|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
1-404 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 923.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 1 MKLPIYLDYSATTPVDPRVAEKMMQCLTLDGNFGNPASRSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 81 LAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 161 QDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMHGGGHERGMR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 241 SGTLPVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGVKDMEEVYLNGDLEQGAPNILNVSFNYVEGESLIMALKDL 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 321 AVSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYTIKLVRNSIGRLRDLSPLWEMFKQGVDLNSIE 400
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIE 400
|
....
gi 1238450932 401 WSHH 404
Cdd:PRK14012 401 WAHH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
1-404 |
0e+00 |
|
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131061 [Multi-domain] Cd Length: 402 Bit Score: 794.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 1 MKLPIYLDYSATTPVDPRVAEKMMQCLTLDgnFGNPASRSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDN 80
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 81 LAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV 160
Cdd:TIGR02006 79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 161 QDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 241 SGTLPVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGVKDMEEVYLNGDLEQGAPNILNVSFNYVEGESLIMALKDL 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 321 AVSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYTIKLVRNSIGRLRDLSPLWEMFKQGVDLNSIE 400
Cdd:TIGR02006 319 AVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIE 398
|
....
gi 1238450932 401 WSHH 404
Cdd:TIGR02006 399 WAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
2-384 |
0e+00 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 673.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 2 KLPIYLDYSATTPVDPRVAEKMMQCLTldGNFGNPASrSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDNL 81
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLT--EYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 82 AIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQ 161
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 162 DIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRkpRIRIEAQMHGGGHERGMRS 241
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 242 GTLPVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGVKD-MEEVYLNGDLEQGAPNILNVSFNYVEGESLIMAL--K 318
Cdd:COG1104 236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238450932 319 DLAVSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYTIKLVRNSIGRLRDLS 384
Cdd:COG1104 316 GIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-368 |
1.36e-106 |
|
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: 318.81 E-value: 1.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDPRVAEKMMQCLTlDGNfGNPASRSHRFGWHAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYT-DYN-GNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 84 KGAANFyQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:pfam00266 79 LSLGRS-LKPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 163 IATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 236 ERGM-------RSGTLPVHQIVGMGEAYR-IAKEEMETEMARLRTLRNRLWDGVKDMEEVYLNGDLEQgaPNILNVSFNY 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERR--ASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238450932 308 VEGESLIMALKD--LAVSSGSACTsaslEPSYVLRALgmtdelaHSSIRFSLGRFTTEEEIDY 368
Cdd:pfam00266 316 VHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-367 |
1.15e-73 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 234.28 E-value: 1.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDPRVAEKMMQCLTLDGnfGNPASRSHRFGWHAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 84 KGAAnFYQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:cd06453 79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 163 IATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRkpriRIEAQM---HGGG----- 234
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKE----ELLEEMppyGGGGemiee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 235 --------HERGMR--SGTLPVHQIVGMGEAYRIAKEE-METEMARLRTLRNRLWDGVKDMEEVYLNGDLEQGAPnIlnV 303
Cdd:cd06453 234 vsfeettyADLPHKfeAGTPNIAGAIGLGAAIDYLEKIgMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAG-V--V 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238450932 304 SFNyVEG---ESLIMAL--KDLAVSSGSACTsaslEPsyVLRALGMTdelahSSIRFSLGRFTTEEEID 367
Cdd:cd06453 311 SFN-LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFGLYNTEEEID 367
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
54-235 |
1.48e-21 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 96.85 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 54 ARNQIADLVGA-DPREIVFTSGATESDNLAIK--GAANFyqKKGKHIITSKTEHKA--------------------VLDT 110
Cdd:NF041166 294 AREKVRRFIGApSVDEIIFVRGTTEAINLVAKswGRQNI--GAGDEIIVSHLEHHAnivpwqqlaqetgaklrvipVDDS 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 111 crqleregfevtylapqsnGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPI 190
Cdd:NF041166 372 -------------------GQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPV 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238450932 191 DLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprirIEAQM---HGGGH 235
Cdd:NF041166 433 DVQALDADFFVFSGHKVFGPTGIGVVYGKRD----LLEAMppwQGGGN 476
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
1-404 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 923.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 1 MKLPIYLDYSATTPVDPRVAEKMMQCLTLDGNFGNPASRSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 81 LAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 161 QDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMHGGGHERGMR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 241 SGTLPVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGVKDMEEVYLNGDLEQGAPNILNVSFNYVEGESLIMALKDL 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 321 AVSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYTIKLVRNSIGRLRDLSPLWEMFKQGVDLNSIE 400
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIE 400
|
....
