|
Name |
Accession |
Description |
Interval |
E-value |
| PbpC |
COG4953 |
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ... |
57-308 |
3.01e-85 |
|
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443980 [Multi-domain] Cd Length: 773 Bit Score: 271.71 E-value: 3.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 57 PAGAWLTAKLLPaPPMLEGVPFSSALTDRHGTLLELRLAEDGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPAL 136
Cdd:COG4953 22 ALALWALDRLFP-LPLLFAVPYSTVVLDRDGTLLRAFLAADGQWRLPVPLDEVSPRYLQALLAYEDRRFYYHPGVNPLAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 137 FRALWGTVTH--RPMGASTLTMQLARIRLGlETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAAR 214
Cdd:COG4953 101 LRAAWQNLRSgrIVSGGSTLTMQVARLLEP-RPRTLSGKLRQILRALQLERRYSKDEILELYLNLAPYGGNIEGVEAASL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 215 VWFGRAPAELTAAQAASLTIVPQNPVARRPGR--EAWREAFSRVGESLIAEGVFPETLAPAMRPEAAPAVtgPGKLPHLA 292
Cdd:COG4953 180 AYFGKPPSRLSLAEAALLAVLPQAPSRRRPDRnpERARAARDRVLARLAEAGVIDAEEAALALLEPVPAR--RRPLPQLA 257
|
250
....*....|....*.
gi 495817802 293 RHDARLVAALAPGERV 308
Cdd:COG4953 258 PHLARRLLRQLPGGTR 273
|
|
| PBP_1c |
TIGR02073 |
penicillin-binding protein 1C; This subfamily of the penicillin binding proteins includes the ... |
69-306 |
1.75e-72 |
|
penicillin-binding protein 1C; This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273954 [Multi-domain] Cd Length: 727 Bit Score: 236.93 E-value: 1.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 69 APPMLEGVPFSSALTDRHGTLLELRLAEDGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTVTH-- 146
Cdd:TIGR02073 1 PPPLLFHRPSSTVVLDRHGTLLRALLANDGQWRLPVPLEDISPKFLQALLLYEDKRFYWHPGVNPLALLRAAWQNLTNgr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 147 RPMGASTLTMQLARIRLGLETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAARVWFGRAPAELTA 226
Cdd:TIGR02073 81 RVSGGSTLTMQLARLLDPELSRTLTGKLRQMWRAIQLEARYSKREILEAYLNLAPYGGNLEGLRAASLIYFGKEPSSLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 227 AQAASLTIVPQNPVARRPGR--EAWREAFSRVGESLIAEGVF-PETLAPAmrpEAAPAVTGPGKLPHLARHDARLVAALA 303
Cdd:TIGR02073 161 AEAALLAALPQAPSARRLDRlpKAAKAARDRLLDRMVEQGPDdSEQVALA---ALEPLPALPEPLPQLAPHFALKLLRAR 237
|
...
gi 495817802 304 PGE 306
Cdd:TIGR02073 238 PEI 240
|
|
| Transgly |
pfam00912 |
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ... |
86-256 |
1.19e-57 |
|
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
Pssm-ID: 459993 [Multi-domain] Cd Length: 177 Bit Score: 183.49 E-value: 1.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 86 HGTLLElrlAEDGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTVT--HRPMGASTLTMQLARIRL 163
Cdd:pfam00912 1 DGTLLA---ELGEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRsgRIVQGGSTITQQLAKNLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 164 GLETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAARVWFGRAPAELTAAQAASLTIVPQNPVARR 243
Cdd:pfam00912 78 LTPERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYN 157
|
170
....*....|....*
gi 495817802 244 PGR--EAWREAFSRV 256
Cdd:pfam00912 158 PLRnpERAKRRRNLV 172
|
|
| PRK11240 |
PRK11240 |
penicillin-binding protein 1C; Provisional |
57-309 |
5.25e-43 |
|
penicillin-binding protein 1C; Provisional
Pssm-ID: 183049 [Multi-domain] Cd Length: 772 Bit Score: 157.17 E-value: 5.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 57 PAGAWLTAKLLPAPpmLEGVPFSSALTDRHGTLLeLRLAE-DGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPA 135
Cdd:PRK11240 20 FLALWLADKLWPLP--LHEVNPARVVVAEDGTPL-WRFADaDGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 136 LFRALWGTVTHRPM--GASTLTMQLARIrLGLETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAA 213
Cdd:PRK11240 97 VARAAWQDLTSGRVisGGSTLTMQVARL-LDPHPRTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAAS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 214 RVWFGRAPAELTAAQAASLTIVPQNPVARRPGREAWR--EAFSRVGESLIAEGVFPETLAPAMRPEaaPAVTGPGKLPHL 291
Cdd:PRK11240 176 WAYLGKSPANLSYAEAALLAVLPQAPSRLRPDRWPERaeAARNKVLERMAEQGVWSAEQVKESREE--PVWLAPRQMPQL 253
|
250
....*....|....*...
