|
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: 930.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 1 MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 81 LAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 161 QDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 241 SGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDL 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIE 400
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIE 400
|
....
gi 1560336866 401 WAHH 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: 801.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 1 MKLPIYLDYSATTPVDPRVAEKMMQFMTMDgtFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDN 80
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 81 LAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV 160
Cdd:TIGR02006 79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 161 QDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 241 SGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDL 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIE 400
Cdd:TIGR02006 319 AVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIE 398
|
....
gi 1560336866 401 WAHH 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: 679.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 2 KLPIYLDYSATTPVDPRVAEKMMQFMTMDgtFGNPASrSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNL 81
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEY--FGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 82 AIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQ 161
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 162 DIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRkpRVRIEAQMHGGGHERGMRS 241
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 242 GTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKD-IEEVYLNGDLEHGAPNILNVSFNYVEGESLIMAL--K 318
Cdd:COG1104 236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560336866 319 DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLS 384
Cdd:COG1104 316 GIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-368 |
4.76e-108 |
|
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: 322.27 E-value: 4.76e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDPRVAEKMMQFMTmdGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYT--DYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 84 KGAANFyQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:pfam00266 79 LSLGRS-LKPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 163 IAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 236 ERGM-------RSGTLPVHQIVGMGEAYR-IAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHgaPNILNVSFNY 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERR--ASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560336866 308 VEGESLIMALKD--LAVSSGSACTsaslEPSYVLRALglndelaHSSIRFSLGRFTTEEEIDY 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 |
6.46e-77 |
|
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: 242.76 E-value: 6.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDPRVAEKMMQFMTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 84 KGAAnFYQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:cd06453 79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 163 IAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRkprvRIEAQM---HGGG----- 234
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKE----ELLEEMppyGGGGemiee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 235 --------HERGMR--SGTLPVHQIVGMGEA--Y--RIAKEEMAtemERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPnI 300
Cdd:cd06453 234 vsfeettyADLPHKfeAGTPNIAGAIGLGAAidYleKIGMEAIA---AHEHELTAYALERLSEIPGVRVYGDAEDRAG-V 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560336866 301 lnVSFNyVEG---ESLIMAL--KDLAVSSGSACTsaslEPsyVLRALGLNdelahSSIRFSLGRFTTEEEID 367
Cdd:cd06453 310 --VSFN-LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFGLYNTEEEID 367
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
54-235 |
2.30e-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: 96.08 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 54 ARNQIADLVGA-DPREIVFTSGATESDNLAIK--GAANFyqKKGKHIITSKTEHKA--------------------VLDT 110
Cdd:NF041166 294 AREKVRRFIGApSVDEIIFVRGTTEAINLVAKswGRQNI--GAGDEIIVSHLEHHAnivpwqqlaqetgaklrvipVDDS 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 111 crqleregfevtylapqrnGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPI 190
Cdd:NF041166 372 -------------------GQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPV 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1560336866 191 DLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprvrIEAQM---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: 930.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 1 MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 81 LAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 161 QDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 241 SGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDL 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIE 400
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIE 400
|
....
gi 1560336866 401 WAHH 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: 801.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 1 MKLPIYLDYSATTPVDPRVAEKMMQFMTMDgtFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDN 80
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 81 LAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV 160
Cdd:TIGR02006 79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 161 QDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 241 SGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDL 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIE 400
Cdd:TIGR02006 319 AVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIE 398
|
....