gi 1238450932 401 WSHH 404
Cdd:PRK14012 401 WAHH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
1-404 |
0e+00 |
|
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131061 [Multi-domain] Cd Length: 402 Bit Score: 794.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 1 MKLPIYLDYSATTPVDPRVAEKMMQCLTLDgnFGNPASRSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDN 80
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 81 LAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV 160
Cdd:TIGR02006 79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 161 QDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 241 SGTLPVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGVKDMEEVYLNGDLEQGAPNILNVSFNYVEGESLIMALKDL 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 321 AVSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYTIKLVRNSIGRLRDLSPLWEMFKQGVDLNSIE 400
Cdd:TIGR02006 319 AVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIE 398
|
....
gi 1238450932 401 WSHH 404
Cdd:TIGR02006 399 WAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
2-384 |
0e+00 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 673.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 2 KLPIYLDYSATTPVDPRVAEKMMQCLTldGNFGNPASrSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDNL 81
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLT--EYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 82 AIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQ 161
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 162 DIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRkpRIRIEAQMHGGGHERGMRS 241
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 242 GTLPVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGVKD-MEEVYLNGDLEQGAPNILNVSFNYVEGESLIMAL--K 318
Cdd:COG1104 236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238450932 319 DLAVSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYTIKLVRNSIGRLRDLS 384
Cdd:COG1104 316 GIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
5-367 |
0e+00 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 576.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDPRVAEKMMQCLTldGNFGNPASRSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIK 84
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLI--EHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 85 GAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIA 164
Cdd:PLN02651 79 GVMHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 165 TIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMHGGGHERGMRSGTL 244
Cdd:PLN02651 159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 245 PVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGVKD-MEEVYLNG--DLEQGAPNILNVSFNYVEGESLIMALKDLA 321
Cdd:PLN02651 239 NTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAkLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1238450932 322 VSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEID 367
Cdd:PLN02651 319 VSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
5-386 |
2.63e-179 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 504.07 E-value: 2.63e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDPRVAEKMMQCLTldGNFGNPASrSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIK 84
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFT--EYFGNPSS-MHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 85 GAANFYQKKgKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIA 164
Cdd:TIGR03402 78 SALAAQPEK-RHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 165 TIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprIRIEAQMHGGGHERGMRSGTL 244
Cdd:TIGR03402 157 EIGEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKG--TRFRPLLRGGHQERGRRAGTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 245 PVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGV-KDMEEVYLNGDLEQGAPNILNVSFNYVEGESLIMAL--KDLA 321
Cdd:TIGR03402 235 NVPGIVGLGKAAELATEHLEEENTRVRALRDRLEAGLlARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLdmEGIC 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238450932 322 VSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYTIKLVRNSIGRLRDLSPL 386
Cdd:TIGR03402 315 ASSGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
5-395 |
6.16e-111 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 330.15 E-value: 6.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDpRVAEKMMQCLTLDgNFGNpASRSHRFGWHAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIK 84
Cdd:PRK02948 2 IYLDYAATTPMS-KEALQTYQKAASQ-YFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 85 GAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIA 164
Cdd:PRK02948 79 SLLNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 165 TIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRrkPRIRIEAQMHGGGHERGMRSGTL 244
Cdd:PRK02948 159 EIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYIN--PQVRWKPVFPGTTHEKGFRPGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 245 PVHQIVGMGEAYRIAKEEMETEMARLRTLRNRLWDGVKDME-EVYLNGDLEQGAPNILNVSFNYVEGEsLIMA---LKDL 320
