|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
1-406 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 883.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDGIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEegKRIGSNLNISFNFVEGESLMMSLR 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLE--QRVPGNLNVSFNYVEGESLIMALK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:PRK14012 319 DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNS 398
|
....*.
gi 1721624170 401 IEWNHH 406
Cdd:PRK14012 399 IEWAHH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
1-406 |
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: 771.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:TIGR02006 79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSLR 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEH--RVPGNLNVSFNYVEGESLIMALK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:TIGR02006 317 DLAVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNS 396
|
....*.
gi 1721624170 401 IEWNHH 406
Cdd:TIGR02006 397 IEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
2-386 |
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: 655.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 2 KLPIYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASrSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDNL 81
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEY--FGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 82 AIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQ 161
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 162 PIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVRLEAIIHGGGHERGMRS 241
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYV--RKGVRLEPLIHGGGQERGLRS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 242 GTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKD-IEEVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSL- 319
Cdd:COG1104 236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPEN--RLPNTLNFSFPGVEGEALLLALd 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624170 320 -RDIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELS 386
Cdd:COG1104 314 lAGIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-369 |
8.33e-104 |
|
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: 311.49 E-value: 8.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTKdgIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSR-EIVFTSGATESDNLAI 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTD--YNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 84 KGAAHFYQtKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:pfam00266 79 LSLGRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 236 ERGM-------RSGTLPVHQIVGMGEAYR-IAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSmeegKRIGSNLNISF 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP----ERRASIISFNF 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721624170 308 NFVEGESLMMSLRD--IAVSSGSACTsaslEPSYVLRAIgrddelaHSSIRFTLGRWTTEEEID 369
Cdd:pfam00266 314 KGVHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVD 366
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-373 |
1.07e-74 |
|
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: 236.98 E-value: 1.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTKDGifGNPASRSHKFGWEAEEAVDVARNQIADLIGA-DSREIVFTSGATESDNLAI 83
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 84 KGAAhFYQTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:cd06453 79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVrLEAI--IHGGG------ 234
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYG--KEEL-LEEMppYGGGGemieev 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 235 -------HERGMR--SGTLPVHQIVGMGEA--Y--RIAKEEMATEMARLTvlrDRLYNGFKDIEEVYVNGSMEegKRIGS 301
Cdd:cd06453 235 sfeettyADLPHKfeAGTPNIAGAIGLGAAidYleKIGMEAIAAHEHELT---AYALERLSEIPGVRVYGDAE--DRAGV 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721624170 302 nlnISFNfVEGE-----SLMMSLRDIAVSSGSACTsaslEPsyVLRAIGrddelAHSSIRFTLGRWTTEEEIDHTIE 373
Cdd:cd06453 310 ---VSFN-LEGIhphdvATILDQYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEIDALVE 371
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
54-235 |
2.16e-20 |
|
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: 93.38 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 54 ARNQIADLIGADS-REIVFTSGATESDNLAIK--GAAHFYQtkGKHIITVKTEHKAVLDTCRQL-EREG--FEVTYLDpe 127
Cdd:NF041166 294 AREKVRRFIGAPSvDEIIFVRGTTEAINLVAKswGRQNIGA--GDEIIVSHLEHHANIVPWQQLaQETGakLRVIPVD-- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 128 EDG--ILD-LAKLkaaIRPDTILVSVMHVNNEMGVIQPIKEIGAICRAK--KIIfhVDATQSVGKIEVNVQDLNVDLMSF 202
Cdd:NF041166 370 DSGqiLLDeYAKL---LNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAgaKVL--VDGAQSVSHMPVDVQALDADFFVF 444
|
170 180 190
....*....|....*....|....*....|....*
gi 1721624170 203 SSHKLYGPKGIGGLYvcRKPRVrLEAI--IHGGGH 235
Cdd:NF041166 445 SGHKVFGPTGIGVVY--GKRDL-LEAMppWQGGGN 476
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
1-406 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 883.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDGIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEegKRIGSNLNISFNFVEGESLMMSLR 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLE--QRVPGNLNVSFNYVEGESLIMALK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:PRK14012 319 DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNS 398
|
....*.
