|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
1-305 |
5.35e-112 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 327.17 E-value: 5.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 1 MDERIRLWTDPTPVHPVPRLAEALGLhpeRLLMKRDDLIGWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMT 80
Cdd:PRK03910 5 RFPRLELAGLPTPLEPLPRLSAALGP---DIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 81 AAAGASLGLDVVLVLEGHE------VAARGNVLLDGLFGARIEW-SGDEGAESRAASVVAELEGAGTRVHRVAFGGSDAH 153
Cdd:PRK03910 82 AAAAAKLGLKCVLLLENPVpteaenYLANGNVLLDDLFGAEIHVvPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 154 SVQGFVDAGHELTAQVGA----VDHVVVALGSGGTMAGLV---EALGPE-RVLGVHCGA--------VAEPRAVVAGFLT 217
Cdd:PRK03910 162 GALGYVACALEIAQQLAEggvdFDAVVVASGSGGTHAGLAaglAALGPDiPVIGVTVSRsaaeqepkVAKLAQATAELLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 218 ErGTGIEAAALRIDADRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGADDRVVLWHSGGVP 297
Cdd:PRK03910 242 L-PTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320
|
....*...
gi 501256392 298 GLFGHADL 305
Cdd:PRK03910 321 ALFAYADA 328
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
4-304 |
5.09e-96 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 286.31 E-value: 5.09e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 4 RIRLWTDPTPVHPVPRLAEALGLhpeRLLMKRDDLIGWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMTAAA 83
Cdd:COG2515 4 RLPLAFLPTPLQPLPRLSAALGV---ELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 84 GASLGLDVVLVLEGHEV-AARGNVLLDGLFGARIEWSGDE---GAESRAASVVAELEGAGTRVHRVAFGGSDAHSVQGFV 159
Cdd:COG2515 81 AAKLGLKCVLVLRGEEPtPLNGNLLLDRLLGAELHFVSRGeyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLGALGYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 160 DAGHELTAQVGAV----DHVVVALGSGGTMAGLVEAL----GPERVLGVHCGAVAEP-RAVVAGFLTERGT---GIEAAA 227
Cdd:COG2515 161 EAAAELAAQLAELgvdfDYIVVASGSGGTLAGLVAGLallgSDTRVIGISVLKGADFlRERVAELARATAAllgLVSRAD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501256392 228 LRIDADRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGADDRVVLWHSGGVPGLFGHAD 304
Cdd:COG2515 241 IELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGYAE 317
|
|
| ACC_deam_rel |
TIGR01275 |
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ... |
11-304 |
1.74e-56 |
|
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).
Pssm-ID: 273533 [Multi-domain] Cd Length: 318 Bit Score: 185.01 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 11 PTPVHPVPRLAEALGLHperLLMKRDDLIGWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMTAAAGASLGLD 90
Cdd:TIGR01275 7 PTPIQYLPRLSDYLGRE---IYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKLGLH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 91 VVLVLEGHEVAA------RGNVLLDGLFGARI-EWSGDEGAESRA-ASVVAE-LEGAGTRVHRVAFGGSDAHSVQGFVDA 161
Cdd:TIGR01275 84 CVLLLRNPIGTTaenyllNGNLLLDDLFGAETrIESCEEYTDIDAqLEELAErLEKEGFKPYVIPVGGSNSLGALGYVEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 162 GHELTAQVGAV---DHVVVALGSGGTMAGL---VEALGPE-RVLGVHCGAVAEPR-----AVVAGFLTERGTGIEAAALR 229
Cdd:TIGR01275 164 ALEIAQQLESEvkfDSIVVASGSGGTIAGLslgLSHLMPDvELVGVTVSRFVADQtdkfvNLVQAIAEGLELTVSAVIPL 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501256392 230 IDaDRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGaDDRVVLWHSGGVPGLFGHAD 304
Cdd:TIGR01275 244 WD-DYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFG-DKPILFIHTGGIPGLFAYHD 316
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
12-295 |
1.17e-49 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 166.83 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 12 TPVHPVPRLAEALGLHPErLLMKRDDLI-GWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMTAAAGASLGLD 90
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVE-IYAKRDDCNsGLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 91 VVLVLEGHEVAAR------GNVLLDGLFGARIEW---SGDEGAESRAASVVAELEGAGTRVHRVAFGGSDaHSVQ--GFV 159