Cdd:PRK02948 237 NVPGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPlPIEVEGHSTSCLPHIIGVTIKGIEGQ-YTMLecnRRGI 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238450932 321 AVSSGSACTSASLEPSYVLRALGMTDELAHSSIRFSLGRFTTEEEIDYTIKLvrnsigrlrdLSPLWEMFKQGVD 395
Cdd:PRK02948 316 AISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHA----------LETIGNQFYRGVK 380
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-368 |
1.36e-106 |
|
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: 318.81 E-value: 1.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDPRVAEKMMQCLTlDGNfGNPASRSHRFGWHAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYT-DYN-GNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 84 KGAANFyQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:pfam00266 79 LSLGRS-LKPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 163 IATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 236 ERGM-------RSGTLPVHQIVGMGEAYR-IAKEEMETEMARLRTLRNRLWDGVKDMEEVYLNGDLEQgaPNILNVSFNY 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERR--ASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238450932 308 VEGESLIMALKD--LAVSSGSACTsaslEPSYVLRALgmtdelaHSSIRFSLGRFTTEEEIDY 368
Cdd:pfam00266 316 VHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
5-374 |
4.64e-78 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 246.59 E-value: 4.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVdPR-VAEKMMQCLTLDGnfGNPASRSHRFGWHAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLA 82
Cdd:COG0520 17 VYLDNAATGQK-PRpVIDAIRDYYEPYN--ANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEAINLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 83 IKGAANFyqKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQ 161
Cdd:COG0520 94 AYGLGRL--KPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 162 DIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprirIEAQM---HGGGH--- 235
Cdd:COG0520 172 PVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRE----LLEALppfLGGGGmie 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 236 ------------ERGMRSGTLPVHQIVGMGEA--Y--RIAKEEMEtemARLRTLRNRLWDGVKDME--EVYLNGDLEQGA 297
Cdd:COG0520 248 wvsfdgttyadlPRRFEAGTPNIAGAIGLGAAidYleAIGMEAIE---ARERELTAYALEGLAAIPgvRILGPADPEDRS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 298 PnIlnVSFNyVEG---ESLIMALKDL--AVSSGSACTsaslEPsyVLRALGMTdelahSSIRFSLGRFTTEEEIDYTIKL 372
Cdd:COG0520 325 G-I--VSFN-VDGvhpHDVAALLDDEgiAVRAGHHCA----QP--LMRRLGVP-----GTVRASFHLYNTEEEIDRLVEA 389
|
..
gi 1238450932 373 VR 374
Cdd:COG0520 390 LK 391
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-367 |
1.15e-73 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 234.28 E-value: 1.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDPRVAEKMMQCLTLDGnfGNPASRSHRFGWHAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 84 KGAAnFYQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:cd06453 79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 163 IATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRkpriRIEAQM---HGGG----- 234
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKE----ELLEEMppyGGGGemiee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 235 --------HERGMR--SGTLPVHQIVGMGEAYRIAKEE-METEMARLRTLRNRLWDGVKDMEEVYLNGDLEQGAPnIlnV 303
Cdd:cd06453 234 vsfeettyADLPHKfeAGTPNIAGAIGLGAAIDYLEKIgMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAG-V--V 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238450932 304 SFNyVEG---ESLIMAL--KDLAVSSGSACTsaslEPsyVLRALGMTdelahSSIRFSLGRFTTEEEID 367
Cdd:cd06453 311 SFN-LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFGLYNTEEEID 367
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
5-367 |
4.28e-48 |
|
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 131034 [Multi-domain] Cd Length: 403 Bit Score: 168.60 E-value: 4.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDPRVAEKMMQCLTLDgnFGNPASRSHRFGWHAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:TIGR01979 20 VYLDSAATSQKPQQVIDAVAEYYRNS--NANVHRGIHTLSVRATEAYEAVREKVAKFINAaSDEEIVFTRGTTESINLVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 84 KGAANFYQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:TIGR01979 98 YSWGDSNLKAGDEIVISEMEHHANIVPWQLLaERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLVAITHVSNVLGTVNP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 163 IATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprirIEAQM---HGGGherGM 239
Cdd:TIGR01979 178 VEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEE----LLEQMppfLGGG---EM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 240 ------------------RSGTLPVHQIVGMGEAYRIAKE-EMETEMARLRTLRNRLWDGVKDMEEVYLNGDL---EQGA 297
Cdd:TIGR01979 251 iaevsfeettyneaphkfEAGTPNIAGVIGLGAAIDYLEAiGLENIEAHEHELTAYALERLGEIPGLRIYGPRdaeDRGG 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238450932 298 PnilnVSFNyVEGE-----SLIMALKDLAVSSGSACTsaslEPsyVLRALGmtdelAHSSIRFSLGRFTTEEEID 367