gi 1560336866 401 WAHH 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: 679.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 2 KLPIYLDYSATTPVDPRVAEKMMQFMTMDgtFGNPASrSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNL 81
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEY--FGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 82 AIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQ 161
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 162 DIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRkpRVRIEAQMHGGGHERGMRS 241
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 242 GTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKD-IEEVYLNGDLEHGAPNILNVSFNYVEGESLIMAL--K 318
Cdd:COG1104 236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560336866 319 DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLS 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: 585.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDPRVAEKMMQFMTmdGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIK 84
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLI--EHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 85 GAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIA 164
Cdd:PLN02651 79 GVMHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 165 AIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTL 244
Cdd:PLN02651 159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 245 PVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKD-IEEVYLNG--DLEHGAPNILNVSFNYVEGESLIMALKDLA 321
Cdd:PLN02651 239 NTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAkLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1560336866 322 VSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEID 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 |
0e+00 |
|
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: 510.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDPRVAEKMMQFMTmdGTFGNPASrSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIK 84
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFT--EYFGNPSS-MHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 85 GAANFYQKKgKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIA 164
Cdd:TIGR03402 78 SALAAQPEK-RHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 165 AIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprVRIEAQMHGGGHERGMRSGTL 244
Cdd:TIGR03402 157 EIGEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKG--TRFRPLLRGGHQERGRRAGTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 245 PVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGI-KDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMAL--KDLA 321
Cdd:TIGR03402 235 NVPGIVGLGKAAELATEHLEEENTRVRALRDRLEAGLlARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLdmEGIC 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560336866 322 VSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPL 386
Cdd:TIGR03402 315 ASSGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
5-395 |
5.12e-111 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 330.54 E-value: 5.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDpRVAEKMMQFMTMDgTFGNpASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIK 84
Cdd:PRK02948 2 IYLDYAATTPMS-KEALQTYQKAASQ-YFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 85 GAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIA 164
Cdd:PRK02948 79 SLLNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 165 AIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRrkPRVRIEAQMHGGGHERGMRSGTL 244
Cdd:PRK02948 159 EIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYIN--PQVRWKPVFPGTTHEKGFRPGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 245 PVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIE-EVYLNGDLEHGAPNILNVSFNYVEGEsLIMA---LKDL 320
Cdd:PRK02948 237 NVPGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPlPIEVEGHSTSCLPHIIGVTIKGIEGQ-YTMLecnRRGI 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560336866 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELvrksigrlrdLSPLWEMYKQGVD 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 |
4.76e-108 |
|
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: 322.27 E-value: 4.76e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDPRVAEKMMQFMTmdGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYT--DYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 84 KGAANFyQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:pfam00266 79 LSLGRS-LKPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 163 IAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 236 ERGM-------RSGTLPVHQIVGMGEAYR-IAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHgaPNILNVSFNY 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERR--ASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560336866 308 VEGESLIMALKD--LAVSSGSACTsaslEPSYVLRALglndelaHSSIRFSLGRFTTEEEIDY 368
Cdd:pfam00266 316 VHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
5-375 |
1.31e-80 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 253.14 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVdPR-VAEKMMQFMTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLA 82
Cdd:COG0520 17 VYLDNAATGQK-PRpVIDAIRDYYEPYN--ANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEAINLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 83 IKGAANFyqKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQ 161
Cdd:COG0520 94 AYGLGRL--KPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 162 DIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGG------- 234
