|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-332 |
4.95e-75 |
|
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440550 [Multi-domain] Cd Length: 368 Bit Score: 236.16 E-value: 4.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 2 TAIWSLDTEAFYQNAVKVKN----NEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMN 77
Cdd:COG0787 3 PAWAEIDLDALRHNLRVLRAlagpGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 78 PV--YDFDLVKRYDIHMTLPSLNYYYKYKQDL----KGIHVHLEYENLLHRSGFRnIEEIREVLKDHDQnnQDKMIISGI 151
Cdd:COG0787 83 GVppEDLELAIEYDLEPVVHSLEQLEALAAAArrlgKPLPVHLKVDTGMNRLGFR-PEEAPALAARLAA--LPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 152 WTHFGYADEFDVDEYKMERDAWLNLINTLLNENYHFDMIHSQNSASYFRENQMllpHHTHARVGIALYGSRPYS-LINEE 230
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEA---HFDMVRPGIALYGLSPSPeVAADL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 231 RITQSLTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILKSRA-KHEAIINGKRYPIR-ALMMSHMFI 308
Cdd:COG0787 237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRD-TRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVgRVSMDQIMV 315
|
330 340
....*....|....*....|....*..
gi 487749212 309 EVDD--EVHAQDEVILYNKD-IRIDEF 332
Cdd:COG0787 316 DVTDipDVKVGDEVVLFGEQgITADEL 342
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
18-332 |
1.29e-61 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family.
Pssm-ID: 143481 [Multi-domain] Cd Length: 367 Bit Score: 201.57 E-value: 1.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 18 KVKNNEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMNPVY--DFDLVKRYDIHMTLP 95
Cdd:cd00430 21 LLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGGTPpeEAEEAIEYDLTPTVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 96 SLNYYYKY----KQDLKGIHVHLEYENLLHRSGFRnIEEIREVLKDHDQnnQDKMIISGIWTHFGYADEFDVDEYKMERD 171
Cdd:cd00430 101 SLEQAEALsaaaARLGKTLKVHLKIDTGMGRLGFR-PEEAEELLEALKA--LPGLELEGVFTHFATADEPDKAYTRRQLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 172 AWLNLINTLLNENYHFDMIHSQNSASYFRenqMLLPHHTHARVGIALYGSRP-YSLINEERITQSLTVKGNVIQVRDVNK 250
Cdd:cd00430 178 RFLEALAELEEAGIPPPLKHLANSAAILR---FPEAHFDMVRPGIALYGLYPsPEVKSPLGLKPVMSLKARVVQVKTVPA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 251 GDYCGYSFAFEVKNDhTQLAVVDIGYGDGIlkSRA---KHEAIINGKRYPIR-ALMMSHMFIEVDDEVHAQ--DEVILYN 324
Cdd:cd00430 255 GEGVSYGRTYTAPRP-TRIATLPVGYADGY--PRAlsnKGEVLIRGKRAPIVgRVCMDQTMVDVTDIPDVKvgDEVVLFG 331
|
330
....*....|..
gi 487749212 325 KD----IRIDEF 332
Cdd:cd00430 332 RQgdeeITAEEL 343
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-331 |
1.58e-49 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 169.97 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 7 LDTEAFYQNAVKVKN----NEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMNPVY-- 80
Cdd:PRK00053 8 IDLDALRHNLRQIRKhappKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGGFFpa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 81 -DFDLVKRYDIHMTLPSLNYYYKYKQ--DLKGIHVHLEYENLLHRSGFRnIEEIREVLKDHDQNNQdkMIISGIWTHFGY 157
Cdd:PRK00053 88 eDLPLIIAYNLTTAVHSLEQLEALEKaeLGKPLKVHLKIDTGMHRLGVR-PEEAEAALERLLACPN--VRLEGIFSHFAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 158 ADEFDVDEYKMERDAWLNLINTLLNENyhFDMIHSQNSASYFRENQMllpHHTHARVGIALYGSRP--YSLINEERITQS 235
Cdd:PRK00053 165 ADEPDNSYTEQQLNRFEAALAGLPGKG--KPLRHLANSAAILRWPDL---HFDWVRPGIALYGLSPsgEPLGLDFGLKPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 236 LTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILKS-RAKHEAIINGKRYPI--RaLMMSHMFIEV-- 310
Cdd:PRK00053 240 MTLKSSLIAVRELKAGEGVGYGGTFTAERD-TRIAVVPIGYADGYPRNlPSGTPVLVNGRRVPIvgR-VSMDQLTVDLgp 317
|
330 340
....*....|....*....|.