Cdd:TIGR01979 331 I----ISFN-VEGVhphdvGTILDEEGIAVRSGHHCA----QP--LMRRFG-----VPATCRASFYIYNTEEDID 389
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
5-383 |
2.78e-36 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 137.19 E-value: 2.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTPVDPRVAEKMMQCLTlDGNfgnpaSRSHRfGWH-----AEEAVDIARNQIADLVGA-DPREIVFTSGATES 78
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYYE-EYN-----SNVHR-GIHalsakATDAYELARKKVAAFINAsTSREIVFTRNATEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 79 DNLAIK--GAANFyqKKGKHIITSKTEHKAVLdTCRQL--EREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVN 154
Cdd:PLN02855 107 INLVAYtwGLANL--KPGDEVILSVAEHHSNI-VPWQLvaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 155 NEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMhGGG 234
Cdd:PLN02855 184 NVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPPFL-GGG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 235 H-------------ERGMR--SGTLPVHQIVGMGEA--Y-------RIAKEEMEtemarlrtLRNRLWDGVKDMEEVYLN 290
Cdd:PLN02855 263 EmisdvfldhstyaPPPSRfeAGTPAIGEAIGLGAAidYlseigmdRIHEYEVE--------LGTYLYEKLSSVPGVRIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 291 GDLEQGAPNILN-VSFNyVEG------ESLIMALKDLAVSSGSACTsaslEPSYvlRALGMTdelahSSIRFSLGRFTTE 363
Cdd:PLN02855 335 GPKPSEGVGRAAlCAFN-VEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLGVN-----ASARASLYFYNTK 402
|
410 420
....*....|....*....|
gi 1238450932 364 EEIDYTIKLVRNSIGRLRDL 383
Cdd:PLN02855 403 EEVDAFIHALKDTIAFFSSF 422
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
41-220 |
3.13e-28 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 114.46 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 41 HRFGWHAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQL-EREG 118
Cdd:PRK09295 59 HTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 119 FEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVD 198
Cdd:PRK09295 139 AELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCD 218
|
170 180
....*....|....*....|..
gi 1238450932 199 LMSFSGHKIYGPKGIGALYVRR 220
Cdd:PRK09295 219 FYVFSGHKLYGPTGIGILYVKE 240
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
5-234 |
8.17e-28 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 113.21 E-value: 8.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDySATTPVDPR-VAEKMMQCLTLDGnfGNPASRSHRFGWHAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLA 82
Cdd:PRK10874 21 VYLD-SAATALKPQaVIEATQQFYSLSA--GNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 83 IKGAANFYQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQ 161
Cdd:PRK10874 98 AQSYARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238450932 162 DIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprirIEAQM---HGGG 234
Cdd:PRK10874 178 DLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSE----LLEAMspwQGGG 249
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
54-235 |
1.48e-21 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 96.85 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 54 ARNQIADLVGA-DPREIVFTSGATESDNLAIK--GAANFyqKKGKHIITSKTEHKA--------------------VLDT 110
Cdd:NF041166 294 AREKVRRFIGApSVDEIIFVRGTTEAINLVAKswGRQNI--GAGDEIIVSHLEHHAnivpwqqlaqetgaklrvipVDDS 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 111 crqleregfevtylapqsnGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPI 190
Cdd:NF041166 372 -------------------GQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPV 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238450932 191 DLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprirIEAQM---HGGGH 235
Cdd:NF041166 433 DVQALDADFFVFSGHKVFGPTGIGVVYGKRD----LLEAMppwQGGGN 476
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
69-219 |
3.24e-11 |
|
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: 61.63 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 69 IVFTSGATESDNLAIKGAAnfyqKKGKHIITSKTEHKAVldTCRQLEREGFE---VTYLAPQSNGIIDLKELEAAMRDDT 145
Cdd:cd01494 20 AVFVPSGTGANEAALLALL----GPGDEVIVDANGHGSR--YWVAAELAGAKpvpVPVDDAGYGGLDVAILEELKAKPNV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238450932 146 ILVSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQL---KVDLMSFSGHKIYGPKGIGALYVR 219
Cdd:cd01494 94 ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIpegGADVVTFSLHKNLGGEGGGVVIVK 170
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
113-284 |
8.80e-11 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 62.69 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 113 QLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTI-LVSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPID 191
Cdd:cd06451 92 MAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIkAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 192 LSQLKVDLMsFSG-HKIYG-PKGIGALYVRRKPRIRIEAQM-HGGGH-----------ERGMRSGTLPVHQIVGMGEAYR 257
Cdd:cd06451 172 MDEWGVDVA-YTGsQKALGaPPGLGPIAFSERALERIKKKTkPKGFYfdlllllkywgEGYSYPHTPPVNLLYALREALD 250
|
170 180
....*....|....*....|....*...
