|
Name |
Accession |
Description |
Interval |
E-value |
| 2am3keto_CoA |
TIGR01822 |
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ... |
27-458 |
0e+00 |
|
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130881 [Multi-domain] Cd Length: 393 Bit Score: 708.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLS 105
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG----------------------------REVLNFCANNYLGLS 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 106 SHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNH 185
Cdd:TIGR01822 53 SHPDLIQAAKDALDEHGFGMSSVRFICGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 186 ASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATG 263
Cdd:TIGR01822 133 ASIIDGVRLCKAKRYRYANNDMADLEAQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 264 FLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSN 343
Cdd:TIGR01822 213 FLGPTGRGSHELCGVMGRVDIITGTLGKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 344 TIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPK 423
Cdd:TIGR01822 293 ELRDRLWANTRY--------------FRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPK 358
|
410 420 430
....*....|....*....|....*....|....*
gi 530419680 424 GKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 458
Cdd:TIGR01822 359 GQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
31-458 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 639.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVdgvSGGpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:PRK06939 9 LREELEEIKAEGLYKEERVITSPQGADITV---ADG------------------------KEVINFCANNYLGLANHPEL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:PRK06939 62 IAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPT 268
Cdd:PRK06939 142 GVRLCKAKRYRYANNDMADLEAQLKEAKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGEN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 269 GRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQS 348
Cdd:PRK06939 222 GRGTVEHFGVMDRVDIITGTLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 349 MAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARI 428
Cdd:PRK06939 302 LWENARY--------------FREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARI 367
|
410 420 430
....*....|....*....|....*....|
gi 530419680 429 RVQISAVHSEEDIDRCVEAFVEVGRLHGAL 458
Cdd:PRK06939 368 RTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
31-453 |
0e+00 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 526.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:COG0156 5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG----------------------------REVLNFSSNDYLGLANHPRV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:COG0156 57 IEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIID 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGR 270
Cdd:COG0156 137 GARLSGAKVVRFRHNDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 271 GTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMA 350
Cdd:COG0156 217 GLVEHFGLEDRVDIIMGTLSKAL-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 351 AKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRV 430
Cdd:COG0156 296 ENIAY--------------FREGLKELGFDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRI 361
|
410 420
....*....|....*....|...
gi 530419680 431 QISAVHSEEDIDRCVEAFVEVGR 453
Cdd:COG0156 362 TLSAAHTEEDIDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
91-452 |
6.99e-155 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 443.16 E-value: 6.99e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 91 SGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEA 170
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 171 LLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASR 249
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 250 YGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVV 329
Cdd:cd06454 161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 330 GCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLK 408
Cdd:cd06454 240 AAALAALEVLQGGPERRERLQENVRY--------------LRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLE 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530419680 409 RGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 452
Cdd:cd06454 306 RGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
91-448 |
4.71e-56 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 189.44 E-value: 4.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 91 SGILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYD 162
Cdd:pfam00155 1 TDKINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 163 ANAGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMD 234
Cdd:pfam00155 74 ANIEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 235 GDIAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLV 308
Cdd:pfam00155 150 GTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 309 SLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPI 388
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDY--------------LRDGLQAAGLSVLPSQAGF 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530419680 389 CPVMLGDARLASRMADDMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 448
Cdd:pfam00155 295 FLLTGLDPETAKELAQVLLEEvGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| 2am3keto_CoA |
TIGR01822 |
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ... |
27-458 |
0e+00 |
|
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130881 [Multi-domain] Cd Length: 393 Bit Score: 708.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLS 105
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG----------------------------REVLNFCANNYLGLS 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 106 SHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNH 185
Cdd:TIGR01822 53 SHPDLIQAAKDALDEHGFGMSSVRFICGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 186 ASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATG 263
Cdd:TIGR01822 133 ASIIDGVRLCKAKRYRYANNDMADLEAQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 264 FLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSN 343
Cdd:TIGR01822 213 FLGPTGRGSHELCGVMGRVDIITGTLGKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 344 TIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPK 423
Cdd:TIGR01822 293 ELRDRLWANTRY--------------FRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPK 358
|
410 420 430
....*....|....*....|....*....|....*
gi 530419680 424 GKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 458
Cdd:TIGR01822 359 GQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
31-458 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 639.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVdgvSGGpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:PRK06939 9 LREELEEIKAEGLYKEERVITSPQGADITV---ADG------------------------KEVINFCANNYLGLANHPEL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:PRK06939 62 IAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPT 268
