITPNETEAEILTGIEVTDEedAEKAAEKLLEK-GVKNVIITLGSKGALLVSKDESKL-IPAFKVKAVDTTAAGDTFN 249
|
90 100 110
....*....|....*....|....*....|....*.
gi 751364364 469 AVTAPLVAAGCPMHQVGFVGNAAGAIKVGIIGHRSS 504
Cdd:TIGR02152 250 GAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSS 285
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
206-500 |
1.60e-05 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 46.54 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 206 ILMVGDTIIDEYNYVEGMERSSKEQLVATLfksREVFAGGIIATANHVADLVREVEVVTVLGEDDTWEDLVRASVKPNVK 285
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDL---RREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 286 L-TILYRPEAPTT----------RKTRFIEPTYVRKLfEVYHMDDRPYAADVV----ERLDSVLAERLPEADVVVVTDFG 350
Cdd:cd01942 79 TsHVRVVDEDSTGvafiltdgddNQIAYFYPGAMDEL-EPNDEADPDGLADIVhlssGPGLIELARELAAGGITVSFDPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 351 HGMLTPSTINLLqersKFLtvntqtnagnlgfnfatkyRRADYLCIDHREARFT---TADKYSDVAVLVGEkipalidce 427
Cdd:cd01942 158 QELPRLSGEELE----EIL-------------------ERADILFVNDYEAELLkerTGLSEAELASGVRV--------- 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751364364 428 kLIVTSGFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLA--VTAplVAAGCPMHQVGFVGNAAGAIKVGIIG 500
Cdd:cd01942 206 -VVVTLGPKGAIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAgfLYG--LLRGYDLEESLRLGNLAASLKVERRG 277
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
392-504 |
8.50e-05 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 392 DYLCIDHREARFTTADKYSDVAV-LVGEKIPALIDCEKLIVTSGFHGCLSYERGGSVQRVPAFTKQVVDTVGAGDALLAV 470
Cdd:PTZ00292 200 SLFCVNEVEAALITGMEVTDTESaFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGS 279
|
90 100 110
....*....|....*....|....*....|....
gi 751364364 471 TAPLVAAGCPMHQVGFVGNAAGAIKVGIIGHRSS 504
Cdd:PTZ00292 280 MAYFMSRGKDLKESCKRANRIAAISVTRHGTQSS 313
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
448-505 |
1.09e-03 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 41.01 E-value: 1.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751364364 448 QRVPAFTKQVVDTVGAGD----ALlaVTAPLvaAGCPMHQ-VGFvGNAAGAIKVGIIGHRSSV 505
Cdd:PRK11142 236 QRVPGFRVQAVDTIAAGDtfngAL--VTALL--EGKPLPEaIRF-AHAAAAIAVTRKGAQPSI 293
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
42-110 |
1.57e-03 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 40.82 E-value: 1.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751364364 42 GVFDLLHMGHVRHLEAARREGTKLCVTLTGDRFV--NKGPgrPIFPEGLRAEMLAACQYVDWVAVNhAPTA 110
Cdd:PLN02406 60 GCFDMMHYGHANALRQARALGDELVVGVVSDEEIiaNKGP--PVTPMHERMIMVSGVKWVDEVIPD-APYA 127
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
388-469 |
1.64e-03 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 40.76 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 388 YRRADYLCIDHREARFTTA--DKYSDVAVlvgekipALI--DCEKLIVTSGFHGCLSYERGGSvQRVPAFTKQVVDTVGA 463
Cdd:PLN02323 195 WDEADIIKVSDEEVEFLTGgdDPDDDTVV-------KLWhpNLKLLLVTEGEEGCRYYTKDFK-GRVEGFKVKAVDTTGA 266
|
....*.
gi 751364364 464 GDALLA 469
Cdd:PLN02323 267 GDAFVG 272
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
391-502 |
2.58e-03 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 39.90 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751364364 391 ADYLCIDHREAR-FTTADKYSDVAVLVGekiPALIDCEKLIVTSGFHGCLSYErGGSVQRVPAFTK-QVVDTVGAGDA-- 466
Cdd:cd01168 201 VDILFGNEEEAEaLAEAETTDDLEAALK---LLALRCRIVVITQGAKGAVVVE-GGEVYPVPAIPVeKIVDTNGAGDAfa 276
|
90 100 110
....*....|....*....|....*....|....*....
gi 751364364 467 ---LLAVTaplvaAGCPMHQVGFVGNAAGAIKVGIIGHR 502
Cdd:cd01168 277 ggfLYGLV-----QGEPLEECIRLGSYAAAEVIQQLGPR 310
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
418-483 |
5.78e-03 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 38.76 E-value: 5.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751364364 418 EKIPALIDCEKLIVTSGFHGCLSYERGGsVQRVPAFTKQVVDTVGAGDALLA-VTAPLVAAGCPMHQ 483
Cdd:PRK09434 205 YALADRYPIALLLVTLGAEGVLVHTRGQ-VQHFPAPSVDPVDTTGAGDAFVAgLLAGLSQAGLWTDE 270
|
|
| |