gi 1238450932 258 -IAKEEMETEMARLRTLRNRLWDGVKDM 284
Cdd:cd06451 251 lILEEGLENRWARHRRLAKALREGLEAL 278
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
56-219 |
2.84e-10 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 61.07 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 56 NQIADLVGADPREI--VFTSGATESDNLAIKGAANFYQKKGKH----------IITSKTEHKAVLDTCRQLEREGFEVTY 123
Cdd:cd06450 45 NWLAKLFGLPSEDAdgVFTSGGSESNLLALLAARDRARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVKVRLVPV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 124 lapQSNGIIDLKELEAAMRDD------TILVSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPID-----L 192
Cdd:cd06450 125 ---DEDGRMDPEALEAAIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPeprhlD 201
|
170 180 190
....*....|....*....|....*....|
gi 1238450932 193 SQLK-VDLMSFSGHKiYG--PKGIGALYVR 219
Cdd:cd06450 202 FGIErVDSISVDPHK-YGlvPLGCSAVLVR 230
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
113-284 |
2.25e-09 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 58.61 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 113 QLEREGFEVTYLAPQSNGIIDLKELEAAMRDDTI----LVSIMHVNNEIGVVQDIATIGEM--CRARGIIYHVDATQSVG 186
Cdd:PLN02409 102 QMQRLNFDVDVVESPWGQGADLDILKSKLRQDTNhkikAVCVVHNETSTGVTNDLAGVRKLldCAQHPALLLVDGVSSIG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 187 KLPIDLSQLKVDL-MSFSGHKIYGPKGIG----------ALYVRRKPRIRIEAQMHGGGHERGMRSG-TLPVHQIVGMGE 254
Cdd:PLN02409 182 ALDFRMDEWGVDVaLTGSQKALSLPTGLGivcaspkaleASKTAKSPRVFFDWADYLKFYKLGTYWPyTPSIQLLYGLRA 261
|
170 180 190
....*....|....*....|....*....|.
gi 1238450932 255 AYRIAKEE-METEMARLRTLRNRLWDGVKDM 284
Cdd:PLN02409 262 ALDLIFEEgLENVIARHARLGEATRLAVEAW 292
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
56-379 |
4.59e-09 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 57.92 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 56 NQIADLVGADPREI-VFTSGATESdNL-AIKGA-----ANFYQKKGKH------IITSKTEH----KA--VLDtcrqLER 116
Cdd:COG0076 114 RWLADLLGLPEGAGgVFTSGGTEA-NLlALLAArdralARRVRAEGLPgaprprIVVSEEAHssvdKAarLLG----LGR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 117 EGfeVTYLAPQSNGIIDLKELEAAMRDD------TILV-----SIMHvnneiGVVQDIATIGEMCRARGIIYHVDAtqSV 185
Cdd:COG0076 189 DA--LRKVPVDEDGRMDPDALEAAIDEDraaglnPIAVvatagTTNT-----GAIDPLAEIADIAREHGLWLHVDA--AY 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 186 G-------KLPIDLSQL-KVDLMSFSGHKiYG--PKGIGALYVRRKPRIRIEAQMH--------GGGHE---------RG 238
Cdd:COG0076 260 GgfalpspELRHLLDGIeRADSITVDPHK-WLyvPYGCGAVLVRDPELLREAFSFHasylgpadDGVPNlgdytlelsRR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 239 MRSgtLPVH---QIVGMgEAYRiakeEMeteMARLRTLRNRLWDGVKDMEEVYLNGDleqgaPNILNVSFNYVEGES--- 312
Cdd:COG0076 339 FRA--LKLWatlRALGR-EGYR----EL---IERCIDLARYLAEGIAALPGFELLAP-----PELNIVCFRYKPAGLdee 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 313 --LIMALKDLAVSSGSA-CTSASLEPSYVLRAlgmtdelahsSIRfslGRFTTEEEIDYTIKLVRNSIGR 379
Cdd:COG0076 404 daLNYALRDRLRARGRAfLSPTKLDGRVVLRL----------VVL---NPRTTEDDVDALLDDLREAAAE 460
|
|
| PRK05939 |
PRK05939 |
cystathionine gamma-synthase family protein; |
92-182 |
2.80e-07 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 235650 [Multi-domain] Cd Length: 397 Bit Score: 52.00 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 92 KKGKHIITSK---TEHKAVLDTCRQLereGFEVTYLAPqsngiIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIATIGE 168
Cdd:PRK05939 84 RAGDHLVSSQflfGNTNSLFGTLRGL---GVEVTMVDA-----TDVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGA 155
|
90
....*....|....