Cdd:PRK06939 142 GVRLCKAKRYRYANNDMADLEAQLKEAKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGEN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 269 GRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQS 348
Cdd:PRK06939 222 GRGTVEHFGVMDRVDIITGTLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 349 MAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARI 428
Cdd:PRK06939 302 LWENARY--------------FREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARI 367
|
410 420 430
....*....|....*....|....*....|
gi 530419680 429 RVQISAVHSEEDIDRCVEAFVEVGRLHGAL 458
Cdd:PRK06939 368 RTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
31-453 |
0e+00 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 526.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:COG0156 5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG----------------------------REVLNFSSNDYLGLANHPRV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:COG0156 57 IEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIID 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGR 270
Cdd:COG0156 137 GARLSGAKVVRFRHNDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 271 GTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMA 350
Cdd:COG0156 217 GLVEHFGLEDRVDIIMGTLSKAL-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 351 AKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRV 430
Cdd:COG0156 296 ENIAY--------------FREGLKELGFDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRI 361
|
410 420
....*....|....*....|...
gi 530419680 431 QISAVHSEEDIDRCVEAFVEVGR 453
Cdd:COG0156 362 TLSAAHTEEDIDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
91-452 |
6.99e-155 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 443.16 E-value: 6.99e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 91 SGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEA 170
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 171 LLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASR 249
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 250 YGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVV 329
Cdd:cd06454 161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 330 GCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLK 408
Cdd:cd06454 240 AAALAALEVLQGGPERRERLQENVRY--------------LRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLE 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530419680 409 RGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 452
Cdd:cd06454 306 RGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
93-448 |
2.93e-127 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 373.14 E-value: 2.93e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 93 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALL 172
Cdd:TIGR00858 18 LLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISALV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 173 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGA 252
Cdd:TIGR00858 98 GKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAERYGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 253 LVFMDECHATGFLGPTGRGTDELLGVM-DQVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGC 331
Cdd:TIGR00858 178 WLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLINRARTLIFSTALPPAVAAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 332 ASKALDLLmgsntivQSMAAKTQrcdsqqgRLGGGETWFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGI 411
Cdd:TIGR00858 257 ALAALELI-------QEEPWRRE-------KLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQGI 322
|
330 340 350
....*....|....*....|....*....|....*..
gi 530419680 412 FVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 448
Cdd:TIGR00858 323 FVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
31-452 |
1.98e-114 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 341.37 E-value: 1.98e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:PRK05958 7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG----------------------------RRMLNFASNDYLGLARHPRL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:PRK05958 59 IAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLID 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQKHRlRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGR 270
Cdd:PRK05958 139 GARLSRARVRRYPHNDVDALEALLAKWRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 271 GTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLmgsntivqsm 349
Cdd:PRK05958 218 GLAAEAGLaGEPDVILVGTLGKAL-GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRIL---------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 350 aaktQRCDSQQGRLGGGETWFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIR 429
Cdd:PRK05958 287 ----RREPERRERLAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLR 362
|
410 420
....*....|....*....|...
gi 530419680 430 VQISAVHSEEDIDRCVEAFVEVG 452
Cdd:PRK05958 363 ITLTAAHTEADIDRLLEALAEAL 385
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
96-453 |
7.04e-100 |
|
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273820 [Multi-domain] Cd Length: 402 Bit Score: 304.73 E-value: 7.04e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 96 FCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDAN-AGLFE-ALLT 173
Cdd:TIGR01821 50 WCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLATlAKII 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 174 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGAL 253
Cdd:TIGR01821 130 PGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 254 VFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAS 333
Cdd:TIGR01821 210 TYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 334 KALDLLMGSntivqsmaaKTQRcDSQQGRLgggeTWFRSKMEAAGF-TISGASHpICPVMLGDARLASRMADDML-KRGI 411
Cdd:TIGR01821 289 ASIRHLKES---------QDLR-RAHQENV----KRLKNLLEALGIpVIPNPSH-IVPVIIGDAALCKKVSDLLLnKHGI 353
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530419680 412 FVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 453
Cdd:TIGR01821 354 YVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWD 395
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
96-451 |
1.08e-87 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 273.65 E-value: 1.08e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 96 FCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEAL--LT 173
Cdd:PRK13392 51 WCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 174 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGAL 253
Cdd:PRK13392 131 PGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNAL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 254 VFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAS 333
Cdd:PRK13392 211 TYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGAT 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 334 KALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKR-GIF 412
Cdd:PRK13392 290 AAIRHLKTSQTERDAHQDRVAA--------------LKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEhGIY 355
|
330 340 350
....*....|....*....|....*....|....*....