gi 495817802 292 ARHDARLVAALAPGERVR 309
Cdd:PRK11240 254 APLFARMMLGKSKSDKIV 271
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PbpC |
COG4953 |
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ... |
57-308 |
3.01e-85 |
|
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443980 [Multi-domain] Cd Length: 773 Bit Score: 271.71 E-value: 3.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 57 PAGAWLTAKLLPaPPMLEGVPFSSALTDRHGTLLELRLAEDGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPAL 136
Cdd:COG4953 22 ALALWALDRLFP-LPLLFAVPYSTVVLDRDGTLLRAFLAADGQWRLPVPLDEVSPRYLQALLAYEDRRFYYHPGVNPLAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 137 FRALWGTVTH--RPMGASTLTMQLARIRLGlETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAAR 214
Cdd:COG4953 101 LRAAWQNLRSgrIVSGGSTLTMQVARLLEP-RPRTLSGKLRQILRALQLERRYSKDEILELYLNLAPYGGNIEGVEAASL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 215 VWFGRAPAELTAAQAASLTIVPQNPVARRPGR--EAWREAFSRVGESLIAEGVFPETLAPAMRPEAAPAVtgPGKLPHLA 292
Cdd:COG4953 180 AYFGKPPSRLSLAEAALLAVLPQAPSRRRPDRnpERARAARDRVLARLAEAGVIDAEEAALALLEPVPAR--RRPLPQLA 257
|
250
....*....|....*.
gi 495817802 293 RHDARLVAALAPGERV 308
Cdd:COG4953 258 PHLARRLLRQLPGGTR 273
|
|
| PBP_1c |
TIGR02073 |
penicillin-binding protein 1C; This subfamily of the penicillin binding proteins includes the ... |
69-306 |
1.75e-72 |
|
penicillin-binding protein 1C; This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273954 [Multi-domain] Cd Length: 727 Bit Score: 236.93 E-value: 1.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 69 APPMLEGVPFSSALTDRHGTLLELRLAEDGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTVTH-- 146
Cdd:TIGR02073 1 PPPLLFHRPSSTVVLDRHGTLLRALLANDGQWRLPVPLEDISPKFLQALLLYEDKRFYWHPGVNPLALLRAAWQNLTNgr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 147 RPMGASTLTMQLARIRLGLETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAARVWFGRAPAELTA 226
Cdd:TIGR02073 81 RVSGGSTLTMQLARLLDPELSRTLTGKLRQMWRAIQLEARYSKREILEAYLNLAPYGGNLEGLRAASLIYFGKEPSSLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 227 AQAASLTIVPQNPVARRPGR--EAWREAFSRVGESLIAEGVF-PETLAPAmrpEAAPAVTGPGKLPHLARHDARLVAALA 303
Cdd:TIGR02073 161 AEAALLAALPQAPSARRLDRlpKAAKAARDRLLDRMVEQGPDdSEQVALA---ALEPLPALPEPLPQLAPHFALKLLRAR 237
|
...
gi 495817802 304 PGE 306
Cdd:TIGR02073 238 PEI 240
|
|
| Transgly |
pfam00912 |
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ... |
86-256 |
1.19e-57 |
|
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
Pssm-ID: 459993 [Multi-domain] Cd Length: 177 Bit Score: 183.49 E-value: 1.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 86 HGTLLElrlAEDGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTVT--HRPMGASTLTMQLARIRL 163
Cdd:pfam00912 1 DGTLLA---ELGEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRsgRIVQGGSTITQQLAKNLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 164 GLETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAARVWFGRAPAELTAAQAASLTIVPQNPVARR 243
Cdd:pfam00912 78 LTPERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYN 157
|
170
....*....|....*
gi 495817802 244 PGR--EAWREAFSRV 256
Cdd:pfam00912 158 PLRnpERAKRRRNLV 172
|
|
| MrcB |
COG0744 |
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ... |
67-244 |
3.06e-45 |
|
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440507 [Multi-domain] Cd Length: 630 Bit Score: 162.01 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 67 LPAPPMLEGV--PFSSALTDRHGTLLELRLAEDGIYrlkTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTV 144
Cdd:COG0744 41 LPDPEELEDLalPQTSTIYDRDGTLIATLGDENREW---VPLDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 145 THRPM--GASTLTMQLARIRLGLETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAARVWFGRAPA 222
Cdd:COG0744 118 TAGGVvqGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSAS 197
|
170 180
....*....|....*....|..
gi 495817802 223 ELTAAQAASLTIVPQNPVARRP 244
Cdd:COG0744 198 DLTLAEAALLAGLVKAPSYYDP 219
|
|
| PRK11240 |
PRK11240 |
penicillin-binding protein 1C; Provisional |
57-309 |
5.25e-43 |
|
penicillin-binding protein 1C; Provisional
Pssm-ID: 183049 [Multi-domain] Cd Length: 772 Bit Score: 157.17 E-value: 5.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 57 PAGAWLTAKLLPAPpmLEGVPFSSALTDRHGTLLeLRLAE-DGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPA 135
Cdd:PRK11240 20 FLALWLADKLWPLP--LHEVNPARVVVAEDGTPL-WRFADaDGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 136 LFRALWGTVTHRPM--GASTLTMQLARIrLGLETRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAA 213
Cdd:PRK11240 97 VARAAWQDLTSGRVisGGSTLTMQVARL-LDPHPRTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAAS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 214 RVWFGRAPAELTAAQAASLTIVPQNPVARRPGREAWR--EAFSRVGESLIAEGVFPETLAPAMRPEaaPAVTGPGKLPHL 291
Cdd:PRK11240 176 WAYLGKSPANLSYAEAALLAVLPQAPSRLRPDRWPERaeAARNKVLERMAEQGVWSAEQVKESREE--PVWLAPRQMPQL 253
|
250
....*....|....*...