gi 1238450932 169 MCRARGIIYHVDAT 182
Cdd:PRK05939 156 LCRERGLLYVVDNT 169
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
5-234 |
5.15e-07 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 51.79 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 5 IYLDYSATTpvdpRVAEKMMQCLTLDGN---FGNPASRSHRfGWHAEEAVDIARNQIADLVGADPRE--IVFTSGATESd 79
Cdd:PLN02724 36 VYLDHAGAT----LYSESQLEAALADFSsnvYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 80 nLAIKGAAnFYQKKGKHIITSKTEHKAVLDTcRQ--LEREG------FEVTYLAPQSNGIIDLKELEAAMRDDTILVSIM 151
Cdd:PLN02724 110 -LKLVGET-FPWSSESHFCYTLENHNSVLGI-REyaLEKGAaaiavdIEEAANQPTNSQGSVVVKSRGLQRRNTSKLQKR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 152 HVNNE----------------------IGVVQDIATIGEMCRARGIIYhVDATQSVGKLPIDLSQLKVDLMSFSGHKIYG 209
Cdd:PLN02724 187 EDDGEaynlfafpsecnfsgakfpldlVKLIKDNQHSNFSKSGRWMVL-LDAAKGCGTSPPDLSRYPADFVVVSFYKIFG 265
|
250 260
....*....|....*....|....*.
gi 1238450932 210 -PKGIGALYVRRKPRIRIEAQMHGGG 234
Cdd:PLN02724 266 yPTGLGALLVRRDAAKLLKKKYFGGG 291
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
58-232 |
1.23e-06 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 50.08 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 58 IADLVGADprEIVFTSGATEsdnlAIKGAANFYQKKGKHIITSK----TEHKAVldtcrqlEREGFEVtYLAPQS---NG 130
Cdd:cd06452 53 LAEFLGMD--EARVTPGARE----GKFAVMHSLCEKGDWVVVDGlahyTSYVAA-------ERAGLNV-REVPNTghpEY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 131 IIDLKE----LEAAMRDDTILVS---IMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFS 203
Cdd:cd06452 119 HITPEGyaevIEEVKDEFGKPPAlalLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGS 198
|
170 180 190
....*....|....*....|....*....|..
gi 1238450932 204 GHKIY---GPKGIGALYVRRKPRIRIEAQMHG 232
Cdd:cd06452 199 GHKSMaasAPIGVLATTEEWADIVFRTSQMFK 230
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
114-220 |
1.66e-06 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 49.53 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 114 LEREGFEVTYLAPQSNGIIDLKELEAAM-RDDTIL-VSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPID 191
Cdd:PRK13479 99 AEYLGIAHVVLDTGEDEPPDAAEVEAALaADPRIThVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPID 178
|
90 100 110
....*....|....*....|....*....|
gi 1238450932 192 LSQLKVD-LMSFSGHKIYGPKGIGALYVRR 220
Cdd:PRK13479 179 IAELGIDaLISSANKCIEGVPGFGFVIARR 208
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
55-371 |
1.11e-05 |
|
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: 46.95 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 55 RNQIADLVG------ADPREIVFTSGATEsdnlAIKGAANFYQKKGKHIITSK---TEHKAVldtcrqLEREGFEVTY-- 123
Cdd:cd00609 42 REAIAEWLGrrggvdVPPEEIVVTNGAQE----ALSLLLRALLNPGDEVLVPDptyPGYEAA------ARLAGAEVVPvp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 124 LAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV---QDIATIGEMCRARGII--------------YHVDATQSVG 186
Cdd:cd00609 112 LDEEGGFLLDLELLEAAKTPKTKLLYLNNPNNPTGAVlseEELEELAELAKKHGILiisdeayaelvydgEPPPALALLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 187 KLPIDLSqlkvdLMSFSghKIYGPKG--IGALYVRRKPRIRIEAQMHgggherGMRSGTLPVHQIVGMGEAYRIAKEEME 264
Cdd:cd00609 192 AYERVIV-----LRSFS--KTFGLPGlrIGYLIAPPEELLERLKKLL------PYTTSGPSTLSQAAAAAALDDGEEHLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 265 TEMARLRTLRNRLWDGVKDMEEVYLNGDleQGAPNILnvsfnyvegeslimaLKDLAVSSGSACTSASLEPSYVLRALGM 344
Cdd:cd00609 259 ELRERYRRRRDALLEALKELGPLVVVKP--SGGFFLW---------------LDLPEGDDEEFLERLLLEAGVVVRPGSA 321
|
330 340
....*....|....*....|....*..