gi 530419680 413 VIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEV 451
Cdd:PRK13392 356 IQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAI 394
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
84-456 |
1.50e-64 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 215.78 E-value: 1.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 84 IHLLSFTSGILNFCANNYLGLSSH-----PEVIQAglqaLEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYP 158
Cdd:PLN02483 93 LKRTTKTRRCLNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 159 SCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA------QKHRLR---LVATDG 229
Cdd:PLN02483 169 MGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqpRTHRPWkkiIVIVEG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 230 AFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPGPLV 308
Cdd:PLN02483 249 IYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSF-GSCGGYIAGSKELI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 309 SLLRQRARPYLFSNSLPPAVVGCASKALDLLM---GSNTIVQSMAaktqrcdsqqgRLGGGETWFRSKMEAAGFTISGAS 385
Cdd:PLN02483 328 QYLKRTCPAHLYATSMSPPAVQQVISAIKVILgedGTNRGAQKLA-----------QIRENSNFFRSELQKMGFEVLGDN 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530419680 386 -HPICPVML-GDARLA--SRmadDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHG 456
Cdd:PLN02483 397 dSPVMPIMLyNPAKIPafSR---ECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVG 468
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
93-448 |
2.47e-57 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 196.43 E-value: 2.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 93 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEAL- 171
Cdd:PLN02955 104 LLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIg 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 172 ------------LTPED-AVLSDELNHASIIDGIRLCK----AHKYRYRHLDMADLEAKLQEAQKHRlRLVATDGAFSMD 234
Cdd:PLN02955 184 svasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDSLFSMD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 235 GDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKAlGGASGGYTTGPGPLVSLLRQR 314
Cdd:PLN02955 263 GDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQLIQSR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 315 ARPYLFSNSLPPAVVGCASKAldllmgsntIVQSMAAKTQRCdsqqgrlgggETWFRSK--MEAAGFTISGashPICPVM 392
Cdd:PLN02955 342 GRSFIFSTAIPVPMAAAAYAA---------VVVARKEKWRRK----------AIWERVKefKALSGVDISS---PIISLV 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530419680 393 LGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 448
Cdd:PLN02955 400 VGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
91-448 |
4.71e-56 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 189.44 E-value: 4.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 91 SGILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYD 162
Cdd:pfam00155 1 TDKINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 163 ANAGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMD 234
Cdd:pfam00155 74 ANIEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 235 GDIAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLV 308
Cdd:pfam00155 150 GTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 309 SLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPI 388
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDY--------------LRDGLQAAGLSVLPSQAGF 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530419680 389 CPVMLGDARLASRMADDMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 448
Cdd:pfam00155 295 FLLTGLDPETAKELAQVLLEEvGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
49-451 |
1.41e-49 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 175.70 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 49 VITSRQGPHIRVDGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSV 128
Cdd:PLN02822 95 VLESAAGPHTIING----------------------------KDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 129 RFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMA 208
Cdd:PLN02822 147 RGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDME 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 209 DLEAKLQE-------AQKHRlRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MD 280
Cdd:PLN02822 227 SLRNTLEKltaenkrKKKLR-RYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 281 QVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIV----QSMAAKTQRC 356
Cdd:PLN02822 306 KIDIITAAMGHALATE-GGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLaklkENIALLHKGL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 357 DSQQGrlgggetwfrskmeaagftISGASHPICPVML-----------GDARLASRMADDMLKR-GIFVIGFSYPVVPKG 424
Cdd:PLN02822 385 SDIPG-------------------LSIGSNTLSPIVFlhlekstgsakEDLSLLEHIADRMLKEdSVLVVVSKRSTLDKC 445
|
410 420
....*....|....*....|....*....