Cdd:cd06449 80 CVLVQENWVPYSDavydrvGNILLSRIMGADVRLvsaGFDIGIRKSFEEAAEEVEAKGGKPYVIPAGGSE-HPLGglGYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 160 DAGHELTAQ----VGAVDHVVVALGSGGTMAGLV---EALGPE-RVLGVHCGAVAEP------RAVVAGfLTERGTGIEA 225
Cdd:cd06449 159 GFVLEIAQQeeelGFKFDSIVVCSVTGSTHAGLSvglAALGRQrRVIGIDASAKPEKtkaqvlRIAQAK-LAEEGLEVKE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 226 AALRIDADRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGADDRVVLWHSGG 295
Cdd:cd06449 238 EDVVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
11-294 |
1.76e-30 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 116.26 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 11 PTPVHPVPRLAEALGLhpeRLLMKRDDLIGwgGGGNKARKLEHSLGRAVARGATTVVTTgAAQSNHARMTAAAGASLGLD 90
Cdd:pfam00291 7 PTPLVRLPRLSKELGV---DVYLKLESLNP--TGSFKDRGALNLLLRLKEGEGGKTVVE-ASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 91 VVLVLegHEVAARGNVLLDGLFGARIEWSGD--EGAESRAASVVAELEGAgTRVHrvafGGSDAHSVQGFVDAGHELTAQ 168
Cdd:pfam00291 81 VTIVV--PEDAPPGKLLLMRALGAEVVLVGGdyDEAVAAARELAAEGPGA-YYIN----QYDNPLNIEGYGTIGLEILEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 169 VG-AVDHVVVALGSGGTMAGLVEAL---GPE-RVLGVH-CGAVAEPRAVVAGFLTER------------GTGIEAAALRI 230
Cdd:pfam00291 154 LGgDPDAVVVPVGGGGLIAGIARGLkelGPDvRVIGVEpEGAPALARSLAAGRPVPVpvadtiadglgvGDEPGALALDL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501256392 231 DADRVGPGYAHLTDEAREALVLVARTTGILLDPtyTARAAAGLAAAVGDGSIGADDRVVLWHSG 294
Cdd:pfam00291 234 LDEYVGEVVTVSDEEALEAMRLLARREGIVVEP--SSAAALAALKLALAGELKGGDRVVVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
1-305 |
5.35e-112 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 327.17 E-value: 5.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 1 MDERIRLWTDPTPVHPVPRLAEALGLhpeRLLMKRDDLIGWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMT 80
Cdd:PRK03910 5 RFPRLELAGLPTPLEPLPRLSAALGP---DIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 81 AAAGASLGLDVVLVLEGHE------VAARGNVLLDGLFGARIEW-SGDEGAESRAASVVAELEGAGTRVHRVAFGGSDAH 153
Cdd:PRK03910 82 AAAAAKLGLKCVLLLENPVpteaenYLANGNVLLDDLFGAEIHVvPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 154 SVQGFVDAGHELTAQVGA----VDHVVVALGSGGTMAGLV---EALGPE-RVLGVHCGA--------VAEPRAVVAGFLT 217
Cdd:PRK03910 162 GALGYVACALEIAQQLAEggvdFDAVVVASGSGGTHAGLAaglAALGPDiPVIGVTVSRsaaeqepkVAKLAQATAELLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 218 ErGTGIEAAALRIDADRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGADDRVVLWHSGGVP 297
Cdd:PRK03910 242 L-PTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320
|
....*...
gi 501256392 298 GLFGHADL 305
Cdd:PRK03910 321 ALFAYADA 328
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
4-304 |
5.09e-96 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 286.31 E-value: 5.09e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 4 RIRLWTDPTPVHPVPRLAEALGLhpeRLLMKRDDLIGWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMTAAA 83
Cdd:COG2515 4 RLPLAFLPTPLQPLPRLSAALGV---ELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 84 GASLGLDVVLVLEGHEV-AARGNVLLDGLFGARIEWSGDE---GAESRAASVVAELEGAGTRVHRVAFGGSDAHSVQGFV 159
Cdd:COG2515 81 AAKLGLKCVLVLRGEEPtPLNGNLLLDRLLGAELHFVSRGeyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLGALGYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 160 DAGHELTAQVGAV----DHVVVALGSGGTMAGLVEAL----GPERVLGVHCGAVAEP-RAVVAGFLTERGT---GIEAAA 227
Cdd:COG2515 161 EAAAELAAQLAELgvdfDYIVVASGSGGTLAGLVAGLallgSDTRVIGISVLKGADFlRERVAELARATAAllgLVSRAD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501256392 228 LRIDADRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGADDRVVLWHSGGVPGLFGHAD 304
Cdd:COG2515 241 IELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGYAE 317
|
|
| ACC_deam_rel |
TIGR01275 |
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ... |
11-304 |
1.74e-56 |
|
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).