gi 1238450932 345 TDELAHSSIRFSLGrfTTEEEIDYTIK 371
Cdd:cd00609 322 FGEGGEGFVRLSFA--TPEEELEEALE 346
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
58-213 |
1.46e-05 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 46.85 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 58 IADLVGADprEIVFTSGATESdnlaiKGA-ANFYQKKGKHIITSK----TEHKAVldtcrqlEREGFEVtYLAPQS---N 129
Cdd:PRK09331 72 LAEFLGMD--EARVTHGAREG-----KFAvMHSLCKKGDYVVLDGlahyTSYVAA-------ERAGLNV-REVPKTgypE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 130 GIIDLKE----LEAAMRDDTILVSIM---HVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSF 202
Cdd:PRK09331 137 YKITPEAyaekIEEVKEETGKPPALAlltHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVG 216
|
170
....*....|....
gi 1238450932 203 SGHKIY---GPKGI 213
Cdd:PRK09331 217 SGHKSMaasAPSGV 230
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
56-260 |
1.90e-05 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 46.26 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 56 NQIADLVGAdPREI-------VFTSGATESDNLAIKGAA----NFYQKKGKHIITSKTEHKAVLDTCRQLERE------- 117
Cdd:pfam00282 86 NWLGEMLGL-PAEFlgqegggVLQPGSSESNLLALLAARtkwiKRMKAAGKPADSSGILAKLVAYTSDQAHSSiekaaly 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 118 -GFEVTYLAPQSNGIIDLKELEAA-MRDDTILVSIMHVNNEIGVV-----QDIATIGEMCRARGIIYHVDATQSVGKL-- 188
Cdd:pfam00282 165 gGVKLREIPSDDNGKMRGMDLEKAiEEDKENGLIPFFVVATLGTTgsgafDDLQELGDICAKHNLWLHVDAAYGGSAFic 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238450932 189 ----PIDLSQLKVDLMSFSGHKIYG-PKGIGALYVRRKPRIRIEAQMHGGGHERGMRSGTLPVHQIvGMGEAYRIAK 260
Cdd:pfam00282 245 pefrHWLFGIERADSITFNPHKWMLvLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYDTGHKQI-PLSRRFRILK 320
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
1-182 |
1.10e-04 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 44.12 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 1 MKLPIYLdysATTPVDPRVAEKMMQCLTLDGNF-----GNPAsrshrfgwhaeeaVDIARNQIADLVGADPrEIVFTSGA 75
Cdd:cd00614 3 VAPPIYQ---TSTFVFPSPAEAADLFALREGGYiysriGNPT-------------VDALEKKLAALEGGEA-ALAFSSGM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 76 TesdnlAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLERE-GFEVTYLAPQsngiiDLKELEAAMRDDTILVSIMHVN 154
Cdd:cd00614 66 A-----AISTVLLALLKAGDHVVASDDLYGGTYRLFERLLPKlGIEVTFVDPD-----DPEALEAAIKPETKLVYVESPT 135
|
170 180
....*....|....*....|....*...