gi 530419680 425 K--ARIRVQISAVHSEEDIDRCVEAFVEV 451
Cdd:PLN02822 446 RlpVGIRLFVSAGHTESDILKASESLKRV 474
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
47-451 |
2.19e-48 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 170.96 E-value: 2.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 47 ERVITSRQGPHIrVDGVSGGPGTVIFPGlplphlsccihllsftsgilnfcaNNYLGLSSHPEVIQAGLQALEEFGAGL- 125
Cdd:PRK07179 35 ERVNKNWNGKHL-VLGKTPGPDAIILQS------------------------NDYLNLSGHPDIIKAQIAALQEEGDSLv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 126 -SSVrFICGTQSIHKnLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRH 204
Cdd:PRK07179 90 mSAV-FLHDDSPKPQ-FEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 205 LDMADLEAKLQEaqkHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTI 284
Cdd:PRK07179 168 NDVDHLRRQIER---HGPGIIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 285 INSTLGKALGGaSGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLmgsntivqsmaaktQRCDSQQGRLG 364
Cdd:PRK07179 245 ITASLAKAFAG-RAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVI--------------ESADDRRARLH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 365 GGETWFRSKMEAAGFTISGASHpICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDR- 443
Cdd:PRK07179 310 ANARFLREGLSELGYNIRSESQ-IIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRv 388
|
410
....*....|.
gi 530419680 444 ---CVEAFVEV 451
Cdd:PRK07179 389 levCREARDEV 399
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
94-447 |
2.08e-43 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 156.99 E-value: 2.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 94 LNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLT 173
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 174 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADL----------EAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEI 243
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 244 CCLASRYGALVFMDECHATGFLGPTGRGTDELLGV--MDQVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFS 321
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 322 NSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRCDSqqgRLGGGETWFRSKMEAAGFTISGASHPICPVMLGDAR---- 397
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYS---TLTNSSHPYALKLRNRLVITSDPISPIIYLRLSDQEatrr 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 530419680 398 -----LASRMADDMLKRGIFVI--GFSYPVVPKGKAR--IRVQISAVHSEEDIDRCVEA 447
Cdd:PLN03227 317 tdetlILDQIAHHSLSEGVAVVstGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
93-457 |
1.80e-42 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 154.75 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 93 ILNFCANNYLGLSSHPEVIQAGLQALEEFGA-GLSSVRFICGTQsIHKNLEAKIARFHQREdAILYPSCYDANAGLFEAL 171
Cdd:PRK07505 48 FVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRVRSQ-ILKDLEEALSELFGAS-VLTFTSCSAAHLGILPLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 172 ----LTPEDAVLS--DELNHASIIDGIRLCkAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMdGDIAPLQEICC 245
Cdd:PRK07505 126 asghLTGGVPPHMvfDKNAHASLNILKGIC-ADETEVETIDHNDLDALEDICKTNKTVAYVADGVYSM-GGIAPVKELLR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 246 LASRYGALVFMDECHATGFLGPTGRG--TDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNS 323
Cdd:PRK07505 204 LQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDAEQIELILRYAGPLAFSQS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 324 LPPAVVGCASKALDLlmgsntivqsmaAKTQRCDSQQGRLGGGETWFRSKMEAagfTISGASHPICPVMLGDARLASRMA 403
Cdd:PRK07505 284 LNVAALGAILASAEI------------HLSEELDQLQQKLQNNIALFDSLIPT---EQSGSFLPIRLIYIGDEDTAIKAA 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 530419680 404 DDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGA 457
Cdd:PRK07505 349 KQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA 402
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
90-339 |
2.67e-23 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 101.01 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 90 TSGILNFCANNYLGLSSHPEV---IQAGLQAL------EEFGAGLSsvRFICGTQSIHKNLEAKIARFHQREDAILYPSC 160
Cdd:PRK05937 3 ESLSIDFVTNDFLGFSRSDTLvheVEKRYRLYcrqfphAQLGYGGS--RAILGPSSLLDDLEHKIAHFHGAPEAFIVPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 161 YDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLR--LVATDGAFSMDGDIA 238
Cdd:PRK05937 81 YMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGriFIFVCSVYSFKGTLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 239 PLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGvMDQVTIINSTLGKALGgasggyTTGPGPLVSL-----LRQ 313
Cdd:PRK05937 161 PLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALG------SMGAALLSSSevkqdLML 233
|
250 260
....*....|....*....|....*.