Cdd:COG0520 172 PVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPPFLGGGGmiewvsf 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 235 -----HERGMR--SGTLPVHQIVGMGEA--Y--RIAKEEMAtemERLRGLRNRLWNGIKDIE--EVYLNGDLEHGAPnIl 301
Cdd:COG0520 252 dgttyADLPRRfeAGTPNIAGAIGLGAAidYleAIGMEAIE---ARERELTAYALEGLAAIPgvRILGPADPEDRSG-I- 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560336866 302 nVSFNyVEG---ESLIMALKDL--AVSSGSACTsaslEPsyVLRALGLNdelahSSIRFSLGRFTTEEEIDYTIELVRK 375
Cdd:COG0520 327 -VSFN-VDGvhpHDVAALLDDEgiAVRAGHHCA----QP--LMRRLGVP-----GTVRASFHLYNTEEEIDRLVEALKK 392
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-367 |
6.46e-77 |
|
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: 242.76 E-value: 6.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDPRVAEKMMQFMTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 84 KGAAnFYQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:cd06453 79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 163 IAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRkprvRIEAQM---HGGG----- 234
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKE----ELLEEMppyGGGGemiee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 235 --------HERGMR--SGTLPVHQIVGMGEA--Y--RIAKEEMAtemERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPnI 300
Cdd:cd06453 234 vsfeettyADLPHKfeAGTPNIAGAIGLGAAidYleKIGMEAIA---AHEHELTAYALERLSEIPGVRVYGDAEDRAG-V 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560336866 301 lnVSFNyVEG---ESLIMAL--KDLAVSSGSACTsaslEPsyVLRALGLNdelahSSIRFSLGRFTTEEEID 367
Cdd:cd06453 310 --VSFN-LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFGLYNTEEEID 367
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
5-377 |
1.30e-51 |
|
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: 177.85 E-value: 1.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDPRVAEKMMQFMTMDgtFGNPASRSHRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:TIGR01979 20 VYLDSAATSQKPQQVIDAVAEYYRNS--NANVHRGIHTLSVRATEAYEAVREKVAKFINAaSDEEIVFTRGTTESINLVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 84 KGAANFYQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQD 162
Cdd:TIGR01979 98 YSWGDSNLKAGDEIVISEMEHHANIVPWQLLaERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLVAITHVSNVLGTVNP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 163 IAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprvrIEAQM---HGGGherGM 239
Cdd:TIGR01979 178 VEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEE----LLEQMppfLGGG---EM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 240 ------------------RSGTLPVHQIVGMGEAYRIAKE-EMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEhGAPNI 300
Cdd:TIGR01979 251 iaevsfeettyneaphkfEAGTPNIAGVIGLGAAIDYLEAiGLENIEAHEHELTAYALERLGEIPGLRIYGPRD-AEDRG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 301 LNVSFNyVEGE-----SLIMALKDLAVSSGSACTsaslEPsyVLRALGLndelaHSSIRFSLGRFTTEEEIDYTIELVRK 375
Cdd:TIGR01979 330 GIISFN-VEGVhphdvGTILDEEGIAVRSGHHCA----QP--LMRRFGV-----PATCRASFYIYNTEEDIDALVEALKK 397
|
..
gi 1560336866 376 SI 377
Cdd:TIGR01979 398 VR 399
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
5-383 |
6.26e-36 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 136.42 E-value: 6.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTPVDPRVAEKMMQFMTMDGTfgNPASRSHRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAI 83
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYYEEYNS--NVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINLVA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 84 K--GAANFyqKKGKHIITSKTEHKAVLdTCRQL--EREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGV 159
Cdd:PLN02855 112 YtwGLANL--KPGDEVILSVAEHHSNI-VPWQLvaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 160 VQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMhGGGH---- 235
Cdd:PLN02855 189 ILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPPFL-GGGEmisd 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 236 ---------ERGMR--SGTLPVHQIVGMGEA--Y--RIAKEEM-ATEMErlrgLRNRLWNGIKDIEEVYLNG----DLEH 295
Cdd:PLN02855 268 vfldhstyaPPPSRfeAGTPAIGEAIGLGAAidYlsEIGMDRIhEYEVE----LGTYLYEKLSSVPGVRIYGpkpsEGVG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 296 GAPnilNVSFNyVEG------ESLIMALKDLAVSSGSACTsaslEPSYvlRALGLNdelahSSIRFSLGRFTTEEEIDYT 369
Cdd:PLN02855 344 RAA---LCAFN-VEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLGVN-----ASARASLYFYNTKEEVDAF 408
|
410
....*....|....
gi 1560336866 370 IELVRKSIGRLRDL 383
Cdd:PLN02855 409 IHALKDTIAFFSSF 422
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
5-234 |
4.04e-29 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 117.06 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDySATTPVDPR-VAEKMMQFMTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLA 82
Cdd:PRK10874 21 VYLD-SAATALKPQaVIEATQQFYSLSA--GNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 83 IKGAANFYQKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQ 161
Cdd:PRK10874 98 AQSYARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560336866 162 DIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprvrIEAQM---HGGG 234
Cdd:PRK10874 178 DLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSE----LLEAMspwQGGG 249
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
41-220 |
5.44e-29 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 116.77 E-value: 5.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 41 HRFGWQAEEAVDIARNQIADLVGA-DPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQL-EREG 118
Cdd:PRK09295 59 HTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 119 FEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVD 198
Cdd:PRK09295 139 AELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCD 218
|
170 180
....*....|....*....|..