gi 1238450932 155 NEIGVVQDIATIGEMCRARGIIYHVDAT 182
Cdd:cd00614 136 NPTLKVVDIEAIAELAHEHGALLVVDNT 163
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
91-174 |
3.38e-04 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 42.43 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 91 QKKGKHIITSKT---EHKAVLDTcrQLEREGFEVTYLaPQSNGIIDLKELEAAMRDDTILVsIMHVNNEIGVVQDIATIG 167
Cdd:PRK00451 151 ITKRKKVLVSGAvhpEYREVLKT--YLKGQGIEVVEV-PYEDGVTDLEALEAAVDDDTAAV-VVQYPNFFGVIEDLEEIA 226
|
....*..
gi 1238450932 168 EMCRARG 174
Cdd:PRK00451 227 EIAHAGG 233
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
55-180 |
1.06e-03 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 40.75 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 55 RNQIADLVGADP-------REIVFTSGATESDNLAIKGAANfyqkKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQ 127
Cdd:pfam00155 45 REALAKFLGRSPvlkldreAAVVFGSGAGANIEALIFLLAN----PGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSN 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238450932 128 SNGIiDLKELEAAMRDDTILVSIMHVNNEIGVV---QDIATIGEMCRARGIIYHVD 180
Cdd:pfam00155 121 DFHL-DFDALEAALKEKPKVVLHTSPHNPTGTVatlEELEKLLDLAKEHNILLLVD 175
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
58-290 |
2.19e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 39.51 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 58 IADLVGADprEIVFTSGATESDNLAIKGAAnfyqKKGKHIITSKTEHkAVLDTCRQL-EREGFEVTYLAPQSNGIIDLKE 136
Cdd:pfam01212 41 VAELFGKE--AALFVPSGTAANQLALMAHC----QRGDEVICGEPAH-IHFDETGGHaELGGVQPRPLDGDEAGNMDLED 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 137 LEAAMRDDTI-------LVSIMHVNNEIG--VV--QDIATIGEMCRARGIIYHVDATQ------SVGKLPIDLSQLkVDL 199
Cdd:pfam01212 114 LEAAIREVGAdifpptgLISLENTHNSAGgqVVslENLREIAALAREHGIPVHLDGARfanaavALGVIVKEITSY-ADS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 200 MSFSGHKIYGpKGIGALYVRRKPRI--RIE-AQMHGGgherGMR-SGTLPVHQIVGMGEAYRIAKEemETEMARLRTLRN 275
Cdd:pfam01212 193 VTMCLSKGLG-APVGSVLAGSDDFIakAIRqRKYLGG----GLRqAGVLAAAGLRALEEGVARLAR--DHATARRLAEGL 265
|
250
....*....|....*
gi 1238450932 276 RLWDGVkDMEEVYLN 290
Cdd:pfam01212 266 ELLRLA-IPRRVYTN 279
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
28-176 |
3.80e-03 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 39.25 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 28 TLDGNFGNPAS---------RSHRF-GWHAEEAVDIARNQIADLVGADP------REIVFTSGATESDNLAIKGAANfyq 91
Cdd:TIGR01265 42 SVFGNLRTDPEaeeavkdalRSGKFnGYAPSVGALAAREAVAEYLSSDLpgkltaDDVVLTSGCSQAIEICIEALAN--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 92 kKGKHIITSKTEHKAVLDTCRQLereGFEVTY--LAPQSNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV---QDIATI 166
Cdd:TIGR01265 119 -PGANILVPRPGFPLYDTRAAFS---GLEVRLydLLPEKDWEIDLDGLESLADEKTVAIVVINPSNPCGSVfsrDHLQKI 194
|
170
....*....|
gi 1238450932 167 GEMCRARGII 176
Cdd:TIGR01265 195 AEVAEKLGIP 204
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
124-234 |
4.64e-03 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 38.89 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238450932 124 LAPQSNGIIDLKELEAAMRDDTI------LVSIMHVNnEIGVV---QDIATIGEMCRARGIIYHVD------ATQSVGKL 188
Cdd:COG2008 103 PVPGEDGKLTPEDLEAAIRPGDVhfpqpgLVSLENTT-EGGTVyplEELRAIAAVAREHGLPLHLDgarlfnAAAALGVS 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238450932 189 PIDLSQLkVDLMSFSghkiyGPKGIGAL----------YVRRKPRIRieaQMHGGG 234
Cdd:COG2008 182 LAEITAG-VDSVSFG-----LTKGLGAPggavlagdpeFIEEARRWR---KRLGGL 228
|
|
| |