Pssm-ID: 273533 [Multi-domain] Cd Length: 318 Bit Score: 185.01 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 11 PTPVHPVPRLAEALGLHperLLMKRDDLIGWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMTAAAGASLGLD 90
Cdd:TIGR01275 7 PTPIQYLPRLSDYLGRE---IYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKLGLH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 91 VVLVLEGHEVAA------RGNVLLDGLFGARI-EWSGDEGAESRA-ASVVAE-LEGAGTRVHRVAFGGSDAHSVQGFVDA 161
Cdd:TIGR01275 84 CVLLLRNPIGTTaenyllNGNLLLDDLFGAETrIESCEEYTDIDAqLEELAErLEKEGFKPYVIPVGGSNSLGALGYVEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 162 GHELTAQVGAV---DHVVVALGSGGTMAGL---VEALGPE-RVLGVHCGAVAEPR-----AVVAGFLTERGTGIEAAALR 229
Cdd:TIGR01275 164 ALEIAQQLESEvkfDSIVVASGSGGTIAGLslgLSHLMPDvELVGVTVSRFVADQtdkfvNLVQAIAEGLELTVSAVIPL 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501256392 230 IDaDRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGaDDRVVLWHSGGVPGLFGHAD 304
Cdd:TIGR01275 244 WD-DYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFG-DKPILFIHTGGIPGLFAYHD 316
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
12-295 |
1.17e-49 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 166.83 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 12 TPVHPVPRLAEALGLHPErLLMKRDDLI-GWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMTAAAGASLGLD 90
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVE-IYAKRDDCNsGLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 91 VVLVLEGHEVAAR------GNVLLDGLFGARIEW---SGDEGAESRAASVVAELEGAGTRVHRVAFGGSDaHSVQ--GFV 159
Cdd:cd06449 80 CVLVQENWVPYSDavydrvGNILLSRIMGADVRLvsaGFDIGIRKSFEEAAEEVEAKGGKPYVIPAGGSE-HPLGglGYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 160 DAGHELTAQ----VGAVDHVVVALGSGGTMAGLV---EALGPE-RVLGVHCGAVAEP------RAVVAGfLTERGTGIEA 225
Cdd:cd06449 159 GFVLEIAQQeeelGFKFDSIVVCSVTGSTHAGLSvglAALGRQrRVIGIDASAKPEKtkaqvlRIAQAK-LAEEGLEVKE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 226 AALRIDADRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGADDRVVLWHSGG 295
Cdd:cd06449 238 EDVVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
|
|
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
4-304 |
4.13e-44 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 153.12 E-value: 4.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 4 RIRLWTDPTPVHPVPRLAEALGLHperLLMKRDDLIGWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMTAAA 83
Cdd:PRK14045 14 RVELIPWETPIQYLPNISRELGAD---VYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVTGLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 84 GASLGLDVVLVLEGHEVaARGNVLLDGLFG--ARIEWSGDEGAESRAASVVA-ELEGAGTRVHRVAFGGSDAHSVQGFVD 160
Cdd:PRK14045 91 AKKLGLDAVLVLRGKEE-LKGNYLLDKIMGieTRVYEAKDSFELMKYAEEVAeELKGEGRKPYIIPPGGASPVGTLGYVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 161 AGHELTAQVGAV----DHVVVALGSGGTMAGLVEALG----PERVLGVHCGAVAEPRAVVAGFLTERGT---GIEAAALR 229
Cdd:PRK14045 170 AVGEIATQVKKLgvrfDSIVVAVGSGGTLAGLSLGLAilnaEWRVVGIAVGSFGEKMKEKVKNLVKKTKellGVKVKVQE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501256392 230 IDADRVGPG-YAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGadDRVVLWHSGGVPGLFGHAD 304
Cdd:PRK14045 250 PELYDYSFGeYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKGELG--EKILFIHTGGISGTFHYGD 323