gi 487749212 311 DDEVHAQDEVILYNKDIRIDE 331
Cdd:PRK00053 318 DPQDKVGDEVTLWGEALTAED 338
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
6-331 |
2.04e-45 |
|
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is to generate D-alanine for cell wall formation. With D-alanine-D-alanine ligase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route. It is a monomer with one pyridoxal phosphate per subunit. In E. coli, the ortholog is duplicated so that a second isozyme, DadX, is present. DadX, a paralog of the biosynthetic Alr, is induced by D- or L-alanine and is involved in catabolism. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129583 [Multi-domain] Cd Length: 367 Bit Score: 159.06 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 6 SLDTEAFYQNAVKVKNNEP----IMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMNPVYD 81
Cdd:TIGR00492 6 EIDLAALKHNLSAIRNHIGpkskIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGGFFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 82 FDLVK--RYDIHMTLPSLNYYYKYKQDL----KGIHVHLEYENLLHRSGFRNIEEIREVLKDHDQNNQDKmiISGIWTHF 155
Cdd:TIGR00492 86 EDLKIlaAWDLTTTVHSVEQLQALEEALlkepKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLE--LEGIFSHF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 156 GYADEFDVDEYKMERDAWLNLINTLLNENYHFDMIHSQNSAS--YFRENqmllpHHTHARVGIALYGSRPYSLINEERIT 233
Cdd:TIGR00492 164 ATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAilNWPES-----HFDMVRPGIILYGLYPSADMSDGAPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 234 Q---SLTVKGNVIQVRDVNKGDYCGYSFAFeVKNDHTQLAVVDIGYGDGI---LKSRAkhEAIINGKRYPIR-ALMMSHM 306
Cdd:TIGR00492 239 GlkpVLSLTSKIIQVRTVKKGEPVSYGGTF-TAEEDTRIGVVAIGYADGYpraLSNGT--PVLVNGKRVPIVgRVCMDMI 315
|
330 340
....*....|....*....|....*..
gi 487749212 307 FIEV--DDEVHAQDEVILYNKDIRIDE 331
Cdd:TIGR00492 316 MVDLgpDLQDKTGDEVILWGEEISIDE 342
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
7-223 |
4.70e-43 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 148.53 E-value: 4.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 7 LDTEAFYQNAVKVKN----NEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMNPVY-- 80
Cdd:pfam01168 1 IDLDALRHNLRRLRRragpGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 81 DFDLVKRYDIHMTLPSLNYYYKY----KQDLKGIHVHLEYENLLHRSGFRnIEEIREVLKDHDQNnqDKMIISGIWTHFG 156
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALaaaaRRLGKPLRVHLKIDTGMGRLGFR-PEEALALLARLAAL--PGLRLEGLMTHFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749212 157 YADEFDVDEYKMERDAWLNLINTLLNENYHFDMIHSQNSASYFRENQmllpHHTHARVGIALYGSRP 223
Cdd:pfam01168 158 CADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPL----HFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
236-349 |
6.45e-25 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 97.52 E-value: 6.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 236 LTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILKSRAKHEAIINGKRYPIRA-LMMSHMFIEVDD-- 312