gi 1721624170 401 IEWNHH 406
Cdd:PRK14012 399 IEWAHH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
1-406 |
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: 771.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:TIGR02006 79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSLR 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEH--RVPGNLNVSFNYVEGESLIMALK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:TIGR02006 317 DLAVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNS 396
|
....*.
gi 1721624170 401 IEWNHH 406
Cdd:TIGR02006 397 IEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
2-386 |
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: 655.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 2 KLPIYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASrSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDNL 81
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEY--FGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 82 AIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQ 161
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 162 PIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVRLEAIIHGGGHERGMRS 241
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYV--RKGVRLEPLIHGGGQERGLRS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 242 GTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKD-IEEVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSL- 319
Cdd:COG1104 236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPEN--RLPNTLNFSFPGVEGEALLLALd 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624170 320 -RDIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELS 386
Cdd:COG1104 314 lAGIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
5-369 |
0e+00 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 568.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDNLAIK 84
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEH--FGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 85 GAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQPIK 164
Cdd:PLN02651 79 GVMHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 165 EIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMRSGTL 244
Cdd:PLN02651 159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 245 PVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKD-IEEVYVNGSMEEGKRIGSNLNISFNFVEGESLMMSLRDIA 323
Cdd:PLN02651 239 NTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAkLGGVRVNGPRDPEKRYPGTLNLSFAYVEGESLLMGLKEVA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1721624170 324 VSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEID 369
Cdd:PLN02651 319 VSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
5-397 |
1.24e-110 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 329.77 E-value: 1.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTKdgIFGNpASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDNLAIK 84
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQ--YFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 85 GAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQPIK 164
Cdd:PRK02948 79 SLLNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 165 EIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVRLEAIIHGGGHERGMRSGTL 244
Cdd:PRK02948 159 EIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYI--NPQVRWKPVFPGTTHEKGFRPGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 245 PVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIE-EVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSL--RD 321
Cdd:PRK02948 237 NVPGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPlPIEVEGHSTS--CLPHIIGVTIKGIEGQYTMLECnrRG 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624170 322 IAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIvkkaivklreLSPLWEMFKEGVD 397
Cdd:PRK02948 315 IAISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHA----------LETIGNQFYRGVK 380
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-369 |
8.33e-104 |
|
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: 311.49 E-value: 8.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTKdgIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSR-EIVFTSGATESDNLAI 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTD--YNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 84 KGAAHFYQtKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:pfam00266 79 LSLGRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 236 ERGM-------RSGTLPVHQIVGMGEAYR-IAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSmeegKRIGSNLNISF 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP----ERRASIISFNF 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721624170 308 NFVEGESLMMSLRD--IAVSSGSACTsaslEPSYVLRAIgrddelaHSSIRFTLGRWTTEEEID 369
Cdd:pfam00266 314 KGVHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVD 366
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
5-379 |
4.56e-77 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 243.89 E-value: 4.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTKDGifGNPASRSHKFGWEAEEAVDVARNQIADLIGADSR-EIVFTSGATESDNLAI 83
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYN--ANVHRGAHELSAEATDAYEAAREKVARFIGAASPdEIIFTRGTTEAINLVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 84 KGAAHFyqTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:COG0520 95 YGLGRL--KPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKprvRLEAII--HGGGH----- 235
Cdd:COG0520 173 VKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRE---LLEALPpfLGGGGmiewv 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 236 ----------ERGMRSGTLPVHQIVGMGEA--Y--RIAKEEMAtemARLTVLRDRLYNGFKDIEEVYVNGSMEEGKRIGS 301
Cdd:COG0520 250 sfdgttyadlPRRFEAGTPNIAGAIGLGAAidYleAIGMEAIE---ARERELTAYALEGLAAIPGVRILGPADPEDRSGI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 302 nlnISFNfVEGE-----SLMMSLRDIAVSSGSACTsaslEPsyVLRAIGrddelAHSSIRFTLGRWTTEEEIDHTIEIVK 376
Cdd:COG0520 327 ---VSFN-VDGVhphdvAALLDDEGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFHLYNTEEEIDRLVEALK 391
|
...