gi 530419680 314 RARPYLFSNSLPPAVVGCASKALDLL 339
Cdd:PRK05937 234 NSPPLRYSTGLPPHLLISIQVAYDFL 259
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
138-303 |
2.33e-16 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 76.65 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 138 HKNLEAKIARFHQ--REDAILYPSCYDANAGLFEALLTPEDAVLSDELNHAS---IIDGIRLCKAHKYRYRHLDMADLEA 212
Cdd:cd01494 2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 213 KLQEAQKHRLR--LVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGflgptGRGTDELLGVMDQVTIINSTLG 290
Cdd:cd01494 82 AILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|...
gi 530419680 291 KALGGASGGYTTG 303
Cdd:cd01494 157 KNLGGEGGGVVIV 169
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
141-450 |
2.91e-08 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 55.43 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 141 LEAKIARFHQR--------EDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAhKYRYRHLD----MA 208
Cdd:cd00609 41 LREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPVPLDeeggFL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 209 DLEAKLQEAQKHRLRLVA-------TDGAFSMDGdiapLQEICCLASRYGALVFMDECHatGFLGPTGRGTDELLGV-MD 280
Cdd:cd00609 120 LDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLdAY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 281 QVTIINSTLGKALGGAS--GGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAsKALDLlmGSNTIVQSMAAKTQRCDs 358
Cdd:cd00609 194 ERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAA-AALDD--GEEHLEELRERYRRRRD- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 359 qqgrlgggetWFRSKMEAAGFTI----SGASHpicpVMLG-----DARLASRMAddmLKRGIFVIGFSYPvVPKGKARIR 429
Cdd:cd00609 270 ----------ALLEALKELGPLVvvkpSGGFF----LWLDlpegdDEEFLERLL---LEAGVVVRPGSAF-GEGGEGFVR 331
|
330 340
....*....|....*....|.
gi 530419680 430 vqISAVHSEEDIDRCVEAFVE 450
Cdd:cd00609 332 --LSFATPEEELEEALERLAE 350
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
170-263 |
8.51e-06 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 47.83 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 170 ALLTPEDAVLSDELNHASIIDGIR-LCKAHKYRYR--------HLDMADLEAKLQEaqkhRLRLVATDGAFSMDGDIAPL 240
Cdd:COG0520 98 GRLKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP----RTKLVAVTHVSNVTGTVNPV 173
|
90 100
....*....|....*....|...
gi 530419680 241 QEICCLASRYGALVFMDECHATG 263
Cdd:COG0520 174 KEIAALAHAHGALVLVDGAQSVP 196
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
108-356 |
2.70e-04 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 43.00 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 108 PEVIQAGLQALEEF-GAGLSSV-RFicGTQSIHK--NLEAKIARFHQREDA--ILYPS-CYDANA----GLFEALLTPED 176
Cdd:pfam00266 13 QEVLDAIQEYYTDYnGNVHRGVhTL--GKEATQAyeEAREKVAEFINAPSNdeIIFTSgTTEAINlvalSLGRSLKPGDE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 177 AVLSDELNHASIIDGIRLCKAHKYRYR--------HLDMADLEAKLqeaqKHRLRLVATDGAFSMDGDIAPLQEICCLAS 248
Cdd:pfam00266 91 IVITEMEHHANLVPWQELAKRTGARVRvlpldedgLLDLDELEKLI----TPKTKLVAITHVSNVTGTIQPVPEIGKLAH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419680 249 RYGALVFMDECHATG--------------------FLGPTGRG----TDELLGVMDqvtiinstlgKALGGasGGYTTGP 304
Cdd:pfam00266 167 QYGALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIGvlygRRDLLEKMP----------PLLGG--GGMIETV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 530419680 305 GplVSLLRQRARPYLFSNSLPP--AVVGCAsKALDLLM--GSNTIVQSMAAKTQRC 356
Cdd:pfam00266 235 S--LQESTFADAPWKFEAGTPNiaGIIGLG-AALEYLSeiGLEAIEKHEHELAQYL 287
|
|
|