gi 1560336866 199 LMSFSGHKIYGPKGIGALYVRR 220
Cdd:PRK09295 219 FYVFSGHKLYGPTGIGILYVKE 240
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
54-235 |
2.30e-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: 96.08 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 54 ARNQIADLVGA-DPREIVFTSGATESDNLAIK--GAANFyqKKGKHIITSKTEHKA--------------------VLDT 110
Cdd:NF041166 294 AREKVRRFIGApSVDEIIFVRGTTEAINLVAKswGRQNI--GAGDEIIVSHLEHHAnivpwqqlaqetgaklrvipVDDS 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 111 crqleregfevtylapqrnGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPI 190
Cdd:NF041166 372 -------------------GQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPV 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1560336866 191 DLSQLKVDLMSFSGHKIYGPKGIGALYVRRKprvrIEAQM---HGGGH 235
Cdd:NF041166 433 DVQALDADFFVFSGHKVFGPTGIGVVYGKRD----LLEAMppwQGGGN 476
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
56-376 |
3.57e-12 |
|
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: 66.84 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 56 NQIADLVGADPREI--VFTSGATESDNLAIKGAANFYQKKGKH----------IITSKTEHKAVLDTCRQLEREGFEVTY 123
Cdd:cd06450 45 NWLAKLFGLPSEDAdgVFTSGGSESNLLALLAARDRARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVKVRLVPV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 124 LAPQRngiIDLKELEAAMRDD------TILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPID-----L 192
Cdd:cd06450 125 DEDGR---MDPEALEAAIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPeprhlD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 193 SQLK-VDLMSFSGHKiYG--PKGIGALYvrrkprVRIEAQMHggghergmrsgTLPVHQIVGMGEAyriakeemateMER 269
Cdd:cd06450 202 FGIErVDSISVDPHK-YGlvPLGCSAVL------VRALKLWA-----------TLRRFGRDGYGEH-----------IDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 270 LRGLRNRLWNGIKDIEEVYLNGDlehgaPNILNVSFNYVEGES---LIMALKDLAVSSGSActsaslepsyVLRALGLND 346
Cdd:cd06450 253 IVDLAKYLAELIRADPGFELLGE-----PNLSLVCFRLKPSVKldeLNYDLSDRLNERGGW----------HVPATTLGG 317
|
330 340 350
....*....|....*....|....*....|.
gi 1560336866 347 elaHSSIRFS-LGRFTTEEEIDYTIELVRKS 376
Cdd:cd06450 318 ---PNVLRFVvTNPLTTRDDADALLEDIERA 345
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
69-219 |
3.94e-12 |
|
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: 64.33 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 69 IVFTSGATESDNLAIKGAAnfyqKKGKHIITSKTEHKAVldTCRQLEREGFE---VTYLAPQRNGIIDLKELEAAMRDDT 145
Cdd:cd01494 20 AVFVPSGTGANEAALLALL----GPGDEVIVDANGHGSR--YWVAAELAGAKpvpVPVDDAGYGGLDVAILEELKAKPNV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560336866 146 ILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQL---KVDLMSFSGHKIYGPKGIGALYVR 219
Cdd:cd01494 94 ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIpegGADVVTFSLHKNLGGEGGGVVIVK 170
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
56-379 |
7.83e-11 |
|
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: 63.31 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 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 1560336866 117 EGfeVTYLAPQRNGIIDLKELEAAMRDD------TILV-----SIMHvnneiGVVQDIAAIGEMCRARGIIYHVDAtqSV 185
Cdd:COG0076 189 DA--LRKVPVDEDGRMDPDALEAAIDEDraaglnPIAVvatagTTNT-----GAIDPLAEIADIAREHGLWLHVDA--AY 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 186 G-------KLPIDLSQL-KVDLMSFSGHKiYG--PKGIGALYVRRKPRVRIEAQMH--------GGGHE---------RG 238
Cdd:COG0076 260 GgfalpspELRHLLDGIeRADSITVDPHK-WLyvPYGCGAVLVRDPELLREAFSFHasylgpadDGVPNlgdytlelsRR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 239 MRSgtLPVH---QIVGMgEAYRiakeEMateMERLRGLRNRLWNGIKDIEEVYLNGDlehgaPNILNVSFNYVEGES--- 312
Cdd:COG0076 339 FRA--LKLWatlRALGR-EGYR----EL---IERCIDLARYLAEGIAALPGFELLAP-----PELNIVCFRYKPAGLdee 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 313 --LIMALKDLAVSSGSA-CTSASLEPSYVLRALGLNDelahssirfslgrFTTEEEIDYTIELVRKSIGR 379
Cdd:COG0076 404 daLNYALRDRLRARGRAfLSPTKLDGRVVLRLVVLNP-------------RTTEDDVDALLDDLREAAAE 460
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
113-284 |
9.18e-10 |
|
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: 59.61 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 113 QLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTI-LVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPID 191
Cdd:cd06451 92 MAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIkAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 192 LSQLKVDLMsFSG-HKIYG-PKGIGALYVRRKPRVRIEAQM-HGGGH-----------ERGMRSGTLPVHQIVGMGEAYR 257
Cdd:cd06451 172 MDEWGVDVA-YTGsQKALGaPPGLGPIAFSERALERIKKKTkPKGFYfdlllllkywgEGYSYPHTPPVNLLYALREALD 250
|
170 180
....*....|....*....|....*...