gi 1721624170 377 KAI 379
Cdd:COG0520 392 KLA 394
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-373 |
1.07e-74 |
|
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: 236.98 E-value: 1.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTKDGifGNPASRSHKFGWEAEEAVDVARNQIADLIGA-DSREIVFTSGATESDNLAI 83
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 84 KGAAhFYQTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:cd06453 79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVrLEAI--IHGGG------ 234
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYG--KEEL-LEEMppYGGGGemieev 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 235 -------HERGMR--SGTLPVHQIVGMGEA--Y--RIAKEEMATEMARLTvlrDRLYNGFKDIEEVYVNGSMEegKRIGS 301
Cdd:cd06453 235 sfeettyADLPHKfeAGTPNIAGAIGLGAAidYleKIGMEAIAAHEHELT---AYALERLSEIPGVRVYGDAE--DRAGV 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721624170 302 nlnISFNfVEGE-----SLMMSLRDIAVSSGSACTsaslEPsyVLRAIGrddelAHSSIRFTLGRWTTEEEIDHTIE 373
Cdd:cd06453 310 ---VSFN-LEGIhphdvATILDQYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEIDALVE 371
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
5-385 |
7.29e-37 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 138.73 E-value: 7.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTkdGIFGNPASRSHKFGWEAEEAVDVARNQIADLIGA-DSREIVFTSGATESDNLAI 83
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYYE--EYNSNVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINLVA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 84 K--GAAHFYQtkGKHIITVKTEHKAVLdTCRQL--EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGV 159
Cdd:PLN02855 112 YtwGLANLKP--GDEVILSVAEHHSNI-VPWQLvaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 160 IQPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYvcRKPRVrLEAI--IHGGGH-- 235
Cdd:PLN02855 189 ILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLW--GKSDL-LESMppFLGGGEmi 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 236 -----------ERGMR--SGTLPVHQIVGMGEA--Y-------RIAKEEMAtemarltvLRDRLYNGFKDIEEVYVNGSM 293
Cdd:PLN02855 266 sdvfldhstyaPPPSRfeAGTPAIGEAIGLGAAidYlseigmdRIHEYEVE--------LGTYLYEKLSSVPGVRIYGPK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 294 EEGKRIGSNLnISFNfVEG------ESLMMSLRDIAVSSGSACTsaslEPSYvlRAIGrddelAHSSIRFTLGRWTTEEE 367
Cdd:PLN02855 338 PSEGVGRAAL-CAFN-VEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLG-----VNASARASLYFYNTKEE 404
|
410
....*....|....*...
gi 1721624170 368 IDHTIEIVKKAIVKLREL 385
Cdd:PLN02855 405 VDAFIHALKDTIAFFSSF 422
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
5-218 |
3.78e-31 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 122.94 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEY------MTKDGIfgnpasrsHKFGWEAEEAVDVARNQIADLIGADSRE-IVFTSGATE 77
Cdd:PRK09295 25 AYLDSAASAQKPSQVIDAEAEFyrhgyaAVHRGI--------HTLSAQATEKMENVRKQAALFINARSAEeLVFVRGTTE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 78 SDNLAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNE 156
Cdd:PRK09295 97 GINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721624170 157 MGVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYV 218
Cdd:PRK09295 177 LGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYV 238
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
5-234 |
7.00e-23 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 99.34 E-value: 7.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDERVAKKMMEYMTKDGifGNPASRSHKFGWEAEEAVDVARNQIADLIGA-DSREIVFTSGATESDNLAI 83