gi 495817802 292 ARHDARLVAALAPGERVR 309
Cdd:PRK11240 254 APLFARMMLGKSKSDKIV 271
|
|
| MrcA |
COG5009 |
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]; |
101-239 |
5.22e-33 |
|
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 444033 [Multi-domain] Cd Length: 785 Bit Score: 128.35 E-value: 5.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 101 RLKTPLSEIPP----AWIAAtihyEDRWFAKHPGVNVPALFRALWGTVT--HRPMGASTLTMQLAR-IRLGLEtRSVSGK 173
Cdd:COG5009 66 RIPVPIEEIPPllinAFLAA----EDKRFYEHPGVDPIGIARAAVVNLRtgRRVQGGSTITQQVAKnFLLSPE-RTLTRK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495817802 174 LAQIFWALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAARVWFGRAPAELTAAQAASLTIVPQNP 239
Cdd:COG5009 141 IKEAILALRIEQELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAP 206
|
|
| mrcA |
PRK11636 |
penicillin-binding protein 1a; Provisional |
101-239 |
4.70e-21 |
|
penicillin-binding protein 1a; Provisional
Pssm-ID: 183248 [Multi-domain] Cd Length: 850 Bit Score: 93.66 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 101 RLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTVT--HRPMGASTLTMQLARIRLGLETRSVSGKLAQIF 178
Cdd:PRK11636 66 RIPLTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFsgHASQGASTITQQLARNFFLSPERTLMRKIKEAF 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495817802 179 WALRYEAHYAKDEILEAYLNLAPYGGNIEGAGAAARVWFGRAPAELTAAQAASLTIVPQNP 239
Cdd:PRK11636 146 LAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAP 206
|
|
| PRK14850 |
PRK14850 |
penicillin-binding protein 1b; Provisional |
89-232 |
2.52e-17 |
|
penicillin-binding protein 1b; Provisional
Pssm-ID: 237835 [Multi-domain] Cd Length: 764 Bit Score: 82.20 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 89 LLELRLAEDGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTVT--HRPMGASTLTMQLARIRLGLE 166
Cdd:PRK14850 145 LIAMLYSPEGKKRLFIPRNQYPEMLIKTLLAIEDKYFYEHDGIHLSSIGRAFLVNLMsgHTIQGGSTLTQQLVKNLFLTN 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 167 TRSVSGKLAQIFWALRYEAHYAKDEILEAYLNLAPYGGN----IEGAGAAARVWFGRAPAELTAAQAASL 232
Cdd:PRK14850 225 TRSLWRKINEIYMALILDRFYSKDRILELYLNEVYLGQDgneqIRGFPLASIYYFGRPINELNLDQYALL 294
|
|
| PRK13481 |
PRK13481 |
glycosyltransferase; Provisional |
105-218 |
6.33e-15 |
|
glycosyltransferase; Provisional
Pssm-ID: 184078 [Multi-domain] Cd Length: 232 Bit Score: 72.53 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 105 PLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTVTHRPM-GASTLTMQLARIRLGLETRSVSGKLAQIFWALRY 183
Cdd:PRK13481 49 SADNMPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRDVqGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRV 128
|
90 100 110
....*....|....*....|....*....|....*
gi 495817802 184 EAHYAKDEILEAYLNLAPYGGNIEGAGAAARVWFG 218
Cdd:PRK13481 129 EKQYSKNEILSFYLNNIYFGDNQYTLEGAANHYFG 163
|
|
| mrcB |
PRK09506 |
bifunctional glycosyl transferase/transpeptidase; Reviewed |
97-232 |
1.51e-13 |
|
bifunctional glycosyl transferase/transpeptidase; Reviewed
Pssm-ID: 236544 [Multi-domain] Cd Length: 830 Bit Score: 70.95 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495817802 97 DGIYRLKTPLSEIPPAWIAATIHYEDRWFAKHPGVNVPALFRALWGTVT--HRPMGASTLTMQLARIRLGLETRSVSGKL 174
Cdd:PRK09506 207 NGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTagRTVQGGSTLTQQLVKNLFLSNERSLWRKA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495817802 175 AQIFWALRYEAHYAKDEILEAYLN---LAPYGGN-IEGAGAAARVWFGRAPAELTAAQAASL 232
Cdd:PRK09506 287 NEAYMALIMDARYSKDRILELYLNevyLGQSGDDqIRGFPLASLYYFGRPVEELSLDQQALL 348
|
|
|