gi 1560336866 258 -IAKEEMATEMERLRGLRNRLWNGIKDI 284
Cdd:cd06451 251 lILEEGLENRWARHRRLAKALREGLEAL 278
|
|
| PRK05939 |
PRK05939 |
cystathionine gamma-synthase family protein; |
40-182 |
7.39e-08 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 235650 [Multi-domain] Cd Length: 397 Bit Score: 53.92 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 40 SHRFGWQAEEAVDIARNQIADL---VGAdpreIVFTSGATesdnlAIkgAANFYQ--KKGKHIITSK---TEHKAVLDTC 111
Cdd:PRK05939 38 GFTYARQGTPTTAALEAKITKMeggVGT----VCFATGMA-----AI--AAVFLTllRAGDHLVSSQflfGNTNSLFGTL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560336866 112 RQLereGFEVTYLAPqrngiIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDAT 182
Cdd:PRK05939 107 RGL---GVEVTMVDA-----TDVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGALCRERGLLYVVDNT 169
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
113-282 |
1.76e-07 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 52.84 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 113 QLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTI----LVSIMHVNNEIGVVQDIAAIGEM--CRARGIIYHVDATQSVG 186
Cdd:PLN02409 102 QMQRLNFDVDVVESPWGQGADLDILKSKLRQDTNhkikAVCVVHNETSTGVTNDLAGVRKLldCAQHPALLLVDGVSSIG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 187 KLPIDLSQLKVDL-MSFSGHKIYGPKGIG----------ALYVRRKPRVRIEAQMHGGGHERGMRSG-TLPVHQIVGMGE 254
Cdd:PLN02409 182 ALDFRMDEWGVDVaLTGSQKALSLPTGLGivcaspkaleASKTAKSPRVFFDWADYLKFYKLGTYWPyTPSIQLLYGLRA 261
|
170 180
....*....|....*....|....*....
gi 1560336866 255 AYRIAKEE-MATEMERLRGLRNRLWNGIK 282
Cdd:PLN02409 262 ALDLIFEEgLENVIARHARLGEATRLAVE 290
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
5-234 |
3.27e-07 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 52.56 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 5 IYLDYSATTpvdpRVAEKMMQFMTMDGT---FGNPASRSHRfGWQAEEAVDIARNQIADLVGADPRE--IVFTSGATESd 79
Cdd:PLN02724 36 VYLDHAGAT----LYSESQLEAALADFSsnvYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 80 nLAIKGAAnFYQKKGKHIITSKTEHKAVLDTcRQ--LEREG--------------------FEVTYLAPQRNGIIDLKEL 137
Cdd:PLN02724 110 -LKLVGET-FPWSSESHFCYTLENHNSVLGI-REyaLEKGAaaiavdieeaanqptnsqgsVVVKSRGLQRRNTSKLQKR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 138 EAamRDDTILVSIMHVN----------NEIGVVQDIAAIGEMCRARGIIYhVDATQSVGKLPIDLSQLKVDLMSFSGHKI 207
Cdd:PLN02724 187 ED--DGEAYNLFAFPSEcnfsgakfplDLVKLIKDNQHSNFSKSGRWMVL-LDAAKGCGTSPPDLSRYPADFVVVSFYKI 263
|
250 260
....*....|....*....|....*...