Cdd:PRK10874 21 VYLDSAATALKPQAVIEATQQFYSLSA--GNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 84 KGAAHFYQTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:PRK10874 99 QSYARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYvcRKPRvRLEAII--HGGG 234
Cdd:PRK10874 179 LARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLY--GKSE-LLEAMSpwQGGG 249
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
54-235 |
2.16e-20 |
|
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: 93.38 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 54 ARNQIADLIGADS-REIVFTSGATESDNLAIK--GAAHFYQtkGKHIITVKTEHKAVLDTCRQL-EREG--FEVTYLDpe 127
Cdd:NF041166 294 AREKVRRFIGAPSvDEIIFVRGTTEAINLVAKswGRQNIGA--GDEIIVSHLEHHANIVPWQQLaQETGakLRVIPVD-- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 128 EDG--ILD-LAKLkaaIRPDTILVSVMHVNNEMGVIQPIKEIGAICRAK--KIIfhVDATQSVGKIEVNVQDLNVDLMSF 202
Cdd:NF041166 370 DSGqiLLDeYAKL---LNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAgaKVL--VDGAQSVSHMPVDVQALDADFFVF 444
|
170 180 190
....*....|....*....|....*....|....*
gi 1721624170 203 SSHKLYGPKGIGGLYvcRKPRVrLEAI--IHGGGH 235
Cdd:NF041166 445 SGHKVFGPTGIGVVY--GKRDL-LEAMppWQGGGN 476
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
45-218 |
5.77e-14 |
|
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: 69.33 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 45 WEAEEAVdvarnqiADLIGADSREIVFTSGATESDNLAIKGAAhfyqTKGKHIITVKTEHKAVldTCRQLEREGFEVTYL 124
Cdd:cd01494 3 EELEEKL-------ARLLQPGNDKAVFVPSGTGANEAALLALL----GPGDEVIVDANGHGSR--YWVAAELAGAKPVPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 125 --DPEEDGILDLAKL-KAAIRPDTILVSVMHVNNEMGVIQPIKEIGAICRAKKIIFHVDATQSVG---KIEVNVQDLNVD 198
Cdd:cd01494 70 pvDDAGYGGLDVAILeELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGaspAPGVLIPEGGAD 149
|
170 180
....*....|....*....|
gi 1721624170 199 LMSFSSHKLYGPKGIGGLYV 218
Cdd:cd01494 150 VVTFSLHKNLGGEGGGVVIV 169
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
115-282 |
1.99e-13 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 70.89 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 115 EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEM--GVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVNV 192
Cdd:COG0075 94 ERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETstGVLNPLEEIGALAKEHGALLIVDAVSSLGGVPLDM 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 193 QDLNVDLMSFSSHK-LYGPKGIGglYVCRKPRVrLEAIihgggHERGMRS------------------GTLPVHQIVGMG 253
Cdd:COG0075 174 DEWGIDVVVSGSQKcLMLPPGLA--FVAVSERA-LEAI-----EARKLPSyyldlklwlkywekgqtpYTPPVSLLYALR 245
|
170 180 190
....*....|....*....|....*....|
gi 1721624170 254 EAYRIAKEE-MATEMARLTVLRDRLYNGFK 282
Cdd:COG0075 246 EALDLILEEgLENRFARHRRLAEALRAGLE 275
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
13-218 |
2.40e-11 |
|
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: 64.53 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 13 TPMDERVAKKMMEYMTKdGIFGNPASRSHKFgweAE-EAVDVarNQIADLIGADSREI--VFTSGATESDNLAIKGAAHF 89
Cdd:cd06450 7 TTMDPPALLLEMLTSAK-NAIDFTWDESPAA---TEmEAEVV--NWLAKLFGLPSEDAdgVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 90 YQTKGKH----------IITVKTEHKAVLDTCRQLEREgfeVTYLDPEEDGILDLAKLKAAIRPD------TILVSVMHV 153
Cdd:cd06450 81 ARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVK---VRLVPVDEDGRMDPEALEAAIDEDkaeglnPIMVVATAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624170 154 NNEMGVIQPIKEIGAICRAKKIIFHVDAT------------QSVGKIEvnvqdlNVDLMSFSSHKLYG-PKGIGGLYV 218
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAyggfllpfpeprHLDFGIE------RVDSISVDPHKYGLvPLGCSAVLV 229
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