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
3-303 |
5.63e-39 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 139.78 E-value: 5.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 3 ERIRLWTDPTPVHPVPRLAEALGLHPErLLMKRDDL-IGWGGGGNKARKLEHSLGRAVARGATTVVTTGAAQSNHARMTA 81
Cdd:PRK12390 7 PRYPLTFGPTPIHPLKRLSAHLGGKVE-LYAKREDCnSGLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHTRQVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 82 AAGASLGLDVVLVLEG---HEVAAR---GNVLLDGLFGA--RIEWSG-DEGAESRAASVVAELEGAGTRVHRVAFGGSDa 152
Cdd:PRK12390 86 AVAAHLGMKCVLVQENwvnYEDAVYdrvGNILLSRIMGAdvRLVPDGfDIGIRKSWEDALEDVRAAGGKPYAIPAGASD- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 153 HSVQ--GFVDAGHELTAQ---VG-AVDHVVVALGSGGTMAGLV---EALG-PERVLGVHCGA-VAEPRAVVAGF------ 215
Cdd:PRK12390 165 HPLGglGFVGFAEEVRAQeaeLGfKFDYIVVCSVTGSTQAGMVvgfAADGrARRVIGIDASAkPEQTRAQVLRIarntae 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 216 LTERGTGIEAAALRIDADRVGPGYAHLTDEAREALVLVARTTGILLDPTYTARAAAGLAAAVGDGSIGADDRVVLWHSGG 295
Cdd:PRK12390 245 LVELGRDITEDDVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSKVLYAHLGG 324
|
....*...
gi 501256392 296 VPGLFGHA 303
Cdd:PRK12390 325 VPALNAYS 332
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
11-294 |
1.76e-30 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 116.26 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 11 PTPVHPVPRLAEALGLhpeRLLMKRDDLIGwgGGGNKARKLEHSLGRAVARGATTVVTTgAAQSNHARMTAAAGASLGLD 90
Cdd:pfam00291 7 PTPLVRLPRLSKELGV---DVYLKLESLNP--TGSFKDRGALNLLLRLKEGEGGKTVVE-ASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 91 VVLVLegHEVAARGNVLLDGLFGARIEWSGD--EGAESRAASVVAELEGAgTRVHrvafGGSDAHSVQGFVDAGHELTAQ 168
Cdd:pfam00291 81 VTIVV--PEDAPPGKLLLMRALGAEVVLVGGdyDEAVAAARELAAEGPGA-YYIN----QYDNPLNIEGYGTIGLEILEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 169 VG-AVDHVVVALGSGGTMAGLVEAL---GPE-RVLGVH-CGAVAEPRAVVAGFLTER------------GTGIEAAALRI 230
Cdd:pfam00291 154 LGgDPDAVVVPVGGGGLIAGIARGLkelGPDvRVIGVEpEGAPALARSLAAGRPVPVpvadtiadglgvGDEPGALALDL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501256392 231 DADRVGPGYAHLTDEAREALVLVARTTGILLDPtyTARAAAGLAAAVGDGSIGADDRVVLWHSG 294
Cdd:pfam00291 234 LDEYVGEVVTVSDEEALEAMRLLARREGIVVEP--SSAAALAALKLALAGELKGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
12-295 |
3.78e-16 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 76.40 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 12 TPVHPVPRLAEALGlhpERLLMKRDDLIGwgGGGNKARKLEHSLGRAVARG---ATTVVTtgAAQSNHARMTAAAGASLG 88
Cdd:cd00640 1 TPLVRLKRLSKLGG---ANIYLKLEFLNP--TGSFKDRGALNLILLAEEEGklpKGVIIE--STGGNTGIALAAAAARLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 89 LDVVLVLEghEVAARGNVLLDGLFGARIEWSGD--EGAESRAASVVAELEGAGtrvhrVAFGGSDAHSVQGFVDAGHELT 166
Cdd:cd00640 74 LKCTIVMP--EGASPEKVAQMRALGAEVVLVPGdfDDAIALAKELAEEDPGAY-----YVNQFDNPANIAGQGTIGLEIL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 167 AQVG--AVDHVVVALGSGGTMAGLVEALgpervlgvhcgavaepravVAGFLTERGTGIEAAALRIDadrvgpgyahlTD 244
Cdd:cd00640 147 EQLGgqKPDAVVVPVGGGGNIAGIARAL-------------------KELLPNVKVIGVEPEVVTVS-----------DE 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 501256392 245 EAREALVLVARTTGILLDPTyTARAAAGLAAAVGDGsiGADDRVVLWHSGG 295