gi 1560336866 208 YG-PKGIGALYVRRKPRVRIEAQMHGGG 234
Cdd:PLN02724 264 FGyPTGLGALLVRRDAAKLLKKKYFGGG 291
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
114-220 |
7.33e-07 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 50.68 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 114 LEREGFEVTYLAPQRNGIIDLKELEAAM-RDDTIL-VSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPID 191
Cdd:PRK13479 99 AEYLGIAHVVLDTGEDEPPDAAEVEAALaADPRIThVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPID 178
|
90 100 110
....*....|....*....|....*....|
gi 1560336866 192 LSQLKVD-LMSFSGHKIYGPKGIGALYVRR 220
Cdd:PRK13479 179 IAELGIDaLISSANKCIEGVPGFGFVIARR 208
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
58-232 |
1.02e-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: 50.47 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 58 IADLVGADprEIVFTSGATEsdnlAIKGAANFYQKKGKHIITSKTEHKAvldtcrqleregfevTYLAPQRNGII----- 132
Cdd:cd06452 53 LAEFLGMD--EARVTPGARE----GKFAVMHSLCEKGDWVVVDGLAHYT---------------SYVAAERAGLNvrevp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 133 ----------------DLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLK 196
Cdd:cd06452 112 ntghpeyhitpegyaeVIEEVKDEFGKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELG 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 1560336866 197 VDLMSFSGHKIY---GPKGIGALYVRRKPRVRIEAQMHG 232
Cdd:cd06452 192 ADFIVGSGHKSMaasAPIGVLATTEEWADIVFRTSQMFK 230
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
1-182 |
3.14e-06 |
|
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: 48.74 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 1 MKLPIYLdysATTPVDPRVAEKMMQFMTMDGTF-----GNPAsrshrfgwqaeeaVDIARNQIADLVGADPrEIVFTSGA 75
Cdd:cd00614 3 VAPPIYQ---TSTFVFPSPAEAADLFALREGGYiysriGNPT-------------VDALEKKLAALEGGEA-ALAFSSGM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 76 TesdnlAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLERE-GFEVTYLAPQrngiiDLKELEAAMRDDTILVSIMHVN 154
Cdd:cd00614 66 A-----AISTVLLALLKAGDHVVASDDLYGGTYRLFERLLPKlGIEVTFVDPD-----DPEALEAAIKPETKLVYVESPT 135
|
170 180
....*....|....*....|....*...
gi 1560336866 155 NEIGVVQDIAAIGEMCRARGIIYHVDAT 182
Cdd:cd00614 136 NPTLKVVDIEAIAELAHEHGALLVVDNT 163
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
58-213 |
1.22e-05 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 46.85 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 58 IADLVGADprEIVFTSGATESdnlaiKGA-ANFYQKKGKHIITSK----TEHKAVldtcrqlEREGFEVTY--LAPQRNG 130
Cdd:PRK09331 72 LAEFLGMD--EARVTHGAREG-----KFAvMHSLCKKGDYVVLDGlahyTSYVAA-------ERAGLNVREvpKTGYPEY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 131 IIDLKE----LEAAMRDDTILVSIM---HVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFS 203
Cdd:PRK09331 138 KITPEAyaekIEEVKEETGKPPALAlltHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGS 217
|
170
....*....|...