113-282 |
1.90e-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: 61.92 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 113 QLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTI-LVSVMHVNNEMGVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVN 191
Cdd:cd06451 92 MAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIkAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 192 VQDLNVDLMSFSSHK-LYGPKGIGglYVCRKPRVrLEAIIHGGGH---------------ERGMRSGTLPVHQIVGMGEA 255
Cdd:cd06451 172 MDEWGVDVAYTGSQKaLGAPPGLG--PIAFSERA-LERIKKKTKPkgfyfdlllllkywgEGYSYPHTPPVNLLYALREA 248
|
170 180 190
....*....|....*....|....*....|....*
gi 1721624170 256 YRIAKEE-------MATEMARltVLRDRLYN-GFK 282
Cdd:cd06451 249 LDLILEEglenrwaRHRRLAK--ALREGLEAlGLK 281
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
56-228 |
5.07e-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: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 56 NQIADLIGADSREI-VFTSGATESdNL-AIKGA-----AHFYQTKGKH------IITVKTEH----KA--VLDtcrqLER 116
Cdd:COG0076 114 RWLADLLGLPEGAGgVFTSGGTEA-NLlALLAArdralARRVRAEGLPgaprprIVVSEEAHssvdKAarLLG----LGR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 117 EGfeVTYLDPEEDGILDLAKLKAAIRPD------TILV-----SVMHvnnemGVIQPIKEIGAICRAKKIIFHVDA---- 181
Cdd:COG0076 189 DA--LRKVPVDEDGRMDPDALEAAIDEDraaglnPIAVvatagTTNT-----GAIDPLAEIADIAREHGLWLHVDAaygg 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624170 182 --------TQSVGKIEvnvqdlNVDLMSFSSHK-LYGPKGIGGLYVcRKPRVRLEA 228
Cdd:COG0076 262 falpspelRHLLDGIE------RADSITVDPHKwLYVPYGCGAVLV-RDPELLREA 310
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
114-214 |
7.11e-08 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 53.76 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 114 LEREGFEVTYLDPEEDGILDLAKLKAAIR--PDTILVSVMHVNNEMGVIQPIKEIGAICRA--KKIIfhVDATQSVGKIE 189
Cdd:PRK13479 99 AEYLGIAHVVLDTGEDEPPDAAEVEAALAadPRITHVALVHCETTTGILNPLDEIAAVAKRhgKRLI--VDAMSSFGAIP 176
|
90 100
....*....|....*....|....*.
gi 1721624170 190 VNVQDLNVDLMSFSSHK-LYGPKGIG 214
Cdd:PRK13479 177 IDIAELGIDALISSANKcIEGVPGFG 202
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
58-295 |
8.74e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 53.37 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 58 IADLIGADSreIVFTSGATESDNLAIkgAAHFyqTKGKHIITVKTEHkAVLDTCRQL-EREGFEVTYLDPEEDGILDLAK 136
Cdd:pfam01212 41 VAELFGKEA--ALFVPSGTAANQLAL--MAHC--QRGDEVICGEPAH-IHFDETGGHaELGGVQPRPLDGDEAGNMDLED 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 137 LKAAIRPDTI-------LVSVMHVNNEMG--VIQP--IKEIGAICRAKKIIFHVDATQ---SVGKIEVNVQDL--NVDLM 200
Cdd:pfam01212 114 LEAAIREVGAdifpptgLISLENTHNSAGgqVVSLenLREIAALAREHGIPVHLDGARfanAAVALGVIVKEItsYADSV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 201 SFSSHK-LYGPkgIGGLYVCRKPRVRlEAI----IHGGgherGMR-SGTLPVHQIVGMGEAYRIAKEemATEMARltvlr 274
Cdd:pfam01212 194 TMCLSKgLGAP--VGSVLAGSDDFIA-KAIrqrkYLGG----GLRqAGVLAAAGLRALEEGVARLAR--DHATAR----- 259
|
250 260
....*....|....*....|....*.
gi 1721624170 275 dRLYNGFKDI-----EEVYVNGSMEE 295
Cdd:pfam01212 260 -RLAEGLELLrlaipRRVYTNTHMVY 284
|
|
| PRK05939 |
PRK05939 |
cystathionine gamma-synthase family protein; |
93-182 |
6.85e-07 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 235650 [Multi-domain] Cd Length: 397 Bit Score: 50.84 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 93 KGKHIIT---VKTEHKAVLDTCRQLereGFEVTYLDPEedgilDLAKLKAAIRPDTILVSVMHVNNEMGVIQPIKEIGAI 169
Cdd:PRK05939 85 AGDHLVSsqfLFGNTNSLFGTLRGL---GVEVTMVDAT-----DVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGAL 156
|
90
....*....|...