Cdd:smart01005 2 MTLKARVIQVREVPAGETVGYGATFTADRD-TRIATVPIGYADGYPRALSNGPVLINGQRVPVVGrVSMDQLMVDVTDip 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 487749212 313 EVHAQDEVILYNKD-IRIDEFTFKGVGANSEQLSAMNH 349
Cdd:smart01005 81 DVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGP 118
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-332 |
4.95e-75 |
|
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440550 [Multi-domain] Cd Length: 368 Bit Score: 236.16 E-value: 4.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 2 TAIWSLDTEAFYQNAVKVKN----NEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMN 77
Cdd:COG0787 3 PAWAEIDLDALRHNLRVLRAlagpGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 78 PV--YDFDLVKRYDIHMTLPSLNYYYKYKQDL----KGIHVHLEYENLLHRSGFRnIEEIREVLKDHDQnnQDKMIISGI 151
Cdd:COG0787 83 GVppEDLELAIEYDLEPVVHSLEQLEALAAAArrlgKPLPVHLKVDTGMNRLGFR-PEEAPALAARLAA--LPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 152 WTHFGYADEFDVDEYKMERDAWLNLINTLLNENYHFDMIHSQNSASYFRENQMllpHHTHARVGIALYGSRPYS-LINEE 230
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEA---HFDMVRPGIALYGLSPSPeVAADL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 231 RITQSLTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILKSRA-KHEAIINGKRYPIR-ALMMSHMFI 308
Cdd:COG0787 237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRD-TRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVgRVSMDQIMV 315
|
330 340
....*....|....*....|....*..
gi 487749212 309 EVDD--EVHAQDEVILYNKD-IRIDEF 332
Cdd:COG0787 316 DVTDipDVKVGDEVVLFGEQgITADEL 342
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
18-332 |
1.29e-61 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family.
Pssm-ID: 143481 [Multi-domain] Cd Length: 367 Bit Score: 201.57 E-value: 1.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 18 KVKNNEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMNPVY--DFDLVKRYDIHMTLP 95
Cdd:cd00430 21 LLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGGTPpeEAEEAIEYDLTPTVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 96 SLNYYYKY----KQDLKGIHVHLEYENLLHRSGFRnIEEIREVLKDHDQnnQDKMIISGIWTHFGYADEFDVDEYKMERD 171
Cdd:cd00430 101 SLEQAEALsaaaARLGKTLKVHLKIDTGMGRLGFR-PEEAEELLEALKA--LPGLELEGVFTHFATADEPDKAYTRRQLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 172 AWLNLINTLLNENYHFDMIHSQNSASYFRenqMLLPHHTHARVGIALYGSRP-YSLINEERITQSLTVKGNVIQVRDVNK 250
Cdd:cd00430 178 RFLEALAELEEAGIPPPLKHLANSAAILR---FPEAHFDMVRPGIALYGLYPsPEVKSPLGLKPVMSLKARVVQVKTVPA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 251 GDYCGYSFAFEVKNDhTQLAVVDIGYGDGIlkSRA---KHEAIINGKRYPIR-ALMMSHMFIEVDDEVHAQ--DEVILYN 324
Cdd:cd00430 255 GEGVSYGRTYTAPRP-TRIATLPVGYADGY--PRAlsnKGEVLIRGKRAPIVgRVCMDQTMVDVTDIPDVKvgDEVVLFG 331
|
330
....*....|..