gi 1560336866 204 GHKIY---GPKGI 213
Cdd:PRK09331 218 GHKSMaasAPSGV 230
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
56-260 |
4.02e-05 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 45.49 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 56 NQIADLVGAdPREI-------VFTSGATESDNLAIKGAA----NFYQKKGKHIITSKTEHKAVLDTCRQLERE------- 117
Cdd:pfam00282 86 NWLGEMLGL-PAEFlgqegggVLQPGSSESNLLALLAARtkwiKRMKAAGKPADSSGILAKLVAYTSDQAHSSiekaaly 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 118 -GFEVTYLAPQRNGIIDLKELEAA-MRDDTILVSIMHVNNEIGVV-----QDIAAIGEMCRARGIIYHVDATQSVGKL-- 188
Cdd:pfam00282 165 gGVKLREIPSDDNGKMRGMDLEKAiEEDKENGLIPFFVVATLGTTgsgafDDLQELGDICAKHNLWLHVDAAYGGSAFic 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560336866 189 ----PIDLSQLKVDLMSFSGHKIYG-PKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIvGMGEAYRIAK 260
Cdd:pfam00282 245 pefrHWLFGIERADSITFNPHKWMLvLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYDTGHKQI-PLSRRFRILK 320
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
4-182 |
4.04e-05 |
|
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440391 [Multi-domain] Cd Length: 389 Bit Score: 45.43 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 4 PIYLdysATTPVDPRVAEKMMQFMTMD-----GTFGNPASRshrfgwQAEEAvdiarnqIADLVGADpREIVFTSG-Ate 77
Cdd:COG0626 24 PIYL---TSTFVFPSAEALAARFAGEEggyiySRYGNPTRR------ALEEA-------LAALEGGE-AALAFASGmA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 78 sdnlAIkGAANFYQ-KKGKHIITSKTEHKAVLDTCRQ-LEREGFEVTYLAPQrngiiDLKELEAAMRDDTILV---SIMH 152
Cdd:COG0626 85 ----AI-SAVLLALlKAGDHVVASDDLYGGTRRLLDKvLARFGIEVTFVDPT-----DLAAVEAAIRPNTKLVfleTPSN 154
|
170 180 190
....*....|....*....|....*....|
gi 1560336866 153 VNNEigvVQDIAAIGEMCRARGIIYHVDAT 182
Cdd:COG0626 155 PTLE---VVDIAAIAAIAHAAGALLVVDNT 181
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
55-375 |
6.86e-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: 44.64 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 55 RNQIADLVG------ADPREIVFTSGATEsdnlAIKGAANFYQKKGKHIITSK---TEHKAVldtcrqLEREGFEVTY-- 123
Cdd:cd00609 42 REAIAEWLGrrggvdVPPEEIVVTNGAQE----ALSLLLRALLNPGDEVLVPDptyPGYEAA------ARLAGAEVVPvp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 124 LAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV---QDIAAIGEMCRARGII--------------YHVDATQSVG 186
Cdd:cd00609 112 LDEEGGFLLDLELLEAAKTPKTKLLYLNNPNNPTGAVlseEELEELAELAKKHGILiisdeayaelvydgEPPPALALLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 187 KLPIDLSqlkvdLMSFSghKIYGPKG--IGALYVRRKPRVRIEAQMHgggherGMRSGTLPVHQIVGMGEAYRIAKEEMA 264
Cdd:cd00609 192 AYERVIV-----LRSFS--KTFGLPGlrIGYLIAPPEELLERLKKLL------PYTTSGPSTLSQAAAAAALDDGEEHLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 265 TEMERLRGLRNRLWNGIKDIEEVYLNGDleHGAPNI-LNVSFNYVEGESLIMALKD-LAVSSGSACtsaslepsyvlral 342
Cdd:cd00609 259 ELRERYRRRRDALLEALKELGPLVVVKP--SGGFFLwLDLPEGDDEEFLERLLLEAgVVVRPGSAF-------------- 322
|
330 340 350
....*....|....*....|....*....|...
gi 1560336866 343 glnDELAHSSIRFSLGrfTTEEEIDYTIELVRK 375
Cdd:cd00609 323 ---GEGGEGFVRLSFA--TPEEELEEALERLAE 350
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
91-174 |
1.18e-04 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 43.97 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 91 QKKGKHIITSKT---EHKAVLDTcrQLEREGFEVTYLaPQRNGIIDLKELEAAMRDDTILVsIMHVNNEIGVVQDIAAIG 167
Cdd:PRK00451 151 ITKRKKVLVSGAvhpEYREVLKT--YLKGQGIEVVEV-PYEDGVTDLEALEAAVDDDTAAV-VVQYPNFFGVIEDLEEIA 226
|
....*..