gi 1721624170 170 CRAKKIIFHVDAT 182
Cdd:PRK05939 157 CRERGLLYVVDNT 169
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
91-177 |
8.11e-06 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 47.83 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 91 QTKGKHIITVKT---EHKAVLDTcrQLEREGFEVTYLDPEeDGILDLAKLKAAIRPDTILVSVMHvNNEMGVIQPIKEIG 167
Cdd:PRK00451 151 ITKRKKVLVSGAvhpEYREVLKT--YLKGQGIEVVEVPYE-DGVTDLEALEAAVDDDTAAVVVQY-PNFFGVIEDLEEIA 226
|
90
....*....|
gi 1721624170 168 AICRAKKIIF 177
Cdd:PRK00451 227 EIAHAGGALF 236
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
55-377 |
1.67e-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: 46.57 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 55 RNQIADLIG------ADSREIVFTSGATEsdnlAIKGAAHFYQTKGKHIITVK---TEHKAVldtcrqLEREGFEVTY-- 123
Cdd:cd00609 42 REAIAEWLGrrggvdVPPEEIVVTNGAQE----ALSLLLRALLNPGDEVLVPDptyPGYEAA------ARLAGAEVVPvp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 124 LDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP---IKEIGAICRAKKII--------------FHVDATQSVG 186
Cdd:cd00609 112 LDEEGGFLLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILiisdeayaelvydgEPPPALALLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 187 KIEvNVqdlnVDLMSFSshKLYGPKG--IGGLYVCRKPRVRLEAIIHgggherGMRSGTLPVHQIVGMGEAYRIAKEEMA 264
Cdd:cd00609 192 AYE-RV----IVLRSFS--KTFGLPGlrIGYLIAPPEELLERLKKLL------PYTTSGPSTLSQAAAAAALDDGEEHLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 265 TEMARLTVLRDRLYNGFKDIEEVYVNGSMeegkriGSNLnisfnfvegesLMMSLRDIavSSGSACTSASLEPSYVLRAI 344
Cdd:cd00609 259 ELRERYRRRRDALLEALKELGPLVVVKPS------GGFF-----------LWLDLPEG--DDEEFLERLLLEAGVVVRPG 319
|
330 340 350
....*....|....*....|....*....|...
gi 1721624170 345 GRDDELAHSSIRFTLGrwTTEEEIDHTIEIVKK 377
Cdd:cd00609 320 SAFGEGGEGFVRLSFA--TPEEELEEALERLAE 350
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
58-213 |
4.81e-05 |
|
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: 45.07 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 58 IADLIGADsrEIVFTSGATEsdnlAIKGAAHFYQTKGKHIITVK----TEHKAVldtcrqlEREGFEVT----------Y 123
Cdd:cd06452 53 LAEFLGMD--EARVTPGARE----GKFAVMHSLCEKGDWVVVDGlahyTSYVAA-------ERAGLNVRevpntghpeyH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 124 LDPEEDG-ILDLAKLKAAIRPDTILVSvmHVNNEMGVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSF 202
Cdd:cd06452 120 ITPEGYAeVIEEVKDEFGKPPALALLT--HVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVG 197
|
170
....*....|....
gi 1721624170 203 SSHKLY---GPKGI 213
Cdd:cd06452 198 SGHKSMaasAPIGV 211
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
58-259 |
1.73e-04 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 43.37 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 58 IADLIGADSREIVFTSGATESDNLAIKGAAHFYQTKGKHII--TVKTEHKAVLDTCrqLEREGFEVTYLDPEEDGILDLA 135
Cdd:cd00613 73 LCELTGMDVANASLQDEATAAAEAAGLAAIRAYHKRNKVLVpdSAHPTNPAVARTR--GEPLGIEVVEVPSDEGGTVDLE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 136 KLKAAIRPDTILVSVMHVNNEmGVI-QPIKEIGAICRAKKIIFHVDATQsvgkieVNVQ------DLNVDLMSFSSHKLY 208
Cdd:cd00613 151 ALKEEVSEEVAALMVQYPNTL-GVFeDLIKEIADIAHSAGALVYVDGDN------LNLTglkppgEYGADIVVGNLQKTG 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721624170 209 GPKGIGGLYV----CRKPRVRLeaiihggghergmrsgtLPVHqIVGMGE------AYRIA 259
Cdd:cd00613 224 VPHGGGGPGAgffaVKKELVRF-----------------LPGR-LVGVTKdaegnrAFRLA 266
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
12-180 |
1.17e-03 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 40.78 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 12 TTPMDErvakkMMEYMTKdgifgnpASRSHKfGWEAEEAVDVARNQIADLIGADsrEIVFTSGATESDNLAIKGAAHFYQ 91
Cdd:cd06502 8 TGPTPE-----MLEAMAA-------ANVGDD-VYGEDPTTAKLEARAAELFGKE--AALFVPSGTAANQLALAAHTQPGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 92 T----KGKHIITvktehkavlDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPD-------TILVSVMHVNNEMGVI 160
Cdd:cd06502 73 SvichETAHIYT---------DEAGAPEFLSGVKLLPVPGENGKLTPEDLEAAIRPRddihfppPSLVSLENTTEGGTVY 143
|
170 180
....*....|....*....|..