Cdd:cd00640 197 EALEAIRLLAREEGILVEPS-SAAALAAALKLAKKL--GKGKTVVVILTGG 244
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
2-290 |
1.10e-07 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 52.51 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 2 DERIRLWTDPTPVHPVPRLAEALGlhpERLLMKRDdligwggGGN-----KARKLEHSLGRAVARGATTVV--TTGaaqs 74
Cdd:COG0498 57 EKAVSLGEGGTPLVKAPRLADELG---KNLYVKEE-------GHNptgsfKDRAMQVAVSLALERGAKTIVcaSSG---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 75 NHARMTAAAGASLGLDVVlVLEGHEVAARGNVLLDGLFGARiewsgdegaesraasvVAELEG----AGTRVHRVA--FG 148
Cdd:COG0498 123 NGSAALAAYAARAGIEVF-VFVPEGKVSPGQLAQMLTYGAH----------------VIAVDGnfddAQRLVKELAadEG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 149 GSDAHSVQ-GFVDA----GHELTAQVGAV-DHVVVALGSGGTMAGLVEALGPERVLGVH------CGAVAEPRA-VVAGF 215
Cdd:COG0498 186 LYAVNSINpARLEGqktyAFEIAEQLGRVpDWVVVPTGNGGNILAGYKAFKELKELGLIdrlprlIAVQATGCNpILTAF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 216 LTERGTgIE-------AAALRI-----------DADRVGPGYAHLTD-EAREALVLVARTTGILLDPTyTARAAAGLAAA 276
Cdd:COG0498 266 ETGRDE-YEperpetiAPSMDIgnpsngeralfALRESGGTAVAVSDeEILEAIRLLARREGIFVEPA-TAVAVAGLRKL 343
|
330
....*....|....
gi 501256392 277 VGDGSIGADDRVVL 290
Cdd:COG0498 344 REEGEIDPDEPVVV 357
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
3-200 |
2.27e-07 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 51.58 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 3 ERIRLWTDPTPVHPVPRLAEALGLhpeRLLMKRDDL--IG---WGGGGNKARKLehslgrAVARGATTVVT--TGaaqsN 75
Cdd:COG1171 16 ARIAGVVRRTPLLRSPTLSERLGA---EVYLKLENLqpTGsfkLRGAYNALASL------SEEERARGVVAasAG----N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 76 HARMTAAAGASLGLDVVLVLegHEVAARGNVllDGL--FGARIEWSGDEGAESRAASV-VAELEGAgTRVHrvAFggSDA 152
Cdd:COG1171 83 HAQGVAYAARLLGIPATIVM--PETAPAVKV--AATraYGAEVVLHGDTYDDAEAAAAeLAEEEGA-TFVH--PF--DDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501256392 153 HSVQGFVDAGHELTAQVGAVDHVVVALGSGGTMAGL---VEALGPE-RVLGV 200
Cdd:COG1171 154 DVIAGQGTIALEILEQLPDLDAVFVPVGGGGLIAGVaaaLKALSPDiRVIGV 205
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
81-261 |
4.19e-05 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 44.43 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 81 AAAGASLGLDVVLVLEghEVAARGNVLLDGLFGARIEWSGDEGAESraasvvaeLEGAGTRVHRVAFGGSDAHSVQGF-- 158
Cdd:cd01561 69 AMVAAAKGYRFIIVMP--ETMSEEKRKLLRALGAEVILTPEAEADG--------MKGAIAKARELAAETPNAFWLNQFen 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 159 ---VDA-----GHELTAQV-GAVDHVVVALGSGGTMAGLVEALgPERVLGVHCGAVAEPRAVVAGFLTERGTGIEAaalr 229
Cdd:cd01561 139 panPEAhyettAPEIWEQLdGKVDAFVAGVGTGGTITGVARYL-KEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEG---- 213
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501256392 230 IDADRVGP--------GYAHLTD-EAREALVLVARTTGILL 261
Cdd:cd01561 214 IGAGFIPEnldrslidEVVRVSDeEAFAMARRLAREEGLLV 254
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
11-92 |
1.67e-04 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 42.91 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 11 PTPVHPVPRLAEALGlhPERLLMKRDDLIGWGgggnkARKLEHSLGRA-VAR--GATTVVT-TGAAQsnHARMTAAAGAS 86
Cdd:cd06446 34 PTPLYRAKRLSEYLG--GAKIYLKREDLNHTG-----AHKINNALGQAlLAKrmGKKRVIAeTGAGQ--HGVATATACAL 104
|
....*.