gi 487749212 325 KD----IRIDEF 332
Cdd:cd00430 332 RQgdeeITAEEL 343
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-331 |
1.58e-49 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 169.97 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 7 LDTEAFYQNAVKVKN----NEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMNPVY-- 80
Cdd:PRK00053 8 IDLDALRHNLRQIRKhappKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGGFFpa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 81 -DFDLVKRYDIHMTLPSLNYYYKYKQ--DLKGIHVHLEYENLLHRSGFRnIEEIREVLKDHDQNNQdkMIISGIWTHFGY 157
Cdd:PRK00053 88 eDLPLIIAYNLTTAVHSLEQLEALEKaeLGKPLKVHLKIDTGMHRLGVR-PEEAEAALERLLACPN--VRLEGIFSHFAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 158 ADEFDVDEYKMERDAWLNLINTLLNENyhFDMIHSQNSASYFRENQMllpHHTHARVGIALYGSRP--YSLINEERITQS 235
Cdd:PRK00053 165 ADEPDNSYTEQQLNRFEAALAGLPGKG--KPLRHLANSAAILRWPDL---HFDWVRPGIALYGLSPsgEPLGLDFGLKPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 236 LTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILKS-RAKHEAIINGKRYPI--RaLMMSHMFIEV-- 310
Cdd:PRK00053 240 MTLKSSLIAVRELKAGEGVGYGGTFTAERD-TRIAVVPIGYADGYPRNlPSGTPVLVNGRRVPIvgR-VSMDQLTVDLgp 317
|
330 340
....*....|....*....|.
gi 487749212 311 DDEVHAQDEVILYNKDIRIDE 331
Cdd:PRK00053 318 DPQDKVGDEVTLWGEALTAED 338
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
6-331 |
2.04e-45 |
|
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is to generate D-alanine for cell wall formation. With D-alanine-D-alanine ligase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route. It is a monomer with one pyridoxal phosphate per subunit. In E. coli, the ortholog is duplicated so that a second isozyme, DadX, is present. DadX, a paralog of the biosynthetic Alr, is induced by D- or L-alanine and is involved in catabolism. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129583 [Multi-domain] Cd Length: 367 Bit Score: 159.06 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 6 SLDTEAFYQNAVKVKNNEP----IMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMNPVYD 81
Cdd:TIGR00492 6 EIDLAALKHNLSAIRNHIGpkskIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGGFFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 82 FDLVK--RYDIHMTLPSLNYYYKYKQDL----KGIHVHLEYENLLHRSGFRNIEEIREVLKDHDQNNQDKmiISGIWTHF 155
Cdd:TIGR00492 86 EDLKIlaAWDLTTTVHSVEQLQALEEALlkepKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLE--LEGIFSHF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 156 GYADEFDVDEYKMERDAWLNLINTLLNENYHFDMIHSQNSAS--YFRENqmllpHHTHARVGIALYGSRPYSLINEERIT 233
Cdd:TIGR00492 164 ATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAilNWPES-----HFDMVRPGIILYGLYPSADMSDGAPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 234 Q---SLTVKGNVIQVRDVNKGDYCGYSFAFeVKNDHTQLAVVDIGYGDGI---LKSRAkhEAIINGKRYPIR-ALMMSHM 306
Cdd:TIGR00492 239 GlkpVLSLTSKIIQVRTVKKGEPVSYGGTF-TAEEDTRIGVVAIGYADGYpraLSNGT--PVLVNGKRVPIVgRVCMDMI 315
|
330 340
....*....|....*....|....*..
gi 487749212 307 FIEV--DDEVHAQDEVILYNKDIRIDE 331
Cdd:TIGR00492 316 MVDLgpDLQDKTGDEVILWGEEISIDE 342
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
7-223 |
4.70e-43 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 148.53 E-value: 4.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 7 LDTEAFYQNAVKVKN----NEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMNPVY-- 80
Cdd:pfam01168 1 IDLDALRHNLRRLRRragpGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 81 DFDLVKRYDIHMTLPSLNYYYKY----KQDLKGIHVHLEYENLLHRSGFRnIEEIREVLKDHDQNnqDKMIISGIWTHFG 156
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALaaaaRRLGKPLRVHLKIDTGMGRLGFR-PEEALALLARLAAL--PGLRLEGLMTHFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749212 157 YADEFDVDEYKMERDAWLNLINTLLNENYHFDMIHSQNSASYFRENQmllpHHTHARVGIALYGSRP 223
Cdd:pfam01168 158 CADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPL----HFDMVRPGIALYGLSP 220
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
25-326 |
2.75e-39 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This subfamily is composed of Enterococcus gallinarum VanT and similar proteins. VanT is a membrane-bound serine racemase (EC 5.1.1.18) that is essential for vancomycin resistance in Enterococcus gallinarum. It converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. The C-terminal region of this protein contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, which is homologous to the fold type III PLP-dependent enzyme, bacterial alanine racemase (AR). AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. On the basis of this similarity, it has been suggested that dimer formation of VanT is required for its catalytic activity, and that it catalyzes the racemization of serine in a mechanistically similar manner to that of alanine by bacterial AR. Some biochemical evidence indicates that VanT also exhibits alanine racemase activity and plays a role in the racemization of L-alanine. VanT contains a unique N-terminal transmembrane domain, which may function as an L-serine transporter. VanT serine racemases are not related to eukaryotic serine racemases, which are fold type II PLP-dependent enzymes.