gi 1560336866 168 EMCRARG 174
Cdd:PRK00451 227 EIAHAGG 233
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
58-276 |
2.47e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 42.59 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 58 IADLVGADprEIVFTSGATESDNLAIKGAAnfyqKKGKHIITSKTEHkAVLDTCRQL-EREGFEVTYLAPQRNGIIDLKE 136
Cdd:pfam01212 41 VAELFGKE--AALFVPSGTAANQLALMAHC----QRGDEVICGEPAH-IHFDETGGHaELGGVQPRPLDGDEAGNMDLED 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 137 LEAAMRDDTI-------LVSIMHVNNEIG--VV--QDIAAIGEMCRARGIIYHVDATQ------SVGKLPIDLSQLkVDL 199
Cdd:pfam01212 114 LEAAIREVGAdifpptgLISLENTHNSAGgqVVslENLREIAALAREHGIPVHLDGARfanaavALGVIVKEITSY-ADS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 200 MSFSGHKIYGpKGIGAL------YVRRKPRVRieaQMHGGgherGMRSGTLPV--------HQIVGMGEAYRIAkEEMAT 265
Cdd:pfam01212 193 VTMCLSKGLG-APVGSVlagsddFIAKAIRQR---KYLGG----GLRQAGVLAaaglraleEGVARLARDHATA-RRLAE 263
|
250
....*....|.
gi 1560336866 266 EMERLRGLRNR 276
Cdd:pfam01212 264 GLELLRLAIPR 274
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
124-234 |
7.37e-04 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 41.21 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 124 LAPQRNGIIDLKELEAAMRDDTI------LVSIMHVNnEIGVV---QDIAAIGEMCRARGIIYHVD------ATQSVGKL 188
Cdd:COG2008 103 PVPGEDGKLTPEDLEAAIRPGDVhfpqpgLVSLENTT-EGGTVyplEELRAIAAVAREHGLPLHLDgarlfnAAAALGVS 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1560336866 189 PIDLSQLkVDLMSFSghkiyGPKGIGAL----------YVRRKPRVRieaQMHGGG 234
Cdd:COG2008 182 LAEITAG-VDSVSFG-----LTKGLGAPggavlagdpeFIEEARRWR---KRLGGL 228
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
55-180 |
2.94e-03 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 39.60 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 55 RNQIADLVGADP-------REIVFTSGATESDNLAIKGAANfyqkKGKHIITSKTEHKAVLDTCRqleREGFEVTY--LA 125
Cdd:pfam00155 45 REALAKFLGRSPvlkldreAAVVFGSGAGANIEALIFLLAN----PGDAILVPAPTYASYIRIAR---LAGGEVVRypLY 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1560336866 126 PQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVV---QDIAAIGEMCRARGIIYHVD 180
Cdd:pfam00155 118 DSNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVatlEELEKLLDLAKEHNILLLVD 175
|
|
| PRK06234 |
PRK06234 |
methionine gamma-lyase; Provisional |
92-169 |
6.79e-03 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 168478 [Multi-domain] Cd Length: 400 Bit Score: 38.27 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 92 KKGKHIITSKTEHK---AVLdtCRQLEREGFEVTYLAPQrngiiDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGE 168
Cdd:PRK06234 101 KAGDHVVASDTLYGctfALL--NHGLTRYGVEVTFVDTS-----NLEEVRNALKANTKVVYLETPANPTLKVTDIKAISN 173
|
.
gi 1560336866 169 M 169
Cdd:PRK06234 174 I 174
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
92-176 |
6.93e-03 |
|
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440172 [Multi-domain] Cd Length: 442 Bit Score: 38.47 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336866 92 KKGKHIITSKT---EHKAVLDTcrQLEREGFEVTYLAPQrNGIIDLKELEAAMRDDTILVSIMHVNNEiGVVQDIAAIGE 168
Cdd:COG0403 153 KRSNKVLVSEDvhpQTRAVLKT--YAEPLGIEVVEVPDE-DGVTDLEALKALLDDDVAGVLVQYPNFF-GVIEDLRAIAE 228
|
....*...
gi 1560336866 169 MCRARGII 176
Cdd:COG0403 229 AAHAAGAL 236
|
|
| |