gi 501256392 87 LGLDVV 92
Cdd:cd06446 105 FGLECE 110
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
12-290 |
2.25e-04 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 42.20 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 12 TPVHPVPRLAEALGLhpERLLMKRDdligwggGGN-----KARKLEHSLGRAVARGATTVV--TTGaaqsNHARMTAAAG 84
Cdd:cd01563 23 TPLVRAPRLGERLGG--KNLYVKDE-------GLNptgsfKDRGMTVAVSKAKELGVKAVAcaSTG----NTSASLAAYA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 85 ASLGLD-VVLVLEGhevAARGNVLLDGLFGAR-IEWSGDEGAESRAASVVAElEGAGTRVHRVafggsDAHSVQGFVDAG 162
Cdd:cd01563 90 ARAGIKcVVFLPAG---KALGKLAQALAYGATvLAVEGNFDDALRLVRELAE-ENWIYLSNSL-----NPYRLEGQKTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 163 HELTAQVG--AVDHVVVALGSGGTM------------AGLVEALgPeRVLGV---HCGAVAepRAVVAGF-LTERGTGIE 224
Cdd:cd01563 161 FEIAEQLGweVPDYVVVPVGNGGNItaiwkgfkelkeLGLIDRL-P-RMVGVqaeGAAPIV--RAFKEGKdDIEPVENPE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 225 --AAALRI----------DADRVGPGYA-HLTDEA-REALVLVARTTGILLDPTyTARAAAGLAAAVGDGSIGADDRVVL 290
Cdd:cd01563 237 tiATAIRIgnpasgpkalRAVRESGGTAvAVSDEEiLEAQKLLARTEGIFVEPA-SAASLAGLKKLREEGIIDKGERVVV 315
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
3-200 |
8.73e-04 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 40.32 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 3 ERIRLWTDPTPVHPvprlAEALGLHPERLLMKRDDLigWGGGGNKARKlehSLGRAVARGATTVVTTGAAQSNHARMTAA 82
Cdd:PRK08246 15 QRIAPHIRRTPVLE----ADGAGFGPAPVWLKLEHL--QHTGSFKARG---AFNRLLAAPVPAAGVVAASGGNAGLAVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 83 AGASLGLDVVLVLEGHEVAARGNVLLDglFGARIEWSGDEGAESRAASVVAELEGAGTRVHrvAFGGSDAHSVQGFVdaG 162
Cdd:PRK08246 86 AAAALGVPATVFVPETAPPAKVARLRA--LGAEVVVVGAEYADALEAAQAFAAETGALLCH--AYDQPEVLAGAGTL--G 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 501256392 163 HELTAQVGAVDHVVVALGSGGTMAGLVEALGPE-RVLGV 200
Cdd:PRK08246 160 LEIEEQAPGVDTVLVAVGGGGLIAGIAAWFEGRaRVVAV 198
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
81-208 |
5.34e-03 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 37.72 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501256392 81 AAAGASLGLDVVLVLEGHEVAARGNVLLdgLFGARIEW----SGDEGAESRAASVVAELEG----------AGTRVHRVA 146
Cdd:COG0031 80 AMVAAAKGYRLILVMPETMSKERRALLR--AYGAEVVLtpgaEGMKGAIDKAEELAAETPGafwpnqfenpANPEAHYET 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501256392 147 FGGsdahsvqgfvdaghELTAQV-GAVDHVVVALGSGGTMAGLVEALGpERVLGVHCGAVaEP 208
Cdd:COG0031 158 TGP--------------EIWEQTdGKVDAFVAGVGTGGTITGVGRYLK-ERNPDIKIVAV-EP 204
|
|
| |