Pssm-ID: 143498 [Multi-domain] Cd Length: 368 Bit Score: 142.88 E-value: 2.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 25 IMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRK--IAPEATIFLMNPVYDFDLVKRYDIHMTLPSLNYYYK 102
Cdd:cd06825 28 LMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREagIKGEILILGYTPPVRAKELKKYSLTQTLISEAYAEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 103 YKQDLKGIHVHLEYENLLHRSGFrNIEEIREVLKDHDQNNQDkmiISGIWTHFGYAD---EFDVDEYKMERDAWLNLINT 179
Cdd:cd06825 108 LSKYAVNIKVHLKVDTGMHRLGE-SPEDIDSILAIYRLKNLK---VSGIFSHLCVSDsldEDDIAFTKHQIACFDQVLAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 180 LLNENYHFDMIHSQNsaSYFRENQMLLpHHTHARVGIALYG--SRPyslinEERITQS------LTVKGNVIQVRDVNKG 251
Cdd:cd06825 184 LKARGIEVGKIHIQS--SYGILNYPDL-KYDYVRPGILLYGvlSDP-----NDPTKLGldlrpvLSLKAKVILVRKVAKG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 252 DYCGYSFAFeVKNDHTQLAVVDIGYGDGILKSRAKHEA--IINGKRYPIRALM-MSHMFIEVDD--EVHAQDEVILYNKD 326
Cdd:cd06825 256 EAVGYGRLF-VASRTTRIATVSIGYADGYPRSLSNQKAyvLINGKRAPIIGNIcMDQLMVDVTDipEVKEGDTATLIGQD 334
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
25-332 |
2.30e-26 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 110.43 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 25 IMAVVKnnAYHYGL-EFAVKTFLKAE-INTFSTTSLNEAIRVRKIAPEATIFLMNP-VYDFDLVKR-------YDIHmTL 94
Cdd:PRK11930 486 IMCMVK--AFAYGSgSYEIAKLLQEHrVDYLAVAYADEGVSLRKAGITLPIMVMNPePTSFDTIIDyklepeiYSFR-LL 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 95 PSLNYYYKyKQDLKGIHVHLEYENLLHRSGFR--NIEEIREVLKDHDqnnqdKMIISGIWTHFGYADEFDVDEYKMERDA 172
Cdd:PRK11930 563 DAFIKAAQ-KKGITGYPIHIKIDTGMHRLGFEpeDIPELARRLKKQP-----ALKVRSVFSHLAGSDDPDHDDFTRQQIE 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 173 WLNLINTLLNENYHFDMI-HSQNSA--SYFRENQMLLphhthARVGIALYGSRPYSLINEErITQSLTVKGNVIQVRDVN 249
Cdd:PRK11930 637 LFDEGSEELQEALGYKPIrHILNSAgiERFPDYQYDM-----VRLGIGLYGVSASGAGQQA-LRNVSTLKTTILQIKHVP 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 250 KGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILK--SRAKHEAIINGKRYPIRA-LMMSHMFIEVDDeVHAQ--DEVILYN 324
Cdd:PRK11930 711 KGETVGYGRKGVVTKP-SRIATIPIGYADGLNRrlGNGVGYVLVNGQKAPIVGnICMDMCMIDVTD-IDAKegDEVIIFG 788
|
....*...