gi 1721624170 161 QP--IKEIGAICRAKKIIFHVD 180
Cdd:cd06502 144 PLdeLKAISALAKENGLPLHLD 165
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
58-213 |
1.78e-03 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 40.30 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 58 IADLIGADsrEIVFTSGATESdnlaiKGA-AHFYQTKGKHIITVK----TEHKAVldtcrqlEREGFEVTYLDPEE--DG 130
Cdd:PRK09331 72 LAEFLGMD--EARVTHGAREG-----KFAvMHSLCKKGDYVVLDGlahyTSYVAA-------ERAGLNVREVPKTGypEY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 131 ILDLAKLKAAIR---------PDTILVSvmHVNNEMGVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMS 201
Cdd:PRK09331 138 KITPEAYAEKIEevkeetgkpPALALLT--HVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIV 215
|
170
....*....|....*
gi 1721624170 202 FSSHKLY---GPKGI 213
Cdd:PRK09331 216 GSGHKSMaasAPSGV 230
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
126-180 |
1.91e-03 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 40.05 E-value: 1.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721624170 126 PEEDGILDLAKLKAAIRPDTI------LVSVMHVNnEMGVIQP---IKEIGAICRAKKIIFHVD 180
Cdd:COG2008 105 PGEDGKLTPEDLEAAIRPGDVhfpqpgLVSLENTT-EGGTVYPleeLRAIAAVAREHGLPLHLD 167
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
5-108 |
2.58e-03 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 40.24 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 5 IYLDYAATTPMDErvakKMMEYMTKD---GIFGNPASRSHKfGWEAEEAVDVARNQIADLIGADSRE--IVFTSGATESd 79
Cdd:PLN02724 36 VYLDHAGATLYSE----SQLEAALADfssNVYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAA- 109
|
90 100
....*....|....*....|....*....
gi 1721624170 80 nLAIKGAAhFYQTKGKHIITVKTEHKAVL 108
Cdd:PLN02724 110 -LKLVGET-FPWSSESHFCYTLENHNSVL 136
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
65-181 |
2.71e-03 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 39.54 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 65 DSREIVFTSGATESDNLAIKGAAHfyqtKGKHIItvktehkAVLDTCRQL----EREGFEVTYLD-PEEDGIL-DLAKLK 138
Cdd:PRK07324 79 KPENILQTNGATGANFLVLYALVE----PGDHVI-------SVYPTYQQLydipESLGAEVDYWQlKEENGWLpDLDELR 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1721624170 139 AAIRPDTILVSVMHVNNEMGVIQP---IKEIGAICRAkkiifhVDA 181
Cdd:PRK07324 148 RLVRPNTKLICINNANNPTGALMDrayLEEIVEIARS------VDA 187
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|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
103-181 |
3.21e-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: 39.63 E-value: 3.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624170 103 EHKAVLDTcrQLEREGFEVTYLdPEEDGILDLAKLKAAIRPDTILVSVMHVNNEmGVIQPIKEIGAICRAKKIIFHVDA 181
Cdd:COG0403 167 QTRAVLKT--YAEPLGIEVVEV-PDEDGVTDLEALKALLDDDVAGVLVQYPNFF-GVIEDLRAIAEAAHAAGALVIVAA 241
|
|
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