gi 487749212 325 KDIRIDEF 332
Cdd:PRK11930 789 EELPVTEL 796
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
6-331 |
3.75e-26 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; This subfamily is composed mainly of proteobacterial alanine racemases (EC 5.1.1.1), fold type III PLP-dependent enzymes that catalyze the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. hese proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143500 [Multi-domain] Cd Length: 354 Bit Score: 106.81 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 6 SLDTEAFYQNAVKVKNNEP---IMAVVKNNAYHYGLEFAVKTFLKAEinTFSTTSLNEAIRVRKIAPEATIFLMNPVYDF 82
Cdd:cd06827 5 TIDLAALRHNLRLVRELAPnskILAVVKANAYGHGLVRVAKALADAD--GFAVACIEEALALREAGITKPILLLEGFFSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 83 D---LVKRYDIHMTLPS---LNYYYKYKQDLKgIHVHLEYENLLHRSGFRNiEEIREVLKDHDQNNQDKMIisGIWTHFG 156
Cdd:cd06827 83 DelpLAAEYNLWTVVHSeeqLEWLEQAALSKP-LNVWLKLDSGMHRLGFSP-EEYAAAYQRLKASPNVASI--VLMTHFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 157 YADEFDvDEYKMERdawLNLINTLLNENYHFDMIHsqNSASYFRENQmllPHHTHARVGIALYGSRPY--SLINEERITQ 234
Cdd:cd06827 159 CADEPD-SPGTAKQ---LAIFEQATAGLPGPRSLA--NSAAILAWPE---AHGDWVRPGIMLYGASPFadKSGADLGLKP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 235 SLTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILKSrAKHEA--IINGKRYPI--RALM-MshMFIE 309
Cdd:cd06827 230 VMTLSSEIIAVRELKAGESVGYGATWTAPRP-MRIGVVAIGYGDGYPRH-APSGTpvLVNGQRTPLvgRVSMdM--LTVD 305
|
330 340
....*....|....*....|....
gi 487749212 310 VDDEVHAQ--DEVILYNKDIRIDE 331
Cdd:cd06827 306 LTDLPEAKvgDPVELWGKGLPVDE 329
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
236-349 |
6.45e-25 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 97.52 E-value: 6.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 236 LTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILKSRAKHEAIINGKRYPIRA-LMMSHMFIEVDD-- 312
Cdd:smart01005 2 MTLKARVIQVREVPAGETVGYGATFTADRD-TRIATVPIGYADGYPRALSNGPVLINGQRVPVVGrVSMDQLMVDVTDip 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 487749212 313 EVHAQDEVILYNKD-IRIDEFTFKGVGANSEQLSAMNH 349
Cdd:smart01005 81 DVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGP 118
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
4-332 |
1.48e-16 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 80.05 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 4 IW-SLDTEAFYQNAVKVK----NNEPIMAVVKNNAYHYGLEFAVKTFLKAEINTFSTTSLNEAIRVRKIAPEATIFLMN- 77
Cdd:PRK13340 41 AWlEISPGAFRHNIKTLRsllaNKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRVRs 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 78 -PVYDFDLVKRYDIHMTLPSLNYYYKY----KQDLKGIHVHLEY------ENLLHRSGFRNIEEIREVLKdhdqnnQDKM 146
Cdd:PRK13340 121 aSPAEIEQALRYDLEELIGDDEQAKLLaaiaKKNGKPIDIHLALnsggmsRNGLDMSTARGKWEALRIAT------LPSL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 147 IISGIWTHFGYADEFDVDEyKMER----DAWLNLINTLLNENYhfdMIHSQNSASYFRenqmlLP--HHTHARVGIALYG 220
Cdd:PRK13340 195 GIVGIMTHFPNEDEDEVRW-KLAQfkeqTAWLIGEAGLKREKI---TLHVANSYATLN-----VPeaHLDMVRPGGILYG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 221 SRpysLINEERITQSLTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGILKSRA-KHEAIINGKRYPI- 298
Cdd:PRK13340 266 DR---HPANTEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRD-SRLANLPVGYSDGYPRHASnKAPVLINGQRAPVv 341
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 487749212 299 -RALMMSHMfIEVDD--EVHAQDEVILY----NKDIRIDEF 332
Cdd:PRK13340 342 gRVSMNTLM-VDVTDipNVKPGDEVVLFgkqgNAEITVDEV 381
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
236-332 |
1.53e-16 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 75.10 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 236 LTVKGNVIQVRDVNKGDYCGYSFAFEVKNDhTQLAVVDIGYGDGIlkSRA---KHEAIINGKRYPIRALM-MSHMFIEVD 311
Cdd:pfam00842 2 MTLKSRVIQVKTVPAGEGVGYGRTYTAERD-TRIATVPIGYADGY--PRAlsnRGEVLINGKRAPIVGRVcMDQLMVDVT 78
|
90 100
....*....|....*....|....*..
gi 487749212 312 D--EVHAQDEVILYNKD----IRIDEF 332
Cdd:pfam00842 79 DvpEVKVGDEVTLFGKQgdeeITADEL 105
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
6-279 |
5.02e-08 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 53.97 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 6 SLDTEAFYQNAVKVKNNEP---IMAVVKNNAYHYGLEfAVKTFLKAEiNTFSTTSLNEAIRVRKIAPEATIFLMNPVYDF 82
Cdd:PRK03646 7 SLDLQALKQNLSIVREAAPgarVWSVVKANAYGHGIE-RIWSALGAT-DGFAVLNLEEAITLRERGWKGPILMLEGFFHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 83 DLVKRYDIH--MTLPSLNYYYKYKQDL---KGIHVHLEYENLLHRSGFRNiEEIREVlkdHDQ----NNQDKMIIsgiWT 153
Cdd:PRK03646 85 QDLELYDQHrlTTCVHSNWQLKALQNArlkAPLDIYLKVNSGMNRLGFQP-ERVQTV---WQQlramGNVGEMTL---MS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 154 HFGYADEFDVDEYKMER--------DAWLNLIN---TLLNENYHFDMIhsqnsasyfrenqmllphhthaRVGIALYGSR 222
Cdd:PRK03646 158 HFARADHPDGISEAMARieqaaeglECERSLSNsaaTLWHPQAHFDWV----------------------RPGIILYGAS 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 223 PYSLINE--ERITQS-LTVKGNVIQVRDVNKGDYCGYSFAFeVKNDHTQLAVVDIGYGDG 279
Cdd:PRK03646 216 PSGQWRDiaNTGLRPvMTLSSEIIGVQTLKAGERVGYGGRY-TARREQRIGIVAAGYADG 274
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
25-216 |
2.34e-07 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.
Pssm-ID: 143484 [Multi-domain] Cd Length: 211 Bit Score: 50.78 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 25 IMAVVKNNAYhygLEFAvKTFLkAEINTFSTTSLNEAIRVRK--IAPEATIFLMNPVYDFDL---VKRYDIHMTLPSLNY 99
Cdd:cd06808 18 LFAVVKANAN---PEVA-RTLA-ALGTGFDVASLGEALLLRAagIPPEPILFLGPCKQVSELedaAEQGVIVVTVDSLEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749212 100 YYKYKQ----DLKGIHVHLEY--ENLLHRSGFRN--IEEIREVLKDHDQNNqdkmiISGIWTHFGYADEfDVDEYKMERD 171
Cdd:cd06808 93 LEKLEEaalkAGPPARVLLRIdtGDENGKFGVRPeeLKALLERAKELPHLR-----LVGLHTHFGSADE-DYSPFVEALS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487749212 172 AWLNLINTLLNENYHFDMIHSQNSASYFRENQMLLPHHTHARVGI 216
Cdd:cd06808 167 RFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGTFIIVEPGR 211
|
|
| |
